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Protein

WASH complex subunit CCDC53

Gene

CCDC53

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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 seems 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 regulation of the fission of tubules that serve as transport intermediates during endosome sorting (PubMed:19922875, PubMed:20498093).2 Publications

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
WASH complex subunit CCDC53
Alternative name(s):
Coiled-coil domain-containing protein 53
Gene namesi
Name:CCDC53
ORF Names:AD-016, CGI-116, x0009
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:24256. CCDC53.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. intracellular membrane-bounded organelle Source: HPA
  3. WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672169.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194WASH complex subunit CCDC53PRO_0000076201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y3C0.
PaxDbiQ9Y3C0.
PRIDEiQ9Y3C0.

PTM databases

PhosphoSiteiQ9Y3C0.

Expressioni

Gene expression databases

BgeeiQ9Y3C0.
CleanExiHS_CCDC53.
ExpressionAtlasiQ9Y3C0. baseline and differential.
GenevestigatoriQ9Y3C0.

Organism-specific databases

HPAiHPA038338.
HPA038339.

Interactioni

Subunit structurei

Component of the WASH core complex also described as WASH regulatory complex (SHRC) composed of WASH (WASH1, WASH2P or WASH3P), FAM21, 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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCRS1Q96EZ83EBI-712969,EBI-348259
PBXIP1Q96AQ63EBI-712969,EBI-740845

Protein-protein interaction databases

BioGridi119225. 34 interactions.
IntActiQ9Y3C0. 21 interactions.
MINTiMINT-1369211.
STRINGi9606.ENSP00000240079.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3C0.
SMRiQ9Y3C0. Positions 15-67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili46 – 7429Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the CCDC53 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG261899.
GeneTreeiENSGT00390000014084.
HOGENOMiHOG000006526.
HOVERGENiHBG009789.
InParanoidiQ9Y3C0.
KOiK18463.
OMAiHTVRFLN.
PhylomeDBiQ9Y3C0.
TreeFamiTF318955.

Family and domain databases

InterProiIPR019309. WASH_CCDC53.
[Graphical view]
PfamiPF10152. DUF2360. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y3C0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDEDGLPLMG SGIDLTKVPA IQQKRTVAFL NQFVVHTVQF LNRFSTVCEE
60 70 80 90 100
KLADLSLRIQ QIETTLNILD AKLSSIPGLD DVTVEVSPLN VTSVTNGAHP
110 120 130 140 150
EATSEQPQQN STQDSGLQES EVSAENILTV AKDPRYARYL KMVQVGVPVM
160 170 180 190
AIRNKMISEG LDPDLLERPD APVPDGESEK TVEESSDSES SFSD
Length:194
Mass (Da):21,173
Last modified:November 1, 1999 - v1
Checksum:iB0CCF1AE76CDA6D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811D → G in BAD97059. 1 PublicationCurated
Sequence conflicti110 – 1101N → S in AAH10889. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155655 mRNA. Translation: AAF67012.1.
AF151874 mRNA. Translation: AAD34111.1.
CR457171 mRNA. Translation: CAG33452.1.
AK223339 mRNA. Translation: BAD97059.1.
AK314970 mRNA. Translation: BAG37471.1.
CH471054 Genomic DNA. Translation: EAW97687.1.
BC010889 mRNA. Translation: AAH10889.1.
CCDSiCCDS44959.1.
RefSeqiNP_057137.1. NM_016053.3.
UniGeneiHs.405692.

Genome annotation databases

EnsembliENST00000240079; ENSP00000240079; ENSG00000120860.
GeneIDi51019.
KEGGihsa:51019.
UCSCiuc010svw.2. human.

Polymorphism databases

DMDMi6831732.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155655 mRNA. Translation: AAF67012.1.
AF151874 mRNA. Translation: AAD34111.1.
CR457171 mRNA. Translation: CAG33452.1.
AK223339 mRNA. Translation: BAD97059.1.
AK314970 mRNA. Translation: BAG37471.1.
CH471054 Genomic DNA. Translation: EAW97687.1.
BC010889 mRNA. Translation: AAH10889.1.
CCDSiCCDS44959.1.
RefSeqiNP_057137.1. NM_016053.3.
UniGeneiHs.405692.

3D structure databases

ProteinModelPortaliQ9Y3C0.
SMRiQ9Y3C0. Positions 15-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119225. 34 interactions.
IntActiQ9Y3C0. 21 interactions.
MINTiMINT-1369211.
STRINGi9606.ENSP00000240079.

PTM databases

PhosphoSiteiQ9Y3C0.

Polymorphism databases

DMDMi6831732.

Proteomic databases

MaxQBiQ9Y3C0.
PaxDbiQ9Y3C0.
PRIDEiQ9Y3C0.

Protocols and materials databases

DNASUi51019.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000240079; ENSP00000240079; ENSG00000120860.
GeneIDi51019.
KEGGihsa:51019.
UCSCiuc010svw.2. human.

Organism-specific databases

CTDi51019.
GeneCardsiGC12M102406.
HGNCiHGNC:24256. CCDC53.
HPAiHPA038338.
HPA038339.
neXtProtiNX_Q9Y3C0.
PharmGKBiPA142672169.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG261899.
GeneTreeiENSGT00390000014084.
HOGENOMiHOG000006526.
HOVERGENiHBG009789.
InParanoidiQ9Y3C0.
KOiK18463.
OMAiHTVRFLN.
PhylomeDBiQ9Y3C0.
TreeFamiTF318955.

Miscellaneous databases

ChiTaRSiCCDC53. human.
GeneWikiiCCDC53.
GenomeRNAii51019.
NextBioi53536.
PROiQ9Y3C0.

Gene expression databases

BgeeiQ9Y3C0.
CleanExiHS_CCDC53.
ExpressionAtlasiQ9Y3C0. baseline and differential.
GenevestigatoriQ9Y3C0.

Family and domain databases

InterProiIPR019309. WASH_CCDC53.
[Graphical view]
PfamiPF10152. DUF2360. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adrenal gland.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: Placenta.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Prostate.
  8. "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.
  9. "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.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCCD53_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3C0
Secondary accession number(s): B2RC74
, Q53FF0, Q6IAI4, Q96QK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: February 4, 2015
This is version 100 of the entry and version 1 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).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.