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Protein

COMM domain-containing protein 1

Gene

Commd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. Modulates Na+ transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression through regulation of its ubiquitination. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001CopperSequence analysis
Metal bindingi109 – 1091CopperSequence analysis
Metal bindingi133 – 1331CopperSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport, Ubl conjugation pathway

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
COMM domain-containing protein 1
Alternative name(s):
Protein Murr1
Gene namesi
Name:Commd1
Synonyms:Murr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:109474. Commd1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Endosome membrane By similarity
  • Cytoplasmic vesicle By similarity
  • Early endosome By similarity
  • Recycling endosome By similarity

  • Note: Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188COMM domain-containing protein 1PRO_0000077385Add
BLAST

Post-translational modificationi

Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ8K4M5.
MaxQBiQ8K4M5.
PaxDbiQ8K4M5.
PRIDEiQ8K4M5.

PTM databases

PhosphoSiteiQ8K4M5.

Expressioni

Gene expression databases

BgeeiQ8K4M5.
CleanExiMM_COMMD1.
ExpressionAtlasiQ8K4M5. baseline and differential.
GenevisibleiQ8K4M5. MM.

Interactioni

Subunit structurei

Monomer, homodimer. Can form heterodimers with other COMM domain-containing proteins but only certain combinations may exist in vivo. 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; in the complex interacts directly with SOCS1 and CUL2. Interacts directly with ATP7B (via the N-terminal region). Interacts with CCS, CDKN2A, RELA, REL, RELB, NFKB1/p105, NFKB2/p100, NFKBIB, SCNN1D, SCNN1B, CFTR, CLU, SGK1, AKT1, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5, CUL7, HIF1A. Identified in a complex with NF-kappa-B. Interacts directly with SLC12A2. Interacts with CCDC22, CCDC93 and C16orf62 homolog; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22, CCDC93 and C16orf62 homolog.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8K4M5. 1 interaction.
STRINGi10090.ENSMUSP00000124719.

Structurei

3D structure databases

ProteinModelPortaliQ8K4M5.
SMRiQ8K4M5. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 18569COMMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 122122Sufficient for interaction with SLC12A2By similarityAdd
BLAST
Regioni124 – 18865Required for binding to PtdIns(4,5)P2By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 COMM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IWFF. Eukaryota.
ENOG4111IWI. LUCA.
GeneTreeiENSGT00390000012029.
HOVERGENiHBG051067.
InParanoidiQ8K4M5.
OMAiGELEGCK.
PhylomeDBiQ8K4M5.
TreeFamiTF332823.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q8K4M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGDLEGGKS LSGLLSGLAQ NAFHGHSGVT EELLHSQLYP EVPPEEFRPF
60 70 80 90 100
LAKMRGLLKS IASADMDFNQ LEAFLTAQTK KQGGITSEQA AVISKFWKSH
110 120 130 140 150
KIKIRESLMK QSRWDNGLRG LSWRVDGKSQ SRHSTQIHSP VAIIELEFGK
160 170 180
NGQESEFLCL EFDEVKVKQI LKKLSEVEES INRLMQAA
Length:188
Mass (Da):20,996
Last modified:August 16, 2004 - v2
Checksum:iEEEC6489BC59B483
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → H in AAH51210 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK133507 mRNA. Translation: BAE21693.1.
AB089806 Genomic DNA. Translation: BAC07535.1.
AB104816 mRNA. Translation: BAC57942.1.
BC030052 mRNA. Translation: AAH30052.1.
BC051210 mRNA. Translation: AAH51210.1.
CCDSiCCDS24472.1.
RefSeqiNP_653097.2. NM_144514.2.
UniGeneiMm.259903.
Mm.451238.

Genome annotation databases

EnsembliENSMUST00000159081; ENSMUSP00000124719; ENSMUSG00000051355.
GeneIDi17846.
KEGGimmu:17846.
UCSCiuc007iel.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK133507 mRNA. Translation: BAE21693.1.
AB089806 Genomic DNA. Translation: BAC07535.1.
AB104816 mRNA. Translation: BAC57942.1.
BC030052 mRNA. Translation: AAH30052.1.
BC051210 mRNA. Translation: AAH51210.1.
CCDSiCCDS24472.1.
RefSeqiNP_653097.2. NM_144514.2.
UniGeneiMm.259903.
Mm.451238.

3D structure databases

ProteinModelPortaliQ8K4M5.
SMRiQ8K4M5. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K4M5. 1 interaction.
STRINGi10090.ENSMUSP00000124719.

PTM databases

PhosphoSiteiQ8K4M5.

Proteomic databases

EPDiQ8K4M5.
MaxQBiQ8K4M5.
PaxDbiQ8K4M5.
PRIDEiQ8K4M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000159081; ENSMUSP00000124719; ENSMUSG00000051355.
GeneIDi17846.
KEGGimmu:17846.
UCSCiuc007iel.1. mouse.

Organism-specific databases

CTDi150684.
MGIiMGI:109474. Commd1.

Phylogenomic databases

eggNOGiENOG410IWFF. Eukaryota.
ENOG4111IWI. LUCA.
GeneTreeiENSGT00390000012029.
HOVERGENiHBG051067.
InParanoidiQ8K4M5.
OMAiGELEGCK.
PhylomeDBiQ8K4M5.
TreeFamiTF332823.

Miscellaneous databases

PROiQ8K4M5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K4M5.
CleanExiMM_COMMD1.
ExpressionAtlasiQ8K4M5. baseline and differential.
GenevisibleiQ8K4M5. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Ovary and Uterus.
  2. "The mouse Murr1 gene is imprinted in the adult brain, presumably due to transcriptional interference by the antisense-oriented U2af1-rs1 gene."
    Wang Y., Joh K., Masuko S., Yatsuki H., Soejima H., Nabetani A., Beechey C.V., Okinami S., Mukai T.
    Mol. Cell. Biol. 24:270-279(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
    Strain: C57BL/6J.
  3. "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] OF 5-188.
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiCOMD1_MOUSE
AccessioniPrimary (citable) accession number: Q8K4M5
Secondary accession number(s): Q3V012
, Q80WG2, Q80Z41, Q8BNL9, Q8K2S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.