Q9NQA3 (WASH6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
WAS protein family homolog 6

Alternative name(s):
Protein FAM39A

Gene names

Name:	WASH6P
Synonyms:	CXYorf1, FAM39A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Subunit structure	Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Interacts (via WHD1 region) with FAM21C; the interaction is direct By similarity.
Subcellular location	Early endosome membrane By similarity. Recycling endosome membrane By similarity. Note: Localization to the endodome membrane is mediated via its interaction with FAM21 By similarity.
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 (Ref.4). It is therefore difficult to determine which gene is functional or not. The gene encoding for this protein is located in the pseudoautosomal region 2 (PAR2) of X and Y chromosomes.
Sequence similarities	Belongs to the WASH1 family. Contains 1 WH2 domain.
Sequence caution	The sequence CAB96818.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transport
Cellular component	Endosome Membrane
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Arp2/3 complex-mediated actin nucleation Inferred from sequence or structural similarity. Source: UniProtKB retrograde transport, endosome to Golgi Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	WASH complex Inferred from sequence or structural similarity. Source: UniProtKB early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW alpha-tubulin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	WAS protein family homolog 6		PRO_0000344530
Regions
	Domain	343 – 365	23	WH2
	Region	1 – 149	149	WHD1
	Compositional bias	250 – 312	63	Pro-rich
Amino acid modifications
	Modified residue	327	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9NQA3 [UniParc]. Last modified January 19, 2010. Version 3. Checksum: 7B1217DC3CF9DDAA	FASTA	447	47,990
	10 20 30 40 50 60 MAFHEMQAHK NALGTSGEQQ AADITGPTPH QGGWKQVEQS RSQVQAIGEK VSLAQAKIEK 70 80 90 100 110 120 IKGSKKAIKV FSSAKYPAPE RLQEYGSIFT GAQDPGLQRR PRHRIQSKHR PLDERALQEK 130 140 150 160 170 180 LKDFPVCVST KPEPEDDAEE GLGGLPSNIS SVSSLLLFNT TENLYKKYVF LDPLAGAVTK 190 200 210 220 230 240 THVMLGAETE EKLFDAPLSI SKREQLEQQV PENYFYVPDL GQVPEIDVPS YLPDLPSIAN 250 260 270 280 290 300 DLMYSADLGP GIAPSAPGTI PELPTFHTEV AEPLKADLQD GVLTPPPPPP PPPPAPEVLA 310 320 330 340 350 360 SAPPLPPSTA APVGQGARQD DGSSSASPSV QGAPREVVDP SGGWATLLES IRQAGGIGKA 370 380 390 400 410 420 KLRSMKERKL EKKKQKEQEQ VRATSQGGHL MSDLFNKLVM RRKGISGKGP GAGEGPGGAF 430 440 ARVSDSIPPV PPPQQPQAEE DEDDWES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differentially regulated and evolved genes in the fully sequenced Xq/Yq pseudoautosomal region." Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F., Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A., Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S., Mercadante G., Pannone E., Archidiacono N. , Rocchi M., Schlessinger D., D'Urso M. Hum. Mol. Genet. 9:395-401(2000) [PubMed: 10655549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE DUPLICATION.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-447. Tissue: Placenta.
[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: 18159949] [Abstract] Cited for: GENE DUPLICATION.
[5]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ271736 Genomic DNA. Translation: CAB96818.1. Sequence problems. CR595583 mRNA. No translation available.
IPI	IPI00641177.
UniGene	Hs.446466.
3D structure databases
ProteinModelPortal	Q9NQA3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NQA3.
PTM databases
PhosphoSite	Q9NQA3.
Polymorphism databases
DMDM	284018158.
Proteomic databases
PRIDE	Q9NQA3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000285718; ENSP00000285718; ENSG00000182484. ENST00000359512; ENSP00000352498; ENSG00000182484.
Organism-specific databases
GeneCards	GC0XP155250.
H-InvDB	HIX0176556. HIX0177643.
HGNC	HGNC:31685. WASH6P.
HPA	HPA002689.
neXtProt	NX_Q9NQA3.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06658.
GeneTree	ENSGT00390000016717.
HOVERGEN	HBG066686.
InParanoid	Q9NQA3.
OrthoDB	EOG4J9N04.
Gene expression databases
Bgee	Q9NQA3.
Genevestigator	Q9NQA3.
Family and domain databases
InterPro	IPR021854. WASH_WASH. [Graphical view]
Pfam	PF11945. DUF3462. 1 hit. [Graphical view]
PROSITE	PS51082. WH2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

WASH6_HUMAN

Accession

Primary (citable) accession number: Q9NQA3
Secondary accession number(s): A6NGF1, Q8N305

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	January 19, 2010
Last modified:	January 25, 2012
This is version 50 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.