WASC4_HUMAN
ID WASC4_HUMAN Reviewed; 1173 AA.
AC Q2M389; Q2NL83; Q8IW61; Q8N5W7; Q9NVD6; Q9UPW7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=WASH complex subunit 4 {ECO:0000312|HGNC:HGNC:29174};
DE AltName: Full=Strumpellin and WASH-interacting protein {ECO:0000303|PubMed:21498477};
DE Short=SWIP {ECO:0000303|PubMed:21498477};
DE AltName: Full=WASH complex subunit SWIP {ECO:0000305};
GN Name=WASHC4 {ECO:0000312|HGNC:HGNC:29174};
GN Synonyms=KIAA1033 {ECO:0000312|HGNC:HGNC:29174};
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 MRNA] (ISOFORM 1), AND VARIANT ILE-901.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-901.
RC TISSUE=Cervix, Heart, Lung, Placenta, and 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 [5]
RP FUNCTION OF THE WASH COMPLEX, AND IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [6]
RP IDENTIFICATION IN THE WASH CORE COMPLEX, FUNCTION OF THE WASH CORE COMPLEX,
RP AND INTERACTION WITH WASHC5.
RX PubMed=20498093; DOI=10.1073/pnas.0913293107;
RA Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z., Rosen M.K.,
RA Billadeau D.D.;
RT "WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein
RT (WASP) family are controlled by analogous structurally related complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [8]
RP FUNCTION, IDENTIFICATION IN THE WASH COMPLEX, INVOLVEMENT IN MRT43, VARIANT
RP MRT43 ARG-1019, AND CHARACTERIZATION OF VARIANT MRT43 ARG-1019.
RX PubMed=21498477; DOI=10.1093/hmg/ddr158;
RA Ropers F., Derivery E., Hu H., Garshasbi M., Karbasiyan M., Herold M.,
RA Nurnberg G., Ullmann R., Gautreau A., Sperling K., Varon R., Rajab A.;
RT "Identification of a novel candidate gene for non-syndromic autosomal
RT recessive intellectual disability: the WASH complex member SWIP.";
RL Hum. Mol. Genet. 20:2585-2590(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1154, AND IDENTIFICATION BY
RP 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).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23676666; DOI=10.1091/mbc.e13-02-0088;
RA Ryder P.V., Vistein R., Gokhale A., Seaman M.N., Puthenveedu M.A.,
RA Faundez V.;
RT "The WASH complex, an endosomal Arp2/3 activator, interacts with the
RT Hermansky-Pudlak syndrome complex BLOC-1 and its cargo
RT phosphatidylinositol-4-kinase type IIalpha.";
RL Mol. Biol. Cell 24:2269-2284(2013).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-901, AND IDENTIFICATION BY MASS
RP 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).
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.
CC {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093,
CC ECO:0000303|PubMed:21498477}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P),
CC WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. The WASH core
CC complex associates via WASHC2 with the F-actin-capping protein dimer
CC (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or
CC substoichiometric manner which was initially described as WASH complex.
CC {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093,
CC ECO:0000303|PubMed:21498477}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:23676666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2M389-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M389-2; Sequence=VSP_024208, VSP_024209;
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 43
CC (MRT43) [MIM:615817]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:21498477}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SWIP family. {ECO:0000305}.
CC -!- CAUTION: One study reported a nucleation-promoting factor (NPF)
CC activity towards the Arp2/3 complex using partially purified samples of
CC the WASH complex (PubMed:19922875). In another study, the in vitro
CC reconstituted and purified recombinant WASH core complex, consisting of
CC WASHC3, WASHC4, WASHC5, WASHC1 and the N-terminal residues 1-356 of
CC WASHC2, did not show activity toward Arp2/3 complex (PubMed:20498093).
CC {ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10851.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA82985.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB028956; BAA82985.1; ALT_INIT; mRNA.
DR EMBL; AK001657; BAA91816.1; -; mRNA.
DR EMBL; BC031358; AAH31358.1; -; mRNA.
DR EMBL; AC016257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040936; AAH40936.1; -; mRNA.
DR EMBL; BC104992; AAI04993.1; -; mRNA.
DR EMBL; BC104994; AAI04995.1; -; mRNA.
DR EMBL; BC110850; AAI10851.1; ALT_SEQ; mRNA.
DR CCDS; CCDS41826.1; -. [Q2M389-1]
DR RefSeq; NP_001280569.1; NM_001293640.1.
DR RefSeq; NP_056090.1; NM_015275.2. [Q2M389-1]
DR AlphaFoldDB; Q2M389; -.
DR BioGRID; 116913; 75.
DR ComplexPortal; CPX-1163; WASH complex, variant WASHC1/WASHC2C.
DR ComplexPortal; CPX-1168; WASH complex, variant WASH2P/WASHC2C.
DR ComplexPortal; CPX-1169; WASH complex, variant WASH3P/WASHC2C.
DR ComplexPortal; CPX-1170; WASH complex, variant WASH4P/WASHC2C.
DR ComplexPortal; CPX-1171; WASH complex, variant WASH6P/WASHC2C.
DR ComplexPortal; CPX-1172; WASH complex, variant WASHC1/WASHC2A.
DR ComplexPortal; CPX-1173; WASH complex, variant WASH2P/WASHC2A.
DR ComplexPortal; CPX-1174; WASH complex, variant WASH3P/WASHC2A.
DR ComplexPortal; CPX-1175; WASH complex, variant WASH4P/WASHC2A.
DR ComplexPortal; CPX-1176; WASH complex, variant WASH6P/WASHC2A.
DR CORUM; Q2M389; -.
DR IntAct; Q2M389; 21.
DR MINT; Q2M389; -.
DR STRING; 9606.ENSP00000484713; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR iPTMnet; Q2M389; -.
DR PhosphoSitePlus; Q2M389; -.
DR BioMuta; WASHC4; -.
DR DMDM; 296452861; -.
DR EPD; Q2M389; -.
DR jPOST; Q2M389; -.
DR MassIVE; Q2M389; -.
DR MaxQB; Q2M389; -.
DR PaxDb; Q2M389; -.
DR PeptideAtlas; Q2M389; -.
DR PRIDE; Q2M389; -.
DR ProteomicsDB; 61366; -. [Q2M389-1]
DR ProteomicsDB; 61367; -. [Q2M389-2]
DR Antibodypedia; 56699; 41 antibodies from 15 providers.
DR DNASU; 23325; -.
DR Ensembl; ENST00000332180.10; ENSP00000328062.6; ENSG00000136051.15. [Q2M389-1]
DR GeneID; 23325; -.
DR KEGG; hsa:23325; -.
DR MANE-Select; ENST00000332180.10; ENSP00000328062.6; NM_015275.3; NP_056090.1.
DR UCSC; uc001tld.4; human. [Q2M389-1]
DR CTD; 23325; -.
DR DisGeNET; 23325; -.
DR GeneCards; WASHC4; -.
DR HGNC; HGNC:29174; WASHC4.
DR HPA; ENSG00000136051; Low tissue specificity.
DR MalaCards; WASHC4; -.
DR MIM; 615748; gene.
DR MIM; 615817; phenotype.
DR neXtProt; NX_Q2M389; -.
DR OpenTargets; ENSG00000136051; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA128394626; -.
DR VEuPathDB; HostDB:ENSG00000136051; -.
DR eggNOG; KOG3578; Eukaryota.
DR GeneTree; ENSGT00390000002524; -.
DR InParanoid; Q2M389; -.
DR OrthoDB; 186054at2759; -.
DR PhylomeDB; Q2M389; -.
DR TreeFam; TF324604; -.
DR PathwayCommons; Q2M389; -.
DR SignaLink; Q2M389; -.
DR SIGNOR; Q2M389; -.
DR BioGRID-ORCS; 23325; 41 hits in 1029 CRISPR screens.
DR ChiTaRS; KIAA1033; human.
DR GenomeRNAi; 23325; -.
DR Pharos; Q2M389; Tdark.
DR PRO; PR:Q2M389; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q2M389; protein.
DR Bgee; ENSG00000136051; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; Q2M389; baseline and differential.
DR Genevisible; Q2M389; HS.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:MGI.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0140591; P:nuclear envelope budding; ISS:FlyBase.
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 InterPro; IPR028191; WASH-4_N.
DR InterPro; IPR028283; WASH-7_C.
DR InterPro; IPR028282; WASH-7_central.
DR InterPro; IPR027307; WASH7.
DR PANTHER; PTHR31409; PTHR31409; 1.
DR Pfam; PF14746; WASH-7_C; 1.
DR Pfam; PF14744; WASH-7_mid; 1.
DR Pfam; PF14745; WASH-7_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Disease variant; Endosome;
KW Intellectual disability; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..1173
FT /note="WASH complex subunit 4"
FT /id="PRO_0000282575"
FT REGION 705..1173
FT /note="Sufficient for interaction with WASHC5"
FT /evidence="ECO:0000269|PubMed:20498093"
FT REGION 1142..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1135..1161
FT /evidence="ECO:0000255"
FT COMPBIAS 1142..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1154
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 839..851
FT /note="VNFTYQFLKKKFY -> KWAFTAWRGGPRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024208"
FT VAR_SEQ 852..1173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024209"
FT VARIANT 323
FT /note="V -> L (in dbSNP:rs34434425)"
FT /id="VAR_031417"
FT VARIANT 599
FT /note="T -> S (in dbSNP:rs1345092)"
FT /id="VAR_057825"
FT VARIANT 901
FT /note="V -> I (in dbSNP:rs1663564)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:21269460"
FT /id="VAR_031418"
FT VARIANT 1019
FT /note="P -> R (in MRT43; reduced expression of the protein;
FT alters the WASH complex; dbSNP:rs587777411)"
FT /evidence="ECO:0000269|PubMed:21498477"
FT /id="VAR_071384"
FT CONFLICT 293
FT /note="R -> Q (in Ref. 2; BAA91816)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="W -> R (in Ref. 2; BAA91816)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="T -> A (in Ref. 2; BAA91816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1173 AA; 136403 MW; FD073D5F21127DED CRC64;
MAVETLSPDW EFDRVDDGSQ KIHAEVQLKN YGKFLEEYTS QLRRIEDALD DSIGDVWDFN
LDPIALKLLP YEQSSLLELI KTENKVLNKV ITVYAALCCE IKKLKYEAET KFYNGLLFYG
EGATDASMVE GDCQIQMGRF ISFLQELSCF VTRCYEVVMN VVHQLAALYI SNKIAPKIIE
TTGVHFQTMY EHLGELLTVL LTLDEIIDNH ITLKDHWTMY KRLLKSVHHN PSKFGIQEEK
LKPFEKFLLK LEGQLLDGMI FQACIEQQFD SLNGGVSVSK NSTFAEEFAH SIRSIFANVE
AKLGEPSEID QRDKYVGICG LFVLHFQIFR TIDKKFYKSL LDICKKVPAI TLTANIIWFP
DNFLIQKIPA AAKLLDRKSL QAIKIHRDTF LQQKAQSLTK DVQSYYVFVS SWMMKMESIL
SKEQRMDKFA EDLTNRCNVF IQGFLYAYSI STIIKTTMNL YMSMQKPMTK TSVKALCRLV
ELLKAIEHMF YRRSMVVADS VSHITQHLQH QALHSISVAK KRVISDKKYS EQRLDVLSAL
VLAENTLNGP STKQRRLIVS LALSVGTQMK TFKDEELFPL QVVMKKLDLI SELRERVQTQ
CDCCFLYWHR AVFPIYLDDV YENAVDAARL HYMFSALRDC VPAMMHARHL ESYEILLDCY
DKEIMEILNE HLLDKLCKEI EKDLRLSVHT HLKLDDRNPF KVGMKDLALF FSLNPIRFFN
RFIDIRAYVT HYLDKTFYNL TTVALHDWAT YSEMRNLATQ RYGLVMTEAH LPSQTLEQGL
DVLEIMRNIH IFVSRYLYNL NNQIFIERTS NNKHLNTINI RHIANSIRTH GTGIMNTTVN
FTYQFLKKKF YIFSQFMYDE HIKSRLIKDI RFFREIKDQN DHKYPFDRAE KFNRGIRKLG
VTPEGQSYLD QFRQLISQIG NAMGYVRMIR SGGLHCSSNA IRFVPDLEDI VNFEELVKEE
GLAEETLKAA RHLDSVLSDH TRNSAEGTEY FKMLVDVFAP EFRRPKNIHL RNFYIIVPPL
TLNFVEHSIS CKEKLNKKNK IGAAFTDDGF AMGVAYILKL LDQYREFDSL HWFQSVREKY
LKEIRAVAKQ QNVQSASQDE KLLQTMNLTQ KRLDVYLQEF ELLYFSLSSA RIFFRADKTA
AEENQEKKEK EEETKTSNGD LSDSTVSADP VVK
