DOCK7_MOUSE
ID DOCK7_MOUSE Reviewed; 2130 AA.
AC Q8R1A4; Q45V78; Q5PRE6; Q6PJ17; Q9CSB6; Q9CXM7;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Dedicator of cytokinesis protein 7;
DE AltName: Full=Protein moonlight {ECO:0000303|PubMed:19202056};
GN Name=Dock7; Synonyms=Gm430, Kiaa1771, Mnlt {ECO:0000303|PubMed:19202056};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-587.
RC STRAIN=BALB/cJ;
RA Yamauchi J., Miyamoto Y., Takashima S., Tanoue A.;
RT "Characterization of a novel GEF Dock7.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 811-2130 (ISOFORM 2).
RC STRAIN=C57BL/6J, FVB/N, and NMRI; TISSUE=Head, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1404-2130 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1856-2130 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900 AND SER-1428, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1422 AND SER-1428, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP INTERACTION WITH CRY1.
RX PubMed=19129230; DOI=10.1093/nar/gkn1013;
RA Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
RT "Molecular characterization of Mybbp1a as a co-repressor on the Period2
RT promoter.";
RL Nucleic Acids Res. 37:1115-1126(2009).
RN [10]
RP FUNCTION, AND INVOLVEMENT IN MNLT PHENOTYPE.
RX PubMed=19202056; DOI=10.1073/pnas.0813208106;
RA Blasius A.L., Brandl K., Crozat K., Xia Y., Khovananth K., Krebs P.,
RA Smart N.G., Zampolli A., Ruggeri Z.M., Beutler B.A.;
RT "Mice with mutations of Dock7 have generalized hypopigmentation and white-
RT spotting but show normal neurological function.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2706-2711(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-182; THR-450;
RP SER-862; SER-864; SER-896; SER-900; THR-907; SER-910; SER-929; SER-1420;
RP SER-1422; SER-1424 AND SER-1428, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION, AND INTERACTION WITH TACC3.
RX PubMed=22842144; DOI=10.1038/nn.3171;
RA Yang Y.T., Wang C.L., Van Aelst L.;
RT "DOCK7 interacts with TACC3 to regulate interkinetic nuclear migration and
RT cortical neurogenesis.";
RL Nat. Neurosci. 15:1201-1210(2012).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1952, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF),
CC which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP
CC for free GTP. Does not have a GEF activity for CDC42. Required for
CC STMN1 'Ser-15' phosphorylation during axon formation and consequently
CC for neuronal polarization (By similarity). As part of the DISP complex,
CC may regulate the association of septins with actin and thereby regulate
CC the actin cytoskeleton (By similarity). Has a role in pigmentation
CC (PubMed:19202056). Involved in the regulation of cortical neurogenesis
CC through the control of radial glial cells (RGCs) proliferation versus
CC differentiation; negatively regulates the basal-to-apical interkinetic
CC nuclear migration of RGCs by antagonizing the microtubule growth-
CC promoting function of TACC3 (PubMed:22842144).
CC {ECO:0000250|UniProtKB:Q96N67, ECO:0000269|PubMed:19202056,
CC ECO:0000269|PubMed:22842144}.
CC -!- SUBUNIT: Component of the DOCK7-induced septin displacement/DISP
CC complex, at least composed of DOCK7, LRCH3 and MYO6 (By similarity).
CC Interacts with TSC1 (By similarity). Interacts with nucleotide-free
CC RAC1 and RAC3 (By similarity). Interacts with TACC3. Interacts with
CC CRY1. Interacts with NOD2 (By similarity).
CC {ECO:0000250|UniProtKB:Q96N67, ECO:0000269|PubMed:19129230,
CC ECO:0000269|PubMed:22842144}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:Q96N67}. Note=Enriched in the developing axons
CC of hippocampal neurons. {ECO:0000250|UniProtKB:Q96N67}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R1A4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1A4-2; Sequence=VSP_007708;
CC -!- DOMAIN: The DOCKER domain mediates GEF activity.
CC {ECO:0000250|UniProtKB:Q96N67}.
CC -!- DISEASE: Note=Defects in Dock7 are responsible for the moonlight
CC phenotype (mnlt). mnlt/mnlt mice display an overall lightened coat
CC color and hypopigmentation of the belly and distal extremities,
CC particularly the paws, tail tip, and genitalia.
CC {ECO:0000269|PubMed:19202056}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24823.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH86672.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB28798.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL627349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ109674; AAZ17650.1; -; mRNA.
DR EMBL; BC024823; AAH24823.2; ALT_INIT; mRNA.
DR EMBL; BC024917; AAH24917.3; -; mRNA.
DR EMBL; BC086672; AAH86672.1; ALT_INIT; mRNA.
DR EMBL; AK122554; BAC65836.1; -; mRNA.
DR EMBL; AK013336; BAB28798.3; ALT_INIT; mRNA.
DR EMBL; AK014226; BAB29215.1; -; mRNA.
DR CCDS; CCDS71425.1; -. [Q8R1A4-2]
DR CCDS; CCDS89783.1; -. [Q8R1A4-1]
DR AlphaFoldDB; Q8R1A4; -.
DR SMR; Q8R1A4; -.
DR IntAct; Q8R1A4; 9.
DR STRING; 10090.ENSMUSP00000030286; -.
DR iPTMnet; Q8R1A4; -.
DR PhosphoSitePlus; Q8R1A4; -.
DR jPOST; Q8R1A4; -.
DR MaxQB; Q8R1A4; -.
DR PaxDb; Q8R1A4; -.
DR PeptideAtlas; Q8R1A4; -.
DR PRIDE; Q8R1A4; -.
DR ProteomicsDB; 279758; -. [Q8R1A4-1]
DR ProteomicsDB; 279759; -. [Q8R1A4-2]
DR UCSC; uc008tup.2; mouse. [Q8R1A4-1]
DR MGI; MGI:1914549; Dock7.
DR eggNOG; KOG1997; Eukaryota.
DR InParanoid; Q8R1A4; -.
DR PhylomeDB; Q8R1A4; -.
DR Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR ChiTaRS; Dock7; mouse.
DR PRO; PR:Q8R1A4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R1A4; protein.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0045200; P:establishment of neuroblast polarity; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08696; C2_Dock-C; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR037808; C2_Dock-C.
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 PANTHER; PTHR23317; PTHR23317; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF11878; DUF3398; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil;
KW Developmental protein; Differentiation;
KW Guanine-nucleotide releasing factor; Methylation; Neurogenesis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2130
FT /note="Dedicator of cytokinesis protein 7"
FT /id="PRO_0000189996"
FT DOMAIN 561..727
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1668..2104
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 137..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..395
FT /evidence="ECO:0000255"
FT COILED 2076..2102
FT /evidence="ECO:0000255"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 907
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 909
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT MOD_RES 1420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 1952
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96N67"
FT VAR_SEQ 1822..1826
FT /note="STGWE -> DGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007708"
SQ SEQUENCE 2130 AA; 241438 MW; 936B564638C1FC1D CRC64;
MAERRAFAQK ISRTVAAEVR KQISGQYSGS PQLLKNLNIV GNISHHTTVP LTEAVDPVDL
EDYLVTHPLS GDSGPLRDLV EFPPDDIEVV YSPRDCRTLV SAVPEESEMD PHVRDCIRSY
TEDWAVVVRK YHKLGTGFNP NTLDKQKERQ KGLPRQVFES DEAPDGSSYQ DEQDDLKRRS
MSIDDTPRGS WACSIFDLKN SLPDALLPNL LDRTPNEEID HQNDDQRKSN RHKELFALHP
SPDEEEPIER LSVPDVPKEH FGQRLLVKCL SLKFEIEIEP IFASLALYDV KEKKKISENF
YFDLNSEQMK GLLRPHVPPA AITTLARSAI FSITYPSQDV FLVIKLEKVL QQGDIGECAE
PYMIFKEADA TKNKEKLEKL KSQADQFCQR LGKYRMPFAW TAIHLMNIVS SAGSLERDST
EVEISTGERK GSWSERRNSS LVGRRSLERT TSGDDACNLT SFRPATLTVA NFFKQEGDRL
SDEDLYKFLA DMRRPSSVLR RLRPITAQLK IDISPAPENP HYCLTPELLQ VKLYPDSRVR
PTREILEFPA RDVYVPNTTY RNLLYIYPQS LNFANRQGSA RNITVKVQFM YGEDPSNAMP
VIFGKSSCSE FSKEAYTAVV YHNRSPDFHE EIKVKLPATL TDHHHLLFTF YHVSCQQKQN
TPLETPVGYT WIPMLQNGRL KTGQFCLPVS LEKPPQAYSV LSPEVPLPGM KWVDNHKGVF
NVEVVAVSSI HTQDPYLDKF FALVNALDEH MFPVRIGDMR IMENNLESEL KSSISALNSS
QLEPVVRFLH LLLDKLILLV VRPPVIAGQI VNLGQASFEA MASIINRLHK NLEGNHDQHG
RNNLLASYIY YVFRLPNTYP NSPSPGPGGL GGSVHYATMA RSAVRPASLN LNRSRSLSNS
NPDISGTPTS PDDEVRSIIG SKGLDRSNSW VNTGPKAAPW GSNPSPSAES TQAMDRSCNR
MSSHTETSSF LQTLTGRLPT KKLFHEELAL QWVVCSGSVR ESALQQAWFF FELMVKSMVH
HLYFNDKLDA PRESRFPERF MDDIAALVST IAGDVVSRFQ KDTEMVERLN TSLAFFLNDL
LSVMDRGFVF SLIKSCYKQV SAKLYSLPNP SVLVSLRLDF LRIICSHEHY VTLNLPCSLL
TPPASPSPSV SSATSQSSGF STSVQDQKIA NMFELSLPFR QQHYLAGLVL TELALILDPD
AEGLFGLHKK VINMVHNLLS THDSDPRYSD PQIKARVAML YLPLIGIIME TVPQLYDFTE
SHNQRGRPIC IAPDDYDSES GSMISQTVAM AIAGTSVPQL TRPGSFLLTS TSGRQHTTFS
AESSRSLLIC LLWVLKNADE TVLQKWFTDL SVLQLNRLLD LLYLCVSCFE YKGKKVFERM
NSLTFKKSKD MRAKLEEAIL GSIGARQEMV RRSRGQLERS PSGSAFGSQE NLRWRKDMTH
WRQNSEKLDK SRAEIEHEAL IDGNLATEAN LIILDTLEII VQTVSVTESK ESILGGVLKV
LLQSMACNQS AVYLQHCFAT QRALVSKFPE LLFEEETEQC ADLCLRLLRH CSSSISTIRS
HASASLYLLM RQNFEIGNNF ARVKMQVTMS LSSLVGTSQN FNEEFLRRSL KTILTYAEED
LELRETTFPD QVQDLVFNLH MILSDTVKMK EHQEDPEMLI DLMYRIAKGY QTSPDLRLTW
LQNMAGKHSE RSNHAEAAQC LVHSAALVAE YLSMLEDRKY LPVGCVTFQN ISSNVLEESA
VSDDVVSPDE EGICSGKYFT ESGLVGLLEQ AAASFSMAGM YEAVNEVYKV LIPIHEANRD
AKKLSTIHGK LQEAFSKIVH QSTGWERMFG TYFRVGFYGT KFGDLDEQEF VYKEPAITKL
AEISHRLEGF YGERFGEDVL EVIKDSNPVD KCKLDPNKAY IQITYVEPFF DTYEMKDRIT
YFDKNYNLRR FMYCTPFTLD GRAHGELHEQ FKRKTILTTS HAFPYIKTRV NVTHKEEIIL
TPIEVAIEDM QKKTQELAFA THQDPADPKM LQMVLQGSVG TTVNQGPLEV AQVFLSEIPG
DPKLFRHHNK LRLCFKDFTK RCEDALRKNK SLIGPDQKEY QRELERNYHR LKEALQPLIN
RKIPQLYKAV LPVTCHRDSF SRMSLRKMEL
