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Protein

COMM domain-containing protein 6

Gene

COMMD6

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

Functioni

May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF-kappa-B. Inhibits TNF-induced NFKB1 activation.1 Publication2 Publications

GO - Molecular functioni

  • NF-kappaB binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
COMM domain-containing protein 6
Gene namesi
Name:COMMD6
ORF Names:MSTP076
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:24015. COMMD6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241W → A: Does not abolish homodimerization and interaction with COMMD1. Does not abolish repression of TNF-induced NFKB1 activation. Abolishes repression of TNF-induced NFKB1 activation; when associated with A-41. 1 Publication
Mutagenesisi41 – 411P → A: Does not abolish homodimerization and interaction with COMMD1. Does not abolish repression of TNF-induced NFKB1 activation. Abolishes repression of TNF-induced NFKB1 activation; when associated with A-24. 1 Publication

Organism-specific databases

PharmGKBiPA134906013.

Polymorphism and mutation databases

DMDMi51315937.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8585COMM domain-containing protein 6PRO_0000077398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ7Z4G1.
MaxQBiQ7Z4G1.
PRIDEiQ7Z4G1.

PTM databases

iPTMnetiQ7Z4G1.
PhosphoSiteiQ7Z4G1.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in brain, heart, skeletal muscle, lung, pancreas, liver, kidney, small intestine and placenta.2 Publications

Gene expression databases

BgeeiQ7Z4G1.
CleanExiHS_COMMD6.
ExpressionAtlasiQ7Z4G1. baseline and differential.
GenevisibleiQ7Z4G1. HS.

Organism-specific databases

HPAiHPA060266.

Interactioni

Subunit structurei

Homodimer. Can only homodimerize with isoform 1. Interacts directly with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105. Does not interact with NFKBIB. Interacts with CCDC22, CCDC93, SCNN1B, CUL4A.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC22O608267EBI-1550081,EBI-3943153
COMMD1Q8N66812EBI-1550081,EBI-1550112

GO - Molecular functioni

  • NF-kappaB binding Source: MGI

Protein-protein interaction databases

BioGridi128071. 30 interactions.
IntActiQ7Z4G1. 10 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ7Z4G1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 8568COMMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 COMM domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000018369.
HOGENOMiHOG000038017.
HOVERGENiHBG051071.
InParanoidiQ7Z4G1.
OMAiKSQVTNQ.
OrthoDBiEOG757CZR.
PhylomeDBiQ7Z4G1.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q7Z4G1-1) [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
MEASSEPPLD AKSDVTNQLV DFQWKLGMAV SSDTCRSLKY PYVAVMLKVA
60 70 80
DHSGQVKTKC FEMTIPQFQN FYRQFKEIAA VIETV
Length:85
Mass (Da):9,638
Last modified:October 1, 2003 - v1
Checksum:iFBF29F240EA8756B
GO
Isoform 2 (identifier: Q7Z4G1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-69: Q → QPQLLATSSLLSAS

Show »
Length:98
Mass (Da):10,908
Checksum:iBADF400B61D3C3FB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521H → N.
Corresponds to variant rs1063485 [ dbSNP | Ensembl ].
VAR_048813

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 691Q → QPQLLATSSLLSAS in isoform 2. CuratedVSP_026593

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542161 mRNA. Translation: AAS22243.1.
AF169971 mRNA. Translation: AAQ13599.1.
AL137244 Genomic DNA. Translation: CAI12417.1.
AL137244 Genomic DNA. Translation: CAQ09795.1.
BC117391 mRNA. Translation: AAI17392.1.
BC143912 mRNA. Translation: AAI43913.1.
BC171758 mRNA. Translation: AAI71758.1.
CCDSiCCDS9451.1. [Q7Z4G1-1]
CCDS9452.1. [Q7Z4G1-2]
RefSeqiNP_987091.1. NM_203495.3. [Q7Z4G1-1]
NP_987093.1. NM_203497.3. [Q7Z4G1-2]
UniGeneiHs.508266.
Hs.713055.

Genome annotation databases

EnsembliENST00000355801; ENSP00000348054; ENSG00000188243. [Q7Z4G1-2]
ENST00000377615; ENSP00000366841; ENSG00000188243. [Q7Z4G1-1]
ENST00000406936; ENSP00000385660; ENSG00000188243. [Q7Z4G1-1]
GeneIDi170622.
UCSCiuc001vjn.3. human. [Q7Z4G1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542161 mRNA. Translation: AAS22243.1.
AF169971 mRNA. Translation: AAQ13599.1.
AL137244 Genomic DNA. Translation: CAI12417.1.
AL137244 Genomic DNA. Translation: CAQ09795.1.
BC117391 mRNA. Translation: AAI17392.1.
BC143912 mRNA. Translation: AAI43913.1.
BC171758 mRNA. Translation: AAI71758.1.
CCDSiCCDS9451.1. [Q7Z4G1-1]
CCDS9452.1. [Q7Z4G1-2]
RefSeqiNP_987091.1. NM_203495.3. [Q7Z4G1-1]
NP_987093.1. NM_203497.3. [Q7Z4G1-2]
UniGeneiHs.508266.
Hs.713055.

3D structure databases

ProteinModelPortaliQ7Z4G1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128071. 30 interactions.
IntActiQ7Z4G1. 10 interactions.

PTM databases

iPTMnetiQ7Z4G1.
PhosphoSiteiQ7Z4G1.

Polymorphism and mutation databases

DMDMi51315937.

Proteomic databases

EPDiQ7Z4G1.
MaxQBiQ7Z4G1.
PRIDEiQ7Z4G1.

Protocols and materials databases

DNASUi170622.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355801; ENSP00000348054; ENSG00000188243. [Q7Z4G1-2]
ENST00000377615; ENSP00000366841; ENSG00000188243. [Q7Z4G1-1]
ENST00000406936; ENSP00000385660; ENSG00000188243. [Q7Z4G1-1]
GeneIDi170622.
UCSCiuc001vjn.3. human. [Q7Z4G1-1]

Organism-specific databases

CTDi170622.
GeneCardsiCOMMD6.
HGNCiHGNC:24015. COMMD6.
HPAiHPA060266.
MIMi612377. gene.
neXtProtiNX_Q7Z4G1.
PharmGKBiPA134906013.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000018369.
HOGENOMiHOG000038017.
HOVERGENiHBG051071.
InParanoidiQ7Z4G1.
OMAiKSQVTNQ.
OrthoDBiEOG757CZR.
PhylomeDBiQ7Z4G1.

Miscellaneous databases

ChiTaRSiCOMMD6. human.
GenomeRNAii170622.
NextBioi89064.
PROiQ7Z4G1.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z4G1.
CleanExiHS_COMMD6.
ExpressionAtlasiQ7Z4G1. baseline and differential.
GenevisibleiQ7Z4G1. HS.

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] (ISOFORM 1), FUNCTION, INTERACTION WITH COMMD1; RELA; RELB AND NFKB1, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [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).
    Tissue: Brain.
  5. "Characterization of COMMD protein-protein interactions in NF-kappaB signalling."
    de Bie P., van de Sluis B., Burstein E., Duran K.J., Berger R., Duckett C.S., Wijmenga C., Klomp L.W.
    Biochem. J. 398:63-71(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COMMD1, SUBUNIT, MUTAGENESIS OF TRP-24 AND PRO-41, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORM 2).
  6. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 CUL4A, 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: INTERACTION WITH SCNN1B.
  10. Cited for: INTERACTION WITH CCDC22.
  11. Cited for: INTERACTION WITH CCDC93.

Entry informationi

Entry nameiCOMD6_HUMAN
AccessioniPrimary (citable) accession number: Q7Z4G1
Secondary accession number(s): A6NF28, B7ZLN0, Q5TBK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: April 13, 2016
This is version 102 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 13
    Human chromosome 13: 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

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.