ID RHG12_HUMAN Reviewed; 846 AA.
AC Q8IWW6; B1ANY0; B1ANY1; B1ANY2; Q504X1; Q86UB3; Q8IWW7; Q8N3L1; Q9NT76;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=Rho GTPase-activating protein 12;
DE AltName: Full=Rho-type GTPase-activating protein 12;
GN Name=ARHGAP12;
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).
RA Mao Y., Xie Y., Zhang Z.;
RT "Cloning and characterization of a novel human gene.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-846 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta, and Uterus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND TYR-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-213; SER-215;
RP SER-240 AND SER-592, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-215; SER-240 AND
RP TYR-243, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; THR-230; THR-231;
RP SER-240 AND SER-592, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IWW6-4; Q9UPX8-4: SHANK2; NbExp=3; IntAct=EBI-11959591, EBI-11959011;
CC Q8IWW6-4; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-11959591, EBI-6550597;
CC Q8IWW6-4; O00401: WASL; NbExp=3; IntAct=EBI-11959591, EBI-957615;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=ARHGAP12b;
CC IsoId=Q8IWW6-1; Sequence=Displayed;
CC Name=2; Synonyms=ARHGAP12a;
CC IsoId=Q8IWW6-2; Sequence=VSP_010327;
CC Name=3;
CC IsoId=Q8IWW6-3; Sequence=VSP_010326, VSP_010328;
CC Name=4;
CC IsoId=Q8IWW6-4; Sequence=VSP_010328;
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DR EMBL; AY033594; AAK52311.1; -; mRNA.
DR EMBL; AY033595; AAK52312.1; -; mRNA.
DR EMBL; AL390715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834250; CAD38926.2; -; mRNA.
DR EMBL; AL137485; CAB70766.1; -; mRNA.
DR EMBL; CH471072; EAW85980.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85983.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85985.1; -; Genomic_DNA.
DR EMBL; BC051811; AAH51811.1; -; mRNA.
DR EMBL; BC094719; AAH94719.1; -; mRNA.
DR CCDS; CCDS59214.1; -. [Q8IWW6-3]
DR CCDS; CCDS59215.1; -. [Q8IWW6-2]
DR CCDS; CCDS59216.1; -. [Q8IWW6-4]
DR CCDS; CCDS7170.1; -. [Q8IWW6-1]
DR PIR; T46471; T46471.
DR RefSeq; NP_001257624.1; NM_001270695.1. [Q8IWW6-4]
DR RefSeq; NP_001257625.1; NM_001270696.1. [Q8IWW6-2]
DR RefSeq; NP_001257626.1; NM_001270697.1.
DR RefSeq; NP_001257627.1; NM_001270698.1.
DR RefSeq; NP_001257628.1; NM_001270699.1. [Q8IWW6-3]
DR RefSeq; NP_060757.4; NM_018287.6. [Q8IWW6-1]
DR RefSeq; XP_005252701.1; XM_005252644.1. [Q8IWW6-3]
DR AlphaFoldDB; Q8IWW6; -.
DR SMR; Q8IWW6; -.
DR BioGRID; 125122; 68.
DR IntAct; Q8IWW6; 18.
DR STRING; 9606.ENSP00000345808; -.
DR GlyGen; Q8IWW6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IWW6; -.
DR MetOSite; Q8IWW6; -.
DR PhosphoSitePlus; Q8IWW6; -.
DR BioMuta; ARHGAP12; -.
DR DMDM; 47117238; -.
DR EPD; Q8IWW6; -.
DR jPOST; Q8IWW6; -.
DR MassIVE; Q8IWW6; -.
DR MaxQB; Q8IWW6; -.
DR PaxDb; 9606-ENSP00000345808; -.
DR PeptideAtlas; Q8IWW6; -.
DR ProteomicsDB; 62408; -.
DR ProteomicsDB; 70913; -. [Q8IWW6-1]
DR ProteomicsDB; 70914; -. [Q8IWW6-2]
DR ProteomicsDB; 70915; -. [Q8IWW6-3]
DR Pumba; Q8IWW6; -.
DR ABCD; Q8IWW6; 3 sequenced antibodies.
DR Antibodypedia; 26325; 71 antibodies from 20 providers.
DR DNASU; 94134; -.
DR Ensembl; ENST00000311380.8; ENSP00000310984.4; ENSG00000165322.18. [Q8IWW6-3]
DR Ensembl; ENST00000344936.7; ENSP00000345808.2; ENSG00000165322.18. [Q8IWW6-1]
DR Ensembl; ENST00000375250.9; ENSP00000364399.5; ENSG00000165322.18. [Q8IWW6-2]
DR Ensembl; ENST00000396144.8; ENSP00000379448.4; ENSG00000165322.18. [Q8IWW6-4]
DR GeneID; 94134; -.
DR KEGG; hsa:94134; -.
DR MANE-Select; ENST00000344936.7; ENSP00000345808.2; NM_018287.7; NP_060757.4.
DR UCSC; uc001ivy.3; human. [Q8IWW6-1]
DR AGR; HGNC:16348; -.
DR CTD; 94134; -.
DR DisGeNET; 94134; -.
DR GeneCards; ARHGAP12; -.
DR HGNC; HGNC:16348; ARHGAP12.
DR HPA; ENSG00000165322; Low tissue specificity.
DR MIM; 610577; gene.
DR neXtProt; NX_Q8IWW6; -.
DR OpenTargets; ENSG00000165322; -.
DR PharmGKB; PA24957; -.
DR VEuPathDB; HostDB:ENSG00000165322; -.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_015883_6_1_1; -.
DR InParanoid; Q8IWW6; -.
DR OMA; PECHYAT; -.
DR OrthoDB; 5395569at2759; -.
DR PhylomeDB; Q8IWW6; -.
DR TreeFam; TF329345; -.
DR PathwayCommons; Q8IWW6; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q8IWW6; -.
DR SIGNOR; Q8IWW6; -.
DR BioGRID-ORCS; 94134; 21 hits in 1163 CRISPR screens.
DR ChiTaRS; ARHGAP12; human.
DR GenomeRNAi; 94134; -.
DR Pharos; Q8IWW6; Tbio.
DR PRO; PR:Q8IWW6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IWW6; Protein.
DR Bgee; ENSG00000165322; Expressed in buccal mucosa cell and 206 other cell types or tissues.
DR ExpressionAtlas; Q8IWW6; baseline and differential.
DR Genevisible; Q8IWW6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:UniProtKB.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13233; PH_ARHGAP9-like; 1.
DR CDD; cd04403; RhoGAP_ARHGAP27_15_12_9; 1.
DR CDD; cd12070; SH3_ARHGAP12; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035491; ARHGAP12_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR23176:SF107; RHO GTPASE-ACTIVATING PROTEIN 12; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16618; SH3-WW_linker; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..846
FT /note="Rho GTPase-activating protein 12"
FT /id="PRO_0000056713"
FT DOMAIN 12..74
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 265..298
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 358..391
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 463..575
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 656..844
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 152..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 243
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 317..363
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010326"
FT VAR_SEQ 433..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010327"
FT VAR_SEQ 458..462
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_010328"
FT VARIANT 442
FT /note="F -> S (in dbSNP:rs2808096)"
FT /id="VAR_024454"
FT CONFLICT 70
FT /note="K -> R (in Ref. 4; CAD38926)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="Q -> P (in Ref. 4; CAD38926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 96254 MW; 274CF06B47F02DDC CRC64;
MKMADRSGKI IPGQVYIEVE YDYEYEAKDR KIVIKQGERY ILVKKTNDDW WQVKPDENSK
AFYVPAQYVK EVTRKALMPP VKQVAGLPNN STKIMQSLHL QRSTENVNKL PELSSFGKPS
SSVQGTGLIR DANQNFGPSY NQGQTVNLSL DLTHNNGKFN NDSHSPKVSS QNRTRSFGHF
PGPEFLDVEK TSFSQEQSCD SAGEGSERIH QDSESGDELS SSSTEQIRAT TPPNQGRPDS
PVYANLQELK ISQSALPPLP GSPAIQINGE WETHKDSSGR CYYYNRGTQE RTWKPPRWTR
DASISKGDFQ NPGDQELLSS EENYYSTSYS QSDSQCGSPP RGWSEELDER GHTLYTSDYT
NEKWLKHVDD QGRQYYYSAD GSRSEWELPK YNASSQQQRE IIKSRSLDRR LQEPIVLTKW
RHSTIVLDTN DKESPTASKP CFPENESSPS SPKHQDTASS PKDQEKYGLL NVTKIAENGK
KVRKNWLSSW AVLQGSSLLF TKTQGSSTSW FGSNQSKPEF TVDLKGATIE MASKDKSSKK
NVFELKTRQG TELLIQSDND TVINDWFKVL SSTINNQAVE TDEGIEEEIP DSPGIEKHDK
EKEQKDPKKL RSFKVSSIDS SEQKKTKKNL KKFLTRRPTL QAVREKGYIK DQVFGSNLAN
LCQRENGTVP KFVKLCIEHV EEHGLDIDGI YRVSGNLAVI QKLRFAVNHD EKLDLNDSKW
EDIHVITGAL KMFFRELPEP LFTFNHFNDF VNAIKQEPRQ RVAAVKDLIR QLPKPNQDTM
QILFRHLRRV IENGEKNRMT YQSIAIVFGP TLLKPEKETG NIAVHTVYQN QIVELILLEL
SSIFGR
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