ARAP1_HUMAN
ID ARAP1_HUMAN Reviewed; 1450 AA.
AC Q96P48; A3KLL7; B2RTS2; O94879; Q4LDD5; Q59FI7; Q6PHS3; Q8WU51; Q96HP6;
AC Q96L71;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1;
DE AltName: Full=Centaurin-delta-2;
DE Short=Cnt-d2;
GN Name=ARAP1; Synonyms=CENTD2, KIAA0782;
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 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11804590; DOI=10.1016/s1097-2765(02)00428-8;
RA Miura K., Jacques K.M., Stauffer S., Kubosaki A., Zhu K., Hirsch D.S.,
RA Resau J., Zheng Y., Randazzo P.A.;
RT "ARAP1: a point of convergence for Arf and Rho signaling.";
RL Mol. Cell 9:109-119(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RA Krugmann S., Coadwell J., Stephens L.R., Hawkins P.T.;
RT "ARAP1 splice variants in man and mouse.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Randazzo P.A., Yoon H.-Y., Miura K.;
RT "Human ARAP1b.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLU-1047.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 792-1450 (ISOFORMS 2/3/5).
RC TISSUE=Brain, and Pancreas;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 315-1450 (ISOFORM 1).
RA Hong W.;
RT "KIAA0782 as a member (centaurin delta2) of the ArfGAP centaurin family.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND IDENTIFICATION BY
RP 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 [11]
RP INTERACTION WITH TNFRSF10A, AND SUBCELLULAR LOCATION.
RX PubMed=18165900; DOI=10.1007/s10495-007-0171-8;
RA Simova S., Klima M., Cermak L., Sourkova V., Andera L.;
RT "Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of
RT TRAIL-R1/DR4 to the plasma membrane.";
RL Apoptosis 13:423-436(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; TYR-431 AND SER-1435,
RP AND 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738 AND SER-1435, AND
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; TYR-504; SER-738 AND
RP SER-1428, AND 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).
CC -!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-
CC activating protein that modulates actin cytoskeleton remodeling by
CC regulating ARF and RHO family members. Is activated by
CC phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can
CC be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2)
CC binding, albeit with lower efficiency. Has a preference for ARF1 and
CC ARF5 (By similarity). {ECO:0000250, ECO:0000269|PubMed:11804590}.
CC -!- SUBUNIT: Interacts with TNFRSF10A. {ECO:0000269|PubMed:18165900}.
CC -!- INTERACTION:
CC Q96P48; P46108: CRK; NbExp=3; IntAct=EBI-710003, EBI-886;
CC Q96P48; O00220: TNFRSF10A; NbExp=4; IntAct=EBI-710003, EBI-518861;
CC Q96P48; P12956: XRCC6; NbExp=2; IntAct=EBI-710003, EBI-353208;
CC Q96P48; PRO_0000037576 [P27958]; Xeno; NbExp=3; IntAct=EBI-710003, EBI-8753518;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane;
CC Peripheral membrane protein. Cell membrane. Note=Associated with Golgi
CC stacks in resting cells. Throughout the cytoplasm and in surface
CC protrusion in cells that are in the process of attaching to a surface
CC and spreading.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=6;
CC IsoId=Q96P48-6; Sequence=Displayed;
CC Name=1;
CC IsoId=Q96P48-1; Sequence=VSP_036607, VSP_036608;
CC Name=2;
CC IsoId=Q96P48-2; Sequence=VSP_036607, VSP_036608, VSP_000311;
CC Name=3;
CC IsoId=Q96P48-3; Sequence=VSP_000311;
CC Name=4;
CC IsoId=Q96P48-4; Sequence=VSP_015000;
CC Name=5;
CC IsoId=Q96P48-5; Sequence=VSP_014998, VSP_015001, VSP_000311;
CC Name=7;
CC IsoId=Q96P48-7; Sequence=VSP_015000, VSP_043530, VSP_000311;
CC -!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, spleen, kidney,
CC liver, placenta, lung, peripheral blood leukocytes, adrenal gland, bone
CC marrow, brain, lymph node, mammary gland, prostate, spinal cord,
CC stomach, thyroid and trachea. {ECO:0000269|PubMed:11804590}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34502.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD92710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY049732; AAL12169.1; -; mRNA.
DR EMBL; AJ621557; CAF21317.1; -; mRNA.
DR EMBL; AB018325; BAA34502.2; ALT_INIT; mRNA.
DR EMBL; AY553630; AAT36325.1; -; mRNA.
DR EMBL; AB209473; BAD92710.1; ALT_INIT; mRNA.
DR EMBL; AP002381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008315; AAH08315.1; -; mRNA.
DR EMBL; BC021244; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC056401; AAH56401.1; -; mRNA.
DR EMBL; BC140792; AAI40793.1; -; mRNA.
DR EMBL; AF411983; AAL04167.1; -; mRNA.
DR CCDS; CCDS41687.1; -. [Q96P48-6]
DR CCDS; CCDS44671.1; -. [Q96P48-7]
DR CCDS; CCDS8217.2; -. [Q96P48-4]
DR PIR; C59431; C59431.
DR RefSeq; NP_001035207.1; NM_001040118.2. [Q96P48-6]
DR RefSeq; NP_001128662.1; NM_001135190.1. [Q96P48-7]
DR RefSeq; NP_056057.2; NM_015242.4. [Q96P48-4]
DR PDB; 4X1V; X-ray; 1.58 A; B=76-91.
DR PDBsum; 4X1V; -.
DR AlphaFoldDB; Q96P48; -.
DR SMR; Q96P48; -.
DR BioGRID; 125548; 39.
DR IntAct; Q96P48; 20.
DR MINT; Q96P48; -.
DR STRING; 9606.ENSP00000377233; -.
DR GlyGen; Q96P48; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96P48; -.
DR MetOSite; Q96P48; -.
DR PhosphoSitePlus; Q96P48; -.
DR BioMuta; ARAP1; -.
DR DMDM; 226694321; -.
DR EPD; Q96P48; -.
DR jPOST; Q96P48; -.
DR MassIVE; Q96P48; -.
DR MaxQB; Q96P48; -.
DR PaxDb; Q96P48; -.
DR PeptideAtlas; Q96P48; -.
DR PRIDE; Q96P48; -.
DR ProteomicsDB; 77622; -. [Q96P48-6]
DR ProteomicsDB; 77623; -. [Q96P48-1]
DR ProteomicsDB; 77624; -. [Q96P48-2]
DR ProteomicsDB; 77625; -. [Q96P48-3]
DR ProteomicsDB; 77626; -. [Q96P48-4]
DR ProteomicsDB; 77627; -. [Q96P48-5]
DR ProteomicsDB; 77628; -. [Q96P48-7]
DR Antibodypedia; 30876; 185 antibodies from 30 providers.
DR DNASU; 116985; -.
DR Ensembl; ENST00000334211.12; ENSP00000335506.8; ENSG00000186635.15. [Q96P48-4]
DR Ensembl; ENST00000359373.9; ENSP00000352332.5; ENSG00000186635.15. [Q96P48-3]
DR Ensembl; ENST00000393605.7; ENSP00000377230.3; ENSG00000186635.15. [Q96P48-1]
DR Ensembl; ENST00000393609.8; ENSP00000377233.3; ENSG00000186635.15. [Q96P48-6]
DR Ensembl; ENST00000429686.5; ENSP00000403127.1; ENSG00000186635.15. [Q96P48-7]
DR GeneID; 116985; -.
DR KEGG; hsa:116985; -.
DR MANE-Select; ENST00000393609.8; ENSP00000377233.3; NM_001040118.3; NP_001035207.1.
DR UCSC; uc001osr.4; human. [Q96P48-6]
DR CTD; 116985; -.
DR DisGeNET; 116985; -.
DR GeneCards; ARAP1; -.
DR HGNC; HGNC:16925; ARAP1.
DR HPA; ENSG00000186635; Low tissue specificity.
DR MIM; 606646; gene.
DR neXtProt; NX_Q96P48; -.
DR OpenTargets; ENSG00000186635; -.
DR PharmGKB; PA164715867; -.
DR VEuPathDB; HostDB:ENSG00000186635; -.
DR eggNOG; KOG1117; Eukaryota.
DR GeneTree; ENSGT00940000157424; -.
DR InParanoid; Q96P48; -.
DR OMA; SVIKAGW; -.
DR OrthoDB; 98944at2759; -.
DR PhylomeDB; Q96P48; -.
DR TreeFam; TF105769; -.
DR PathwayCommons; Q96P48; -.
DR Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q96P48; -.
DR SIGNOR; Q96P48; -.
DR BioGRID-ORCS; 116985; 21 hits in 1083 CRISPR screens.
DR ChiTaRS; ARAP1; human.
DR GeneWiki; CENTD2; -.
DR GenomeRNAi; 116985; -.
DR Pharos; Q96P48; Tbio.
DR PRO; PR:Q96P48; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96P48; protein.
DR Bgee; ENSG00000186635; Expressed in granulocyte and 180 other tissues.
DR ExpressionAtlas; Q96P48; baseline and differential.
DR Genevisible; Q96P48; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0030037; P:actin filament reorganization involved in cell cycle; TAS:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037858; RhoGAP_ARAP.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 3.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 5.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Golgi apparatus; GTPase activation; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1450
FT /note="Arf-GAP with Rho-GAP domain, ANK repeat and PH
FT domain-containing protein 1"
FT /id="PRO_0000074214"
FT DOMAIN 6..70
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 327..419
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 440..529
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 535..660
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 743..850
FT /note="PH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 954..1139
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 1172..1261
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 1274..1396
FT /note="PH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 550..576
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 89..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 504
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..760
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014998"
FT VAR_SEQ 1..245
FT /note="Missing (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_015000"
FT VAR_SEQ 1..240
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804590, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.9"
FT /id="VSP_036607"
FT VAR_SEQ 241..249
FT /note="APARVMTKK -> MTLSGSRGQ (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804590, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.9"
FT /id="VSP_036608"
FT VAR_SEQ 604..664
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043530"
FT VAR_SEQ 761..767
FT /note="QDRRARE -> MDASGKG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015001"
FT VAR_SEQ 1320..1330
FT /note="Missing (in isoform 2, isoform 3, isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_000311"
FT VARIANT 358
FT /note="R -> Q (in dbSNP:rs34976830)"
FT /id="VAR_055529"
FT VARIANT 1047
FT /note="Q -> E (in dbSNP:rs56200889)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_061023"
FT CONFLICT 1408
FT /note="V -> M (in Ref. 8; AAH56401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1450 AA; 162192 MW; A4B6CCC28EC4CD0D CRC64;
MAEAGDAALS VAEWLRALHL EQYTGLFEQH GLVWATECQG LSDTRLMDMG MLLPGHRRRI
LAGLLRAHTS PAPAPRPTPR PVPMKRHIFR SPPVPATPPE PLPTTTEDEG LPAAPPIPPR
RSCLPPTCFT TPSTAAPDPV LPPLPAKRHL AELSVPPVPP RTGPPRLLVS LPTKEEESLL
PSLSSPPQPQ SEEPLSTLPQ GPPQPPSPPP CPPEIPPKPV RLFPEFDDSD YDEVPEEGPG
APARVMTKKE EPPPSRVPRA VRVASLLSEG EELSGDDQGD EEEDDHAYEG VPNGGWHTSS
LSLSLPSTIA APHPMDGPPG GSTPVTPVIK AGWLDKNPPQ GSYIYQKRWV RLDTDHLRYF
DSNKDAYSKR FISVACISHV AAIGDQKFEV ITNNRTFAFR AESDVERKEW MQALQQAMAE
QRARARLSSA YLLGVPGSEQ PDRAGSLELR GFKNKLYVAV VGDKVQLYKN LEEYHLGIGI
TFIDMSVGNV KEVDRRSFDL TTPYRIFSFS ADSELEKEQW LEAMQGAIAE ALSTSEVAER
IWAAAPNRFC ADCGAPQPDW ASINLCVVIC KRCAGEHRGL GAGVSKVRSL KMDRKVWTET
LIELFLQLGN GAGNRFWAAN VPPSEALQPS SSPSTRRCHL EAKYREGKYR RYHPLFGNQE
ELDKALCAAV TTTDLAETQA LLGCGAGINC FSGDPEAPTP LALAEQAGQT LQMEFLRNNR
TTEVPRLDSM KPLEKHYSVV LPTVSHSGFL YKTASAGKLL QDRRAREEFS RRWCVLGDGV
LSYFENERAV TPNGEIRASE IVCLAVPPPD THGFEHTFEV YTEGERLYLF GLESAEQAHE
WVKCIAKAFV PPLAEDLLAR DFERLGRLPY KAGLSLQRAQ EGWFSLSGSE LRAVFPEGPC
EEPLQLRKLQ ELSIQGDSEN QVLVLVERRR TLYIQGERRL DFMGWLGAIQ KAAASMGDTL
SEQQLGDSDI PVIVYRCVDY ITQCGLTSEG IYRKCGQTSK TQRLLESLRQ DARSVHLKEG
EQHVDDVSSA LKRFLRDLPD GLFTRAQRLT WLEASEIEDE EEKVSRYREL LVRLPPVNRA
TVKALISHLY CVQCFSDTNQ MNVHNLAIVF GPTLFQTDGQ DYKAGRVVED LINHYVVVFS
VDEEELRKQR EEITAIVKMR VAGTASGTQH AGDFICTVYL EEKKAETEQH IKVPASMTAE
ELTLEILDRR NVGIREKDYW TCFEVNEREE AERPLHFAEK VLPILHGLGT DSHLVVKKHQ
AMEAMLLYLA SRVGDTKHGM MKFREDRSLL GLGLPSGGFH DRYFILNSSC LRLYKEVRSQ
RPWSGAPETS HRPEKEWPIK SLKVYLGVKK KLRPPTCWGF TVVHETEKHE KQQWYLCCDT
QMELREWFAT FLFVQHDGLV WPSEPSRVSR AVPEVRLGSV SLIPLRGSEN EMRRSVAAFT
ADPLSLLRNV
