DOC11_HUMAN
ID DOC11_HUMAN Reviewed; 2073 AA.
AC Q5JSL3; A6NMF0; Q66M66; Q6ZUJ5; Q86VU8; Q96MN3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Dedicator of cytokinesis protein 11 {ECO:0000305};
DE AltName: Full=Activated Cdc42-associated guanine nucleotide exchange factor;
DE Short=ACG;
DE AltName: Full=Zizimin-2 {ECO:0000305};
GN Name=DOCK11 {ECO:0000312|HGNC:HGNC:23483}; Synonyms=ZIZ2 {ECO:0000305};
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].
RC TISSUE=Brain;
RX PubMed=16968698; DOI=10.1074/jbc.m606248200;
RA Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT "Identification of a DOCK180-related guanine nucleotide exchange factor
RT that is capable of mediating a positive feedback activation of Cdc42.";
RL J. Biol. Chem. 281:35253-35262(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 811-2073.
RC TISSUE=Synovium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1283-2073.
RC TISSUE=Testis;
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-161, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248 AND SER-440, 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 [8]
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-16; SER-23; SER-306;
RP SER-440; SER-1237 AND SER-1240, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC by exchanging bound GDP for free GTP. Required for marginal zone (MZ)
CC B-cell development, is associated with early bone marrow B-cell
CC development, MZ B-cell formation, MZ B-cell number and marginal
CC metallophilic macrophages morphology. Facilitates filopodia formation
CC through the activation of CDC42. {ECO:0000250|UniProtKB:A2AF47}.
CC -!- SUBUNIT: Interacts with CDC42. {ECO:0000250|UniProtKB:A2AF47}.
CC -!- DOMAIN: The DOCKER domain is necessary for the GEF activity. The DOCKER
CC domain mediates interaction with activated CDC42 in conjunction with
CC residues 66-126. {ECO:0000250|UniProtKB:A2AF47}.
CC -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71253.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86230.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY692226; AAU04438.1; -; mRNA.
DR EMBL; AC007021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471161; EAW89895.1; -; Genomic_DNA.
DR EMBL; AK056684; BAB71253.1; ALT_INIT; mRNA.
DR EMBL; AK125641; BAC86230.1; ALT_INIT; mRNA.
DR EMBL; BC047713; AAH47713.1; -; mRNA.
DR CCDS; CCDS35373.1; -.
DR RefSeq; NP_653259.3; NM_144658.3.
DR AlphaFoldDB; Q5JSL3; -.
DR SMR; Q5JSL3; -.
DR BioGRID; 126589; 36.
DR IntAct; Q5JSL3; 19.
DR MINT; Q5JSL3; -.
DR STRING; 9606.ENSP00000276202; -.
DR GlyGen; Q5JSL3; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q5JSL3; -.
DR MetOSite; Q5JSL3; -.
DR PhosphoSitePlus; Q5JSL3; -.
DR BioMuta; DOCK11; -.
DR DMDM; 158563857; -.
DR EPD; Q5JSL3; -.
DR jPOST; Q5JSL3; -.
DR MassIVE; Q5JSL3; -.
DR MaxQB; Q5JSL3; -.
DR PaxDb; Q5JSL3; -.
DR PeptideAtlas; Q5JSL3; -.
DR PRIDE; Q5JSL3; -.
DR ProteomicsDB; 63163; -.
DR Antibodypedia; 29701; 52 antibodies from 17 providers.
DR DNASU; 139818; -.
DR Ensembl; ENST00000276202.9; ENSP00000276202.7; ENSG00000147251.16.
DR GeneID; 139818; -.
DR KEGG; hsa:139818; -.
DR MANE-Select; ENST00000276202.9; ENSP00000276202.7; NM_144658.4; NP_653259.3.
DR UCSC; uc004eqp.3; human.
DR CTD; 139818; -.
DR DisGeNET; 139818; -.
DR GeneCards; DOCK11; -.
DR HGNC; HGNC:23483; DOCK11.
DR HPA; ENSG00000147251; Low tissue specificity.
DR MIM; 300681; gene.
DR neXtProt; NX_Q5JSL3; -.
DR OpenTargets; ENSG00000147251; -.
DR PharmGKB; PA128394757; -.
DR VEuPathDB; HostDB:ENSG00000147251; -.
DR eggNOG; KOG1997; Eukaryota.
DR GeneTree; ENSGT00940000155658; -.
DR InParanoid; Q5JSL3; -.
DR OrthoDB; 20156at2759; -.
DR PhylomeDB; Q5JSL3; -.
DR TreeFam; TF313629; -.
DR PathwayCommons; Q5JSL3; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q5JSL3; -.
DR BioGRID-ORCS; 139818; 12 hits in 704 CRISPR screens.
DR ChiTaRS; DOCK11; human.
DR GeneWiki; Dock11; -.
DR GenomeRNAi; 139818; -.
DR Pharos; Q5JSL3; Tdark.
DR PRO; PR:Q5JSL3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5JSL3; protein.
DR Bgee; ENSG00000147251; Expressed in parietal pleura and 177 other tissues.
DR ExpressionAtlas; Q5JSL3; baseline and differential.
DR Genevisible; Q5JSL3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08697; C2_Dock-D; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037809; C2_Dock-D.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR021816; DOCK_C/D_N.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23317; PTHR23317; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF11878; DUF3398; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..2073
FT /note="Dedicator of cytokinesis protein 11"
FT /id="PRO_0000299558"
FT DOMAIN 165..272
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 640..818
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1609..2036
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1226..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 248
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AF47"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 813
FT /note="I -> F (in dbSNP:rs16995229)"
FT /id="VAR_034854"
FT CONFLICT 376
FT /note="F -> L (in Ref. 1; AAU04438)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="N -> K (in Ref. 1; AAU04438)"
FT /evidence="ECO:0000305"
FT CONFLICT 1984
FT /note="K -> E (in Ref. 1; AAU04438 and 4; BAB71253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2073 AA; 237671 MW; 558FC01EE5D23B6E CRC64;
MAEVRKFTKR LSKPGTAAEL RQSVSEAVRG SVVLEKAKVV EPLDYENVIA QRKTQIYSDP
LRDLLMFPME DISISVIGRQ RRTVQSTVPE DAEKRAQSLF VKECIKTYST DWHVVNYKYE
DFSGDFRMLP CKSLRPEKIP NHVFEIDEDC EKDEDSSSLC SQKGGVIKQG WLHKANVNST
ITVTMKVFKR RYFYLTQLPD GSYILNSYKD EKNSKESKGC IYLDACIDVV QCPKMRRHAF
ELKMLDKYSH YLAAETEQEM EEWLITLKKI IQINTDSLVQ EKKETVETAQ DDETSSQGKA
ENIMASLERS MHPELMKYGR ETEQLNKLSR GDGRQNLFSF DSEVQRLDFS GIEPDIKPFE
EKCNKRFLVN CHDLTFNILG QIGDNAKGPP TNVEPFFINL ALFDVKNNCK ISADFHVDLN
PPSVREMLWG SSTQLASDGS PKGSSPESYI HGIAESQLRY IQQGIFSVTN PHPEIFLVAR
IEKVLQGNIT HCAEPYIKNS DPVKTAQKVH RTAKQVCSRL GQYRMPFAWA ARPIFKDTQG
SLDLDGRFSP LYKQDSSKLS SEDILKLLSE YKKPEKTKLQ IIPGQLNITV ECVPVDLSNC
ITSSYVPLKP FEKNCQNITV EVEEFVPEMT KYCYPFTIYK NHLYVYPLQL KYDSQKTFAK
ARNIAVCVEF RDSDESDASA LKCIYGKPAG SVFTTNAYAV VSHHNQNPEF YDEIKIELPI
HLHQKHHLLF TFYHVSCEIN TKGTTKKQDT VETPVGFAWV PLLKDGRIIT FEQQLPVSAN
LPPGYLNLND AESRRQCNVD IKWVDGAKPL LKIKSHLEST IYTQDLHVHK FFHHCQLIQS
GSKEVPGELI KYLKCLHAME IQVMIQFLPV ILMQLFRVLT NMTHEDDVPI NCTMVLLHIV
SKCHEEGLDS YLRSFIKYSF RPEKPSAPQA QLIHETLATT MIAILKQSAD FLSINKLLKY
SWFFFEIIAK SMATYLLEEN KIKLPRGQRF PETYHHVLHS LLLAIIPHVT IRYAEIPDES
RNVNYSLASF LKRCLTLMDR GFIFNLINDY ISGFSPKDPK VLAEYKFEFL QTICNHEHYI
PLNLPMAFAK PKLQRVQDSN LEYSLSDEYC KHHFLVGLLL RETSIALQDN YEIRYTAISV
IKNLLIKHAF DTRYQHKNQQ AKIAQLYLPF VGLLLENIQR LAGRDTLYSC AAMPNSASRD
EFPCGFTSPA NRGSLSTDKD TAYGSFQNGH GIKREDSRGS LIPEGATGFP DQGNTGENTR
QSSTRSSVSQ YNRLDQYEIR SLLMCYLYIV KMISEDTLLT YWNKVSPQEL INILILLEVC
LFHFRYMGKR NIARVHDAWL SKHFGIDRKS QTMPALRNRS GVMQARLQHL SSLESSFTLN
HSSTTTEADI FHQALLEGNT ATEVSLTVLD TISFFTQCFK TQLLNNDGHN PLMKKVFDIH
LAFLKNGQSE VSLKHVFASL RAFISKFPSA FFKGRVNMCA AFCYEVLKCC TSKISSTRNE
ASALLYLLMR NNFEYTKRKT FLRTHLQIII AVSQLIADVA LSGGSRFQES LFIINNFANS
DRPMKATAFP AEVKDLTKRI RTVLMATAQM KEHEKDPEML IDLQYSLAKS YASTPELRKT
WLDSMAKIHV KNGDFSEAAM CYVHVAALVA EFLHRKKLFP NGCSAFKKIT PNIDEEGAMK
EDAGMMDVHY SEEVLLELLE QCVDGLWKAE RYEIISEISK LIVPIYEKRR EFEKLTQVYR
TLHGAYTKIL EVMHTKKRLL GTFFRVAFYG QSFFEEEDGK EYIYKEPKLT GLSEISLRLV
KLYGEKFGTE NVKIIQDSDK VNAKELDPKY AHIQVTYVKP YFDDKELTER KTEFERNHNI
SRFVFEAPYT LSGKKQGCIE EQCKRRTILT TSNSFPYVKK RIPINCEQQI NLKPIDVATD
EIKDKTAELQ KLCSSTDVDM IQLQLKLQGC VSVQVNAGPL AYARAFLNDS QASKYPPKKV
SELKDMFRKF IQACSIALEL NERLIKEDQV EYHEGLKSNF RDMVKELSDI IHEQILQEDT
MHSPWMSNTL HVFCAISGTS SDRGYGSPRY AEV
