WASC2_MOUSE
ID WASC2_MOUSE Reviewed; 1334 AA.
AC Q6PGL7; Q3TQ99; Q80TW8; Q80UQ4; Q8CAP0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=WASH complex subunit 2 {ECO:0000312|MGI:MGI:106463};
GN Name=Washc2 {ECO:0000312|MGI:MGI:106463};
GN Synonyms=D6Wsu116e, Fam21, Kiaa0592;
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 MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-284;
RP SER-388; SER-533; SER-613; SER-614; SER-723; SER-747; SER-1169; SER-1172;
RP SER-1173 AND SER-1333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614 AND SER-747, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-322; SER-533;
RP SER-613; SER-614; SER-723; SER-747; SER-752; SER-798; SER-870; SER-873;
RP SER-1169 AND SER-1172, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP INTERACTION WITH TBC1D23.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
CC -!- FUNCTION: Acts as a component of the WASH core complex that functions
CC as a nucleation-promoting factor (NPF) at the surface of endosomes,
CC where it recruits and activates the Arp2/3 complex to induce actin
CC polymerization, playing a key role in the fission of tubules that serve
CC as transport intermediates during endosome sorting. Mediates the
CC recruitment of the WASH core complex to endosome membranes via binding
CC to phospholipids and VPS35 of the retromer CSC. Mediates the
CC recruitment of the F-actin-capping protein dimer to the WASH core
CC complex probably promoting localized F-actin polymerization needed for
CC vesicle scission. Via its C-terminus binds various phospholipids, most
CC strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P),
CC phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol
CC 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma
CC membrane trafficking and recycling of SNX27-retromer-dependent cargo
CC proteins, such as GLUT1. Required for the association of DNAJC13,
CC ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the
CC endosomal recruitment of CCC and retriever complexes subunits COMMD1
CC and CCDC93 as well as the retrievere complex subunit VPS35L.
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex (SHRC) composed of WASHC1, WASHC2, WASHC3, WASHC4
CC and WASHC5; in the complex interacts (via N-terminus) directly with
CC WASHC1. The WASH core complex associates with the F-actin-capping
CC protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a
CC transient or substoichiometric manner which was initially described as
CC WASH complex. Interacts with VPS35; mediates the association with the
CC retromer CSC complex. Interacts with FKBP15. Interacts with CCDC93,
CC CCDC22, VPS35L; indicative for an association of the WASH core complex
CC with the CCC and retriever complexes (By similarity). Directly
CC interacts with TBC1D23 (PubMed:29084197).
CC {ECO:0000250|UniProtKB:Q9Y4E1, ECO:0000269|PubMed:29084197}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGL7-2; Sequence=VSP_030949;
CC -!- DOMAIN: The LFa (leucine-phenylalanine-acidic) motif bind directly to
CC VPS35 of retromer CSC; adjacent motifs can act cooperatively to bind
CC multiple CSCs, although there is significant variability in the
CC affinities of different motifs for retromer.
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49979.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK122320; BAC65602.2; -; Transcribed_RNA.
DR EMBL; AK163765; BAE37485.1; -; mRNA.
DR EMBL; AK038318; BAC29966.1; -; mRNA.
DR EMBL; BC049979; AAH49979.1; ALT_SEQ; mRNA.
DR EMBL; BC056942; AAH56942.1; -; mRNA.
DR CCDS; CCDS20450.1; -. [Q6PGL7-1]
DR RefSeq; NP_080861.2; NM_026585.3. [Q6PGL7-1]
DR AlphaFoldDB; Q6PGL7; -.
DR SMR; Q6PGL7; -.
DR BioGRID; 205711; 9.
DR ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
DR IntAct; Q6PGL7; 4.
DR MINT; Q6PGL7; -.
DR STRING; 10090.ENSMUSP00000038983; -.
DR iPTMnet; Q6PGL7; -.
DR PhosphoSitePlus; Q6PGL7; -.
DR EPD; Q6PGL7; -.
DR jPOST; Q6PGL7; -.
DR MaxQB; Q6PGL7; -.
DR PaxDb; Q6PGL7; -.
DR PeptideAtlas; Q6PGL7; -.
DR PRIDE; Q6PGL7; -.
DR ProteomicsDB; 297839; -. [Q6PGL7-1]
DR ProteomicsDB; 297840; -. [Q6PGL7-2]
DR Ensembl; ENSMUST00000036759; ENSMUSP00000038983; ENSMUSG00000024104. [Q6PGL7-1]
DR GeneID; 28006; -.
DR KEGG; mmu:28006; -.
DR UCSC; uc009djs.2; mouse. [Q6PGL7-1]
DR CTD; 28006; -.
DR MGI; MGI:106463; Washc2.
DR VEuPathDB; HostDB:ENSMUSG00000024104; -.
DR eggNOG; ENOG502QTIY; Eukaryota.
DR GeneTree; ENSGT00940000153997; -.
DR HOGENOM; CLU_267715_0_0_1; -.
DR InParanoid; Q6PGL7; -.
DR OMA; IHTIFYD; -.
DR OrthoDB; 131637at2759; -.
DR PhylomeDB; Q6PGL7; -.
DR TreeFam; TF329309; -.
DR BioGRID-ORCS; 28006; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Fam21; mouse.
DR PRO; PR:Q6PGL7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6PGL7; protein.
DR Bgee; ENSMUSG00000024104; Expressed in cerebellar vermis and 261 other tissues.
DR ExpressionAtlas; Q6PGL7; baseline and differential.
DR Genevisible; Q6PGL7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; IDA:MGI.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:MGI.
DR GO; GO:1905394; F:retromer complex binding; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; IC:ComplexPortal.
DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR InterPro; IPR029341; FAM21/CAPZIP.
DR Pfam; PF15255; CAP-ZIP_m; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1334
FT /note="WASH complex subunit 2"
FT /id="PRO_0000317433"
FT REGION 1..219
FT /note="Sufficient for interaction with WASHC3, WASHC4 and
FT WASHC5; required for interaction with WASHC1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 201..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..594
FT /note="Sufficient for interaction with CCDC93"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 348..1334
FT /note="Interaction with VPS35"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 492..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1334
FT /note="Interaction with phospholipids"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 1014..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1042
FT /note="Required for interaction with F-actin-capping
FT protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 1294..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 358..368
FT /note="LFa 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 441..457
FT /note="LFa 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 476..485
FT /note="LFa 3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 531..542
FT /note="LFa 4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 566..577
FT /note="LFa 5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 658..670
FT /note="LFa 6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 686..698
FT /note="LFa 7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 835..843
FT /note="LFa 8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 852..858
FT /note="LFa 9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 874..884
FT /note="LFa 10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1124..1131
FT /note="LFa 11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1164..1178
FT /note="LFa 12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1194..1202
FT /note="LFa 13"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1227..1233
FT /note="LFa 14"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1255..1263
FT /note="LFa 15"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1283..1292
FT /note="LFa 16"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1323..1331
FT /note="LFa 17"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT COMPBIAS 220..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 866..952
FT /note="SSVPSGGSLFGDDEDDDLFSSAKTQPVVPEKKGTLKKDHPVSLKNQDPLDST
FT QGSKEKSTWKTEPAQDSSGLTPFKSREPSSRIGKI -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_030949"
FT CONFLICT 385
FT /note="L -> S (in Ref. 3; AAH49979)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="P -> S (in Ref. 3; AAH49979)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="A -> V (in Ref. 1; BAC65602)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="N -> S (in Ref. 2; BAC29966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1334 AA; 145311 MW; AD35C3FFAC27C159 CRC64;
MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI
KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQVLKA EAEKAEQEKT
REQKEIDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANERVDL ILEPKDLYID
RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND
QNQHTTQISD EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ
RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG LFSNGQGLFD
DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV SVLLGHPDVS GSTSAPSLKE
LQKHGQPTPG KSSHLPTPAG LFDDDDNDND EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD
EGDLFKEKAE ALPAASVSQT HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED
LFSSQSSSKP KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS
EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA KAVKKTNLFE
DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL PPTSVPSATT KKESVPKVPL
LFSDEEDSEV PSGVKPEDLK VDNARVSPEV GSADVASIAQ KEGLLPASDQ EAGGPSDIFS
SSSPLDKGAK GRTRTVLSLF DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE
LLFSHKLQKD NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL
KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG KIQANLAINP
AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL PGSVEAGVSF DLPAQADTLH
SANKSRVKVR GKRRPQTRAA RRLAAQESSE AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP
RMASGQTSSE TATAPPWEGG PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV
EGAGVMAGEP PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED
LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT LEPNLFDDNI
DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA SKPKSQSAEA ASEQRSEHKV
ASIFDDPLNA FGSQ
