ID LIPA1_HUMAN Reviewed; 1202 AA.
AC Q13136; A6NLE3; Q13135; Q14567; Q8N4I2;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-MAY-2013, entry version 114.
DE RecName: Full=Liprin-alpha-1;
DE AltName: Full=LAR-interacting protein 1;
DE Short=LIP-1;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1;
DE Short=PTPRF-interacting protein alpha-1;
GN Name=PPFIA1; Synonyms=LIP1;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTPRF.
RX PubMed=7796809;
RA Serra-Pages C., Kedersha N.L., Fazikas L., Medley Q.G., Debant A.,
RA Streuli M.;
RT "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil
RT LAR-interacting protein co-localize at focal adhesions.";
RL EMBO J. 14:2827-2838(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 672-1123.
RA Taira T., Iguchi-Ariga S.M., Ariga H.;
RT "Molecular cloning of a cDNA encoding enhancer protein in hsp70
RT gene.";
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH PTPRD; PTPRF AND PTPRS.
RX PubMed=8524829; DOI=10.1073/pnas.92.25.11686;
RA Pulido R., Serra-Pages C., Tang M., Streuli M.;
RT "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-
RT tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma
RT isoforms are expressed in a tissue-specific manner and associate with
RT the LAR-interacting protein LIP.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11686-11690(1995).
RN [6]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PTPRD; PTPRF AND PTPRS.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230; SER-242 AND
RP SER-244, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-693
RP AND THR-1159, AND MASS SPECTROMETRY.
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-244
RP AND SER-448, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. May
CC localize receptor-like tyrosine phosphatases type 2A at specific
CC sites on the plasma membrane, possibly regulating their
CC interaction with the extracellular environment and their
CC association with substrates.
CC -!- SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and
CC liprins-beta. Interacts with the second PTPase domain of PTPRD,
CC PTPRF and PTPRS. Interacts with GIT1, KIF1A and GRIP1 (By
CC similarity).
CC -!- INTERACTION:
CC Q9NS73:MBIP; NbExp=3; IntAct=EBI-745426, EBI-741953;
CC Q14738:PPP2R5D; NbExp=2; IntAct=EBI-745426, EBI-396563;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Colocalizes with PTPRF at
CC the ends of focal adhesions most proximal to the cell nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=LAR-interacting protein 1b, LIP.1b, b;
CC IsoId=Q13136-1; Sequence=Displayed;
CC Name=2; Synonyms=LAR-interacting protein 1a, LIP.1a, a;
CC IsoId=Q13136-2; Sequence=VSP_009391;
CC Note=Due to intron retention. No experimental confirmation
CC available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate
CC homodimerization preferentially and heterodimerization type
CC alpha/alpha. The C-terminal, non-coiled coil regions mediate
CC heterodimerization type alpha/beta and interaction with PTPRD,
CC PTPRF and PTPRS.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC -!- SIMILARITY: Contains 3 SAM (sterile alpha motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08353.1; Type=Frameshift; Positions=1033, 1041, 1045, 1067, 1113;
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DR EMBL; U22815; AAC50172.1; -; mRNA.
DR EMBL; U22816; AAC50173.1; -; mRNA.
DR EMBL; AP002336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034046; AAH34046.1; -; mRNA.
DR EMBL; D49354; BAA08353.1; ALT_FRAME; mRNA.
DR IPI; IPI00163496; -.
DR IPI; IPI00219754; -.
DR PIR; S55553; S55553.
DR RefSeq; NP_003617.1; NM_003626.3.
DR RefSeq; NP_803172.1; NM_177423.2.
DR UniGene; Hs.530749; -.
DR UniGene; Hs.708791; -.
DR ProteinModelPortal; Q13136; -.
DR IntAct; Q13136; 9.
DR MINT; MINT-1460222; -.
DR STRING; 9606.ENSP00000253925; -.
DR PhosphoSite; Q13136; -.
DR DMDM; 42558969; -.
DR PaxDb; Q13136; -.
DR PRIDE; Q13136; -.
DR DNASU; 8500; -.
DR Ensembl; ENST00000253925; ENSP00000253925; ENSG00000131626.
DR Ensembl; ENST00000389547; ENSP00000374198; ENSG00000131626.
DR GeneID; 8500; -.
DR KEGG; hsa:8500; -.
DR UCSC; uc001opn.2; human.
DR UCSC; uc001opo.3; human.
DR CTD; 8500; -.
DR GeneCards; GC11P070116; -.
DR HGNC; HGNC:9245; PPFIA1.
DR HPA; CAB017032; -.
DR MIM; 611054; gene.
DR neXtProt; NX_Q13136; -.
DR PharmGKB; PA33566; -.
DR eggNOG; NOG322697; -.
DR HOGENOM; HOG000017513; -.
DR HOVERGEN; HBG052330; -.
DR InParanoid; Q13136; -.
DR OMA; SVPDFRF; -.
DR OrthoDB; EOG40GCQ1; -.
DR SignaLink; Q13136; -.
DR GenomeRNAi; 8500; -.
DR NextBio; 31805; -.
DR PMAP-CutDB; Q13136; -.
DR ArrayExpress; Q13136; -.
DR Bgee; Q13136; -.
DR CleanEx; HS_PPFIA1; -.
DR Genevestigator; Q13136; -.
DR GermOnline; ENSG00000131626; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR Gene3D; 1.10.150.50; -; 2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR011510; SAM_2.
DR InterPro; IPR021129; SAM_type1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SAM_homology; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 1202 Liprin-alpha-1.
FT /FTId=PRO_0000191026.
FT DOMAIN 878 944 SAM 1.
FT DOMAIN 963 1027 SAM 2.
FT DOMAIN 1051 1120 SAM 3.
FT COILED 34 141 Potential.
FT COILED 176 214 Potential.
FT COILED 249 521 Potential.
FT COILED 623 669 Potential.
FT COILED 847 871 Potential.
FT COILED 1021 1050 Potential.
FT COMPBIAS 17 25 Poly-Gly.
FT MOD_RES 230 230 Phosphothreonine.
FT MOD_RES 239 239 Phosphoserine.
FT MOD_RES 242 242 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 448 448 Phosphoserine.
FT MOD_RES 693 693 Phosphoserine.
FT MOD_RES 1159 1159 Phosphothreonine.
FT VAR_SEQ 1185 1202 NVSGTQRLDSATVRTYSC -> M (in isoform 2).
FT /FTId=VSP_009391.
FT VARIANT 71 71 V -> I (in dbSNP:rs546502).
FT /FTId=VAR_017756.
FT VARIANT 1072 1072 L -> F (in dbSNP:rs11236045).
FT /FTId=VAR_049998.
FT CONFLICT 492 492 E -> G (in Ref. 3; AAH34046).
FT CONFLICT 555 555 P -> T (in Ref. 3; AAH34046).
FT CONFLICT 672 674 LGR -> EFG (in Ref. 4; BAA08353).
FT CONFLICT 800 801 KK -> EE (in Ref. 4; BAA08353).
FT CONFLICT 866 866 E -> G (in Ref. 3; AAH34046).
FT CONFLICT 994 994 L -> Q (in Ref. 4; BAA08353).
FT CONFLICT 1023 1023 C -> S (in Ref. 4; BAA08353).
FT CONFLICT 1044 1044 E -> EVRV (in Ref. 4; BAA08353).
FT CONFLICT 1121 1123 GTD -> PEF (in Ref. 4; BAA08353).
SQ SEQUENCE 1202 AA; 135779 MW; C8CF7C20B298BFB1 CRC64;
MMCEVMPTIS EAEGPPGGGG GHGSGSPSQP DADSHFEQLM VSMLEERDRL LDTLRETQET
LALTQGKLHE VGHERDSLQR QLNTALPQEF AALTKELNVC REQLLEREEE IAELKAERNN
TRLLLEHLEC LVSRHERSLR MTVVKRQAQS PAGVSSEVEV LKALKSLFEH HKALDEKVRE
RLRVALERCS LLEEELGATH KELMILKEQN NQKKTLTDGV LDINHEQENT PSTSGKRSSD
GSLSHEEDLA KVIELQEIIS KQSREQSQMK ERLASLSSHV TELEEDLDTA RKDLIKSEEM
NTKLQRDVRE AMAQKEDMEE RITTLEKRYL AAQREATSVH DLNDKLENEI ANKDSMHRQT
EDKNRQLQER LELAEQKLQQ TLRKAETLPE VEAELAQRVA ALSKAEERHG NIEERLRQME
AQLEEKNQEL QRARQREKMN EEHNKRLSDT VDKLLSESNE RLQLHLKERM AALEDKNSLL
REVESAKKQL EETQHDKDQL VLNIEALRAE LDHMRLRGAS LHHGRPHLGS VPDFRFPMAD
GHTDSYSTSA VLRRPQKGRL AALRDEPSKV QTLNEQDWER AQQASVLANV AQAFESDADV
SDGEDDRDTL LSSVDLLSPS GQADAHTLAM MLQEQLDAIN KEIRLIQEEK ENTEQRAEEI
ESRVGSGSLD NLGRFRSMSS IPPYPASSLA SSSPPGSGRS TPRRIPHSPA REVDRLGVMT
LLPPSREEVR DDKTTIKCET SPPSSPRALR LDRLHKGALH TVSHEDIRDI RNSTGSQDGP
VSNPSSSNSS QDSLHKAPKK KGIKSSIGRL FGKKEKGRPG QTGKEALGQA GVSETDNSSQ
DALGLSKLGG QAEKNRKLQK KHELLEEARR QGLPFAQWDG PTVVVWLELW VGMPAWYVAA
CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE IMSLTSPSAP PTSRTTLAYG
DMNHEWIGNE WLPSLGLPQY RSYFMECLVD ARMLDHLTKK DLRGQLKMVD SFHRNSFQCG
IMCLRRLNYD RKELERKREE SQSEIKDVLV WSNDRVIRWI LSIGLKEYAN NLIESGVHGA
LLALDETFDF SALALLLQIP TQNTQARAVL EREFNNLLVM GTDRRFDEDD DKSFRRAPSW
RKKFRPKDIR GLAAGSAETL PANFRVTSSM SSPSMQPKKM QMDGNVSGTQ RLDSATVRTY
SC
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