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 27-MAR-2024, entry version 150. 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=11; IntAct=EBI-1550310, EBI-3943153; CC Q9Y6G5; Q567U6: CCDC93; NbExp=4; IntAct=EBI-1550310, EBI-1104769; CC Q9Y6G5; Q8N668: COMMD1; NbExp=4; IntAct=EBI-1550310, EBI-1550112; CC Q9Y6G5; Q9GZQ3: COMMD5; NbExp=11; 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 PDB; 8ESD; X-ray; 3.33 A; T=12-202. DR PDB; 8F2R; EM; 3.12 A; J=5-202. DR PDB; 8F2U; EM; 3.53 A; J=1-202. DR PDBsum; 8ESD; -. DR PDBsum; 8F2R; -. DR PDBsum; 8F2U; -. DR AlphaFoldDB; Q9Y6G5; -. DR EMDB; EMD-28825; -. DR SMR; Q9Y6G5; -. DR BioGRID; 119521; 46. DR ComplexPortal; CPX-2211; Commander complex. 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; 9606-ENSP00000274458; -. DR PeptideAtlas; Q9Y6G5; -. DR ProteomicsDB; 86676; -. DR Pumba; Q9Y6G5; -. DR Antibodypedia; 25475; 155 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 AGR; HGNC:30201; -. 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; IHLEQDK; -. DR OrthoDB; 8033at2759; -. DR PhylomeDB; Q9Y6G5; -. DR TreeFam; TF352584; -. DR PathwayCommons; Q9Y6G5; -. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; Q9Y6G5; -. DR BioGRID-ORCS; 51397; 26 hits in 1174 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 189 other cell types or tissues. DR ExpressionAtlas; Q9Y6G5; baseline and differential. 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; COMM DOMAIN CONTAINING PROTEIN 10; 1. DR PANTHER; PTHR12333:SF0; COMM DOMAIN-CONTAINING PROTEIN 10; 1. DR Pfam; PF07258; COMM_domain; 1. DR Pfam; PF21672; COMM_HN; 1. DR PROSITE; PS51269; COMM; 1. DR Genevisible; Q9Y6G5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW 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" FT HELIX 15..24 FT /evidence="ECO:0007829|PDB:8ESD" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:8ESD" FT HELIX 30..41 FT /evidence="ECO:0007829|PDB:8ESD" FT HELIX 54..61 FT /evidence="ECO:0007829|PDB:8ESD" FT HELIX 65..85 FT /evidence="ECO:0007829|PDB:8ESD" FT HELIX 89..98 FT /evidence="ECO:0007829|PDB:8ESD" FT HELIX 103..126 FT /evidence="ECO:0007829|PDB:8ESD" FT STRAND 130..142 FT /evidence="ECO:0007829|PDB:8ESD" FT STRAND 157..166 FT /evidence="ECO:0007829|PDB:8ESD" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:8ESD" FT STRAND 172..180 FT /evidence="ECO:0007829|PDB:8ESD" FT HELIX 181..200 FT /evidence="ECO:0007829|PDB:8ESD" 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 //