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Q8N668 (COMD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
COMM domain-containing protein 1
Alternative name(s):
Protein Murr1
Gene names
Name:COMMD1
Synonyms:C2orf5, MURR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15

Subunit structure

Monomer and homodimer. Interacts (via COMM domain) with COMMD2, COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8 and COMMD10 (via COMM domain). Identified in a complex with an E3 ubiquitin ligase complex composed of TCEB1/elongin C, CUL2, SOCS1 and RBX1. Interacts directly with SOCS1 and CUL2. Interacts directly the N-terminal region of ATP7B. Interacts with CCS, CDKN2A, RELA and NFKBIB. Identified in a complex with NF-kappa-B. Interacts with CLU. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Ref.8 Ref.9 Ref.12 Ref.16

Tissue specificity

Ubiquitous. Highest expression in the liver, with lower expression in brain, lung, placenta, pancreas, small intestine, heart, skeletal muscle, kidney and placenta. Ref.5 Ref.8 Ref.9

Post-translational modification

Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal degradation. Ref.7 Ref.12 Ref.16

Sequence similarities

Contains 1 COMM domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 190189COMM domain-containing protein 1
PRO_0000077384

Regions

Domain118 – 18669COMM

Sites

Metal binding1011Copper Potential
Metal binding1101Copper Potential
Metal binding1341Copper Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.13

Experimental info

Mutagenesis1101M → A: Reduces copper-induced fluorescence change. Ref.10
Mutagenesis1341H → A: Reduces copper-induced fluorescence change. Ref.10

Secondary structure

.............................. 190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8N668 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 9C810AECA67011DC

FASTA19021,178
        10         20         30         40         50         60 
MAAGELEGGK PLSGLLNALA QDTFHGYPGI TEELLRSQLY PEVPPEEFRP FLAKMRGILK 

        70         80         90        100        110        120 
SIASADMDFN QLEAFLTAQT KKQGGITSDQ AAVISKFWKS HKTKIRESLM NQSRWNSGLR 

       130        140        150        160        170        180 
GLSWRVDGKS QSRHSAQIHT PVAIIELELG KYGQESEFLC LEFDEVKVNQ ILKTLSEVEE 

       190 
SISTLISQPN 

« Hide

References

« Hide 'large scale' references
[1]"The canine copper toxicosis gene MURR1 does not cause non-Wilsonian hepatic copper toxicosis."
Mueller T., van de Sluis B.A.J., Zhernakova A., van Binsbergen E., Janecke A.R., Bavdekar A., Pandit A., Weirich-Schwaiger H., Witt H., Ellemunter H., Deutsch J., Denk H., Mueller W., Sternlieb I., Tanner M.S., Wijmenga C.
J. Hepatol. 38:164-168(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Analysis of the human homologue of the canine copper toxicosis gene MURR1 in Wilson disease patients."
Stuehler B., Reichert J., Stremmel W., Schaefer M.
J. Mol. Med. 82:629-634(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Comparative analyses of gene imprinting and CpG island methylation around mouse Murr1 and human syntenic region identify the 5'-portion of U2af1-rs1 CpG island as an imprinting control region."
Zhang Z., Yatsuki H., Wang Y., Joh K., Nabetani A., Hatada I., Soejima H., Iwasaka T., Mukai T.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[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].
Tissue: Ovary and Skin.
[5]"Identification of a new copper metabolism gene by positional cloning in a purebred dog population."
van De Sluis B.A.J., Rothuizen J., Pearson P.L., van Oost B.A., Wijmenga C.
Hum. Mol. Genet. 11:165-173(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein."
Tao T.Y., Liu F., Klomp L., Wijmenga C., Gitlin J.D.
J. Biol. Chem. 278:41593-41596(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP7B.
[7]"A novel role for XIAP in copper homeostasis through regulation of MURR1."
Burstein E., Ganesh L., Dick R.D., van De Sluis B., Wilkinson J.C., Klomp L.W., Wijmenga C., Brewer G.J., Nabel G.J., Duckett C.S.
EMBO J. 23:244-254(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH XIAP.
[8]"COMMD proteins, a novel family of structural and functional homologs of MURR1."
Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A., Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S.
J. Biol. Chem. 280:22222-22232(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RELA; COMMD2; COMMD3; COMMD4; COMMD5; COMMD6; COMMD7; COMMD8 AND COMMD10, IDENTIFICATION IN A COMPLEX WITH NF-KAPPA-B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"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 COMMD6 AND NFKBIB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Characterization and copper binding properties of human COMMD1 (MURR1)."
Narindrasorasak S., Kulkarni P., Deschamps P., She Y.M., Sarkar B.
Biochemistry 46:3116-3128(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF MET-110 AND HIS-134, COPPER-BINDING.
[11]"COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase."
Maine G.N., Mao X., Komarck C.M., Burstein E.
EMBO J. 26:436-447(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH SOCS1 AND CUL2, IDENTIFICATION IN AN E3 UBIQUITIN LIGASE COMPLEX COMPOSED OF TCEB1/ELONGIN C; CUL2; SOCS1 AND RBX1.
[12]"Tumor suppressor ARF promotes non-classic proteasome-independent polyubiquitination of COMMD1."
Huang Y., Wu M., Li H.Y.
J. Biol. Chem. 283:11453-11460(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH CDKN2A.
[13]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"Nucleolar targeting of RelA(p65) is regulated by COMMD1-dependent ubiquitination."
Thoms H.C., Loveridge C.J., Simpson J., Clipson A., Reinhardt K., Dunlop M.G., Stark L.A.
Cancer Res. 70:139-149(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1."
Vonk W.I., Wijmenga C., Berger R., van de Sluis B., Klomp L.W.
J. Biol. Chem. 285:28991-29000(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CCS.
[16]"Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells."
Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A., Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.
Mol. Cancer Res. 8:119-130(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, INTERACTION WITH CLU.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Solution structure of the COMMD1 N-terminal domain."
Sommerhalter M., Zhang Y., Rosenzweig A.C.
J. Mol. Biol. 365:715-721(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-108.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB178811 mRNA. Translation: BAD18972.1.
BC009266 mRNA. Translation: AAH09266.2.
BC022046 mRNA. Translation: AAH22046.1.
RefSeqNP_689729.1. NM_152516.2.
UniGeneHs.468702.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H2MNMR-A1-108[»]
ProteinModelPortalQ8N668.
SMRQ8N668. Positions 1-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127317. 51 interactions.
IntActQ8N668. 25 interactions.
MINTMINT-4140741.
STRING9606.ENSP00000308236.

PTM databases

PhosphoSiteQ8N668.

Polymorphism databases

DMDM51316026.

Proteomic databases

PaxDbQ8N668.
PRIDEQ8N668.

Protocols and materials databases

DNASU150684.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311832; ENSP00000308236; ENSG00000173163.
GeneID150684.
KEGGhsa:150684.
UCSCuc002sbp.3. human.

Organism-specific databases

CTD150684.
GeneCardsGC02P062115.
HGNCHGNC:23024. COMMD1.
HPAHPA034633.
MIM607238. gene.
neXtProtNX_Q8N668.
PharmGKBPA134891368.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46398.
HOGENOMHOG000236295.
HOVERGENHBG051067.
InParanoidQ8N668.
OMALLAQSRW.
PhylomeDBQ8N668.
TreeFamTF332823.

Gene expression databases

ArrayExpressQ8N668.
BgeeQ8N668.
CleanExHS_COMMD1.
GenevestigatorQ8N668.

Family and domain databases

InterProIPR017920. COMM.
IPR009886. HCaRG.
[Graphical view]
PfamPF07258. HCaRG. 1 hit.
[Graphical view]
PROSITEPS51269. COMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOMMD1. human.
EvolutionaryTraceQ8N668.
GeneWikiCOMMD1.
GenomeRNAi150684.
NextBio86500.
PROQ8N668.
SOURCESearch...

Entry information

Entry nameCOMD1_HUMAN
AccessionPrimary (citable) accession number: Q8N668
Secondary accession number(s): Q96GS0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM