LIPB1_HUMAN
ID LIPB1_HUMAN Reviewed; 1011 AA.
AC Q86W92; O75336; Q86X70; Q9NY03; Q9ULJ0;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Liprin-beta-1;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 1;
DE Short=PTPRF-interacting protein-binding protein 1;
DE AltName: Full=hSGT2;
GN Name=PPFIBP1; Synonyms=KIAA1230;
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] (ISOFORM 2), VARIANT LEU-148, TISSUE
RP SPECIFICITY, AND FUNCTION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-148.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT LEU-148.
RA Junjian L., Cheng J., Rouli Z., Jie Z.;
RT "L2, a different isoform of Liprin beta 1, is expressed in high level in
RT liver tissue.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT LEU-148.
RC TISSUE=Brain;
RA Sato T., Jigami Y., Uemura H.;
RT "hSGT2, a liprin related human gene, restores the glycolytic gene
RT expression of the gcr2 mutant of Saccharomyces cerevisiae.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP LEU-148.
RC TISSUE=Brain, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH S100A4.
RX PubMed=11836260; DOI=10.1074/jbc.m110976200;
RA Kriajevska M., Fischer-Larsen M., Moertz E., Vorm O., Tulchinsky E.,
RA Grigorian M., Ambartsumian N., Lukanidin E.;
RT "Liprin beta 1, a member of the family of LAR transmembrane tyrosine
RT phosphatase-interacting proteins, is a new target for the metastasis-
RT associated protein S100A4 (Mts1).";
RL J. Biol. Chem. 277:5229-5235(2002).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; THR-39; SER-40; SER-466;
RP SER-579; SER-601; SER-999; SER-1001; SER-1003 AND THR-1005, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-523 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-322, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40; SER-999 AND
RP SER-1001, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-601 AND SER-794, AND
RP IDENTIFICATION BY MASS 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-540 AND SER-794, 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).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-471, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. Did not bind
CC receptor-like tyrosine phosphatases type 2A.
CC {ECO:0000269|PubMed:9624153}.
CC -!- SUBUNIT: Forms homodimers and heterodimers. Interacts with S100A4 in a
CC calcium-dependent mode. {ECO:0000269|PubMed:11836260}.
CC -!- INTERACTION:
CC Q86W92; P40425: PBX2; NbExp=3; IntAct=EBI-1045582, EBI-348489;
CC Q86W92; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-1045582, EBI-25492395;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86W92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86W92-2; Sequence=VSP_009397, VSP_009398, VSP_009399,
CC VSP_009400;
CC Name=3;
CC IsoId=Q86W92-3; Sequence=VSP_009394;
CC Name=4;
CC IsoId=Q86W92-4; Sequence=VSP_009397;
CC Name=5; Synonyms=L2;
CC IsoId=Q86W92-5; Sequence=VSP_009395, VSP_009396;
CC -!- TISSUE SPECIFICITY: Widely expressed. Absent in liver.
CC {ECO:0000269|PubMed:9624153}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type beta/beta. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type beta/alpha and
CC interaction with S100A4.
CC -!- MISCELLANEOUS: [Isoform 5]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-beta subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA86544.2; Type=Erroneous initiation; 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; AF034802; AAC26103.1; -; mRNA.
DR EMBL; AB033056; BAA86544.2; ALT_INIT; mRNA.
DR EMBL; AJ276680; CAB77544.1; -; mRNA.
DR EMBL; AB049149; BAB39690.1; -; mRNA.
DR EMBL; BC046159; AAH46159.1; ALT_INIT; mRNA.
DR EMBL; BC050281; AAH50281.1; -; mRNA.
DR CCDS; CCDS55812.1; -. [Q86W92-1]
DR CCDS; CCDS55813.1; -. [Q86W92-4]
DR CCDS; CCDS55814.1; -. [Q86W92-3]
DR CCDS; CCDS8713.1; -. [Q86W92-2]
DR RefSeq; NP_001185844.1; NM_001198915.1. [Q86W92-3]
DR RefSeq; NP_001185845.1; NM_001198916.1. [Q86W92-4]
DR RefSeq; NP_003613.3; NM_003622.3. [Q86W92-2]
DR RefSeq; NP_803193.2; NM_177444.2. [Q86W92-1]
DR AlphaFoldDB; Q86W92; -.
DR SMR; Q86W92; -.
DR BioGRID; 114068; 160.
DR DIP; DIP-42195N; -.
DR IntAct; Q86W92; 42.
DR MINT; Q86W92; -.
DR STRING; 9606.ENSP00000314724; -.
DR iPTMnet; Q86W92; -.
DR MetOSite; Q86W92; -.
DR PhosphoSitePlus; Q86W92; -.
DR BioMuta; PPFIBP1; -.
DR DMDM; 90185247; -.
DR EPD; Q86W92; -.
DR jPOST; Q86W92; -.
DR MassIVE; Q86W92; -.
DR MaxQB; Q86W92; -.
DR PaxDb; Q86W92; -.
DR PeptideAtlas; Q86W92; -.
DR PRIDE; Q86W92; -.
DR ProteomicsDB; 70131; -. [Q86W92-1]
DR ProteomicsDB; 70132; -. [Q86W92-2]
DR ProteomicsDB; 70133; -. [Q86W92-3]
DR ProteomicsDB; 70134; -. [Q86W92-4]
DR ProteomicsDB; 70135; -. [Q86W92-5]
DR Antibodypedia; 1098; 166 antibodies from 29 providers.
DR DNASU; 8496; -.
DR Ensembl; ENST00000228425.11; ENSP00000228425.6; ENSG00000110841.14. [Q86W92-2]
DR Ensembl; ENST00000318304.12; ENSP00000314724.8; ENSG00000110841.14. [Q86W92-1]
DR Ensembl; ENST00000535047.5; ENSP00000444046.1; ENSG00000110841.14. [Q86W92-5]
DR Ensembl; ENST00000537927.5; ENSP00000445425.1; ENSG00000110841.14. [Q86W92-3]
DR Ensembl; ENST00000542629.5; ENSP00000443442.1; ENSG00000110841.14. [Q86W92-4]
DR GeneID; 8496; -.
DR KEGG; hsa:8496; -.
DR MANE-Select; ENST00000228425.11; ENSP00000228425.6; NM_003622.4; NP_003613.4. [Q86W92-2]
DR UCSC; uc001rhz.3; human. [Q86W92-1]
DR CTD; 8496; -.
DR DisGeNET; 8496; -.
DR GeneCards; PPFIBP1; -.
DR HGNC; HGNC:9249; PPFIBP1.
DR HPA; ENSG00000110841; Low tissue specificity.
DR MIM; 603141; gene.
DR neXtProt; NX_Q86W92; -.
DR OpenTargets; ENSG00000110841; -.
DR PharmGKB; PA33570; -.
DR VEuPathDB; HostDB:ENSG00000110841; -.
DR eggNOG; KOG1899; Eukaryota.
DR GeneTree; ENSGT01050000244951; -.
DR HOGENOM; CLU_011689_2_0_1; -.
DR InParanoid; Q86W92; -.
DR OMA; QWILSGQ; -.
DR PhylomeDB; Q86W92; -.
DR TreeFam; TF314207; -.
DR PathwayCommons; Q86W92; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; Q86W92; -.
DR BioGRID-ORCS; 8496; 15 hits in 1069 CRISPR screens.
DR ChiTaRS; PPFIBP1; human.
DR GeneWiki; PPFIBP1; -.
DR GenomeRNAi; 8496; -.
DR Pharos; Q86W92; Tbio.
DR PRO; PR:Q86W92; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86W92; protein.
DR Bgee; ENSG00000110841; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; Q86W92; baseline and differential.
DR Genevisible; Q86W92; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR CDD; cd09563; SAM_liprin-beta1_2_repeat1; 1.
DR CDD; cd09566; SAM_liprin-beta1_2_repeat2; 1.
DR CDD; cd09569; SAM_liprin-beta1_2_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037617; Liprin-beta_SAM_rpt_1.
DR InterPro; IPR037618; Liprin-beta_SAM_rpt_2.
DR InterPro; IPR037619; Liprin-beta_SAM_rpt_3.
DR InterPro; IPR030437; PPFIBP1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF16; PTHR12587:SF16; 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; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1011
FT /note="Liprin-beta-1"
FT /id="PRO_0000191034"
FT DOMAIN 647..711
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 719..782
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 804..876
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 156..405
FT /evidence="ECO:0000255"
FT COMPBIAS 472..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8U0"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C8U0"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1005
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_009394"
FT VAR_SEQ 158..170
FT /note="ELLSRTSLETQKL -> VCAEARTKMGFPC (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_009395"
FT VAR_SEQ 171..1011
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_009396"
FT VAR_SEQ 233..263
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9624153"
FT /id="VSP_009397"
FT VAR_SEQ 302
FT /note="D -> DENFKKKLKEKN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9624153"
FT /id="VSP_009398"
FT VAR_SEQ 349
FT /note="K -> KKGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9624153"
FT /id="VSP_009399"
FT VAR_SEQ 544
FT /note="L -> LDRKRSASAPTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9624153"
FT /id="VSP_009400"
FT VARIANT 148
FT /note="V -> L (in dbSNP:rs2194816)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9624153,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT /id="VAR_017758"
FT CONFLICT 308
FT /note="M -> K (in Ref. 6; AAH46159)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="C -> R (in Ref. 1; AAC26103)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="E -> A (in Ref. 1; AAC26103)"
FT /evidence="ECO:0000305"
FT MOD_RES Q86W92-2:523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 1011 AA; 114024 MW; 20E30DD99ACD5A92 CRC64;
MMSDASDMLA AALEQMDGII AGSKALEYSN GIFDCQSPTS PFMGSLRALH LVEDLRGLLE
MMETDEKEGL RCQIPDSTAE TLVEWLQSQM TNGHLPGNGD VYQERLARLE NDKESLVLQV
SVLTDQVEAQ GEKIRDLEFC LEEHREKVNA TEEMLQQELL SRTSLETQKL DLMAEISNLK
LKLTAVEKDR LDYEDKFRDT EGLIQEINDL RLKVSEMDSE RLQYEKKLKS TKSLMAKLSS
MKIKVGQMQY EKQRMEQKWE SLKDELASLK EQLEEKESEV KRLQEKLVCK MKGEGVEIVD
RDIEVQKMKK AVESLMAANE EKDRKIEDLR QCLNRYKKMQ DTVVLAQGKD GEYEELLNSS
SISSLLDAQG FSDLEKSPSP TPVMGSPSCD PFNTSVPEEF HTTILQVSIP SLLPATVSME
TSEKSKLTPK PETSFEENDG NIILGATVDT QLCDKLLTSS LQKSSSLGNL KKETSDGEKE
TIQKTSEDRA PAESRPFGTL PPRPPGQDTS MDDNPFGTRK VRSSFGRGFF KIKSNKRTAS
APNLAETEKE TAEHLDLAGA SSRPKDSQRN SPFQIPPPSP DSKKKSRGIM KLFGKLRRSQ
STTFNPDDMS EPEFKRGGTR ATAGPRLGWS RDLGQSNSDL DMPFAKWTKE QVCNWLMEQG
LGSYLNSGKH WIASGQTLLQ ASQQDLEKEL GIKHSLHRKK LQLALQALGS EEETNHGKLD
FNWVTRWLDD IGLPQYKTQF DEGRVDGRML HYMTVDDLLS LKVVSVLHHL SIKRAIQVLR
INNFEPNCLR RRPSDENTIA PSEVQKWTNH RVMEWLRSVD LAEYAPNLRG SGVHGGLMVL
EPRFNVETMA QLLNIPPNKT LLRRHLATHF NLLIGAEAQH QKRDAMELPD YVLLTATAKV
KPKKLAFSNF GNLRKKKQED GEEYVCPMEL GQASGSASKK GFKPGLDMRL YEEDDLDRLE
QMEDSEGTVR QIGAFSEGIN NLTHMLKEDD MFKDFAARSP SASITDEDSN V
