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Protein

WAS protein family homolog 1

Gene

Wash1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a nucleation-promoting factor at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875). Its assembly in the WASH core complex seems to inhibit its NPF activity and via FAM21 is required for its membrane targeting (By similarity). Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration (PubMed:22114305). In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated in T-cell proliferation and effector function (PubMed:23275443). In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation (PubMed:24886983). Involved in cytokinesis and following polar body extrusion during oocyte meiotic maturation (PubMed:24998208). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling (PubMed:19732055). Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex (By similarity). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (PubMed:23974797).By similarity1 Publication8 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • gamma-tubulin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  • Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  • dendritic cell antigen processing and presentation Source: UniProtKB
  • endosomal transport Source: UniProtKB
  • exocytosis Source: MGI
  • extracellular matrix disassembly Source: MGI
  • negative regulation of autophagy Source: UniProtKB
  • negative regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • oocyte maturation Source: UniProtKB
  • polar body extrusion after meiotic divisions Source: UniProtKB
  • positive regulation of cell migration Source: MGI
  • positive regulation of pseudopodium assembly Source: MGI
  • protein localization to cell surface Source: UniProtKB
  • regulation of immune response Source: UniProtKB
  • regulation of protein ubiquitination Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
  • spindle assembly involved in meiosis Source: UniProtKB
  • T cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
WAS protein family homolog 1
Gene namesi
Name:Wash1
Synonyms:Orf19, Wash
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1916017. Wash1.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB
  • centriole Source: UniProtKB-SubCell
  • centrosome Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • cytosol Source: GOC
  • early endosome Source: UniProtKB
  • early endosome membrane Source: UniProtKB-SubCell
  • invadopodium Source: MGI
  • recycling endosome Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB-SubCell
  • WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475WAS protein family homolog 1PRO_0000390963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki219 – 219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Ubiquitinated at Lys-219 via 'Lys-63'-linked ubiquitin chains by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote endosomal F-actin assembly.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ8VDD8.
MaxQBiQ8VDD8.
PaxDbiQ8VDD8.
PRIDEiQ8VDD8.

PTM databases

iPTMnetiQ8VDD8.
PhosphoSiteiQ8VDD8.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8VDD8.
GenevisibleiQ8VDD8. MM.

Interactioni

Subunit structurei

Component of the WASH core complex also described as WASH regulatory complex SHRC composed of WASH1, FAM21, KIAA1033/SWIP, KIAA0196/strumpellin and CCDC53. The WASH core complex associates with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. Interacts (via WHD1 region) with FAM21; the interaction is direct (By similarity). Interacts with BECN1; WASH1 and AMBRA1 can competetively interact with BECN1 (PubMed:23974797). Interacts with BLOC1S2; may associate with the BLOC-1 complex. Interacts with tubulin gamma chain (TUBG1 or TUBG2) (PubMed:20308062).By similarity2 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • gamma-tubulin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

Protein-protein interaction databases

BioGridi213039. 25 interactions.
IntActiQ8VDD8. 28 interactions.
MINTiMINT-1865463.
STRINGi10090.ENSMUSP00000072220.

Structurei

3D structure databases

ProteinModelPortaliQ8VDD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 39123WH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 167167WHD1Add
BLAST
Regioni1 – 5454Required for WASH complex assemblyBy similarityAdd
BLAST
Regioni357 – 475119VCABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 33165Pro-richAdd
BLAST
Compositional biasi346 – 3494Poly-Ser

Domaini

The VCA (verprolin, cofilin, acidic) domain promotes actin polymerization by the Arp2/3 complex in vitro.By similarity

Sequence similaritiesi

Belongs to the WASH1 family.Curated
Contains 1 WH2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFZ4. Eukaryota.
ENOG410YN2V. LUCA.
GeneTreeiENSGT00390000016717.
HOGENOMiHOG000007381.
HOVERGENiHBG066686.
InParanoidiQ8VDD8.
KOiK18461.
OMAiTHTTLET.
OrthoDBiEOG79PJPR.
PhylomeDBiQ8VDD8.
TreeFamiTF318222.

Family and domain databases

InterProiIPR028290. WASH1.
IPR021854. WASH1_WAHD.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR23331. PTHR23331. 1 hit.
PfamiPF11945. WASH_WAHD. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VDD8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPVKTQCSL AGQLYAVPLI QPDLRREEAI QQVADALQYL QNISGDIFSR
60 70 80 90 100
ISRRVELSRR QLQAISERVS LAQAKIEKIK GSKKAIKVFS SAKYPAPEHL
110 120 130 140 150
QEYGSIFTGA LDPGLQRRPR YRIQSKHRPL DERALQEKLK YFPVCVNTKS
160 170 180 190 200
EPEDEAEEGL GGLPSNISSI SSLLLFNTTE NLYKKYVFLD PLAGAVTKTH
210 220 230 240 250
TMLGTEEEKL FDAPLSISKR EQLERQAPEN YFYVPDLGQV PEIDVPSYLP
260 270 280 290 300
DLPGVADDLM YSADLGPGIA PSAPGAIPEL PAFHTEVAEP LQPELENEVL
310 320 330 340 350
LAAPPPPPPP PPPPPPAPTA LVSTPQPPMF PDMATAAGQV AREEDSSSSM
360 370 380 390 400
AHTASVQGAP KEVVDPSSGR ATLLESIRQA GGIGKAKLRS VKERKLEKKK
410 420 430 440 450
QKEQEQVRAT SQGGDLMSDL FNKLVMRRKG ISGKGPSTGT SEGPGGAFSR
460 470
MSDSIPPLPP PQQPAGDEDE EDWES
Length:475
Mass (Da):51,659
Last modified:March 1, 2002 - v1
Checksum:i4198C8AEE499D3C3
GO

Sequence cautioni

The sequence BAE32561.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Y → C in BAE32561 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ304796 mRNA. Translation: CAC83096.1.
AK033616 mRNA. Translation: BAC28393.1.
AK149967 mRNA. Translation: BAE29201.1.
AK154400 mRNA. Translation: BAE32561.1. Different initiation.
AK159820 mRNA. Translation: BAE35400.1.
AK171737 mRNA. Translation: BAE42641.1.
AK172673 mRNA. Translation: BAE43124.1.
BC025839 mRNA. Translation: AAH25839.1.
CCDSiCCDS28944.1.
RefSeqiNP_001032846.1. NM_001037757.1.
NP_081109.1. NM_026833.1.
XP_006524922.1. XM_006524859.1.
XP_006524923.1. XM_006524860.2.
UniGeneiMm.296545.

Genome annotation databases

EnsembliENSMUST00000072383; ENSMUSP00000072220; ENSMUSG00000024101.
ENSMUST00000116556; ENSMUSP00000112255; ENSMUSG00000024101.
GeneIDi68767.
KEGGimmu:68767.
UCSCiuc008dgy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ304796 mRNA. Translation: CAC83096.1.
AK033616 mRNA. Translation: BAC28393.1.
AK149967 mRNA. Translation: BAE29201.1.
AK154400 mRNA. Translation: BAE32561.1. Different initiation.
AK159820 mRNA. Translation: BAE35400.1.
AK171737 mRNA. Translation: BAE42641.1.
AK172673 mRNA. Translation: BAE43124.1.
BC025839 mRNA. Translation: AAH25839.1.
CCDSiCCDS28944.1.
RefSeqiNP_001032846.1. NM_001037757.1.
NP_081109.1. NM_026833.1.
XP_006524922.1. XM_006524859.1.
XP_006524923.1. XM_006524860.2.
UniGeneiMm.296545.

3D structure databases

ProteinModelPortaliQ8VDD8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213039. 25 interactions.
IntActiQ8VDD8. 28 interactions.
MINTiMINT-1865463.
STRINGi10090.ENSMUSP00000072220.

PTM databases

iPTMnetiQ8VDD8.
PhosphoSiteiQ8VDD8.

Proteomic databases

EPDiQ8VDD8.
MaxQBiQ8VDD8.
PaxDbiQ8VDD8.
PRIDEiQ8VDD8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072383; ENSMUSP00000072220; ENSMUSG00000024101.
ENSMUST00000116556; ENSMUSP00000112255; ENSMUSG00000024101.
GeneIDi68767.
KEGGimmu:68767.
UCSCiuc008dgy.1. mouse.

Organism-specific databases

CTDi100287171.
MGIiMGI:1916017. Wash1.

Phylogenomic databases

eggNOGiENOG410IFZ4. Eukaryota.
ENOG410YN2V. LUCA.
GeneTreeiENSGT00390000016717.
HOGENOMiHOG000007381.
HOVERGENiHBG066686.
InParanoidiQ8VDD8.
KOiK18461.
OMAiTHTTLET.
OrthoDBiEOG79PJPR.
PhylomeDBiQ8VDD8.
TreeFamiTF318222.

Miscellaneous databases

PROiQ8VDD8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDD8.
GenevisibleiQ8VDD8. MM.

Family and domain databases

InterProiIPR028290. WASH1.
IPR021854. WASH1_WAHD.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR23331. PTHR23331. 1 hit.
PfamiPF11945. WASH_WAHD. 1 hit.
[Graphical view]
PROSITEiPS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Cecum and Spleen.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  4. "The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex."
    Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.
    Dev. Cell 17:712-723(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Functional characterization of Wiskott-Aldrich syndrome protein and scar homolog (WASH), a bi-modular nucleation-promoting factor able to interact with biogenesis of lysosome-related organelle subunit 2 (BLOS2) and gamma-tubulin."
    Monfregola J., Napolitano G., D'Urso M., Lappalainen P., Ursini M.V.
    J. Biol. Chem. 285:16951-16957(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BLOC1S2 AND TUBULIN GAMMA CHAIN.
  8. "The Arp2/3 activator WASH regulates alpha5beta1-integrin-mediated invasive migration."
    Zech T., Calaminus S.D., Caswell P., Spence H.J., Carnell M., Insall R.H., Norman J., Machesky L.M.
    J. Cell Sci. 124:3753-3759(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "WASH inhibits autophagy through suppression of Beclin 1 ubiquitination."
    Xia P., Wang S., Du Y., Zhao Z., Shi L., Sun L., Huang G., Ye B., Li C., Dai Z., Hou N., Cheng X., Sun Q., Li L., Yang X., Fan Z.
    EMBO J. 32:2685-2696(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, INTERACTION WITH BECN1.
  10. "WASH knockout T cells demonstrate defective receptor trafficking, proliferation, and effector function."
    Piotrowski J.T., Gomez T.S., Schoon R.A., Mangalam A.K., Billadeau D.D.
    Mol. Cell. Biol. 33:958-973(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Dendritic cells utilize the evolutionarily conserved WASH and retromer complexes to promote MHCII recycling and helper T cell priming."
    Graham D.B., Osborne D.G., Piotrowski J.T., Gomez T.S., Gmyrek G.B., Akilesh H.M., Dani A., Billadeau D.D., Swat W.
    PLoS ONE 9:E98606-E98606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "WASH complex regulates Arp2/3 complex for actin-based polar body extrusion in mouse oocytes."
    Wang F., Zhang L., Zhang G.L., Wang Z.B., Cui X.S., Kim N.H., Sun S.C.
    Sci. Rep. 4:5596-5596(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiWASH1_MOUSE
AccessioniPrimary (citable) accession number: Q8VDD8
Secondary accession number(s): Q3U473
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.