GenomeNet

Database: UniProt
Entry: Q13136
LinkDB: Q13136
Original site: Q13136 
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   01-OCT-2014, entry version 127.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-693
RP   AND THR-1159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-242; SER-244
RP   AND SER-448, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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. {ECO:0000269|PubMed:7796809}.
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). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P19491:Gria2 (xeno); NbExp=2; IntAct=EBI-745426, EBI-77718;
CC       P97879:Grip1 (xeno); NbExp=4; IntAct=EBI-745426, EBI-936113;
CC       Q9NS73:MBIP; NbExp=3; IntAct=EBI-745426, EBI-741953;
CC       Q14738:PPP2R5D; NbExp=2; IntAct=EBI-745426, EBI-396563;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7796809}.
CC       Note=Colocalizes with PTPRF at the ends of focal adhesions most
CC       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. {ECO:0000269|PubMed:7796809,
CC       ECO:0000269|PubMed:9624153}.
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       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 SAM (sterile alpha motif) domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00184}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA08353.1; Type=Frameshift; Positions=1033, 1041, 1045, 1067, 1113; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CCDS; CCDS31627.1; -. [Q13136-1]
DR   CCDS; CCDS31628.1; -. [Q13136-2]
DR   PIR; S55553; S55553.
DR   RefSeq; NP_003617.1; NM_003626.3. [Q13136-1]
DR   RefSeq; NP_803172.1; NM_177423.2. [Q13136-2]
DR   UniGene; Hs.530749; -.
DR   UniGene; Hs.708791; -.
DR   PDB; 1N7F; X-ray; 1.80 A; C/D=1195-1202.
DR   PDBsum; 1N7F; -.
DR   ProteinModelPortal; Q13136; -.
DR   SMR; Q13136; 851-1120.
DR   BioGrid; 114072; 33.
DR   IntAct; Q13136; 16.
DR   MINT; MINT-1460222; -.
DR   STRING; 9606.ENSP00000253925; -.
DR   PhosphoSite; Q13136; -.
DR   DMDM; 42558969; -.
DR   MaxQB; Q13136; -.
DR   PaxDb; Q13136; -.
DR   PRIDE; Q13136; -.
DR   DNASU; 8500; -.
DR   Ensembl; ENST00000253925; ENSP00000253925; ENSG00000131626. [Q13136-1]
DR   Ensembl; ENST00000389547; ENSP00000374198; ENSG00000131626. [Q13136-2]
DR   GeneID; 8500; -.
DR   KEGG; hsa:8500; -.
DR   UCSC; uc001opn.2; human. [Q13136-2]
DR   UCSC; uc001opo.3; human. [Q13136-1]
DR   CTD; 8500; -.
DR   GeneCards; GC11P070116; -.
DR   HGNC; HGNC:9245; PPFIA1.
DR   HPA; CAB017032; -.
DR   HPA; HPA008272; -.
DR   HPA; HPA042271; -.
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; EOG7T7GS7; -.
DR   PhylomeDB; Q13136; -.
DR   TreeFam; TF314207; -.
DR   SignaLink; Q13136; -.
DR   GeneWiki; Liprin-alpha-1; -.
DR   GenomeRNAi; 8500; -.
DR   NextBio; 31805; -.
DR   PMAP-CutDB; Q13136; -.
DR   PRO; PR:Q13136; -.
DR   ArrayExpress; Q13136; -.
DR   Bgee; Q13136; -.
DR   CleanEx; HS_PPFIA1; -.
DR   Genevestigator; Q13136; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
DR   GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR   GO; GO:0090005; P:negative regulation of establishment of protein localization to plasma membrane; IMP:MGI.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 1.10.150.50; -; 2.
DR   InterPro; IPR029515; Liprin.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR021129; SAM_type1.
DR   PANTHER; PTHR12587; PTHR12587; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SSF47769; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW   Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT   CHAIN         1   1202       Liprin-alpha-1.
FT                                /FTId=PRO_0000191026.
FT   DOMAIN      878    944       SAM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00184}.
FT   DOMAIN      963   1027       SAM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00184}.
FT   DOMAIN     1051   1120       SAM 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00184}.
FT   COILED       34    141       {ECO:0000255}.
FT   COILED      176    214       {ECO:0000255}.
FT   COILED      249    521       {ECO:0000255}.
FT   COILED      623    669       {ECO:0000255}.
FT   COILED      847    871       {ECO:0000255}.
FT   COILED     1021   1050       {ECO:0000255}.
FT   COMPBIAS     17     25       Poly-Gly.
FT   MOD_RES     230    230       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   MOD_RES     239    239       Phosphoserine.
FT                                {ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     242    242       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     244    244       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     448    448       Phosphoserine.
FT                                {ECO:0000269|PubMed:21406692}.
FT   MOD_RES     693    693       Phosphoserine.
FT                                {ECO:0000269|PubMed:19690332}.
FT   MOD_RES    1159   1159       Phosphothreonine.
FT                                {ECO:0000269|PubMed:19690332}.
FT   VAR_SEQ    1185   1202       NVSGTQRLDSATVRTYSC -> M (in isoform 2).
FT                                {ECO:0000303|PubMed:7796809}.
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                                {ECO:0000305}.
FT   CONFLICT    555    555       P -> T (in Ref. 3; AAH34046).
FT                                {ECO:0000305}.
FT   CONFLICT    672    674       LGR -> EFG (in Ref. 4; BAA08353).
FT                                {ECO:0000305}.
FT   CONFLICT    800    801       KK -> EE (in Ref. 4; BAA08353).
FT                                {ECO:0000305}.
FT   CONFLICT    866    866       E -> G (in Ref. 3; AAH34046).
FT                                {ECO:0000305}.
FT   CONFLICT    994    994       L -> Q (in Ref. 4; BAA08353).
FT                                {ECO:0000305}.
FT   CONFLICT   1023   1023       C -> S (in Ref. 4; BAA08353).
FT                                {ECO:0000305}.
FT   CONFLICT   1044   1044       E -> EVRV (in Ref. 4; BAA08353).
FT                                {ECO:0000305}.
FT   CONFLICT   1121   1123       GTD -> PEF (in Ref. 4; BAA08353).
FT                                {ECO:0000305}.
FT   STRAND     1198   1201
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
//
DBGET integrated database retrieval system