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   27-MAR-2024, entry version 202.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) 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   PDB; 1N7F; X-ray; 1.80 A; C/D=1195-1202.
DR   PDBsum; 1N7F; -.
DR   AlphaFoldDB; Q13136; -.
DR   SMR; Q13136; -.
DR   BioGRID; 114072; 213.
DR   ELM; Q13136; -.
DR   IntAct; Q13136; 74.
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; 9606-ENSP00000253925; -.
DR   PeptideAtlas; Q13136; -.
DR   ProteomicsDB; 59184; -. [Q13136-1]
DR   ProteomicsDB; 59185; -. [Q13136-2]
DR   Pumba; Q13136; -.
DR   Antibodypedia; 30679; 234 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   Ensembl; ENST00000672559.2; ENSP00000500898.2; ENSG00000288198.2. [Q13136-1]
DR   Ensembl; ENST00000672873.2; ENSP00000500481.2; ENSG00000288198.2. [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   AGR; HGNC:9245; -.
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; DHTFDAQ; -.
DR   OrthoDB; 2906732at2759; -.
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; 27 hits in 1156 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 206 other cell types or tissues.
DR   ExpressionAtlas; Q13136; baseline and differential.
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: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:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0097444; C:spine apparatus; 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:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
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; Transcription Factor, Ets-1; 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; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR   PANTHER; PTHR12587:SF15; LIPRIN-ALPHA-1; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
DR   Genevisible; Q13136; HS.
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
     SC
//