LIPA1_HUMAN
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 03-AUG-2022, entry version 193.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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; DOI=10.1002/j.1460-2075.1995.tb07282.x;
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 LAR-
RT 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., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., 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 project:
RT 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 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-tyrosine-
RT phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are
RT expressed in a tissue-specific manner and associate with the LAR-
RT 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230; SER-242 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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 AND
RP THR-1159, AND IDENTIFICATION 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 [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., Buerckstuemmer T.,
RA 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 AND
RP SER-448, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-239; SER-242;
RP SER-666; SER-693; SER-763 AND SER-1133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND THR-761, 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. May localize
CC receptor-like tyrosine phosphatases type 2A at specific sites on the
CC plasma membrane, possibly regulating their interaction with the
CC extracellular environment and their association with substrates.
CC {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, PTPRF
CC and PTPRS. Interacts with GIT1, KIF1A and GRIP1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q13136; P51946: CCNH; NbExp=6; IntAct=EBI-745426, EBI-741406;
CC Q13136; Q07002: CDK18; NbExp=3; IntAct=EBI-745426, EBI-746238;
CC Q13136; O60941: DTNB; NbExp=6; IntAct=EBI-745426, EBI-740402;
CC Q13136; Q13409-3: DYNC1I2; NbExp=3; IntAct=EBI-745426, EBI-12094038;
CC Q13136; Q14241: ELOA; NbExp=3; IntAct=EBI-745426, EBI-742350;
CC Q13136; Q3B820: FAM161A; NbExp=5; IntAct=EBI-745426, EBI-719941;
CC Q13136; O95995: GAS8; NbExp=3; IntAct=EBI-745426, EBI-1052570;
CC Q13136; Q9NS73: MBIP; NbExp=3; IntAct=EBI-745426, EBI-741953;
CC Q13136; Q15172: PPP2R5A; NbExp=3; IntAct=EBI-745426, EBI-641666;
CC Q13136; Q14738: PPP2R5D; NbExp=5; IntAct=EBI-745426, EBI-396563;
CC Q13136; P40222: TXLNA; NbExp=5; IntAct=EBI-745426, EBI-359793;
CC Q13136; P19491: Gria2; Xeno; NbExp=2; IntAct=EBI-745426, EBI-77718;
CC Q13136; P97879: Grip1; Xeno; NbExp=4; IntAct=EBI-745426, EBI-936113;
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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7796809,
CC ECO:0000269|PubMed:9624153}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type alpha/alpha. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type alpha/beta and
CC interaction with PTPRD, PTPRF and PTPRS.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08353.1; Type=Frameshift; Evidence={ECO:0000305};
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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 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 PDB; 1N7F; X-ray; 1.80 A; C/D=1195-1202.
DR PDBsum; 1N7F; -.
DR AlphaFoldDB; Q13136; -.
DR SMR; Q13136; -.
DR BioGRID; 114072; 164.
DR ELM; Q13136; -.
DR IntAct; Q13136; 64.
DR MINT; Q13136; -.
DR STRING; 9606.ENSP00000253925; -.
DR GlyGen; Q13136; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13136; -.
DR MetOSite; Q13136; -.
DR PhosphoSitePlus; Q13136; -.
DR BioMuta; PPFIA1; -.
DR DMDM; 42558969; -.
DR EPD; Q13136; -.
DR jPOST; Q13136; -.
DR MassIVE; Q13136; -.
DR MaxQB; Q13136; -.
DR PaxDb; Q13136; -.
DR PeptideAtlas; Q13136; -.
DR PRIDE; Q13136; -.
DR ProteomicsDB; 59184; -. [Q13136-1]
DR ProteomicsDB; 59185; -. [Q13136-2]
DR Antibodypedia; 30679; 201 antibodies from 31 providers.
DR DNASU; 8500; -.
DR Ensembl; ENST00000253925.12; ENSP00000253925.7; ENSG00000131626.19. [Q13136-1]
DR Ensembl; ENST00000389547.7; ENSP00000374198.3; ENSG00000131626.19. [Q13136-2]
DR GeneID; 8500; -.
DR KEGG; hsa:8500; -.
DR MANE-Select; ENST00000253925.12; ENSP00000253925.7; NM_003626.5; NP_003617.1.
DR UCSC; uc001opn.3; human. [Q13136-1]
DR CTD; 8500; -.
DR DisGeNET; 8500; -.
DR GeneCards; PPFIA1; -.
DR HGNC; HGNC:9245; PPFIA1.
DR HPA; ENSG00000131626; Low tissue specificity.
DR MIM; 611054; gene.
DR neXtProt; NX_Q13136; -.
DR OpenTargets; ENSG00000131626; -.
DR PharmGKB; PA33566; -.
DR VEuPathDB; HostDB:ENSG00000131626; -.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT01050000244900; -.
DR HOGENOM; CLU_006923_0_0_1; -.
DR InParanoid; Q13136; -.
DR OMA; KERMVAM; -.
DR OrthoDB; 440941at2759; -.
DR PhylomeDB; Q13136; -.
DR TreeFam; TF314207; -.
DR PathwayCommons; Q13136; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; Q13136; -.
DR SIGNOR; Q13136; -.
DR BioGRID-ORCS; 8500; 26 hits in 1082 CRISPR screens.
DR ChiTaRS; PPFIA1; human.
DR GeneWiki; Liprin-alpha-1; -.
DR GenomeRNAi; 8500; -.
DR Pharos; Q13136; Tbio.
DR PRO; PR:Q13136; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13136; protein.
DR Bgee; ENSG00000131626; Expressed in sural nerve and 204 other tissues.
DR ExpressionAtlas; Q13136; baseline and differential.
DR Genevisible; Q13136; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:1903077; P:negative regulation 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 GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR030438; PPFIA1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF15; PTHR12587:SF15; 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; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1202
FT /note="Liprin-alpha-1"
FT /id="PRO_0000191026"
FT DOMAIN 878..944
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 963..1027
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1051..1120
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..141
FT /evidence="ECO:0000255"
FT COILED 176..214
FT /evidence="ECO:0000255"
FT COILED 249..521
FT /evidence="ECO:0000255"
FT COILED 623..669
FT /evidence="ECO:0000255"
FT COILED 847..871
FT /evidence="ECO:0000255"
FT COILED 1021..1050
FT /evidence="ECO:0000255"
FT COMPBIAS 224..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1185..1202
FT /note="NVSGTQRLDSATVRTYSC -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7796809"
FT /id="VSP_009391"
FT VARIANT 71
FT /note="V -> I (in dbSNP:rs546502)"
FT /id="VAR_017756"
FT VARIANT 1072
FT /note="L -> F (in dbSNP:rs11236045)"
FT /id="VAR_049998"
FT CONFLICT 492
FT /note="E -> G (in Ref. 3; AAH34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="P -> T (in Ref. 3; AAH34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 672..674
FT /note="LGR -> EFG (in Ref. 4; BAA08353)"
FT /evidence="ECO:0000305"
FT CONFLICT 800..801
FT /note="KK -> EE (in Ref. 4; BAA08353)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="E -> G (in Ref. 3; AAH34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="L -> Q (in Ref. 4; BAA08353)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="C -> S (in Ref. 4; BAA08353)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="E -> EVRV (in Ref. 4; BAA08353)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121..1123
FT /note="GTD -> PEF (in Ref. 4; BAA08353)"
FT /evidence="ECO:0000305"
FT STRAND 1198..1201
FT /evidence="ECO:0007829|PDB:1N7F"
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
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