WASH1_HUMAN
ID WASH1_HUMAN Reviewed; 465 AA.
AC A8K0Z3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=WASH complex subunit 1 {ECO:0000312|HGNC:HGNC:24361};
DE AltName: Full=CXYorf1-like protein on chromosome 9;
DE AltName: Full=Protein FAM39E;
DE AltName: Full=WAS protein family homolog 1;
GN Name=WASHC1 {ECO:0000312|HGNC:HGNC:24361}; Synonyms=FAM39E, WASH1;
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].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP GENE DUPLICATION.
RX PubMed=10655549; DOI=10.1093/hmg/9.3.395;
RA Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
RA Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
RA Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S.,
RA Mercadante G., Pannone E., Archidiacono N., Rocchi M., Schlessinger D.,
RA D'Urso M.;
RT "Differentially regulated and evolved genes in the fully sequenced Xq/Yq
RT pseudoautosomal region.";
RL Hum. Mol. Genet. 9:395-401(2000).
RN [4]
RP GENE DUPLICATION.
RX PubMed=18159949; DOI=10.1371/journal.pgen.0030237;
RA Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E., Parkhurst S.M.,
RA Trask B.J.;
RT "Human subtelomeric WASH genes encode a new subclass of the WASP family.";
RL PLoS Genet. 3:E237-E237(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASHC2C, TUBULIN-BINDING,
RP AND MUTAGENESIS OF TRP-463.
RX PubMed=19922874; DOI=10.1016/j.devcel.2009.09.009;
RA Gomez T.S., Billadeau D.D.;
RT "A FAM21-containing WASH complex regulates retromer-dependent sorting.";
RL Dev. Cell 17:699-711(2009).
RN [6]
RP FUNCTION, FUNCTION OF THE WASH COMPLEX, AND IDENTIFICATION IN THE WASH
RP 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 [7]
RP IDENTIFICATION IN THE WASH CORE COMPLEX.
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22114305; DOI=10.1242/jcs.080986;
RA Zech T., Calaminus S.D., Caswell P., Spence H.J., Carnell M., Insall R.H.,
RA Norman J., Machesky L.M.;
RT "The Arp2/3 activator WASH regulates alpha5beta1-integrin-mediated invasive
RT migration.";
RL J. Cell Sci. 124:3753-3759(2011).
RN [9]
RP FUNCTION, UBIQUITINATION AT LYS-220, AND MUTAGENESIS OF LYS-220.
RX PubMed=23452853; DOI=10.1016/j.cell.2013.01.051;
RA Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J.,
RA Billadeau D.D., Rosen M.K., Potts P.R.;
RT "Regulation of WASH-dependent actin polymerization and protein trafficking
RT by ubiquitination.";
RL Cell 152:1051-1064(2013).
RN [10]
RP FUNCTION, INTERACTION WITH EXOC1; EXOC4 AND EXOC8, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24344185; DOI=10.1083/jcb.201306162;
RA Monteiro P., Rosse C., Castro-Castro A., Irondelle M., Lagoutte E.,
RA Paul-Gilloteaux P., Desnos C., Formstecher E., Darchen F., Perrais D.,
RA Gautreau A., Hertzog M., Chavrier P.;
RT "Endosomal WASH and exocyst complexes control exocytosis of MT1-MMP at
RT invadopodia.";
RL J. Cell Biol. 203:1063-1079(2013).
RN [11]
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 (PubMed:19922874,
CC PubMed:19922875, PubMed:20498093, PubMed:23452853). Involved in
CC endocytic trafficking of EGF (By similarity). Involved in transferrin
CC receptor recycling. Regulates the trafficking of endosomal alpha5beta1
CC integrin to the plasma membrane and involved in invasive cell migration
CC (PubMed:22114305). In T-cells involved in endosome-to-membrane
CC recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL;
CC proposed to be implicated in T cell proliferation and effector
CC function. In dendritic cells involved in endosome-to-membrane recycling
CC of major histocompatibility complex (MHC) class II probably involving
CC retromer and subsequently allowing antigen sampling, loading and
CC presentation during T-cell activation (By similarity). Involved in
CC Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium
CC invasion independent of ruffling. Involved in the exocytosis of MMP14
CC leading to matrix remodeling during invasive migration and implicating
CC late endosome-to-plasma membrane tubular connections and cooperation
CC with the exocyst complex (PubMed:24344185). Involved in negative
CC regulation of autophagy independently from its role in endosomal
CC sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34
CC activity (By similarity). {ECO:0000250|UniProtKB:C4AMC7,
CC ECO:0000250|UniProtKB:Q8VDD8, ECO:0000269|PubMed:19922874,
CC ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20498093,
CC ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23452853,
CC ECO:0000305|PubMed:20498093}.
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 (PubMed:19922875, PubMed:20498093). Interacts (via WHD1 region) with
CC WASHC2C; the interaction is direct (PubMed:19922874). Interacts with
CC VPS35; mediates the association with the retromer CSC complex.
CC Interacts with FKBP15. Interacts with alpha-tubulin. Interacts with
CC BECN1; this interaction can be competed out by AMBRA1 binding.
CC Interacts with BLOC1S2; may associate with the BLOC-1 complex.
CC Interacts with tubulin gamma chain (TUBG1 or TUBG2) (By similarity).
CC Interacts with EXOC1, EXOC4, EXOC8; in MMP14-positive endosomes in
CC breast tumor cells; indicative for an association with the exocyst
CC complex (PubMed:24344185). Interacts with TBC1D23 (PubMed:29084197).
CC {ECO:0000250|UniProtKB:Q8VDD8, ECO:0000250|UniProtKB:Q9Y4E1,
CC ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:19922875,
CC ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:24344185,
CC ECO:0000269|PubMed:29084197}.
CC -!- INTERACTION:
CC A8K0Z3; Q14457: BECN1; NbExp=3; IntAct=EBI-6160405, EBI-949378;
CC A8K0Z3; Q9NV70: EXOC1; NbExp=2; IntAct=EBI-6160405, EBI-1045313;
CC A8K0Z3; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-6160405, EBI-742102;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:19922874}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8VDD8}. Late endosome
CC {ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:24344185}. Cytoplasmic
CC vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8VDD8}. Note=Localization to the endosome
CC membrane is mediated via its interaction with WASHC2 (PubMed:19922874).
CC Localizes to MMP14-positive late endosomes and transiently to
CC invadipodia (PubMed:24344185). Localized to Salmonella typhimurium
CC entry sites (By similarity). {ECO:0000250|UniProtKB:Q8VDD8,
CC ECO:0000269|PubMed:19922874, ECO:0000269|PubMed:24344185}.
CC -!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
CC polymerization by the Arp2/3 complex in vitro.
CC {ECO:0000250|UniProtKB:C4AMC7}.
CC -!- PTM: Ubiquitinated at Lys-220 via 'Lys-63'-linked ubiquitin chains by
CC the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote
CC endosomal F-actin assembly. {ECO:0000269|PubMed:23452853}.
CC -!- MISCELLANEOUS: WASH genes duplicated to multiple chromosomal ends
CC during primate evolution, with highest copy number reached in humans,
CC whose WASH repertoires probably vary extensively among individuals
CC (PubMed:18159949). It is therefore difficult to determine which gene is
CC functional or not. The telomeric region of chromosome 9p is paralogous
CC to the pericentromeric regions of chromosome 9 as well as to 2q.
CC Paralogous regions contain 7 transcriptional units. Duplicated WASH
CC genes are also present in the Xq/Yq pseudoautosomal region, as well as
CC on chromosome 1 and 15. The chromosome 16 copy seems to be a
CC pseudogene. {ECO:0000305|PubMed:18159949}.
CC -!- SIMILARITY: Belongs to the WASH1 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 any NPF activity towards the Arp2/3 complex
CC (PubMed:20498093). {ECO:0000269|PubMed:19922875,
CC ECO:0000269|PubMed:20498093}.
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DR EMBL; AK289708; BAF82397.1; -; mRNA.
DR EMBL; AL928970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS78375.1; -.
DR RefSeq; NP_878908.4; NM_182905.4.
DR AlphaFoldDB; A8K0Z3; -.
DR SMR; A8K0Z3; -.
DR BioGRID; 938833; 75.
DR ComplexPortal; CPX-1163; WASH complex, variant WASHC1/WASHC2C.
DR ComplexPortal; CPX-1172; WASH complex, variant WASHC1/WASHC2A.
DR CORUM; A8K0Z3; -.
DR IntAct; A8K0Z3; 16.
DR MINT; A8K0Z3; -.
DR STRING; 9606.ENSP00000485627; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR iPTMnet; A8K0Z3; -.
DR MetOSite; A8K0Z3; -.
DR PhosphoSitePlus; A8K0Z3; -.
DR BioMuta; WASHC1; -.
DR jPOST; A8K0Z3; -.
DR MassIVE; A8K0Z3; -.
DR MaxQB; A8K0Z3; -.
DR PeptideAtlas; A8K0Z3; -.
DR PRIDE; A8K0Z3; -.
DR ProteomicsDB; 1843; -.
DR Antibodypedia; 75837; 8 antibodies from 7 providers.
DR DNASU; 100287171; -.
DR Ensembl; ENST00000442898.5; ENSP00000485627.1; ENSG00000181404.17.
DR GeneID; 100287171; -.
DR KEGG; hsa:100287171; -.
DR UCSC; uc010mgm.2; human.
DR CTD; 100287171; -.
DR DisGeNET; 100287171; -.
DR GeneCards; WASHC1; -.
DR HGNC; HGNC:24361; WASHC1.
DR HPA; ENSG00000181404; Low tissue specificity.
DR MIM; 613632; gene.
DR neXtProt; NX_A8K0Z3; -.
DR OpenTargets; ENSG00000181404; -.
DR PharmGKB; PA162409121; -.
DR VEuPathDB; HostDB:ENSG00000181404; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00390000016717; -.
DR HOGENOM; CLU_029156_1_0_1; -.
DR InParanoid; A8K0Z3; -.
DR OMA; RYPASHT; -.
DR OrthoDB; 904881at2759; -.
DR PhylomeDB; A8K0Z3; -.
DR PathwayCommons; A8K0Z3; -.
DR SignaLink; A8K0Z3; -.
DR SIGNOR; A8K0Z3; -.
DR BioGRID-ORCS; 100287171; 54 hits in 187 CRISPR screens.
DR ChiTaRS; WASHC1; human.
DR GenomeRNAi; 100287171; -.
DR Pharos; A8K0Z3; Tbio.
DR PRO; PR:A8K0Z3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; A8K0Z3; protein.
DR Bgee; ENSG00000181404; Expressed in left uterine tube and 98 other tissues.
DR ExpressionAtlas; A8K0Z3; baseline and differential.
DR Genevisible; A8K0Z3; HS.
DR GO; GO:0005776; C:autophagosome; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IMP:UniProtKB.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IMP: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:0031396; P:regulation of protein ubiquitination; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome;
KW Isopeptide bond; Membrane; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..465
FT /note="WASH complex subunit 1"
FT /id="PRO_0000329013"
FT DOMAIN 361..383
FT /note="WH2"
FT REGION 1..167
FT /note="WHD1"
FT REGION 1..54
FT /note="Required for WASH complex assembly"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 297..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..465
FT /note="VCA"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 376..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23452853"
FT MUTAGEN 220
FT /note="K->R: Abolishes ubiquitination by the TRIM27:MAGEL2
FT E3 ubiquitin ligase complex and impairs retrograde
FT transport."
FT /evidence="ECO:0000269|PubMed:23452853"
FT MUTAGEN 463
FT /note="W->A: Impairs retrograde transport from endosome to
FT Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:19922874"
FT CONFLICT 19
FT /note="F -> L (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="Q -> R (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="G -> E (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="P -> S (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="D -> Y (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="H -> D (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="V -> A (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="T -> TAPP (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="P -> S (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..342
FT /note="SSS -> GSN (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="W -> R (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="M -> V (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..392
FT /note="QQ -> KK (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="H -> D (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="V -> A (in Ref. 1; BAF82397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 50328 MW; DBD5DEAFB7019B3E CRC64;
MTPVRMQHSL AGQTYAVPFI QPDLRREEAV QQMADALQYL QKVSGDIFSR ISQQVEQSRS
QVQAIGEKVS LAQAKIEKIK GSKKAIKVFS SAKYPAPGRL QEYGSIFTGA QDPGLQRRPR
HRIQSKHRPL DERALQEKLK DFPVCVSTKP EPEDDAEEGL GGLPSNISSV SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH VMLGAETEEK LFDAPLSISK REQLEQQVPE NYFYVPDLGQ
VPEIHVPSYL PDLPGIANDL MYSADLGPGI APSAPGTIPE LPTFHTEVAE PLKVDLQDGV
LTPPPPPPPP PPAPEVLASA PPLPPSTAAP VGQGARQDDS SSSASPSVQG APREVVDPSG
GWATLLESIR QAGGIGKAKL RSMKERKLEK QQQKEQEQVR ATSQGGHLMS DLFNKLVMRR
KGISGKGPGA GEGPGGAFVR VSDSIPPLPP PQQPQAEEDE DDWES
