Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

WASH complex subunit 7

Gene

KIAA1033

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

Functioni

Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes sems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in the regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093).1 PublicationBy similarity2 Publications

GO - Biological processi

  • endosomal transport Source: UniProtKB
  • endosome organization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
WASH complex subunit 7Curated
Alternative name(s):
Strumpellin and WASH-interacting protein1 Publication
Short name:
SWIP1 Publication
Gene namesi
Name:KIAA1033Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29174. KIAA1033.

Subcellular locationi

GO - Cellular componenti

  • early endosome Source: UniProtKB-SubCell
  • endosome Source: MGI
  • nucleoplasm Source: HPA
  • WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 43 (MRT43)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:615817
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1019 – 10191P → R in MRT43; reduced expression of the protein; alters the WASH complex. 1 Publication
VAR_071384

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiKIAA1033.
MIMi615817. phenotype.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA128394626.

Polymorphism and mutation databases

BioMutaiKIAA1033.
DMDMi296452861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 11731172WASH complex subunit 7PRO_0000282575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei7 – 71PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ2M389.
MaxQBiQ2M389.
PaxDbiQ2M389.
PRIDEiQ2M389.

PTM databases

iPTMnetiQ2M389.
PhosphoSiteiQ2M389.

Expressioni

Gene expression databases

BgeeiQ2M389.
CleanExiHS_KIAA1033.
ExpressionAtlasiQ2M389. baseline and differential.
GenevisibleiQ2M389. HS.

Organism-specific databases

HPAiHPA045666.
HPA046737.

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.1 Publication2 Publications

Protein-protein interaction databases

BioGridi116913. 32 interactions.
IntActiQ2M389. 9 interactions.
MINTiMINT-1198616.
STRINGi9606.ENSP00000328062.

Structurei

3D structure databases

ProteinModelPortaliQ2M389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni705 – 1173469Sufficient for interaction with KIAA01961 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1135 – 116127Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the WASHS7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3578. Eukaryota.
ENOG410XRKB. LUCA.
GeneTreeiENSGT00390000002524.
HOVERGENiHBG106578.
InParanoidiQ2M389.
KOiK18465.
OrthoDBiEOG70087B.
PhylomeDBiQ2M389.
TreeFamiTF324604.

Family and domain databases

InterProiIPR028283. WASH-7_C.
IPR028282. WASH-7_central.
IPR028191. WASH-7_N.
IPR027307. WASH7.
[Graphical view]
PANTHERiPTHR31409:SF0. PTHR31409:SF0. 1 hit.
PfamiPF14746. WASH-7_C. 1 hit.
PF14744. WASH-7_mid. 1 hit.
PF14745. WASH-7_N. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2M389-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVETLSPDW EFDRVDDGSQ KIHAEVQLKN YGKFLEEYTS QLRRIEDALD
60 70 80 90 100
DSIGDVWDFN LDPIALKLLP YEQSSLLELI KTENKVLNKV ITVYAALCCE
110 120 130 140 150
IKKLKYEAET KFYNGLLFYG EGATDASMVE GDCQIQMGRF ISFLQELSCF
160 170 180 190 200
VTRCYEVVMN VVHQLAALYI SNKIAPKIIE TTGVHFQTMY EHLGELLTVL
210 220 230 240 250
LTLDEIIDNH ITLKDHWTMY KRLLKSVHHN PSKFGIQEEK LKPFEKFLLK
260 270 280 290 300
LEGQLLDGMI FQACIEQQFD SLNGGVSVSK NSTFAEEFAH SIRSIFANVE
310 320 330 340 350
AKLGEPSEID QRDKYVGICG LFVLHFQIFR TIDKKFYKSL LDICKKVPAI
360 370 380 390 400
TLTANIIWFP DNFLIQKIPA AAKLLDRKSL QAIKIHRDTF LQQKAQSLTK
410 420 430 440 450
DVQSYYVFVS SWMMKMESIL SKEQRMDKFA EDLTNRCNVF IQGFLYAYSI
460 470 480 490 500
STIIKTTMNL YMSMQKPMTK TSVKALCRLV ELLKAIEHMF YRRSMVVADS
510 520 530 540 550
VSHITQHLQH QALHSISVAK KRVISDKKYS EQRLDVLSAL VLAENTLNGP
560 570 580 590 600
STKQRRLIVS LALSVGTQMK TFKDEELFPL QVVMKKLDLI SELRERVQTQ
610 620 630 640 650
CDCCFLYWHR AVFPIYLDDV YENAVDAARL HYMFSALRDC VPAMMHARHL
660 670 680 690 700
ESYEILLDCY DKEIMEILNE HLLDKLCKEI EKDLRLSVHT HLKLDDRNPF
710 720 730 740 750
KVGMKDLALF FSLNPIRFFN RFIDIRAYVT HYLDKTFYNL TTVALHDWAT
760 770 780 790 800
YSEMRNLATQ RYGLVMTEAH LPSQTLEQGL DVLEIMRNIH IFVSRYLYNL
810 820 830 840 850
NNQIFIERTS NNKHLNTINI RHIANSIRTH GTGIMNTTVN FTYQFLKKKF
860 870 880 890 900
YIFSQFMYDE HIKSRLIKDI RFFREIKDQN DHKYPFDRAE KFNRGIRKLG
910 920 930 940 950
VTPEGQSYLD QFRQLISQIG NAMGYVRMIR SGGLHCSSNA IRFVPDLEDI
960 970 980 990 1000
VNFEELVKEE GLAEETLKAA RHLDSVLSDH TRNSAEGTEY FKMLVDVFAP
1010 1020 1030 1040 1050
EFRRPKNIHL RNFYIIVPPL TLNFVEHSIS CKEKLNKKNK IGAAFTDDGF
1060 1070 1080 1090 1100
AMGVAYILKL LDQYREFDSL HWFQSVREKY LKEIRAVAKQ QNVQSASQDE
1110 1120 1130 1140 1150
KLLQTMNLTQ KRLDVYLQEF ELLYFSLSSA RIFFRADKTA AEENQEKKEK
1160 1170
EEETKTSNGD LSDSTVSADP VVK
Length:1,173
Mass (Da):136,403
Last modified:May 18, 2010 - v2
Checksum:iFD073D5F21127DED
GO
Isoform 2 (identifier: Q2M389-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     839-851: VNFTYQFLKKKFY → KWAFTAWRGGPRL
     852-1173: Missing.

Show »
Length:851
Mass (Da):98,765
Checksum:iD68E00F5406CC64D
GO

Sequence cautioni

The sequence AAI10851.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA82985.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2931R → Q in BAA91816 (PubMed:14702039).Curated
Sequence conflicti608 – 6081W → R in BAA91816 (PubMed:14702039).Curated
Sequence conflicti759 – 7591T → A in BAA91816 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti323 – 3231V → L.
Corresponds to variant rs34434425 [ dbSNP | Ensembl ].
VAR_031417
Natural varianti599 – 5991T → S.
Corresponds to variant rs1345092 [ dbSNP | Ensembl ].
VAR_057825
Natural varianti901 – 9011V → I.Combined sources2 Publications
Corresponds to variant rs1663564 [ dbSNP | Ensembl ].
VAR_031418
Natural varianti1019 – 10191P → R in MRT43; reduced expression of the protein; alters the WASH complex. 1 Publication
VAR_071384

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei839 – 85113VNFTY…KKKFY → KWAFTAWRGGPRL in isoform 2. 1 PublicationVSP_024208Add
BLAST
Alternative sequencei852 – 1173322Missing in isoform 2. 1 PublicationVSP_024209Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028956 mRNA. Translation: BAA82985.1. Different initiation.
AK001657 mRNA. Translation: BAA91816.1.
BC031358 mRNA. Translation: AAH31358.1.
AC016257 Genomic DNA. No translation available.
BC040936 mRNA. Translation: AAH40936.1.
BC104992 mRNA. Translation: AAI04993.1.
BC104994 mRNA. Translation: AAI04995.1.
BC110850 mRNA. Translation: AAI10851.1. Sequence problems.
CCDSiCCDS41826.1. [Q2M389-1]
RefSeqiNP_001280569.1. NM_001293640.1.
NP_056090.1. NM_015275.2. [Q2M389-1]
UniGeneiHs.12144.

Genome annotation databases

EnsembliENST00000332180; ENSP00000328062; ENSG00000136051. [Q2M389-1]
GeneIDi23325.
KEGGihsa:23325.
UCSCiuc001tld.4. human. [Q2M389-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028956 mRNA. Translation: BAA82985.1. Different initiation.
AK001657 mRNA. Translation: BAA91816.1.
BC031358 mRNA. Translation: AAH31358.1.
AC016257 Genomic DNA. No translation available.
BC040936 mRNA. Translation: AAH40936.1.
BC104992 mRNA. Translation: AAI04993.1.
BC104994 mRNA. Translation: AAI04995.1.
BC110850 mRNA. Translation: AAI10851.1. Sequence problems.
CCDSiCCDS41826.1. [Q2M389-1]
RefSeqiNP_001280569.1. NM_001293640.1.
NP_056090.1. NM_015275.2. [Q2M389-1]
UniGeneiHs.12144.

3D structure databases

ProteinModelPortaliQ2M389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116913. 32 interactions.
IntActiQ2M389. 9 interactions.
MINTiMINT-1198616.
STRINGi9606.ENSP00000328062.

PTM databases

iPTMnetiQ2M389.
PhosphoSiteiQ2M389.

Polymorphism and mutation databases

BioMutaiKIAA1033.
DMDMi296452861.

Proteomic databases

EPDiQ2M389.
MaxQBiQ2M389.
PaxDbiQ2M389.
PRIDEiQ2M389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332180; ENSP00000328062; ENSG00000136051. [Q2M389-1]
GeneIDi23325.
KEGGihsa:23325.
UCSCiuc001tld.4. human. [Q2M389-1]

Organism-specific databases

CTDi23325.
GeneCardsiKIAA1033.
H-InvDBHIX0010947.
HGNCiHGNC:29174. KIAA1033.
HPAiHPA045666.
HPA046737.
MalaCardsiKIAA1033.
MIMi615748. gene.
615817. phenotype.
neXtProtiNX_Q2M389.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA128394626.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3578. Eukaryota.
ENOG410XRKB. LUCA.
GeneTreeiENSGT00390000002524.
HOVERGENiHBG106578.
InParanoidiQ2M389.
KOiK18465.
OrthoDBiEOG70087B.
PhylomeDBiQ2M389.
TreeFamiTF324604.

Miscellaneous databases

ChiTaRSiKIAA1033. human.
GenomeRNAii23325.
PROiQ2M389.
SOURCEiSearch...

Gene expression databases

BgeeiQ2M389.
CleanExiHS_KIAA1033.
ExpressionAtlasiQ2M389. baseline and differential.
GenevisibleiQ2M389. HS.

Family and domain databases

InterProiIPR028283. WASH-7_C.
IPR028282. WASH-7_central.
IPR028191. WASH-7_N.
IPR027307. WASH7.
[Graphical view]
PANTHERiPTHR31409:SF0. PTHR31409:SF0. 1 hit.
PfamiPF14746. WASH-7_C. 1 hit.
PF14744. WASH-7_mid. 1 hit.
PF14745. WASH-7_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-901.
    Tissue: Brain.
  2. "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] (ISOFORM 2).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1), VARIANT ILE-901.
    Tissue: Cervix, Heart, Lung, Placenta and Testis.
  5. "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 OF THE WASH COMPLEX, IDENTIFICATION IN THE WASH COMPLEX.
  6. "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: IDENTIFICATION IN THE WASH CORE COMPLEX, FUNCTION OF THE WASH CORE COMPLEX, INTERACTION WITH KIAA0196.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Identification of a novel candidate gene for non-syndromic autosomal recessive intellectual disability: the WASH complex member SWIP."
    Ropers F., Derivery E., Hu H., Garshasbi M., Karbasiyan M., Herold M., Nurnberg G., Ullmann R., Gautreau A., Sperling K., Varon R., Rajab A.
    Hum. Mol. Genet. 20:2585-2590(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE WASH COMPLEX, INVOLVEMENT IN MRT43, VARIANT MRT43 ARG-1019, CHARACTERIZATION OF VARIANT MRT43 ARG-1019.
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIalpha."
    Ryder P.V., Vistein R., Gokhale A., Seaman M.N., Puthenveedu M.A., Faundez V.
    Mol. Biol. Cell 24:2269-2284(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-901, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWASH7_HUMAN
AccessioniPrimary (citable) accession number: Q2M389
Secondary accession number(s): Q2NL83
, Q8IW61, Q8N5W7, Q9NVD6, Q9UPW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 82 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

Caution

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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families
  6. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.