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Protein

WAS protein family homolog 1

Gene

WASH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a nucleation-promoting factor (NPF) 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:19922874, PubMed:19922875, PubMed:20498093, PubMed:23452853). Its assembly in the WASH core complex seems to inhibit its NPF activity and via FAM21 is required for its membrane targeting (PubMed:20498093). Involved in endocytic trafficking of EGF (By similarity). Involved in transferrin receptor recycling. 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. 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 (By similarity). Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. 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 (PubMed:24344185). Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity (By similarity).By similarity1 Publication5 Publications

GO - Molecular functioni

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

GO - Biological processi

  • Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  • endosomal transport Source: UniProtKB
  • exocytosis Source: UniProtKB
  • extracellular matrix disassembly Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of pseudopodium assembly Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • retrograde transport, endosome to Golgi Source: UniProtKB
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
WAS protein family homolog 1
Alternative name(s):
CXYorf1-like protein on chromosome 9
Protein FAM39E
Gene namesi
Name:WASH1
Synonyms:FAM39E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:24361. WASH1.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB-SubCell
  • centriole Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB-KW
  • cytosol Source: GOC
  • early endosome Source: UniProtKB
  • early endosome membrane Source: UniProtKB-SubCell
  • invadopodium Source: UniProtKB
  • late endosome Source: UniProtKB-SubCell
  • 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi220 – 2201K → R: Abolishes ubiquitination by the TRIM27:MAGEL2 E3 ubiquitin ligase complex and impairs retrograde transport. 1 Publication
Mutagenesisi463 – 4631W → A: Impairs retrograde transport from endosome to Golgi apparatus. 1 Publication

Organism-specific databases

PharmGKBiPA162409121.

Polymorphism and mutation databases

BioMutaiWASH1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465WAS protein family homolog 1PRO_0000329013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated at Lys-220 via 'Lys-63'-linked ubiquitin chains by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote endosomal F-actin assembly.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiA8K0Z3.
MaxQBiA8K0Z3.
PaxDbiA8K0Z3.
PeptideAtlasiA8K0Z3.
PRIDEiA8K0Z3.

PTM databases

iPTMnetiA8K0Z3.
PhosphoSiteiA8K0Z3.

Expressioni

Gene expression databases

CleanExiHS_WASH1.
GenevisibleiA8K0Z3. HS.

Organism-specific databases

HPAiHPA002689.

Interactioni

Subunit structurei

Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASH (WASH1, WASH2P or WASH3P), FAM21 (FAM21A or FAM21C), KIAA1033/SWIP, KIAA0196/strumpellin and CCDC53. The WASH core complex associates via FAM21 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 (PubMed:19922875, PubMed:20498093). Interacts (via WHD1 region) with FAM21C; the interaction is direct (PubMed:19922874). Interacts with VPS35; mediates the association with the retromer CSC complex. Interacts with FKBP15. Interacts with alpha-tubulin. Interacts with BECN1; WASH1 and AMBRA1 can competetively interact with BECN1. Interacts with BLOC1S2; may associate with the BLOC-1 complex. Interacts with tubulin gamma chain (TUBG1 or TUBG2) (By similarity). Interacts with EXOC1, EXOC4, EXOC8; in MMP14-positive endosomes in breast tumor cells; indicative for an association with the exocyst complex (PubMed:24344185).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BECN1Q144573EBI-6160405,EBI-949378
EXOC1Q9NV702EBI-6160405,EBI-1045313
EXOC8Q8IYI63EBI-6160405,EBI-742102

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi938833. 9 interactions.
IntActiA8K0Z3. 8 interactions.
STRINGi9606.ENSP00000352498.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini361 – 38323WH2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 167167WHD1Add
BLAST
Regioni1 – 5454Required for WASH complex assemblyBy similarityAdd
BLAST
Regioni349 – 465117VCABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi303 – 33028Pro-richAdd
BLAST

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.Curated

Phylogenomic databases

eggNOGiENOG410IFZ4. Eukaryota.
ENOG410YN2V. LUCA.
GeneTreeiENSGT00390000016717.
HOVERGENiHBG066686.
InParanoidiA8K0Z3.
KOiK18461.
OMAiPNLKGHA.
PhylomeDBiA8K0Z3.

Family and domain databases

InterProiIPR028290. WASH1.
IPR021854. WASH1_WAHD.
[Graphical view]
PANTHERiPTHR23331. PTHR23331. 1 hit.
PfamiPF11945. WASH_WAHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8K0Z3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPVRMQHSL AGQTYAVPFI QPDLRREEAV QQMADALQYL QKVSGDIFSR
60 70 80 90 100
ISQQVEQSRS QVQAIGEKVS LAQAKIEKIK GSKKAIKVFS SAKYPAPGRL
110 120 130 140 150
QEYGSIFTGA QDPGLQRRPR HRIQSKHRPL DERALQEKLK DFPVCVSTKP
160 170 180 190 200
EPEDDAEEGL GGLPSNISSV SSLLLFNTTE NLYKKYVFLD PLAGAVTKTH
210 220 230 240 250
VMLGAETEEK LFDAPLSISK REQLEQQVPE NYFYVPDLGQ VPEIHVPSYL
260 270 280 290 300
PDLPGIANDL MYSADLGPGI APSAPGTIPE LPTFHTEVAE PLKVDLQDGV
310 320 330 340 350
LTPPPPPPPP PPAPEVLASA PPLPPSTAAP VGQGARQDDS SSSASPSVQG
360 370 380 390 400
APREVVDPSG GWATLLESIR QAGGIGKAKL RSMKERKLEK QQQKEQEQVR
410 420 430 440 450
ATSQGGHLMS DLFNKLVMRR KGISGKGPGA GEGPGGAFVR VSDSIPPLPP
460
PQQPQAEEDE DDWES
Length:465
Mass (Da):50,328
Last modified:January 19, 2010 - v2
Checksum:iDBD5DEAFB7019B3E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191F → L in BAF82397 (PubMed:14702039).Curated
Sequence conflicti54 – 541Q → R in BAF82397 (PubMed:14702039).Curated
Sequence conflicti98 – 981G → E in BAF82397 (PubMed:14702039).Curated
Sequence conflicti119 – 1191P → S in BAF82397 (PubMed:14702039).Curated
Sequence conflicti141 – 1411D → Y in BAF82397 (PubMed:14702039).Curated
Sequence conflicti245 – 2451H → D in BAF82397 (PubMed:14702039).Curated
Sequence conflicti294 – 2941V → A in BAF82397 (PubMed:14702039).Curated
Sequence conflicti302 – 3021T → TAPP in BAF82397 (PubMed:14702039).Curated
Sequence conflicti321 – 3211P → S in BAF82397 (PubMed:14702039).Curated
Sequence conflicti340 – 3423SSS → GSN in BAF82397 (PubMed:14702039).Curated
Sequence conflicti362 – 3621W → R in BAF82397 (PubMed:14702039).Curated
Sequence conflicti383 – 3831M → V in BAF82397 (PubMed:14702039).Curated
Sequence conflicti391 – 3922QQ → KK in BAF82397 (PubMed:14702039).Curated
Sequence conflicti407 – 4071H → D in BAF82397 (PubMed:14702039).Curated
Sequence conflicti439 – 4391V → A in BAF82397 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK289708 mRNA. Translation: BAF82397.1.
AL928970 Genomic DNA. No translation available.
CCDSiCCDS78375.1.
RefSeqiNP_878908.4. NM_182905.4.
XP_011515963.1. XM_011517661.1.
UniGeneiHs.446466.
Hs.459573.
Hs.461200.
Hs.521961.
Hs.585931.
Hs.709408.

Genome annotation databases

EnsembliENST00000442898; ENSP00000485627; ENSG00000181404.
GeneIDi100287171.
KEGGihsa:100287171.
UCSCiuc010mgm.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK289708 mRNA. Translation: BAF82397.1.
AL928970 Genomic DNA. No translation available.
CCDSiCCDS78375.1.
RefSeqiNP_878908.4. NM_182905.4.
XP_011515963.1. XM_011517661.1.
UniGeneiHs.446466.
Hs.459573.
Hs.461200.
Hs.521961.
Hs.585931.
Hs.709408.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi938833. 9 interactions.
IntActiA8K0Z3. 8 interactions.
STRINGi9606.ENSP00000352498.

PTM databases

iPTMnetiA8K0Z3.
PhosphoSiteiA8K0Z3.

Polymorphism and mutation databases

BioMutaiWASH1.

Proteomic databases

EPDiA8K0Z3.
MaxQBiA8K0Z3.
PaxDbiA8K0Z3.
PeptideAtlasiA8K0Z3.
PRIDEiA8K0Z3.

Protocols and materials databases

DNASUi100287171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000442898; ENSP00000485627; ENSG00000181404.
GeneIDi100287171.
KEGGihsa:100287171.
UCSCiuc010mgm.2. human.

Organism-specific databases

CTDi100287171.
GeneCardsiWASH1.
H-InvDBHIX0034804.
HGNCiHGNC:24361. WASH1.
HPAiHPA002689.
MIMi613632. gene.
neXtProtiNX_A8K0Z3.
PharmGKBiPA162409121.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFZ4. Eukaryota.
ENOG410YN2V. LUCA.
GeneTreeiENSGT00390000016717.
HOVERGENiHBG066686.
InParanoidiA8K0Z3.
KOiK18461.
OMAiPNLKGHA.
PhylomeDBiA8K0Z3.

Miscellaneous databases

ChiTaRSiWASH1. human.
GenomeRNAii100287171.
PROiA8K0Z3.
SOURCEiSearch...

Gene expression databases

CleanExiHS_WASH1.
GenevisibleiA8K0Z3. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: GENE DUPLICATION.
  4. "Human subtelomeric WASH genes encode a new subclass of the WASP family."
    Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E., Parkhurst S.M., Trask B.J.
    PLoS Genet. 3:E237-E237(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE DUPLICATION.
  5. "A FAM21-containing WASH complex regulates retromer-dependent sorting."
    Gomez T.S., Billadeau D.D.
    Dev. Cell 17:699-711(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FAM21C, TUBULIN-BINDING, MUTAGENESIS OF TRP-463.
  6. "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, FUNCTION OF THE WASH COMPLEX, IDENTIFICATION IN THE WASH COMPLEX.
  7. "WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes."
    Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z., Rosen M.K., Billadeau D.D.
    Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE WASH CORE COMPLEX, FUNCTION OF THE WASH CORE COMPLEX.
  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, SUBCELLULAR LOCATION.
  9. "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION AT LYS-220, MUTAGENESIS OF LYS-220.
  10. Cited for: FUNCTION, INTERACTION WITH EXOC1; EXOC4 AND EXOC8, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiWASH1_HUMAN
AccessioniPrimary (citable) accession number: A8K0Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: January 19, 2010
Last modified: July 6, 2016
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

WASH genes duplicated to multiple chromosomal ends during primate evolution, with highest copy number reached in humans, whose WASH repertoires probably vary extensively among individuals (PubMed:18159949). It is therefore difficult to determine which gene is functional or not. The telomeric region of chromosome 9p is paralogous to the pericentromeric regions of chromosome 9 as well as to 2q. Paralogous regions contain 7 transcriptional units. Duplicated WASH genes are also present in the Xq/Yq pseudoautosomal region, as well as on chromosome 1 and 15. The chromosome 16 copy seems to be a pseudogene.1 Publication

Caution

To demonstrate the interaction with FAM21, a FAM21C construct with FAM21A-specific sequence insertions has been used. In human, FAM21 has undergone evolutionary duplication giving rise to highly homologous family members (PubMed:19922874).Curated
The function of the WASH complex is debated. One study using partially purified samples reported a nucleation-promoting factor (NPF) activity (PubMed:19922875). In another study, the reconstituted and highly purified recombinant WASH core complex did not show activity toward Arp2/3 complex suggesting a rather inhibitory role towards WASH NPF activity (PubMed:20498093).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.