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Database: UniProt
Entry: P05556
LinkDB: P05556
Original site: P05556 
ID   ITB1_HUMAN              Reviewed;         798 AA.
AC   P05556; A8K6N2; D3DRX9; D3DRY3; D3DRY4; D3DRY5; P78466; P78467;
AC   Q13089; Q13090; Q13091; Q13212; Q14622; Q14647; Q29RW2; Q7Z3V1;
AC   Q8WUM6;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   10-APR-2019, entry version 237.
DE   RecName: Full=Integrin beta-1;
DE   AltName: Full=Fibronectin receptor subunit beta;
DE   AltName: Full=Glycoprotein IIa;
DE            Short=GPIIA;
DE   AltName: Full=VLA-4 subunit beta;
DE   AltName: CD_antigen=CD29;
DE   Flags: Precursor;
GN   Name=ITGB1; Synonyms=FNRB, MDF2, MSK12;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=2958481; DOI=10.1083/jcb.105.3.1183;
RA   Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D.,
RA   Ruoslahti E.;
RT   "Amino acid sequence of the human fibronectin receptor.";
RL   J. Cell Biol. 105:1183-1190(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Endometrium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 717-757, CHARACTERIZATION OF
RP   BETA-1B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=7681433; DOI=10.1083/jcb.121.1.171;
RA   Balzac F., Belkin A.M., Koteliansky V.E., Balabanov Y.V., Altruda F.,
RA   Silengo L., Tarone G.;
RT   "Expression and functional analysis of a cytoplasmic domain variant of
RT   the beta 1 integrin subunit.";
RL   J. Cell Biol. 121:171-178(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 717-757, AND FUNCTION.
RX   PubMed=7523423; DOI=10.1083/jcb.127.2.557;
RA   Balzac F., Retta S.F., Albini A., Melchiorri A., Koteliansky V.E.,
RA   Geuna M., Silengo L., Tarone G.;
RT   "Expression of beta 1B integrin isoform in CHO cells results in a
RT   dominant negative effect on cell adhesion and motility.";
RL   J. Cell Biol. 127:557-565(1994).
RN   [9]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Skeletal muscle;
RX   PubMed=2249781; DOI=10.1016/0378-1119(90)90369-3;
RA   Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G.,
RA   Silengo L.;
RT   "A human integrin beta 1 subunit with a unique cytoplasmic domain
RT   generated by alternative mRNA processing.";
RL   Gene 95:261-266(1990).
RN   [10]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=1551917;
RA   Languino L.R., Ruoslahti E.;
RT   "An alternative form of the integrin beta 1 subunit with a variant
RT   cytoplasmic domain.";
RL   J. Biol. Chem. 267:7116-7120(1992).
RN   [11]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Skeletal muscle;
RX   PubMed=7545396; DOI=10.1006/bbrc.1995.2285;
RA   Zhidkova N.I., Belkin A.M., Mayne R.;
RT   "Novel isoform of beta 1 integrin expressed in skeletal and cardiac
RT   muscle.";
RL   Biochem. Biophys. Res. Commun. 214:279-285(1995).
RN   [12]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=7544298; DOI=10.1016/0014-5793(95)00814-P;
RA   van der Flier A., Kuikman I., Baudoin C., van der Neut R.,
RA   Sonnenberg A.;
RT   "A novel beta 1 integrin isoform produced by alternative splicing:
RT   unique expression in cardiac and skeletal muscle.";
RL   FEBS Lett. 369:340-344(1995).
RN   [13]
RP   PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4), AND TISSUE SPECIFICITY.
RX   PubMed=9494094; DOI=10.1042/bj3301255;
RA   Svineng G., Faessler R., Johansson S.;
RT   "Identification of beta1C-2, a novel variant of the integrin beta1
RT   subunit generated by utilization of an alternative splice acceptor
RT   site in exon C.";
RL   Biochem. J. 330:1255-1263(1998).
RN   [14]
RP   PROTEIN SEQUENCE OF 775-784 (ISOFORM 5), IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND INTERACTION WITH ACE2.
RX   PubMed=15276642; DOI=10.1016/j.bbadis.2004.05.005;
RA   Lin Q., Keller R.S., Weaver B., Zisman L.S.;
RT   "Interaction of ACE2 and integrin beta1 in failing human heart.";
RL   Biochim. Biophys. Acta 1689:175-178(2004).
RN   [15]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ECHOVIRUS 1
RP   AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
RX   PubMed=8411387;
RA   Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H.,
RA   Modlin J., Finberg R.W.;
RT   "Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of
RT   human VLA-2.";
RL   J. Virol. 67:6847-6852(1993).
RN   [16]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8567725; DOI=10.1083/jcb.132.1.211;
RA   Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D.,
RA   Maier A., Tarone G., Koteliansky V.E., Burridge K.;
RT   "Beta 1D integrin displaces the beta 1A isoform in striated muscles:
RT   localization at junctional structures and signaling potential in
RT   nonmuscle cells.";
RL   J. Cell Biol. 132:211-226(1996).
RN   [17]
RP   INTERACTION WITH LGALS3BP.
RX   PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA   Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT   "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT   matrix which self-assembles into ring-like structures and binds beta1
RT   integrins, collagens and fibronectin.";
RL   EMBO J. 17:1606-1613(1998).
RN   [18]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT.
RX   PubMed=10397733;
RA   Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
RA   Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
RT   "The Tat protein of human immunodeficiency virus type-1 promotes
RT   vascular cell growth and locomotion by engaging the alpha5beta1 and
RT   alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
RT   growth factor.";
RL   Blood 94:663-672(1999).
RN   [19]
RP   FUNCTION, SUBUNIT, INTERACTION WITH FAP, AND SUBCELLULAR LOCATION.
RX   PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
RA   Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
RA   Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
RT   "A novel protease-docking function of integrin at invadopodia.";
RL   J. Biol. Chem. 274:24947-24952(1999).
RN   [20]
RP   INTERACTION WITH NMRK2.
RC   TISSUE=Heart;
RX   PubMed=10613898; DOI=10.1083/jcb.147.7.1391;
RA   Li J., Mayne R., Wu C.;
RT   "A novel muscle-specific beta 1 integrin binding protein (MIBP) that
RT   modulates myogenic differentiation.";
RL   J. Cell Biol. 147:1391-1398(1999).
RN   [21]
RP   INTERACTION WITH ITGB1BP1.
RX   PubMed=11741838; DOI=10.1093/hmg/10.25.2953;
RA   Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.;
RT   "Interaction between krit1 and icap1alpha infers perturbation of
RT   integrin beta1-mediated angiogenesis in the pathogenesis of cerebral
RT   cavernous malformation.";
RL   Hum. Mol. Genet. 10:2953-2960(2001).
RN   [22]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11919189; DOI=10.1074/jbc.M200200200;
RA   Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C.,
RA   Block M.R., Albiges-Rizo C.;
RT   "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha)
RT   interacts directly with the metastasis suppressor nm23-H2, and both
RT   proteins are targeted to newly formed cell adhesion sites upon
RT   integrin engagement.";
RL   J. Biol. Chem. 277:20895-20902(2002).
RN   [23]
RP   INTERACTION WITH FLNA AND FLNB, AND MUTAGENESIS OF GLY-778 AND
RP   ALA-786.
RX   PubMed=11807098; DOI=10.1083/jcb.200103037;
RA   van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
RA   Takafuta T., Shapiro S.S., Sonnenberg A.;
RT   "Different splice variants of filamin-B affect myogenesis, subcellular
RT   distribution, and determine binding to integrin (beta) subunits.";
RL   J. Cell Biol. 156:361-376(2002).
RN   [24]
RP   INTERACTION WITH ITGB1BP1, AND MUTAGENESIS OF 786-ALA--VAL-791.
RX   PubMed=11807099; DOI=10.1083/jcb.200108030;
RA   Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F.,
RA   Silengo L., Eva A., Tarone G.;
RT   "The integrin cytoplasmic domain-associated protein ICAP-1 binds and
RT   regulates Rho family GTPases during cell spreading.";
RL   J. Cell Biol. 156:377-387(2002).
RN   [25]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PARVOVIRUS
RP   B19 CAPSID PROTEIN.
RX   PubMed=12907437; DOI=10.1182/blood-2003-05-1522;
RA   Weigel-Kelley K.A., Yoder M.C., Srivastava A.;
RT   "Alpha5beta1 integrin as a cellular coreceptor for human parvovirus
RT   B19: requirement of functional activation of beta1 integrin for viral
RT   entry.";
RL   Blood 102:3927-3933(2003).
RN   [26]
RP   FUNCTION, AND INTERACTION WITH ITGB1BP1.
RX   PubMed=12473654; DOI=10.1074/jbc.M211258200;
RA   Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N.,
RA   Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.;
RT   "Disruption of focal adhesions by integrin cytoplasmic domain-
RT   associated protein-1 alpha.";
RL   J. Biol. Chem. 278:6567-6574(2003).
RN   [27]
RP   INTERACTION WITH CCN3.
RX   PubMed=12695522; DOI=10.1074/jbc.M302028200;
RA   Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
RA   Lau L.F.;
RT   "CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
RT   family.";
RL   J. Biol. Chem. 278:24200-24208(2003).
RN   [28]
RP   FUNCTION, AND INTERACTION WITH FBN1.
RX   PubMed=12807887; DOI=10.1074/jbc.M303159200;
RA   Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
RA   Shuttleworth C.A., Humphries M.J., Kielty C.M.;
RT   "Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
RT   by alpha 5 beta 1 and alpha v beta 3 integrins.";
RL   J. Biol. Chem. 278:34605-34616(2003).
RN   [29]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ROTAVIRUS
RP   VP4 PROTEIN.
RX   PubMed=12941907; DOI=10.1128/JVI.77.18.9969-9978.2003;
RA   Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R.,
RA   Robinson M.K., Coulson B.S.;
RT   "Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain
RT   via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by
RT   using VP7 during cell entry.";
RL   J. Virol. 77:9969-9978(2003).
RN   [30]
RP   INTERACTION WITH RANBP9.
RX   PubMed=14722085; DOI=10.1074/jbc.M313515200;
RA   Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
RA   Fabbri M., Pardi R., Bianchi E.;
RT   "RanBPM is a phosphoprotein that associates with the plasma membrane
RT   and interacts with the integrin LFA-1.";
RL   J. Biol. Chem. 279:13027-13034(2004).
RN   [31]
RP   INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
RX   PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
RA   Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT   "NG2 proteoglycan promotes endothelial cell motility and angiogenesis
RT   via engagement of galectin-3 and alpha3beta1 integrin.";
RL   Mol. Biol. Cell 15:3580-3590(2004).
RN   [32]
RP   INTERACTION WITH MYO10.
RX   PubMed=15156152; DOI=10.1038/ncb1136;
RA   Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
RA   Cheney R.E., Stromblad S.;
RT   "Myosin-X provides a motor-based link between integrins and the
RT   cytoskeleton.";
RL   Nat. Cell Biol. 6:523-531(2004).
RN   [33]
RP   FUNCTION, INTERACTION WITH ACAP1, AND SUBCELLULAR LOCATION.
RX   PubMed=16256741; DOI=10.1016/j.devcel.2005.09.012;
RA   Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.;
RT   "Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent
RT   recycling of integrin beta1 to control cell migration.";
RL   Dev. Cell 9:663-673(2005).
RN   [34]
RP   INTERACTION WITH FLNB AND FLNC.
RX   PubMed=16076904; DOI=10.1242/jcs.02484;
RA   Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
RA   Carpen O., Faulkner G., Borradori L.;
RT   "The Z-disc proteins myotilin and FATZ-1 interact with each other and
RT   are connected to the sarcolemma via muscle-specific filamins.";
RL   J. Cell Sci. 118:3739-3749(2005).
RN   [35]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [36]
RP   INTERACTION WITH RAB21.
RX   PubMed=16754960; DOI=10.1083/jcb.200509019;
RA   Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
RA   Ivaska J.;
RT   "Small GTPase Rab21 regulates cell adhesion and controls endosomal
RT   traffic of beta1-integrins.";
RL   J. Cell Biol. 173:767-780(2006).
RN   [37]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA   Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA   Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA   Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [38]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MAMMALIAN
RP   REOVIRUS CAPSID PROTEINS.
RX   PubMed=16501085; DOI=10.1128/JVI.80.6.2760-2770.2006;
RA   Maginnis M.S., Forrest J.C., Kopecky-Bromberg S.A., Dickeson S.K.,
RA   Santoro S.A., Zutter M.M., Nemerow G.R., Bergelson J.M., Dermody T.S.;
RT   "Beta1 integrin mediates internalization of mammalian reovirus.";
RL   J. Virol. 80:2760-2770(2006).
RN   [39]
RP   FUNCTION, INTERACTION WITH KRT1, AND SUBCELLULAR LOCATION.
RX   PubMed=17956333; DOI=10.1042/BST0351292;
RA   Chuang N.N., Huang C.C.;
RT   "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma
RT   NMB7 cells.";
RL   Biochem. Soc. Trans. 35:1292-1294(2007).
RN   [40]
RP   INTERACTION WITH RAB25.
RX   PubMed=17925226; DOI=10.1016/j.devcel.2007.08.012;
RA   Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K.,
RA   Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I.,
RA   McCaffrey M.W., Ozanne B.W., Norman J.C.;
RT   "Rab25 associates with alpha5beta1 integrin to promote invasive
RT   migration in 3D microenvironments.";
RL   Dev. Cell 13:496-510(2007).
RN   [41]
RP   FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION.
RX   PubMed=17158881; DOI=10.1074/jbc.M607008200;
RA   Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
RA   van der Merwe P.A., Mardon H.J., Handford P.A.;
RT   "alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative
RT   studies of molecular determinants underlying integrin-rgd affinity and
RT   specificity.";
RL   J. Biol. Chem. 282:6743-6751(2007).
RN   [42]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA   Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H.,
RA   Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
RA   Kallio M., Ivaska J.;
RT   "Integrin trafficking regulated by Rab21 is necessary for
RT   cytokinesis.";
RL   Dev. Cell 15:371-385(2008).
RN   [43]
RP   FUNCTION.
RX   PubMed=18635536; DOI=10.1074/jbc.M804835200;
RA   Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
RA   Liu F.T., Takada Y.K., Takada Y.;
RT   "Pro-inflammatory secretory phospholipase A2 type IIA binds to
RT   integrins alphavbeta3 and alpha4beta1 and induces proliferation of
RT   monocytic cells in an integrin-dependent manner.";
RL   J. Biol. Chem. 283:26107-26115(2008).
RN   [44]
RP   FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, AND INTERACTION
RP   WITH JAML.
RX   PubMed=19064666; DOI=10.1083/jcb.200805061;
RA   Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O.,
RA   Bourdoulous S.;
RT   "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
RT   in cis by alpha4beta1 integrin activation.";
RL   J. Cell Biol. 183:1159-1173(2008).
RN   [45]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR
RP   VIRUS/HHV-4 GB PROTEIN.
RX   PubMed=17945327; DOI=10.1016/j.virol.2007.09.012;
RA   Xiao J., Palefsky J.M., Herrera R., Berline J., Tugizov S.M.;
RT   "The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to
RT   oral epithelial cells.";
RL   Virology 370:430-442(2008).
RN   [46]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [47]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [48]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [49]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [50]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HHV-5 GB.
RX   PubMed=20660204; DOI=10.1128/JVI.00710-10;
RA   Feire A.L., Roy R.M., Manley K., Compton T.;
RT   "The glycoprotein B disintegrin-like domain binds beta 1 integrin to
RT   mediate cytomegalovirus entry.";
RL   J. Virol. 84:10026-10037(2010).
RN   [51]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [52]
RP   INTERACTION WITH ASAP3.
RX   PubMed=22027826; DOI=10.1074/jbc.M111.278770;
RA   Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X.,
RA   Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.;
RT   "ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal
RT   growth factor-stimulated integrin beta1 recycling in cell migration.";
RL   J. Biol. Chem. 286:43735-43747(2011).
RN   [53]
RP   FUNCTION, INTERACTION WITH FERMT2 AND TLN1, AND MUTAGENESIS OF
RP   VAL-787.
RX   PubMed=21768292; DOI=10.1083/jcb.201007108;
RA   Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
RA   Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
RT   "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT   fibronectin deposition.";
RL   J. Cell Biol. 194:307-322(2011).
RN   [54]
RP   INTERACTION WITH FERMT2.
RX   PubMed=21325030; DOI=10.1242/jcs.076976;
RA   Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J.,
RA   Fukuda K., Qin J., Kretzler M., Wu C.;
RT   "Kindlin-2 regulates podocyte adhesion and fibronectin matrix
RT   deposition through interactions with phosphoinositides and
RT   integrins.";
RL   J. Cell Sci. 124:879-891(2011).
RN   [55]
RP   FUNCTION, BINDING TO CX3CL1, IDENTIFICATION IN A COMPLEX WITH CX3CR1
RP   AND CX3CL1, AND CX3CL1-BINDING REGION.
RX   PubMed=23125415; DOI=10.4049/jimmunol.1200889;
RA   Fujita M., Takada Y.K., Takada Y.;
RT   "Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
RT   fractalkine, and the integrin-binding defective mutant of fractalkine
RT   is an antagonist of CX3CR1.";
RL   J. Immunol. 189:5809-5819(2012).
RN   [56]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [57]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785 AND THR-789, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [58]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-794, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [59]
RP   FUNCTION.
RX   PubMed=25398877; DOI=10.1074/jbc.M114.579946;
RA   Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
RA   Takada Y.K., Takada Y.;
RT   "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
RT   integrin activation through direct binding to a newly identified
RT   binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
RT   alpha5beta1.";
RL   J. Biol. Chem. 290:259-271(2015).
RN   [60]
RP   BINDING TO CX3CL1, AND CX3CL1-BINDING REGION.
RX   PubMed=24789099; DOI=10.1371/journal.pone.0096372;
RA   Fujita M., Takada Y.K., Takada Y.;
RT   "The chemokine fractalkine can activate integrins without CX3CR1
RT   through direct binding to a ligand-binding site distinct from the
RT   classical RGD-binding site.";
RL   PLoS ONE 9:E96372-E96372(2014).
RN   [61]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [62]
RP   FUNCTION, AND INTERACTION WITH IL1B.
RX   PubMed=29030430; DOI=10.1074/jbc.M117.818302;
RA   Takada Y.K., Yu J., Fujita M., Saegusa J., Wu C.Y., Takada Y.;
RT   "Direct binding to integrins and loss of disulfide linkage in
RT   interleukin-1beta (IL-1beta) are involved in the agonistic action of
RT   IL-1beta.";
RL   J. Biol. Chem. 292:20067-20075(2017).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 758-769 IN COMPLEX WITH
RP   ACAP1, INTERACTION WITH ACAP1 AND ITGA5, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF 760-ARG-ARG-761; 762-GLU--PHE-767 AND 768-LYS-GLU-769.
RX   PubMed=22645133; DOI=10.1074/jbc.M112.378810;
RA   Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F.,
RA   Hsu V.W.;
RT   "Mechanistic insights into regulated cargo binding by ACAP1 protein.";
RL   J. Biol. Chem. 287:28675-28685(2012).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-465 IN COMPLEX WITH
RP   ANTIBODY; ITGA5 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT
RP   ASN-269 AND ASN-406, METAL-BINDING SITES, AND SUBUNIT.
RX   PubMed=22451694; DOI=10.1083/jcb.201111077;
RA   Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.;
RT   "Crystal structure of alpha5beta1 integrin ectodomain: atomic details
RT   of the fibronectin receptor.";
RL   J. Cell Biol. 197:131-140(2012).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 784-798 IN COMPLEX WITH
RP   ITGB1BP1, INTERACTION WITH ITGB1BP1, AND MUTAGENESIS OF THR-788;
RP   VAL-790; ASN-792 AND TYR-795.
RX   PubMed=23317506; DOI=10.1016/j.molcel.2012.12.005;
RA   Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.;
RT   "Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin
RT   activation.";
RL   Mol. Cell 49:719-729(2013).
CC   -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
CC       1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
CC       1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
CC       sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
CC       3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
CC       10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
CC       fibronectin. Alpha-4/beta-1 recognizes one or more domains within
CC       the alternatively spliced CS-1 and CS-5 regions of fibronectin.
CC       Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
CC       alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
CC       are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1)
CC       is present in oocytes and is involved in sperm-egg fusion (By
CC       similarity). Integrin alpha-4/beta-1 is a receptor for VCAM1. It
CC       recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1
CC       is a receptor for VCAM1, cytotactin and osteopontin. It recognizes
CC       the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-
CC       1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-
CC       3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of
CC       endothelial cells migration. Integrin alpha-V/beta-1 is a receptor
CC       for vitronectin. Beta-1 integrins recognize the sequence R-G-D in
CC       a wide array of ligands. Isoform 2 interferes with isoform 1
CC       resulting in a dominant negative effect on cell adhesion and
CC       migration (in vitro). When associated with alpha-7/beta-1
CC       integrin, regulates cell adhesion and laminin matrix deposition.
CC       Involved in promoting endothelial cell motility and angiogenesis.
CC       Involved in osteoblast compaction through the fibronectin
CC       fibrillogenesis cell-mediated matrix assembly process and the
CC       formation of mineralized bone nodules. May be involved in up-
CC       regulation of the activity of kinases such as PKC via binding to
CC       KRT1. Together with KRT1 and RACK1, serves as a platform for SRC
CC       activation or inactivation. Plays a mechanistic adhesive role
CC       during telophase, required for the successful completion of
CC       cytokinesis. Integrin alpha-3/beta-1 provides a docking site for
CC       FAP (seprase) at invadopodia plasma membranes in a collagen-
CC       dependent manner and hence may participate in the adhesion,
CC       formation of invadopodia and matrix degradation processes,
CC       promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1)
CC       and may act as its coreceptor in CX3CR1-dependent fractalkine
CC       signaling (PubMed:23125415, PubMed:24789099). ITGA4:ITGB1 and
CC       ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct
CC       from the classical ligand-binding site (site 1) and this induces
CC       integrin conformational changes and enhanced ligand binding to
CC       site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a
CC       receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
CC       adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1
CC       is a receptor for IL1B and binding is essential for IL1B signaling
CC       (PubMed:29030430). {ECO:0000250|UniProtKB:P09055,
CC       ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654,
CC       ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16256741,
CC       ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536,
CC       ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666,
CC       ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:23125415,
CC       ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877,
CC       ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:7523423}.
CC   -!- FUNCTION: Isoform 5: Isoform 5 displaces isoform 1 in striated
CC       muscles. {ECO:0000250}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a
CC       receptor for Human echoviruses 1 and 8.
CC       {ECO:0000269|PubMed:8411387}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for
CC       Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:20660204}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein-
CC       Barr virus/HHV-4. {ECO:0000269|PubMed:17945327}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a
CC       receptor for Human parvovirus B19. {ECO:0000269|PubMed:12907437}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a
CC       receptor for Human rotavirus. {ECO:0000269|PubMed:12941907}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for Mammalian
CC       reovirus. {ECO:0000269|PubMed:16501085}.
CC   -!- FUNCTION: (Microbial infection) In case of HIV-1 infection,
CC       integrin ITGA5:ITGB1 binding to extracellular viral Tat protein
CC       seems to enhance angiogenesis in Kaposi's sarcoma lesions.
CC       {ECO:0000269|PubMed:10397733}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1
CC       associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-
CC       5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
CC       alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction
CC       takes place in oocytes and is involved in sperm-egg fusion (By
CC       similarity). Interacts with seprase FAP (seprase); the interaction
CC       occurs at the cell surface of invadopodia membrane in a collagen-
CC       dependent manner. Binds LGALS3BP and NMRK2, when associated with
CC       alpha-7, but not with alpha-5. Interacts with FGR and HCK.
CC       Interacts (via the cytoplasmic region) with RAB25 (via the
CC       hypervariable C-terminal region). Interacts with RAB21. Interacts
CC       with KRT1 in the presence of RACK1 and SRC. Interacts with JAML;
CC       integrin alpha-4/beta-1 may regulate leukocyte to endothelial
CC       cells adhesion by controlling JAML homodimerization. Interacts
CC       with FLNA, FLNB and RANBP9. Isoform 5 interacts with ACE2. Isoform
CC       1 interacts with the C-terminal region of FLNC. Interacts with
CC       MYO10. Interacts with DAB2. Interacts with FERMT2; the interaction
CC       is inhibited in presence of ITGB1BP1. Interacts with ITGB1BP1 (via
CC       C-terminal region); the interaction is a prerequisite for focal
CC       adhesion disassembly. Interacts with TLN1; the interaction is
CC       prevented by competitive binding of ITGB1BP1. Interacts with
CC       ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Isoform
CC       5 interacts with alpha-7A and alpha-7B in adult skeletal muscle.
CC       Isoform 5 interacts with alpha-7B in cardiomyocytes of adult
CC       heart. Interacts with EMP2; the interaction may be direct or
CC       indirect and ITGB1 has an heterodimer form (By similarity).
CC       ITGA5:ITGB1 interacts with CCN3. ITGA4:ITGB1 is found in a ternary
CC       complex with CX3CR1 and CX3CL1 (PubMed:23125415). ITGA5:ITGB1
CC       interacts with FBN1 (PubMed:12807887, PubMed:17158881).
CC       ITGA5:ITGB1 interacts with IL1B (PubMed:29030430).
CC       {ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:10455171,
CC       ECO:0000269|PubMed:10613898, ECO:0000269|PubMed:11741838,
CC       ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:11807099,
CC       ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:12695522,
CC       ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:14722085,
CC       ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:15181153,
CC       ECO:0000269|PubMed:15276642, ECO:0000269|PubMed:16076904,
CC       ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:16754960,
CC       ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17925226,
CC       ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21325030,
CC       ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:22027826,
CC       ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:22645133,
CC       ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:23317506,
CC       ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:9501082}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
CC       human echoviruses 1 and 8 capsid proteins.
CC       {ECO:0000269|PubMed:8411387}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human
CC       cytomegalovirus/HHV-5 envelope glycoprotein B/gB.
CC       {ECO:0000269|PubMed:20660204}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr
CC       virus/HHV-4 gB protein. {ECO:0000269|PubMed:17945327}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
CC       human parvovirus B19 capsid protein.
CC       {ECO:0000269|PubMed:12907437}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
CC       human rotavirus VP4 protein. {ECO:0000269|PubMed:12941907}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with mammalian reovirus
CC       capsid proteins. {ECO:0000269|PubMed:16501085}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
CC       HIV-1 Tat. {ECO:0000269|PubMed:10397733}.
CC   -!- INTERACTION:
CC       Q9BY76:ANGPTL4; NbExp=2; IntAct=EBI-703066, EBI-2968146;
CC       P03192:BMRF2 (xeno); NbExp=2; IntAct=EBI-703066, EBI-9348955;
CC       P46109:CRKL; NbExp=2; IntAct=EBI-703066, EBI-910;
CC       P32927:CSF2RB; NbExp=5; IntAct=EBI-703066, EBI-1809771;
CC       P78423:CX3CL1; NbExp=2; IntAct=EBI-703066, EBI-15188013;
CC       P17813:ENG; NbExp=3; IntAct=EBI-703066, EBI-2834630;
CC       P05413:FABP3; NbExp=2; IntAct=EBI-703066, EBI-704216;
CC       P21333:FLNA; NbExp=5; IntAct=EBI-703066, EBI-350432;
CC       P17301:ITGA2; NbExp=5; IntAct=EBI-703066, EBI-702960;
CC       P13612:ITGA4; NbExp=4; IntAct=EBI-703066, EBI-703044;
CC       P08648:ITGA5; NbExp=6; IntAct=EBI-703066, EBI-1382311;
CC       P07948:LYN; NbExp=4; IntAct=EBI-703066, EBI-79452;
CC       P18031:PTPN1; NbExp=2; IntAct=EBI-703066, EBI-968788;
CC       P49023:PXN; NbExp=2; IntAct=EBI-6082935, EBI-702209;
CC       P35282:Rab21 (xeno); NbExp=3; IntAct=EBI-703066, EBI-1993555;
CC       Q9Y490:TLN1; NbExp=2; IntAct=EBI-703066, EBI-2462036;
CC       P26039:Tln1 (xeno); NbExp=2; IntAct=EBI-703066, EBI-1039593;
CC       Q71LX4:Tln2 (xeno); NbExp=3; IntAct=EBI-7208579, EBI-2255655;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:10455171};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell
CC       projection, invadopodium membrane {ECO:0000269|PubMed:10455171};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell
CC       projection, ruffle membrane {ECO:0000303|PubMed:10455171}; Single-
CC       pass type I membrane protein {ECO:0000255}. Recycling endosome
CC       {ECO:0000269|PubMed:16256741}. Melanosome
CC       {ECO:0000269|PubMed:17081065}. Cleavage furrow
CC       {ECO:0000269|PubMed:17956333}. Cell projection, lamellipodium
CC       {ECO:0000269|PubMed:11919189}. Cell projection, ruffle
CC       {ECO:0000269|PubMed:11919189}. Cell junction, focal adhesion
CC       {ECO:0000269|PubMed:17158881}. Cell surface
CC       {ECO:0000269|PubMed:17158881}. Note=Isoform 2 does not localize to
CC       focal adhesions. Highly enriched in stage I melanosomes. Located
CC       on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer
CC       cell line, in prometaphase and metaphase, localizes diffusely at
CC       the membrane and in a few intracellular vesicles. In early
CC       telophase, detected mainly on the matrix-facing side of the cells.
CC       By mid-telophase, concentrated to the ingressing cleavage furrow,
CC       mainly to the basal side of the furrow. In late telophase,
CC       concentrated to the extending protrusions formed at the opposite
CC       ends of the spreading daughter cells, in vesicles at the base of
CC       the lamellipodia formed by the separating daughter cells.
CC       Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2
CC       at the edge or peripheral ruffles and lamellipodia during the
CC       early stages of cell spreading on fibronectin or collagen.
CC       Translocates from peripheral focal adhesions sites to fibrillar
CC       adhesions in a ITGB1BP1-dependent manner. Enriched preferentially
CC       at invadopodia, cell membrane protrusions that correspond to sites
CC       of cell invasion, in a collagen-dependent manner. Localized at
CC       plasma and ruffle membranes in a collagen-independent manner.
CC       {ECO:0000269|PubMed:10455171, ECO:0000303|PubMed:10455171}.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane, sarcolemma
CC       {ECO:0000250}. Cell junction {ECO:0000250}. Note=In cardiac
CC       muscle, isoform 5 is found in costameres and intercalated disks.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=Beta-1A;
CC         IsoId=P05556-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta-1B;
CC         IsoId=P05556-2; Sequence=VSP_002741;
CC       Name=3; Synonyms=Beta-1C;
CC         IsoId=P05556-3; Sequence=VSP_002742;
CC       Name=4; Synonyms=Beta-1C-2;
CC         IsoId=P05556-4; Sequence=VSP_002743;
CC       Name=5; Synonyms=Beta-1D;
CC         IsoId=P05556-5; Sequence=VSP_002744;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed, other isoforms
CC       are generally coexpressed with a more restricted distribution.
CC       Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac
CC       muscle, placenta, umbilical vein endothelial cells, neuroblastoma
CC       cells, lymphoma cells, hepatoma cells and astrocytoma cells.
CC       Isoform 3 and isoform 4 are expressed in muscle, kidney, liver,
CC       placenta, cervical epithelium, umbilical vein endothelial cells,
CC       fibroblast cells, embryonal kidney cells, platelets and several
CC       blood cell lines. Isoform 4, rather than isoform 3, is selectively
CC       expressed in peripheral T-cells. Isoform 3 is expressed in non-
CC       proliferating and differentiated prostate gland epithelial cells
CC       and in platelets, on the surface of erythroleukemia cells and in
CC       various hematopoietic cell lines. Isoform 5 is expressed
CC       specifically in striated muscle (skeletal and cardiac muscle).
CC       {ECO:0000269|PubMed:1551917, ECO:0000269|PubMed:2249781,
CC       ECO:0000269|PubMed:7544298, ECO:0000269|PubMed:7545396,
CC       ECO:0000269|PubMed:7681433, ECO:0000269|PubMed:9494094}.
CC   -!- PTM: The cysteine residues are involved in intrachain disulfide
CC       bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD97649.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=CD29 entry;
CC       URL="https://en.wikipedia.org/wiki/CD29";
DR   EMBL; X07979; CAA30790.1; -; mRNA.
DR   EMBL; AK291697; BAF84386.1; -; mRNA.
DR   EMBL; BX537407; CAD97649.1; ALT_INIT; mRNA.
DR   EMBL; AL365203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471072; EAW85948.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85949.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85950.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85951.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85952.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85953.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85954.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85955.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85957.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85958.1; -; Genomic_DNA.
DR   EMBL; CH471072; EAW85959.1; -; Genomic_DNA.
DR   EMBL; BC020057; AAH20057.1; -; mRNA.
DR   EMBL; BC113901; AAI13902.1; -; mRNA.
DR   EMBL; U33879; AAA79832.1; -; Genomic_DNA.
DR   EMBL; U33880; AAA79833.1; -; Genomic_DNA.
DR   EMBL; U33879; AAA79833.1; JOINED; Genomic_DNA.
DR   EMBL; U33882; AAA79834.1; -; Genomic_DNA.
DR   EMBL; U33879; AAA79834.1; JOINED; Genomic_DNA.
DR   EMBL; U33881; AAA79834.1; JOINED; Genomic_DNA.
DR   EMBL; U33882; AAA79835.1; -; Genomic_DNA.
DR   EMBL; U33879; AAA79835.1; JOINED; Genomic_DNA.
DR   EMBL; M34189; AAA59182.1; -; mRNA.
DR   EMBL; M84237; AAA74402.1; -; mRNA.
DR   EMBL; M84237; AAA74403.1; -; mRNA.
DR   EMBL; U28252; AAA81366.1; -; mRNA.
DR   CCDS; CCDS7174.1; -. [P05556-1]
DR   PIR; B27079; B27079.
DR   RefSeq; NP_002202.2; NM_002211.3. [P05556-1]
DR   RefSeq; NP_391988.1; NM_033668.2. [P05556-5]
DR   RefSeq; NP_596867.1; NM_133376.2. [P05556-1]
DR   UniGene; Hs.643813; -.
DR   PDB; 1K11; Model; -; B=786-797.
DR   PDB; 1LHA; Model; -; A=86-543.
DR   PDB; 3G9W; X-ray; 2.16 A; C/D=752-785.
DR   PDB; 3T9K; X-ray; 2.30 A; A/B=758-769.
DR   PDB; 3VI3; X-ray; 2.90 A; B/D=21-465.
DR   PDB; 3VI4; X-ray; 2.90 A; B/D=21-465.
DR   PDB; 4DX9; X-ray; 3.00 A; 6/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z=784-798.
DR   PDB; 4WJK; X-ray; 1.85 A; B=21-465.
DR   PDB; 4WK0; X-ray; 1.78 A; B=21-465.
DR   PDB; 4WK2; X-ray; 2.50 A; B=21-465.
DR   PDB; 4WK4; X-ray; 2.50 A; B=21-465.
DR   PDBsum; 1K11; -.
DR   PDBsum; 1LHA; -.
DR   PDBsum; 3G9W; -.
DR   PDBsum; 3T9K; -.
DR   PDBsum; 3VI3; -.
DR   PDBsum; 3VI4; -.
DR   PDBsum; 4DX9; -.
DR   PDBsum; 4WJK; -.
DR   PDBsum; 4WK0; -.
DR   PDBsum; 4WK2; -.
DR   PDBsum; 4WK4; -.
DR   ProteinModelPortal; P05556; -.
DR   SMR; P05556; -.
DR   BioGrid; 109894; 111.
DR   ComplexPortal; CPX-1794; Integrin alpha5-beta1 complex.
DR   ComplexPortal; CPX-1797; Integrin alpha3-beta1 complex.
DR   ComplexPortal; CPX-1798; Integrin alpha1-beta1 complex.
DR   ComplexPortal; CPX-1801; Integrin alpha2-beta1 complex.
DR   ComplexPortal; CPX-1802; Integrin alpha4-beta1 complex.
DR   ComplexPortal; CPX-1803; Integrin alpha6-beta1 complex.
DR   ComplexPortal; CPX-1804; Integrin alpha7-beta1 complex.
DR   ComplexPortal; CPX-1815; Integrin alpha8-beta1 complex.
DR   ComplexPortal; CPX-1816; Integrin alpha9-beta1 complex.
DR   ComplexPortal; CPX-1817; Integrin alpha10-beta1 complex.
DR   ComplexPortal; CPX-1818; Integrin alpha11-beta1 complex.
DR   ComplexPortal; CPX-1819; Integrin alphav-beta1 complex.
DR   CORUM; P05556; -.
DR   DIP; DIP-312N; -.
DR   ELM; P05556; -.
DR   IntAct; P05556; 86.
DR   MINT; P05556; -.
DR   STRING; 9606.ENSP00000379350; -.
DR   BindingDB; P05556; -.
DR   ChEMBL; CHEMBL1905; -.
DR   DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
DR   GuidetoPHARMACOLOGY; 2455; -.
DR   TCDB; 9.B.87.1.8; the selenoprotein p receptor (selp-receptor) family.
DR   GlyConnect; 1414; -.
DR   GlyConnect; 283; -.
DR   iPTMnet; P05556; -.
DR   PhosphoSitePlus; P05556; -.
DR   SwissPalm; P05556; -.
DR   UniCarbKB; P05556; -.
DR   BioMuta; ITGB1; -.
DR   DMDM; 218563324; -.
DR   EPD; P05556; -.
DR   jPOST; P05556; -.
DR   MaxQB; P05556; -.
DR   PaxDb; P05556; -.
DR   PeptideAtlas; P05556; -.
DR   PRIDE; P05556; -.
DR   ProteomicsDB; 51850; -.
DR   ProteomicsDB; 51851; -. [P05556-2]
DR   ProteomicsDB; 51852; -. [P05556-3]
DR   ProteomicsDB; 51853; -. [P05556-4]
DR   ProteomicsDB; 51854; -. [P05556-5]
DR   DNASU; 3688; -.
DR   Ensembl; ENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
DR   Ensembl; ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
DR   Ensembl; ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
DR   GeneID; 3688; -.
DR   KEGG; hsa:3688; -.
DR   UCSC; uc001iwr.5; human. [P05556-1]
DR   CTD; 3688; -.
DR   DisGeNET; 3688; -.
DR   EuPathDB; HostDB:ENSG00000150093.18; -.
DR   GeneCards; ITGB1; -.
DR   HGNC; HGNC:6153; ITGB1.
DR   HPA; CAB003434; -.
DR   HPA; HPA059297; -.
DR   HPA; HPA069003; -.
DR   MIM; 135630; gene.
DR   neXtProt; NX_P05556; -.
DR   OpenTargets; ENSG00000150093; -.
DR   PharmGKB; PA29953; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P05556; -.
DR   KO; K05719; -.
DR   OMA; VVETPEC; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P05556; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-HSA-1566948; Elastic fibre formation.
DR   Reactome; R-HSA-1566977; Fibronectin matrix formation.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-210991; Basigin interactions.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-3000170; Syndecan interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-416700; Other semaphorin interactions.
DR   Reactome; R-HSA-445144; Signal transduction by L1.
DR   Reactome; R-HSA-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR   Reactome; R-HSA-447041; CHL1 interactions.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   Reactome; R-HSA-8875513; MET interacts with TNS proteins.
DR   SABIO-RK; P05556; -.
DR   SignaLink; P05556; -.
DR   SIGNOR; P05556; -.
DR   ChiTaRS; ITGB1; human.
DR   EvolutionaryTrace; P05556; -.
DR   GeneWiki; CD29; -.
DR   GenomeRNAi; 3688; -.
DR   PRO; PR:P05556; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000150093; Expressed in 245 organ(s), highest expression level in visceral pleura.
DR   ExpressionAtlas; P05556; baseline and differential.
DR   Genevisible; P05556; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0099699; C:integral component of synaptic membrane; IEA:Ensembl.
DR   GO; GO:0034665; C:integrin alpha1-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0034680; C:integrin alpha10-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0034681; C:integrin alpha11-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0034677; C:integrin alpha7-beta1 complex; IEA:Ensembl.
DR   GO; GO:0034678; C:integrin alpha8-beta1 complex; TAS:BHF-UCL.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR   GO; GO:0071438; C:invadopodium membrane; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR   GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; TAS:HGNC.
DR   GO; GO:0032587; C:ruffle membrane; NAS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
DR   GO; GO:0001968; F:fibronectin binding; IPI:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IC:BHF-UCL.
DR   GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR   GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IGI:MGI.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
DR   GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0030030; P:cell projection organization; ISS:ARUK-UCL.
DR   GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEP:BHF-UCL.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR   GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0021943; P:formation of radial glial scaffolds; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0030032; P:lamellipodium assembly; ISS:ARUK-UCL.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; ISS:ARUK-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:2000273; P:positive regulation of signaling receptor activity; IDA:BHF-UCL.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0010710; P:regulation of collagen catabolic process; IDA:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR027071; Integrin_beta-1.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF08725; Integrin_b_cyt; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SMART; SM00423; PSI; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS00243; INTEGRIN_BETA; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Calcium;
KW   Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Endosome; Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Integrin; Isopeptide bond; Magnesium;
KW   Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     20
FT   CHAIN        21    798       Integrin beta-1.
FT                                /FTId=PRO_0000016334.
FT   TOPO_DOM     21    728       Extracellular. {ECO:0000255}.
FT   TRANSMEM    729    751       Helical. {ECO:0000255}.
FT   TOPO_DOM    752    798       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      140    378       VWFA.
FT   REPEAT      466    515       I.
FT   REPEAT      516    559       II.
FT   REPEAT      560    598       III.
FT   REPEAT      599    635       IV.
FT   REGION      207    213       CX3CL1-binding.
FT                                {ECO:0000269|PubMed:23125415}.
FT   REGION      295    314       CX3CL1-binding.
FT                                {ECO:0000269|PubMed:24789099}.
FT   REGION      466    635       Cysteine-rich tandem repeats.
FT   REGION      762    767       Signal for sorting from recycling
FT                                endosomes; interaction with ACAP1.
FT   REGION      785    792       Interaction with ITGB1BP1.
FT   METAL       152    152       Magnesium.
FT   METAL       154    154       Calcium 1; via carbonyl oxygen.
FT   METAL       156    156       Calcium 1.
FT   METAL       157    157       Calcium 1.
FT   METAL       189    189       Calcium 2.
FT   METAL       244    244       Calcium 2.
FT   METAL       246    246       Calcium 2.
FT   METAL       248    248       Calcium 2; via carbonyl oxygen.
FT   METAL       249    249       Calcium 2.
FT   METAL       249    249       Magnesium.
FT   METAL       362    362       Calcium 1; via carbonyl oxygen.
FT   MOD_RES     777    777       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     783    783       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     785    785       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     789    789       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     794    794       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:22451694}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:22451694}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    481    481       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    584    584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   DISULFID     27     45       {ECO:0000269|PubMed:22451694}.
FT   DISULFID     35    464       {ECO:0000269|PubMed:22451694}.
FT   DISULFID     38     64       {ECO:0000269|PubMed:22451694}.
FT   DISULFID     48     75       {ECO:0000269|PubMed:22451694}.
FT   DISULFID    207    213       {ECO:0000269|PubMed:22451694}.
FT   DISULFID    261    301       {ECO:0000269|PubMed:22451694}.
FT   DISULFID    401    415       {ECO:0000269|PubMed:22451694}.
FT   DISULFID    435    462       {ECO:0000269|PubMed:22451694}.
FT   DISULFID    466    691       {ECO:0000305|PubMed:22451694}.
FT   DISULFID    477    489       {ECO:0000250}.
FT   DISULFID    486    525       {ECO:0000250}.
FT   DISULFID    491    500       {ECO:0000250}.
FT   DISULFID    502    516       {ECO:0000250}.
FT   DISULFID    531    536       {ECO:0000250}.
FT   DISULFID    533    568       {ECO:0000250}.
FT   DISULFID    538    553       {ECO:0000250}.
FT   DISULFID    555    560       {ECO:0000250}.
FT   DISULFID    574    579       {ECO:0000250}.
FT   DISULFID    576    607       {ECO:0000250}.
FT   DISULFID    581    590       {ECO:0000250}.
FT   DISULFID    592    599       {ECO:0000250}.
FT   DISULFID    613    618       {ECO:0000250}.
FT   DISULFID    615    661       {ECO:0000250}.
FT   DISULFID    620    630       {ECO:0000250}.
FT   DISULFID    633    636       {ECO:0000250}.
FT   DISULFID    640    649       {ECO:0000250}.
FT   DISULFID    646    723       {ECO:0000250}.
FT   DISULFID    665    699       {ECO:0000250}.
FT   CROSSLNK    794    794       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate. {ECO:0000244|PubMed:25114211}.
FT   VAR_SEQ     778    798       GENPIYKSAVTTVVNPKYEGK -> VSYKTSKKQSGL (in
FT                                isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_002741.
FT   VAR_SEQ     778    798       GENPIYKSAVTTVVNPKYEGK -> SLSVAQPGVQWCDISS
FT                                LQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP (in
FT                                isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_002742.
FT   VAR_SEQ     778    798       GENPIYKSAVTTVVNPKYEGK -> PGVQWCDISSLQPLTS
FT                                RFQQFSCLSLPSTWDYRVKILFIRVP (in isoform
FT                                4). {ECO:0000305}.
FT                                /FTId=VSP_002743.
FT   VAR_SEQ     778    798       GENPIYKSAVTTVVNPKYEGK -> QENPIYKSPINNFKNP
FT                                NYGRKAGL (in isoform 5). {ECO:0000305}.
FT                                /FTId=VSP_002744.
FT   MUTAGEN     760    761       RR->AA: No effect on interaction with
FT                                ACAP1. {ECO:0000269|PubMed:22645133}.
FT   MUTAGEN     762    767       EFAKFE->AAAAAA: Strongly reduces
FT                                interaction with ACAP1 and ability to
FT                                recycle; does not affect
FT                                heterodimerization with ITGA5.
FT                                {ECO:0000269|PubMed:22645133}.
FT   MUTAGEN     762    763       EF->AA: Slightly reduces interaction with
FT                                ACAP1.
FT   MUTAGEN     765    765       K->A: Reduces interaction with ACAP1.
FT   MUTAGEN     766    767       FE->AA: Slightly reduces interaction with
FT                                ACAP1.
FT   MUTAGEN     768    769       KE->AA: No effect on interaction with
FT                                ACAP1. {ECO:0000269|PubMed:22645133}.
FT   MUTAGEN     778    778       G->Q: Loss of beta-1A interaction with
FT                                FLNA and FLNB.
FT                                {ECO:0000269|PubMed:11807098}.
FT   MUTAGEN     786    791       AVTTVV->PINNFK: Does not interact with
FT                                ITGB1BP1. {ECO:0000269|PubMed:11807099}.
FT   MUTAGEN     786    786       A->P: Loss of beta-1A interaction with
FT                                FLNA and FLNB.
FT                                {ECO:0000269|PubMed:11807098}.
FT   MUTAGEN     787    787       V->T: Reduces interaction with ITGB1BP1,
FT                                but not with FERMT2 or TLN1. Inhibits
FT                                fibronectin deposition and mineralized
FT                                bone nodules formation.
FT                                {ECO:0000269|PubMed:21768292}.
FT   MUTAGEN     788    788       T->D: Strongly reduces ITGB1BP1 binding;
FT                                when associated with D-790.
FT                                {ECO:0000269|PubMed:23317506}.
FT   MUTAGEN     790    790       V->D: Strongly reduces ITGB1BP1 binding;
FT                                when associated with D-788.
FT                                {ECO:0000269|PubMed:23317506}.
FT   MUTAGEN     792    792       N->A: Strongly reduces ITGB1BP1 binding;
FT                                when associated with A-795.
FT                                {ECO:0000269|PubMed:23317506}.
FT   MUTAGEN     795    795       Y->A: Strongly reduces ITGB1BP1 binding;
FT                                when associated with A-792.
FT                                {ECO:0000269|PubMed:23317506}.
FT   CONFLICT    112    112       T -> H (in Ref. 1; CAA30790).
FT                                {ECO:0000305}.
FT   CONFLICT    215    215       S -> T (in Ref. 1; CAA30790).
FT                                {ECO:0000305}.
FT   CONFLICT    261    265       CGSLI -> VWMLL (in Ref. 6; AAI13902).
FT                                {ECO:0000305}.
FT   CONFLICT    385    386       EN -> DG (in Ref. 6; AAI13902).
FT                                {ECO:0000305}.
FT   CONFLICT    463    463       E -> V (in Ref. 2; BAF84386).
FT                                {ECO:0000305}.
FT   TURN         26     31       {ECO:0000244|PDB:4WK0}.
FT   HELIX        35     40       {ECO:0000244|PDB:4WK0}.
FT   STRAND       45     47       {ECO:0000244|PDB:4WK0}.
FT   HELIX        61     63       {ECO:0000244|PDB:4WK0}.
FT   STRAND       64     66       {ECO:0000244|PDB:4WK0}.
FT   HELIX        67     71       {ECO:0000244|PDB:4WK0}.
FT   TURN         72     74       {ECO:0000244|PDB:4WK0}.
FT   TURN         77     79       {ECO:0000244|PDB:4WK0}.
FT   STRAND       86     91       {ECO:0000244|PDB:4WK0}.
FT   HELIX       108    110       {ECO:0000244|PDB:4WK0}.
FT   STRAND      118    124       {ECO:0000244|PDB:4WK0}.
FT   STRAND      129    136       {ECO:0000244|PDB:4WK0}.
FT   STRAND      143    150       {ECO:0000244|PDB:4WK0}.
FT   HELIX       153    155       {ECO:0000244|PDB:4WK0}.
FT   HELIX       156    161       {ECO:0000244|PDB:4WK0}.
FT   HELIX       162    164       {ECO:0000244|PDB:4WK0}.
FT   HELIX       165    173       {ECO:0000244|PDB:4WK0}.
FT   TURN        174    176       {ECO:0000244|PDB:4WK0}.
FT   STRAND      180    187       {ECO:0000244|PDB:4WK0}.
FT   TURN        193    195       {ECO:0000244|PDB:4WK0}.
FT   HELIX       200    204       {ECO:0000244|PDB:4WK0}.
FT   STRAND      209    211       {ECO:0000244|PDB:4WK0}.
FT   STRAND      218    227       {ECO:0000244|PDB:4WK0}.
FT   HELIX       229    236       {ECO:0000244|PDB:4WK0}.
FT   STRAND      245    249       {ECO:0000244|PDB:4WK0}.
FT   HELIX       251    260       {ECO:0000244|PDB:4WK0}.
FT   HELIX       262    264       {ECO:0000244|PDB:4WK0}.
FT   STRAND      269    280       {ECO:0000244|PDB:4WK0}.
FT   HELIX       287    291       {ECO:0000244|PDB:4WK0}.
FT   TURN        311    313       {ECO:0000244|PDB:4WK0}.
FT   HELIX       319    328       {ECO:0000244|PDB:4WK0}.
FT   STRAND      331    337       {ECO:0000244|PDB:4WK0}.
FT   HELIX       339    341       {ECO:0000244|PDB:4WK0}.
FT   HELIX       342    351       {ECO:0000244|PDB:4WK0}.
FT   STRAND      352    359       {ECO:0000244|PDB:4WK0}.
FT   STRAND      362    364       {ECO:0000244|PDB:4WK4}.
FT   HELIX       367    379       {ECO:0000244|PDB:4WK0}.
FT   STRAND      382    386       {ECO:0000244|PDB:4WK0}.
FT   STRAND      393    400       {ECO:0000244|PDB:4WK0}.
FT   HELIX       402    404       {ECO:0000244|PDB:4WK0}.
FT   STRAND      406    408       {ECO:0000244|PDB:4WJK}.
FT   HELIX       409    413       {ECO:0000244|PDB:4WK0}.
FT   STRAND      423    432       {ECO:0000244|PDB:4WK0}.
FT   STRAND      437    439       {ECO:0000244|PDB:4WJK}.
FT   STRAND      441    447       {ECO:0000244|PDB:4WK0}.
FT   STRAND      454    461       {ECO:0000244|PDB:4WK0}.
FT   HELIX       752    769       {ECO:0000244|PDB:3G9W}.
FT   HELIX       770    772       {ECO:0000244|PDB:3G9W}.
SQ   SEQUENCE   798 AA;  88415 MW;  DE35979C1625578C CRC64;
     MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT
     SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV
     LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
     RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR
     ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
     CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
     SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI
     GDEVQFEISI TSNKCPKKDS DSFKIRPLGF TEEVEVILQY ICECECQSEG IPESPKCHEG
     NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
     RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE
     ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
     CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEVMVHVVEN
     PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
     PIYKSAVTTV VNPKYEGK
//
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