Human Gene COMMD1 (ENST00000311832.6) from GENCODE V44
  Description: Homo sapiens copper metabolism domain containing 1 (COMMD1), transcript variant 1, mRNA. (from RefSeq NM_152516)
RefSeq Summary (NM_152516): COMMD1 is a regulator of copper homeostasis, sodium uptake, and NF-kappa-B (see MIM 164011) signaling (de Bie et al., 2005 [PubMed 16267171]).[supplied by OMIM, Sep 2009].
Gencode Transcript: ENST00000311832.6
Gencode Gene: ENSG00000173163.11
Transcript (Including UTRs)
   Position: hg38 chr2:61,905,674-62,136,058 Size: 230,385 Total Exon Count: 3 Strand: +
Coding Region
   Position: hg38 chr2:61,905,679-62,135,941 Size: 230,263 Coding Exon Count: 3 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
RNA-Seq ExpressionRNA StructureProtein StructureOther SpeciesGO AnnotationsmRNA Descriptions
PathwaysOther NamesMethods
Data last updated at UCSC: 2023-08-18 00:09:47

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr2:61,905,674-62,136,058)mRNA (may differ from genome)Protein (190 aa)
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-  Comments and Description Text from UniProtKB
  ID: COMD1_HUMAN
DESCRIPTION: RecName: Full=COMM domain-containing protein 1; AltName: Full=Protein Murr1;
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.
SUBUNIT: 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.
INTERACTION: Self; NbExp=2; IntAct=EBI-1550112, EBI-1550112; Q9UBI1:COMMD3; NbExp=3; IntAct=EBI-1550112, EBI-714979; Q9H0A8:COMMD4; NbExp=2; IntAct=EBI-1550112, EBI-1550064; Q7Z4G1:COMMD6; NbExp=2; IntAct=EBI-1550112, EBI-1550081; P25963:NFKBIA; NbExp=3; IntAct=EBI-1550112, EBI-307386; Q04864:REL; NbExp=3; IntAct=EBI-1550112, EBI-307352; Q04206:RELA; NbExp=7; IntAct=EBI-1550112, EBI-73886; Q01201:RELB; NbExp=2; IntAct=EBI-1550112, EBI-357837; P51172:SCNN1D; NbExp=3; IntAct=EBI-1550112, EBI-2547114;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins.
TISSUE SPECIFICITY: Ubiquitous. Highest expression in the liver, with lower expression in brain, lung, placenta, pancreas, small intestine, heart, skeletal muscle, kidney and placenta.
PTM: Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal degradation.
SIMILARITY: Contains 1 COMM domain.

-  Primer design for this transcript
 

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Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: COMMD1
Diseases sorted by gene-association score: wilson disease (18), menkes disease (7), metal metabolism disorder (4)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 13.58 RPKM in Testis
Total median expression: 329.86 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
3' UTR -17.20117-0.147 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR017920 - COMM
IPR009886 - HCaRG

Pfam Domains:
PF07258 - COMM domain

Protein Data Bank (PDB) 3-D Structure
MuPIT help
2H2M - NMR MuPIT


ModBase Predicted Comparative 3D Structure on Q8N668
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
Genome BrowserGenome BrowserGenome BrowserNo orthologNo orthologNo ortholog
Gene Details     
Gene Sorter     
MGIRGDEnsembl   
Protein SequenceProtein SequenceProtein Sequence   
AlignmentAlignmentAlignment   

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding
GO:0008289 lipid binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043325 phosphatidylinositol-3,4-bisphosphate binding
GO:0046872 metal ion binding
GO:0070300 phosphatidic acid binding
GO:0080025 phosphatidylinositol-3,5-bisphosphate binding

Biological Process:
GO:0006351 transcription, DNA-templated
GO:0006355 regulation of transcription, DNA-templated
GO:0006893 Golgi to plasma membrane transport
GO:0015031 protein transport
GO:0031398 positive regulation of protein ubiquitination
GO:0032088 negative regulation of NF-kappaB transcription factor activity
GO:0032434 regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0043687 post-translational protein modification
GO:0048227 plasma membrane to endosome transport
GO:0055070 copper ion homeostasis
GO:1902306 negative regulation of sodium ion transmembrane transport
GO:2000009 negative regulation of protein localization to cell surface

Cellular Component:
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005768 endosome
GO:0005769 early endosome
GO:0005829 cytosol
GO:0010008 endosome membrane
GO:0016020 membrane
GO:0031410 cytoplasmic vesicle
GO:0031462 Cul2-RING ubiquitin ligase complex
GO:0055037 recycling endosome


-  Descriptions from all associated GenBank mRNAs
  AK223607 - Homo sapiens mRNA for MURR1 variant, clone: FCC132E08.
AB178811 - Homo sapiens mRNA for MURR1, exon 1 to 3 and complete cds.
AK294203 - Homo sapiens cDNA FLJ56664 complete cds, highly similar to COMM domain-containing protein 1.
BC022046 - Homo sapiens copper metabolism (Murr1) domain containing 1, mRNA (cDNA clone MGC:27155 IMAGE:4046433), complete cds.
CU692476 - Synthetic construct Homo sapiens gateway clone IMAGE:100022033 5' read COMMD1 mRNA.
HQ447741 - Synthetic construct Homo sapiens clone IMAGE:100071072; CCSB013160_01 copper metabolism (Murr1) domain containing 1 (COMMD1) gene, encodes complete protein.
KJ900279 - Synthetic construct Homo sapiens clone ccsbBroadEn_09673 COMMD1 gene, encodes complete protein.
AB590636 - Synthetic construct DNA, clone: pFN21AE1676, Homo sapiens COMMD1 gene for copper metabolism (Murr1) domain containing 1, without stop codon, in Flexi system.
BC009266 - Homo sapiens copper metabolism (Murr1) domain containing 1, mRNA (cDNA clone IMAGE:3947554), partial cds.
D85433 - Homo sapiens MURR1 mRNA, sequence.
JD182968 - Sequence 163992 from Patent EP1572962.
JD046064 - Sequence 27088 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q8N668 (Reactome details) participates in the following event(s):

R-HSA-8955285 COMMDs displace CAND1 from CRL4 E3 ubiquitin ligase complex
R-HSA-8955289 COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes
R-HSA-8956045 COP9 signalosome deneddylates nuclear CRL4 E3 ubiquitin ligase complex
R-HSA-8952638 AcM-UBE2M transfers NEDD8 to CRL4 E3 ubiquitin ligase complex
R-HSA-8952639 NEDD8:AcM-UBE2M binds CRL4 E3 ubiquitin ligase complex
R-HSA-8952044 AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex
R-HSA-8952618 AcM-UBE2M transfers NEDD8 to CRL1 E3 ubiquitin ligase complex
R-HSA-8952039 NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex
R-HSA-8952620 NEDD8:AcM-UBE2M binds CRL1 E3 ubiquitin ligase complex
R-HSA-8956200 MyrG-DCUN1D3 binds CRL1 E3 ubiquitin ligase complex
R-HSA-8956099 VHL:EloB,C:NEDD8-CUL2:RBX1 complex binds UBXN7
R-HSA-8956103 VHL:EloB,C:NEDD8-CUL2:RBX1 complex binds hydroxyprolyl-HIF-alpha
R-HSA-8956040 COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes
R-HSA-8956106 VHL:EloB,C:NEDD8-CUL2:RBX1 complex ubiquitinylates HIF-alpha
R-HSA-8951664 Neddylation
R-HSA-597592 Post-translational protein modification
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: C2orf5, COMD1_HUMAN, ENST00000311832.1, ENST00000311832.2, ENST00000311832.3, ENST00000311832.4, ENST00000311832.5, MURR1, NM_152516, Q8N668, Q96GS0, uc002sbp.1, uc002sbp.2, uc002sbp.3, uc002sbp.4, uc002sbp.5
UCSC ID: ENST00000311832.6
RefSeq Accession: NM_152516
Protein: Q8N668 (aka COMD1_HUMAN or COM1_HUMAN)

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.