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Protein

COMM domain-containing protein 5

Gene

COMMD5

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). Negatively regulates cell proliferation. Negatively regulates cell cycle G2/M phase transition probably by transactivating p21/CDKN1A through the p53/TP53-independent signaling pathway. Involved in kidney proximal tubule morphogenesis (By similarity). Down-regulates activation of NF-kappa-B (PubMed:15799966).By similarity1 Publication1 Publication

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 5
Alternative name(s):
Hypertension-related calcium-regulated gene protein
Short name:
HCaRG
Gene namesi
Name:COMMD5
ORF Names:HT002
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:17902. COMMD5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134873412.

Polymorphism and mutation databases

BioMutaiCOMMD5.
DMDMi51316093.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 224223COMM domain-containing protein 5PRO_0000077395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9GZQ3.
MaxQBiQ9GZQ3.
PaxDbiQ9GZQ3.
PeptideAtlasiQ9GZQ3.
PRIDEiQ9GZQ3.

PTM databases

PhosphoSiteiQ9GZQ3.

Expressioni

Tissue specificityi

Highly expressed in heart, stomach, jejunum, kidney, liver, and adrenal gland. Expression was generally higher in adult organs than in fetal tissues, particularly in heart, kidney, and liver.2 Publications

Gene expression databases

BgeeiQ9GZQ3.
CleanExiHS_COMMD5.
ExpressionAtlasiQ9GZQ3. baseline and differential.
GenevisibleiQ9GZQ3. HS.

Organism-specific databases

HPAiHPA046905.
HPA046989.

Interactioni

Subunit structurei

Interacts (via COMM domain) with COMMD1 (via COMM domain). Interacts with RELA, RELB, NFKB1/p105. Interacts with CCDC22, CCDC93, SCNN1B, CUL2, CUL3, CUL4A, CUL4B, CUL7.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC22O608265EBI-1550256,EBI-3943153

Protein-protein interaction databases

BioGridi118812. 15 interactions.
IntActiQ9GZQ3. 9 interactions.
STRINGi9606.ENSP00000304544.

Structurei

3D structure databases

ProteinModelPortaliQ9GZQ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini151 – 21565COMMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 COMM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFHH. Eukaryota.
ENOG4111FTK. LUCA.
GeneTreeiENSGT00390000013770.
HOGENOMiHOG000007429.
HOVERGENiHBG051070.
InParanoidiQ9GZQ3.
OMAiPYLHHPG.
PhylomeDBiQ9GZQ3.
TreeFamiTF323880.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9GZQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVGAATPY LHHPGDSHSG RVSFLGAQLP PEVAAMARLL GDLDRSTFRK
60 70 80 90 100
LLKFVVSSLQ GEDCREAVQR LGVSANLPEE QLGALLAGMH TLLQQALRLP
110 120 130 140 150
PTSLKPDTFR DQLQELCIPQ DLVGDLASVV FGSQRPLLDS VAQQQGAWLP
160 170 180 190 200
HVADFRWRVD VAISTSALAR SLQPSVLMQL KLSDGSAYRF EVPTAKFQEL
210 220
RYSVALVLKE MADLEKRCER RLQD
Length:224
Mass (Da):24,670
Last modified:March 1, 2001 - v1
Checksum:iC4CC0563B9FA3240
GO

Sequence cautioni

The sequence AAF14877.1 differs from that shown. Reason: Frameshift at positions 66, 84, 112 and 136. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081T → I in BAA91714 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → T.1 Publication
Corresponds to variant rs1209879 [ dbSNP | Ensembl ].
VAR_020130
Natural varianti69 – 691Q → H.
Corresponds to variant rs421427 [ dbSNP | Ensembl ].
VAR_048812

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290195 mRNA. Translation: AAG09915.1.
AF113540 mRNA. Translation: AAF14877.1. Frameshift.
AK001477 mRNA. Translation: BAA91714.1.
AK023070 mRNA. Translation: BAB14389.1.
CH471162 Genomic DNA. Translation: EAW82033.1.
CH471162 Genomic DNA. Translation: EAW82034.1.
CH471162 Genomic DNA. Translation: EAW82035.1.
CH471162 Genomic DNA. Translation: EAW82036.1.
CH471162 Genomic DNA. Translation: EAW82037.1.
BC002672 mRNA. Translation: AAH02672.1.
BC003055 mRNA. Translation: AAH03055.1.
BC065729 mRNA. Translation: AAH65729.1.
CCDSiCCDS6436.1.
RefSeqiNP_001074472.1. NM_001081003.2.
NP_001074473.1. NM_001081004.2.
NP_001274166.1. NM_001287237.1.
NP_054785.2. NM_014066.3.
UniGeneiHs.493218.
Hs.631856.

Genome annotation databases

EnsembliENST00000305103; ENSP00000304544; ENSG00000170619.
ENST00000402718; ENSP00000385793; ENSG00000170619.
ENST00000450361; ENSP00000394331; ENSG00000170619.
ENST00000543949; ENSP00000445840; ENSG00000170619.
GeneIDi28991.
KEGGihsa:28991.
UCSCiuc003zem.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290195 mRNA. Translation: AAG09915.1.
AF113540 mRNA. Translation: AAF14877.1. Frameshift.
AK001477 mRNA. Translation: BAA91714.1.
AK023070 mRNA. Translation: BAB14389.1.
CH471162 Genomic DNA. Translation: EAW82033.1.
CH471162 Genomic DNA. Translation: EAW82034.1.
CH471162 Genomic DNA. Translation: EAW82035.1.
CH471162 Genomic DNA. Translation: EAW82036.1.
CH471162 Genomic DNA. Translation: EAW82037.1.
BC002672 mRNA. Translation: AAH02672.1.
BC003055 mRNA. Translation: AAH03055.1.
BC065729 mRNA. Translation: AAH65729.1.
CCDSiCCDS6436.1.
RefSeqiNP_001074472.1. NM_001081003.2.
NP_001074473.1. NM_001081004.2.
NP_001274166.1. NM_001287237.1.
NP_054785.2. NM_014066.3.
UniGeneiHs.493218.
Hs.631856.

3D structure databases

ProteinModelPortaliQ9GZQ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118812. 15 interactions.
IntActiQ9GZQ3. 9 interactions.
STRINGi9606.ENSP00000304544.

PTM databases

PhosphoSiteiQ9GZQ3.

Polymorphism and mutation databases

BioMutaiCOMMD5.
DMDMi51316093.

Proteomic databases

EPDiQ9GZQ3.
MaxQBiQ9GZQ3.
PaxDbiQ9GZQ3.
PeptideAtlasiQ9GZQ3.
PRIDEiQ9GZQ3.

Protocols and materials databases

DNASUi28991.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305103; ENSP00000304544; ENSG00000170619.
ENST00000402718; ENSP00000385793; ENSG00000170619.
ENST00000450361; ENSP00000394331; ENSG00000170619.
ENST00000543949; ENSP00000445840; ENSG00000170619.
GeneIDi28991.
KEGGihsa:28991.
UCSCiuc003zem.4. human.

Organism-specific databases

CTDi28991.
GeneCardsiCOMMD5.
H-InvDBHIX0007872.
HGNCiHGNC:17902. COMMD5.
HPAiHPA046905.
HPA046989.
MIMi608216. gene.
neXtProtiNX_Q9GZQ3.
PharmGKBiPA134873412.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFHH. Eukaryota.
ENOG4111FTK. LUCA.
GeneTreeiENSGT00390000013770.
HOGENOMiHOG000007429.
HOVERGENiHBG051070.
InParanoidiQ9GZQ3.
OMAiPYLHHPG.
PhylomeDBiQ9GZQ3.
TreeFamiTF323880.

Miscellaneous databases

ChiTaRSiCOMMD5. human.
GenomeRNAii28991.
NextBioi51913.
PROiQ9GZQ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZQ3.
CleanExiHS_COMMD5.
ExpressionAtlasiQ9GZQ3. baseline and differential.
GenevisibleiQ9GZQ3. 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. "HCaRG, a novel calcium-regulated gene coding for a nuclear protein, is potentially involved in the regulation of cell proliferation."
    Solban N., Jia H.-P., Richard S., Tremblay S., Devlin A.M., Peng J., Gossard F., Guo D.-F., Morel G., Hamet P., Lewanczuk R., Tremblay J.
    J. Biol. Chem. 275:32234-32243(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Parathyroid.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-6.
    Tissue: Hypothalamus.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Skin and Uterus.
  6. Cited for: FUNCTION, INTERACTION WITH COMMD1; RELA; RELB AND NFKB1, TISSUE SPECIFICITY.
  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 CUL2; CUL3; CUL4A; CUL4B AND CUL7, 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.
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOMD5_HUMAN
AccessioniPrimary (citable) accession number: Q9GZQ3
Secondary accession number(s): D3DWN7, Q9NVN6, Q9UHX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 112 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 8
    Human chromosome 8: 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.