COMDA_HUMAN
ID COMDA_HUMAN Reviewed; 202 AA.
AC Q9Y6G5; D3DT07; Q9P077;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=COMM domain-containing protein 10;
GN Name=COMMD10; ORFNames=HSPC305, PTD002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH COMMD1; RELA; RELB;
RP NFKB1 AND NFKB2, AND TISSUE SPECIFICITY.
RX PubMed=15799966; DOI=10.1074/jbc.m501928200;
RA Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A.,
RA Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S.;
RT "COMMD proteins, a novel family of structural and functional homologs of
RT MURR1.";
RL J. Biol. Chem. 280:22222-22232(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary tumor;
RA Fu G., Huang Q., Song H., Peng J., Zhang Q., Mao M., Dai M., Mao Y.,
RA Zhou J., Chen Z., Chen J.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4B AND CUL7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21778237; DOI=10.1074/jbc.m111.278408;
RA Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N.,
RA Burstein E.;
RT "COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates
RT Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-
RT dissociated protein 1) binding.";
RL J. Biol. Chem. 286:32355-32365(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP INTERACTION WITH SCNN1B.
RX PubMed=23637203; DOI=10.1152/ajprenal.00158.2013;
RA Liu Y.F., Swart M., Ke Y., Ly K., McDonald F.J.;
RT "Functional interaction of COMMD3 and COMMD9 with the epithelial sodium
RT channel.";
RL Am. J. Physiol. 305:F80-F89(2013).
RN [12]
RP INTERACTION WITH CCDC22.
RX PubMed=23563313; DOI=10.1172/jci66466;
RA Starokadomskyy P., Gluck N., Li H., Chen B., Wallis M., Maine G.N., Mao X.,
RA Zaidi I.W., Hein M.Y., McDonald F.J., Lenzner S., Zecha A., Ropers H.H.,
RA Kuss A.W., McGaughran J., Gecz J., Burstein E.;
RT "CCDC22 deficiency in humans blunts activation of proinflammatory NF-kappaB
RT signaling.";
RL J. Clin. Invest. 123:2244-2256(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH CCDC93.
RX PubMed=25355947; DOI=10.1091/mbc.e14-06-1073;
RA Phillips-Krawczak C.A., Singla A., Starokadomskyy P., Deng Z.,
RA Osborne D.G., Li H., Dick C.J., Gomez T.S., Koenecke M., Zhang J.S.,
RA Dai H., Sifuentes-Dominguez L.F., Geng L.N., Kaufmann S.H., Hein M.Y.,
RA Wallis M., McGaughran J., Gecz J., van de Sluis B., Billadeau D.D.,
RA Burstein E.;
RT "COMMD1 is linked to the WASH complex and regulates endosomal trafficking
RT of the copper transporter ATP7A.";
RL Mol. Biol. Cell 26:91-103(2015).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase
CC (CRL) complexes (PubMed:21778237). May down-regulate activation of NF-
CC kappa-B (PubMed:15799966). {ECO:0000269|PubMed:15799966,
CC ECO:0000305|PubMed:21778237}.
CC -!- SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain).
CC Interacts with RELA, RELB, NFKB1/p105, NFKB2/p100. Interacts with
CC CCDC22, CCDC93, SCNN1B, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL7.
CC {ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:21778237,
CC ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:23637203,
CC ECO:0000269|PubMed:25355947}.
CC -!- INTERACTION:
CC Q9Y6G5; O60826: CCDC22; NbExp=9; IntAct=EBI-1550310, EBI-3943153;
CC Q9Y6G5; Q567U6: CCDC93; NbExp=3; IntAct=EBI-1550310, EBI-1104769;
CC Q9Y6G5; Q8N668: COMMD1; NbExp=2; IntAct=EBI-1550310, EBI-1550112;
CC Q9Y6G5; Q9GZQ3: COMMD5; NbExp=7; IntAct=EBI-1550310, EBI-1550256;
CC Q9Y6G5; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-1550310, EBI-10226858;
CC Q9Y6G5; P01100: FOS; NbExp=3; IntAct=EBI-1550310, EBI-852851;
CC Q9Y6G5; P50440: GATM; NbExp=3; IntAct=EBI-1550310, EBI-2552594;
CC Q9Y6G5; P31930: UQCRC1; NbExp=3; IntAct=EBI-1550310, EBI-1052596;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus
CC {ECO:0000269|PubMed:21778237}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15799966}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY542165; AAS22247.1; -; mRNA.
DR EMBL; AF078857; AAD44489.1; -; mRNA.
DR EMBL; AF161423; AAF28983.1; ALT_INIT; mRNA.
DR EMBL; AK002147; BAA92108.1; -; mRNA.
DR EMBL; CH471086; EAW48941.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48942.1; -; Genomic_DNA.
DR EMBL; BC005179; AAH05179.1; -; mRNA.
DR CCDS; CCDS34215.1; -.
DR RefSeq; NP_001295009.1; NM_001308080.1.
DR RefSeq; NP_057228.1; NM_016144.3.
DR AlphaFoldDB; Q9Y6G5; -.
DR SMR; Q9Y6G5; -.
DR BioGRID; 119521; 41.
DR CORUM; Q9Y6G5; -.
DR IntAct; Q9Y6G5; 35.
DR MINT; Q9Y6G5; -.
DR STRING; 9606.ENSP00000274458; -.
DR GlyGen; Q9Y6G5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6G5; -.
DR PhosphoSitePlus; Q9Y6G5; -.
DR BioMuta; COMMD10; -.
DR DMDM; 51316122; -.
DR EPD; Q9Y6G5; -.
DR jPOST; Q9Y6G5; -.
DR MassIVE; Q9Y6G5; -.
DR MaxQB; Q9Y6G5; -.
DR PaxDb; Q9Y6G5; -.
DR PeptideAtlas; Q9Y6G5; -.
DR PRIDE; Q9Y6G5; -.
DR ProteomicsDB; 86676; -.
DR Antibodypedia; 25475; 140 antibodies from 18 providers.
DR DNASU; 51397; -.
DR Ensembl; ENST00000274458.9; ENSP00000274458.4; ENSG00000145781.9.
DR GeneID; 51397; -.
DR KEGG; hsa:51397; -.
DR MANE-Select; ENST00000274458.9; ENSP00000274458.4; NM_016144.4; NP_057228.1.
DR UCSC; uc003krt.2; human.
DR CTD; 51397; -.
DR DisGeNET; 51397; -.
DR GeneCards; COMMD10; -.
DR HGNC; HGNC:30201; COMMD10.
DR HPA; ENSG00000145781; Low tissue specificity.
DR MIM; 616704; gene.
DR neXtProt; NX_Q9Y6G5; -.
DR OpenTargets; ENSG00000145781; -.
DR PharmGKB; PA134862606; -.
DR VEuPathDB; HostDB:ENSG00000145781; -.
DR eggNOG; ENOG502QWQ2; Eukaryota.
DR GeneTree; ENSGT00390000001500; -.
DR InParanoid; Q9Y6G5; -.
DR OMA; VEFNHQE; -.
DR OrthoDB; 1549928at2759; -.
DR PhylomeDB; Q9Y6G5; -.
DR TreeFam; TF352584; -.
DR PathwayCommons; Q9Y6G5; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9Y6G5; -.
DR BioGRID-ORCS; 51397; 23 hits in 1081 CRISPR screens.
DR ChiTaRS; COMMD10; human.
DR GenomeRNAi; 51397; -.
DR Pharos; Q9Y6G5; Tbio.
DR PRO; PR:Q9Y6G5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y6G5; protein.
DR Bgee; ENSG00000145781; Expressed in oocyte and 187 other tissues.
DR ExpressionAtlas; Q9Y6G5; baseline and differential.
DR Genevisible; Q9Y6G5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR CDD; cd04758; Commd10; 1.
DR InterPro; IPR017920; COMM.
DR InterPro; IPR037361; COMMD10.
DR PANTHER; PTHR12333; PTHR12333; 1.
DR Pfam; PF07258; COMM_domain; 1.
DR PROSITE; PS51269; COMM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..202
FT /note="COMM domain-containing protein 10"
FT /id="PRO_0000077405"
FT DOMAIN 133..202
FT /note="COMM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00602"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 128
FT /note="I -> S (in dbSNP:rs1129495)"
FT /id="VAR_061122"
SQ SEQUENCE 202 AA; 22966 MW; 4D3C014FE59188CB CRC64;
MAVPAALILR ESPSMKKAVS LINAIDTGRF PRLLTRILQK LHLKAESSFS EEEEEKLQAA
FSLEKQDLHL VLETISFILE QAVYHNVKPA ALQQQLENIH LRQDKAEAFV NTWSSMGQET
VEKFRQRILA PCKLETVGWQ LNLQMAHSAQ AKLKSPQAVL QLGVNNEDSK SLEKVLVEFS
HKELFDFYNK LETIQAQLDS LT
