DOCK5_HUMAN
ID DOCK5_HUMAN Reviewed; 1870 AA.
AC Q9H7D0; B2RNY0; Q5XKD5; Q6AI11; Q6PJS6; Q6ZTS6;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dedicator of cytokinesis protein 5;
GN Name=DOCK5;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-1285.
RC TISSUE=Brain, Skin, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 900-1870 (ISOFORM 1), AND VARIANT
RP ARG-1285.
RC TISSUE=Endothelial cell, and Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1528-1870 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 NOMENCLATURE.
RX PubMed=12432077; DOI=10.1242/jcs.00219;
RA Cote J.-F., Vuori K.;
RT "Identification of an evolutionarily conserved superfamily of DOCK180-
RT related proteins with guanine nucleotide exchange activity.";
RL J. Cell Sci. 115:4901-4913(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1814, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1789; THR-1794; SER-1834 AND
RP SER-1869, 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 [9]
RP FUNCTION, INTERACTION WITH CRK AND CRKL, AND SUBCELLULAR LOCATION.
RX PubMed=19004829; DOI=10.1074/jbc.m808010200;
RA Sanders M.A., Ampasala D., Basson M.D.;
RT "DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell spreading and
RT migration on collagen IV.";
RL J. Biol. Chem. 284:27-35(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1834, 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-818, 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-1766, 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 [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-1756; SER-1766; SER-1789 AND
RP SER-1834, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF
CC proteins activate small GTPases by exchanging bound GDP for free GTP
CC (By similarity). Along with DOCK1, mediates CRK/CRKL regulation of
CC epithelial and endothelial cell spreading and migration on type IV
CC collagen (PubMed:19004829). {ECO:0000250|UniProtKB:B2RY04,
CC ECO:0000269|PubMed:19004829}.
CC -!- SUBUNIT: Interacts with CRK and CRKL. {ECO:0000269|PubMed:19004829}.
CC -!- INTERACTION:
CC Q9H7D0; P46108: CRK; NbExp=3; IntAct=EBI-1773858, EBI-886;
CC Q9H7D0-1; Q14185: DOCK1; NbExp=2; IntAct=EBI-25409131, EBI-446740;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19004829}. Cell
CC membrane {ECO:0000269|PubMed:19004829}. Note=Associated with the edge
CC of the plasma membrane in Caco-2 intestinal epithelial cells spreading
CC on type IV collagen. {ECO:0000269|PubMed:19004829}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H7D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7D0-2; Sequence=VSP_021868;
CC -!- DOMAIN: The DOCKER domain may mediate some GEF activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC86503.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC041005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011877; AAH11877.1; -; mRNA.
DR EMBL; BC041761; AAH41761.2; -; mRNA.
DR EMBL; BC137175; AAI37176.1; -; mRNA.
DR EMBL; BC137176; AAI37177.1; -; mRNA.
DR EMBL; AK024687; BAB14962.1; ALT_INIT; mRNA.
DR EMBL; AK126249; BAC86503.1; ALT_INIT; mRNA.
DR EMBL; CR627414; CAH10503.1; -; mRNA.
DR CCDS; CCDS6047.1; -. [Q9H7D0-1]
DR RefSeq; NP_079216.4; NM_024940.7. [Q9H7D0-1]
DR PDB; 7DPA; EM; 3.80 A; A/D=1-1642.
DR PDBsum; 7DPA; -.
DR AlphaFoldDB; Q9H7D0; -.
DR SMR; Q9H7D0; -.
DR BioGRID; 123062; 111.
DR ELM; Q9H7D0; -.
DR IntAct; Q9H7D0; 76.
DR MINT; Q9H7D0; -.
DR STRING; 9606.ENSP00000276440; -.
DR BindingDB; Q9H7D0; -.
DR ChEMBL; CHEMBL4739705; -.
DR GlyGen; Q9H7D0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H7D0; -.
DR MetOSite; Q9H7D0; -.
DR PhosphoSitePlus; Q9H7D0; -.
DR BioMuta; DOCK5; -.
DR DMDM; 119370380; -.
DR EPD; Q9H7D0; -.
DR jPOST; Q9H7D0; -.
DR MassIVE; Q9H7D0; -.
DR MaxQB; Q9H7D0; -.
DR PaxDb; Q9H7D0; -.
DR PeptideAtlas; Q9H7D0; -.
DR PRIDE; Q9H7D0; -.
DR ProteomicsDB; 81105; -. [Q9H7D0-1]
DR ProteomicsDB; 81106; -. [Q9H7D0-2]
DR Antibodypedia; 2898; 91 antibodies from 16 providers.
DR DNASU; 80005; -.
DR Ensembl; ENST00000276440.12; ENSP00000276440.7; ENSG00000147459.18. [Q9H7D0-1]
DR Ensembl; ENST00000481100.5; ENSP00000429737.1; ENSG00000147459.18. [Q9H7D0-2]
DR GeneID; 80005; -.
DR KEGG; hsa:80005; -.
DR MANE-Select; ENST00000276440.12; ENSP00000276440.7; NM_024940.8; NP_079216.4.
DR UCSC; uc003xef.4; human. [Q9H7D0-1]
DR CTD; 80005; -.
DR DisGeNET; 80005; -.
DR GeneCards; DOCK5; -.
DR HGNC; HGNC:23476; DOCK5.
DR HPA; ENSG00000147459; Tissue enriched (brain).
DR MIM; 616904; gene.
DR neXtProt; NX_Q9H7D0; -.
DR OpenTargets; ENSG00000147459; -.
DR PharmGKB; PA134932307; -.
DR VEuPathDB; HostDB:ENSG00000147459; -.
DR eggNOG; KOG1998; Eukaryota.
DR GeneTree; ENSGT00940000157734; -.
DR HOGENOM; CLU_039802_0_0_1; -.
DR InParanoid; Q9H7D0; -.
DR OMA; EVQQFSY; -.
DR OrthoDB; 102580at2759; -.
DR PhylomeDB; Q9H7D0; -.
DR TreeFam; TF300423; -.
DR PathwayCommons; Q9H7D0; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9H7D0; -.
DR BioGRID-ORCS; 80005; 51 hits in 1069 CRISPR screens.
DR ChiTaRS; DOCK5; human.
DR GeneWiki; Dock5; -.
DR GenomeRNAi; 80005; -.
DR Pharos; Q9H7D0; Tbio.
DR PRO; PR:Q9H7D0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H7D0; protein.
DR Bgee; ENSG00000147459; Expressed in ileal mucosa and 179 other tissues.
DR ExpressionAtlas; Q9H7D0; baseline and differential.
DR Genevisible; Q9H7D0; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007520; P:myoblast fusion; IBA:GO_Central.
DR GO; GO:1904694; P:negative regulation of vascular associated smooth muscle contraction; IMP:BHF-UCL.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:BHF-UCL.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.350; -; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR030717; DOCK5.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45653; PTHR45653; 1.
DR PANTHER; PTHR45653:SF3; PTHR45653:SF3; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..1870
FT /note="Dedicator of cytokinesis protein 5"
FT /id="PRO_0000189992"
FT DOMAIN 8..69
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 443..627
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1231..1642
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1679..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1772..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1795..1810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 818
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1794
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1814
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 1834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 351..1870
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021868"
FT VARIANT 250
FT /note="Q -> R (in dbSNP:rs17053341)"
FT /id="VAR_033886"
FT VARIANT 1023
FT /note="Q -> R (in dbSNP:rs2271111)"
FT /id="VAR_053065"
FT VARIANT 1285
FT /note="K -> R (in dbSNP:rs2659585)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_053066"
FT VARIANT 1836
FT /note="E -> K (in dbSNP:rs35688737)"
FT /id="VAR_033887"
FT CONFLICT 987
FT /note="M -> L (in Ref. 3; BAC86503)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="G -> E (in Ref. 3; BAC86503)"
FT /evidence="ECO:0000305"
FT CONFLICT 1548
FT /note="S -> Y (in Ref. 4; CAH10503)"
FT /evidence="ECO:0000305"
FT CONFLICT 1833
FT /note="N -> S (in Ref. 3; BAC86503)"
FT /evidence="ECO:0000305"
FT CONFLICT 1842
FT /note="P -> S (in Ref. 4; CAH10503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1870 AA; 215309 MW; 947A3DC1190EF7A9 CRC64;
MARWIPTKRQ KYGVAIYNYN ASQDVELSLQ IGDTVHILEM YEGWYRGYTL QNKSKKGIFP
ETYIHLKEAT VEDLGQHETV IPGELPLVQE LTSTLREWAV IWRKLYVNNK LTLFRQLQQM
TYSLIEWRSQ ILSGTLPKDE LAELKKKVTA KIDHGNRMLG LDLVVRDDNG NILDPDETST
IALFKAHEVA SKRIEEKIQE EKSILQNLDL RGQSIFSTIH TYGLYVNFKN FVCNIGEDAE
LFMALYDPDQ STFISENYLI RWGSNGMPKE IEKLNNLQAV FTDLSSMDLI RPRVSLVCQI
VRVGHMELKE GKKHTCGLRR PFGVAVMDIT DIIHGKVDDE EKQHFIPFQQ IAMETYIRQR
QLIMSPLITS HVIGENEPLT SVLNKVIAAK EVNHKGQGLW VSLKLLPGDL TQVQKNFSHL
VDRSTAIARK MGFPEIILPG DVRNDIYVTL IHGEFDKGKK KTPKNVEVTM SVHDEEGKLL
EKAIHPGAGY EGISEYKSVV YYQVKQPCWY ETVKVSIAIE EVTRCHIRFT FRHRSSQETR
DKSERAFGVA FVKLMNPDGT TLQDGRHDLV VYKGDNKKME DAKFYLTLPG TKMEMEEKEL
QASKNLVTFT PSKDSTKDSF QIATLICSTK LTQNVDLLGL LNWRSNSQNI KHNLKKLMEV
DGGEIVKFLQ DTLDALFNIM MEMSDSETYD FLVFDALVFI ISLIGDIKFQ HFNPVLETYI
YKHFSATLAY VKLSKVLNFY VANADDSSKT ELLFAALKAL KYLFRFIIQS RVLYLRFYGQ
SKDGDEFNNS IRQLFLAFNM LMDRPLEEAV KIKGAALKYL PSIINDVKLV FDPVELSVLF
CKFIQSIPDN QLVRQKLNCM TKIVESTLFR QSECREVLLP LLTDQLSGQL DDNSNKPDHE
ASSQLLSNIL EVLDRKDVGA TAVHIQLIME RLLRRINRTV IGMNRQSPHI GSFVACMIAL
LQQMDDSHYS HYISTFKTRQ DIIDFLMETF IMFKDLIGKN VYAKDWMVMN MTQNRVFLRA
INQFAEVLTR FFMDQASFEL QLWNNYFHLA VAFLTHESLQ LETFSQAKRN KIVKKYGDMR
KEIGFRIRDM WYNLGPHKIK FIPSMVGPIL EVTLTPEVEL RKATIPIFFD MMQCEFNFSG
NGNFHMFENE LITKLDQEVE GGRGDEQYKV LLEKLLLEHC RKHKYLSSSG EVFALLVSSL
LENLLDYRTI IMQDESKENR MSCTVNVLNF YKEKKREDIY IRYLYKLRDL HRDCENYTEA
AYTLLLHAEL LQWSDKPCVP HLLQKDSYYV YTQQELKEKL YQEIISYFDK GKMWEKAIKL
SKELAETYES KVFDYEGLGN LLKKRASFYE NIIKAMRPQP EYFAVGYYGQ GFPSFLRNKI
FIYRGKEYER REDFSLRLLT QFPNAEKMTS TTPPGEDIKS SPKQYMQCFT VKPVMSLPPS
YKDKPVPEQI LNYYRANEVQ QFRYSRPFRK GEKDPDNEFA TMWIERTTYT TAYTFPGILK
WFEVKQISTE EISPLENAIE TMELTNERIS NCVQQHAWDR SLSVHPLSML LSGIVDPAVM
GGFSNYEKAF FTEKYLQEHP EDQEKVELLK RLIALQMPLL TEGIRIHGEK LTEQLKPLHE
RLSSCFRELK EKVEKHYGVI TLPPNLTERK QSRTGSIVLP YIMSSTLRRL SITSVTSSVV
STSSNSSDNA PSRPGSDGSI LEPLLERRAS SGARVEDLSL REENSENRIS KFKRKDWSLS
KSQVIAEKAP EPDLMSPTRK AQRPKSLQLM DNRLSPFHGS SPPQSTPLSP PPLTPKATRT
LSSPSLQTDG IAATPVPPPP PPKSKPYEGS QRNSTELAPP LPVRREAKAP PPPPPKARKS
GIPTSEPGSQ
