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Protein

COMM domain-containing protein 3

Gene

COMMD3

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). Modulates Na+ transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits (PubMed:23637203).1 Publication2 Publications

GO - Biological processi

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

Keywords - Biological processi

Ion transport, Sodium transport, Transcription, Transcription regulation, Transport, Ubl conjugation pathway

Keywords - Ligandi

Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
COMM domain-containing protein 3
Alternative name(s):
Protein Bup
Protein PIL
Gene namesi
Name:COMMD3
Synonyms:BUP, C10orf8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23332. COMMD3.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. 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

PharmGKBiPA134864927.

Polymorphism and mutation databases

BioMutaiCOMMD3.
DMDMi51316114.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195COMM domain-containing protein 3PRO_0000077389Add
BLAST

Proteomic databases

MaxQBiQ9UBI1.
PaxDbiQ9UBI1.
PRIDEiQ9UBI1.

PTM databases

PhosphoSiteiQ9UBI1.

Expressioni

Tissue specificityi

Widely expressed with highest expression in thymus.1 Publication

Gene expression databases

BgeeiQ9UBI1.
CleanExiHS_COMMD3.
ExpressionAtlasiQ9UBI1. baseline and differential.
GenevestigatoriQ9UBI1.

Organism-specific databases

HPAiHPA036584.

Interactioni

Subunit structurei

Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL3, CUL4A, CUL4B, CUL5.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COMMD1Q8N6683EBI-714979,EBI-1550112

Protein-protein interaction databases

BioGridi116984. 24 interactions.
IntActiQ9UBI1. 6 interactions.
STRINGi9606.ENSP00000366032.

Structurei

3D structure databases

ProteinModelPortaliQ9UBI1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 19370COMMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 COMM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG43936.
GeneTreeiENSGT00390000015971.
HOGENOMiHOG000231902.
HOVERGENiHBG051068.
InParanoidiQ9UBI1.
OMAiSQSYPEI.
OrthoDBiEOG779P06.
PhylomeDBiQ9UBI1.
TreeFamiTF329267.

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.

Q9UBI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSESVQKG FQMLADPRSF DSNAFTLLLR AAFQSLLDAQ ADEAVLDHPD
60 70 80 90 100
LKHIDPVVLK HCHAAAATYI LEAGKHRADK STLSTYLEDC KFDRERIELF
110 120 130 140 150
CTEYQNNKNS LEILLGSIGR SLPHITDVSW RLEYQIKTNQ LHRMYRPAYL
160 170 180 190
VTLSVQNTDS PSYPEISFSC SMEQLQDLVG KLKDASKSLE RATQL
Length:195
Mass (Da):22,151
Last modified:May 1, 2000 - v1
Checksum:iAC757941FC17F757
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181R → G.
Corresponds to variant rs11552445 [ dbSNP | Ensembl ].
VAR_061121

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542159 mRNA. Translation: AAS22241.1.
AF201948 mRNA. Translation: AAF17240.1.
AF078848 mRNA. Translation: AAD44480.1.
AL158211 Genomic DNA. Translation: CAI15951.1.
CH471072 Genomic DNA. Translation: EAW86149.1.
CH471072 Genomic DNA. Translation: EAW86155.1.
BC022898 mRNA. Translation: AAH22898.1.
CCDSiCCDS7137.1.
RefSeqiNP_036203.1. NM_012071.3.
UniGeneiHs.534398.

Genome annotation databases

EnsembliENST00000376836; ENSP00000366032; ENSG00000148444.
GeneIDi23412.
KEGGihsa:23412.
UCSCiuc001irf.3. human.

Polymorphism and mutation databases

BioMutaiCOMMD3.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542159 mRNA. Translation: AAS22241.1.
AF201948 mRNA. Translation: AAF17240.1.
AF078848 mRNA. Translation: AAD44480.1.
AL158211 Genomic DNA. Translation: CAI15951.1.
CH471072 Genomic DNA. Translation: EAW86149.1.
CH471072 Genomic DNA. Translation: EAW86155.1.
BC022898 mRNA. Translation: AAH22898.1.
CCDSiCCDS7137.1.
RefSeqiNP_036203.1. NM_012071.3.
UniGeneiHs.534398.

3D structure databases

ProteinModelPortaliQ9UBI1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116984. 24 interactions.
IntActiQ9UBI1. 6 interactions.
STRINGi9606.ENSP00000366032.

PTM databases

PhosphoSiteiQ9UBI1.

Polymorphism and mutation databases

BioMutaiCOMMD3.
DMDMi51316114.

Proteomic databases

MaxQBiQ9UBI1.
PaxDbiQ9UBI1.
PRIDEiQ9UBI1.

Protocols and materials databases

DNASUi23412.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376836; ENSP00000366032; ENSG00000148444.
GeneIDi23412.
KEGGihsa:23412.
UCSCiuc001irf.3. human.

Organism-specific databases

CTDi23412.
GeneCardsiGC10P022604.
HGNCiHGNC:23332. COMMD3.
HPAiHPA036584.
neXtProtiNX_Q9UBI1.
PharmGKBiPA134864927.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43936.
GeneTreeiENSGT00390000015971.
HOGENOMiHOG000231902.
HOVERGENiHBG051068.
InParanoidiQ9UBI1.
OMAiSQSYPEI.
OrthoDBiEOG779P06.
PhylomeDBiQ9UBI1.
TreeFamiTF329267.

Miscellaneous databases

ChiTaRSiCOMMD3. human.
GenomeRNAii23412.
NextBioi45607.
PROiQ9UBI1.

Gene expression databases

BgeeiQ9UBI1.
CleanExiHS_COMMD3.
ExpressionAtlasiQ9UBI1. baseline and differential.
GenevestigatoriQ9UBI1.

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 AND NFKB1, TISSUE SPECIFICITY.
  2. "Novel genes expressed in human dendritic cells."
    Li Y., Li N., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Dendritic cell.
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL3; CUL4A; CUL4B AND CUL5, SUBCELLULAR LOCATION.
  9. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SCNN1B.
  10. Cited for: INTERACTION WITH CCDC22.
  11. Cited for: INTERACTION WITH CCDC93.

Entry informationi

Entry nameiCOMD3_HUMAN
AccessioniPrimary (citable) accession number: Q9UBI1
Secondary accession number(s): D3DRU7, Q5T8Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 99 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 10
    Human chromosome 10: 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.