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Protein

COMM domain-containing protein 10

Gene

COMMD10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-kappa-B (PubMed:15799966).1 Publication1 Publication

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
COMM domain-containing protein 10
Gene namesi
Name:COMMD10
ORF Names:HSPC305, PTD002
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:30201. COMMD10.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134862606.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 202201COMM domain-containing protein 10PRO_0000077405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei155 – 1551Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y6G5.
PaxDbiQ9Y6G5.
PRIDEiQ9Y6G5.

PTM databases

PhosphoSiteiQ9Y6G5.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9Y6G5.
CleanExiHS_COMMD10.
ExpressionAtlasiQ9Y6G5. baseline and differential.
GenevestigatoriQ9Y6G5.

Organism-specific databases

HPAiHPA045441.

Interactioni

Subunit structurei

Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105, NFKB2/p100. Interacts with CCDC22, CCDC93, SCNN1B, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL7.5 Publications

Protein-protein interaction databases

BioGridi119521. 11 interactions.
IntActiQ9Y6G5. 5 interactions.
STRINGi9606.ENSP00000274458.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6G5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 20270COMMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 COMM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG78491.
GeneTreeiENSGT00390000001500.
HOGENOMiHOG000253918.
HOVERGENiHBG051075.
InParanoidiQ9Y6G5.
OMAiVNTWSSM.
OrthoDBiEOG7DRJ48.
PhylomeDBiQ9Y6G5.
TreeFamiTF352584.

Family and domain databases

InterProiIPR017920. COMM.
IPR009886. HCaRG.
[Graphical view]
PfamiPF07258. HCaRG. 1 hit.
[Graphical view]
PROSITEiPS51269. COMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Y6G5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPAALILR ESPSMKKAVS LINAIDTGRF PRLLTRILQK LHLKAESSFS
60 70 80 90 100
EEEEEKLQAA FSLEKQDLHL VLETISFILE QAVYHNVKPA ALQQQLENIH
110 120 130 140 150
LRQDKAEAFV NTWSSMGQET VEKFRQRILA PCKLETVGWQ LNLQMAHSAQ
160 170 180 190 200
AKLKSPQAVL QLGVNNEDSK SLEKVLVEFS HKELFDFYNK LETIQAQLDS

LT
Length:202
Mass (Da):22,966
Last modified:November 1, 1999 - v1
Checksum:i4D3C014FE59188CB
GO

Sequence cautioni

The sequence AAF28983.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281I → S.
Corresponds to variant rs1129495 [ dbSNP | Ensembl ].
VAR_061122

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542165 mRNA. Translation: AAS22247.1.
AF078857 mRNA. Translation: AAD44489.1.
AF161423 mRNA. Translation: AAF28983.1. Different initiation.
AK002147 mRNA. Translation: BAA92108.1.
CH471086 Genomic DNA. Translation: EAW48941.1.
CH471086 Genomic DNA. Translation: EAW48942.1.
BC005179 mRNA. Translation: AAH05179.1.
CCDSiCCDS34215.1.
RefSeqiNP_057228.1. NM_016144.2.
UniGeneiHs.483136.

Genome annotation databases

EnsembliENST00000274458; ENSP00000274458; ENSG00000145781.
GeneIDi51397.
KEGGihsa:51397.
UCSCiuc003krt.1. human.

Polymorphism databases

DMDMi51316122.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542165 mRNA. Translation: AAS22247.1.
AF078857 mRNA. Translation: AAD44489.1.
AF161423 mRNA. Translation: AAF28983.1. Different initiation.
AK002147 mRNA. Translation: BAA92108.1.
CH471086 Genomic DNA. Translation: EAW48941.1.
CH471086 Genomic DNA. Translation: EAW48942.1.
BC005179 mRNA. Translation: AAH05179.1.
CCDSiCCDS34215.1.
RefSeqiNP_057228.1. NM_016144.2.
UniGeneiHs.483136.

3D structure databases

ProteinModelPortaliQ9Y6G5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119521. 11 interactions.
IntActiQ9Y6G5. 5 interactions.
STRINGi9606.ENSP00000274458.

PTM databases

PhosphoSiteiQ9Y6G5.

Polymorphism databases

DMDMi51316122.

Proteomic databases

MaxQBiQ9Y6G5.
PaxDbiQ9Y6G5.
PRIDEiQ9Y6G5.

Protocols and materials databases

DNASUi51397.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274458; ENSP00000274458; ENSG00000145781.
GeneIDi51397.
KEGGihsa:51397.
UCSCiuc003krt.1. human.

Organism-specific databases

CTDi51397.
GeneCardsiGC05P115448.
HGNCiHGNC:30201. COMMD10.
HPAiHPA045441.
neXtProtiNX_Q9Y6G5.
PharmGKBiPA134862606.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG78491.
GeneTreeiENSGT00390000001500.
HOGENOMiHOG000253918.
HOVERGENiHBG051075.
InParanoidiQ9Y6G5.
OMAiVNTWSSM.
OrthoDBiEOG7DRJ48.
PhylomeDBiQ9Y6G5.
TreeFamiTF352584.

Miscellaneous databases

GenomeRNAii51397.
NextBioi54929.
PROiQ9Y6G5.

Gene expression databases

BgeeiQ9Y6G5.
CleanExiHS_COMMD10.
ExpressionAtlasiQ9Y6G5. baseline and differential.
GenevestigatoriQ9Y6G5.

Family and domain databases

InterProiIPR017920. COMM.
IPR009886. HCaRG.
[Graphical view]
PfamiPF07258. HCaRG. 1 hit.
[Graphical view]
PROSITEiPS51269. COMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH COMMD1; RELA; RELB; NFKB1 AND NFKB2, TISSUE SPECIFICITY.
  2. Fu G., Huang Q., Song H., Peng J., Zhang Q., Mao M., Dai M., Mao Y., Zhou J., Chen Z., Chen J.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary tumor.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Urinary bladder.
  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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding."
    Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N., Burstein E.
    J. Biol. Chem. 286:32355-32365(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4B AND CUL7, SUBCELLULAR LOCATION.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Functional interaction of COMMD3 and COMMD9 with the epithelial sodium channel."
    Liu Y.F., Swart M., Ke Y., Ly K., McDonald F.J.
    Am. J. Physiol. 305:F80-F89(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCNN1B.
  12. Cited for: INTERACTION WITH CCDC22.
  13. Cited for: INTERACTION WITH CCDC93.

Entry informationi

Entry nameiCOMDA_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6G5
Secondary accession number(s): D3DT07, Q9P077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1999
Last modified: April 1, 2015
This is version 95 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. 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.