ID COMD1_HUMAN Reviewed; 190 AA. AC Q8N668; B4DFQ4; Q96GS0; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 28-FEB-2018, entry version 130. DE RecName: Full=COMM domain-containing protein 1; DE AltName: Full=Protein Murr1; GN Name=COMMD1; Synonyms=C2orf5, MURR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=12547404; DOI=10.1016/S0168-8278(02)00356-2; RA Mueller T., van de Sluis B.A.J., Zhernakova A., van Binsbergen E., RA Janecke A.R., Bavdekar A., Pandit A., Weirich-Schwaiger H., Witt H., RA Ellemunter H., Deutsch J., Denk H., Mueller W., Sternlieb I., RA Tanner M.S., Wijmenga C.; RT "The canine copper toxicosis gene MURR1 does not cause non-Wilsonian RT hepatic copper toxicosis."; RL J. Hepatol. 38:164-168(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=15205742; DOI=10.1007/s00109-004-0557-9; RA Stuehler B., Reichert J., Stremmel W., Schaefer M.; RT "Analysis of the human homologue of the canine copper toxicosis gene RT MURR1 in Wilson disease patients."; RL J. Mol. Med. 82:629-634(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Kidney; RA Zhang Z., Yatsuki H., Wang Y., Joh K., Nabetani A., Hatada I., RA Soejima H., Iwasaka T., Mukai T.; RT "Comparative analyses of gene imprinting and CpG island methylation RT around mouse Murr1 and human syntenic region identify the 5'-portion RT of U2af1-rs1 CpG island as an imprinting control region."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Amygdala; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary, and Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP TISSUE SPECIFICITY. RX PubMed=11809725; DOI=10.1093/hmg/11.2.165; RA van De Sluis B.A.J., Rothuizen J., Pearson P.L., van Oost B.A., RA Wijmenga C.; RT "Identification of a new copper metabolism gene by positional cloning RT in a purebred dog population."; RL Hum. Mol. Genet. 11:165-173(2002). RN [8] RP INTERACTION WITH ATP7B. RX PubMed=12968035; DOI=10.1074/jbc.C300391200; RA Tao T.Y., Liu F., Klomp L., Wijmenga C., Gitlin J.D.; RT "The copper toxicosis gene product Murr1 directly interacts with the RT Wilson disease protein."; RL J. Biol. Chem. 278:41593-41596(2003). RN [9] RP UBIQUITINATION BY XIAP. RX PubMed=14685266; DOI=10.1038/sj.emboj.7600031; RA Burstein E., Ganesh L., Dick R.D., van De Sluis B., Wilkinson J.C., RA Klomp L.W., Wijmenga C., Brewer G.J., Nabel G.J., Duckett C.S.; RT "A novel role for XIAP in copper homeostasis through regulation of RT MURR1."; RL EMBO J. 23:244-254(2004). RN [10] RP FUNCTION, AND INTERACTION WITH SCNN1D. RX PubMed=14645214; DOI=10.1074/jbc.M311155200; RA Biasio W., Chang T., McIntosh C.J., McDonald F.J.; RT "Identification of Murr1 as a regulator of the human delta epithelial RT sodium channel."; RL J. Biol. Chem. 279:5429-5434(2004). RN [11] RP FUNCTION, INTERACTION WITH RELA; REL; RELB; NFKB1; NFKB2; COMMD2; RP COMMD3; COMMD4; COMMD5; COMMD6; COMMD7; COMMD8 AND COMMD10, RP SUBCELLULAR LOCATION, 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 RT of MURR1."; RL J. Biol. Chem. 280:22222-22232(2005). RN [12] RP INTERACTION WITH COMMD6 AND NFKBIB, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=16573520; DOI=10.1042/BJ20051664; RA de Bie P., van de Sluis B., Burstein E., Duran K.J., Berger R., RA Duckett C.S., Wijmenga C., Klomp L.W.; RT "Characterization of COMMD protein-protein interactions in NF-kappaB RT signalling."; RL Biochem. J. 398:63-71(2006). RN [13] RP FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF RP MET-110 AND HIS-134, AND COPPER-BINDING. RX PubMed=17309234; DOI=10.1021/bi0620656; RA Narindrasorasak S., Kulkarni P., Deschamps P., She Y.M., Sarkar B.; RT "Characterization and copper binding properties of human COMMD1 RT (MURR1)."; RL Biochemistry 46:3116-3128(2007). RN [14] RP FUNCTION, SUBUNIT, INTERACTION WITH SOCS1 AND CUL2, AND IDENTIFICATION RP IN AN E3 UBIQUITIN LIGASE COMPLEX COMPOSED OF TCEB1/ELONGIN C; CUL2; RP SOCS1 AND RBX1. RX PubMed=17183367; DOI=10.1038/sj.emboj.7601489; RA Maine G.N., Mao X., Komarck C.M., Burstein E.; RT "COMMD1 promotes the ubiquitination of NF-kappaB subunits through a RT cullin-containing ubiquitin ligase."; RL EMBO J. 26:436-447(2007). RN [15] RP INTERACTION WITH ATP7B. RX PubMed=17919502; DOI=10.1053/j.gastro.2007.07.020; RA de Bie P., van de Sluis B., Burstein E., van de Berghe P.V., RA Muller P., Berger R., Gitlin J.D., Wijmenga C., Klomp L.W.; RT "Distinct Wilson's disease mutations in ATP7B are associated with RT enhanced binding to COMMD1 and reduced stability of ATP7B."; RL Gastroenterology 133:1316-1326(2007). RN [16] RP UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN2A. RX PubMed=18305112; DOI=10.1074/jbc.M708544200; RA Huang Y., Wu M., Li H.Y.; RT "Tumor suppressor ARF promotes non-classic proteasome-independent RT polyubiquitination of COMMD1."; RL J. Biol. Chem. 283:11453-11460(2008). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18940794; DOI=10.1074/jbc.M804766200; RA Burkhead J.L., Morgan C.T., Shinde U., Haddock G., Lutsenko S.; RT "COMMD1 forms oligomeric complexes targeted to the endocytic membranes RT via specific interactions with phosphatidylinositol 4,5- RT bisphosphate."; RL J. Biol. Chem. 284:696-707(2009). RN [19] RP FUNCTION, AND INTERACTION WITH SGK1 AND AKT1. RX PubMed=20237237; DOI=10.1152/ajprenal.00257.2009; RA Ke Y., Butt A.G., Swart M., Liu Y.F., McDonald F.J.; RT "COMMD1 downregulates the epithelial sodium channel through Nedd4-2."; RL Am. J. Physiol. 298:F1445-F1456(2010). RN [20] RP FUNCTION. RX PubMed=20048074; DOI=10.1158/0008-5472.CAN-09-1397; RA Thoms H.C., Loveridge C.J., Simpson J., Clipson A., Reinhardt K., RA Dunlop M.G., Stark L.A.; RT "Nucleolar targeting of RelA(p65) is regulated by COMMD1-dependent RT ubiquitination."; RL Cancer Res. 70:139-149(2010). RN [21] RP FUNCTION, AND INTERACTION WITH CCS. RX PubMed=20595380; DOI=10.1074/jbc.M110.101477; RA Vonk W.I., Wijmenga C., Berger R., van de Sluis B., Klomp L.W.; RT "Cu,Zn superoxide dismutase maturation and activity are regulated by RT COMMD1."; RL J. Biol. Chem. 285:28991-29000(2010). RN [22] RP FUNCTION, INTERACTION WITH HIF1A, AND TISSUE SPECIFICITY. RX PubMed=20458141; DOI=10.1172/JCI40583; RA van de Sluis B., Mao X., Zhai Y., Groot A.J., Vermeulen J.F., RA van der Wall E., van Diest P.J., Hofker M.H., Wijmenga C., Klomp L.W., RA Cho K.R., Fearon E.R., Vooijs M., Burstein E.; RT "COMMD1 disrupts HIF-1alpha/beta dimerization and inhibits human tumor RT cell invasion."; RL J. Clin. Invest. 120:2119-2130(2010). RN [23] RP SUBCELLULAR LOCATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, AND RP INTERACTION WITH CLU. RX PubMed=20068069; DOI=10.1158/1541-7786.MCR-09-0277; RA Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A., RA Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.; RT "Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF- RT kappaB activity in prostate cancer cells."; RL Mol. Cancer Res. 8:119-130(2010). RN [24] 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., RA Buerckstuemmer T., 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 [25] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21741370; DOI=10.1016/j.bbrc.2011.06.149; RA Chang T., Ke Y., Ly K., McDonald F.J.; RT "COMMD1 regulates the delta epithelial sodium channel (deltaENaC) RT through trafficking and ubiquitination."; RL Biochem. Biophys. Res. Commun. 411:506-511(2011). RN [26] RP FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B; CUL5 AND RP CUL7, AND 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) RT regulates Cullin RING ligases by preventing CAND1 (Cullin-associated RT Nedd8-dissociated protein 1) binding."; RL J. Biol. Chem. 286:32355-32365(2011). RN [27] RP FUNCTION, INTERACTION WITH CFTR, AND SUBCELLULAR LOCATION. RX PubMed=21483833; DOI=10.1371/journal.pone.0018334; RA Drevillon L., Tanguy G., Hinzpeter A., Arous N., de Becdelievre A., RA Aissat A., Tarze A., Goossens M., Fanen P.; RT "COMMD1-mediated ubiquitination regulates CFTR trafficking."; RL PLoS ONE 6:E18334-E18334(2011). RN [28] RP INTERACTION WITH ATP7A. RX PubMed=21667063; DOI=10.1007/s00018-011-0743-1; RA Vonk W.I., de Bie P., Wichers C.G., van den Berghe P.V., RA van der Plaats R., Berger R., Wijmenga C., Klomp L.W., RA van de Sluis B.; RT "The copper-transporting capacity of ATP7A mutants associated with RT Menkes disease is ameliorated by COMMD1 as a result of improved RT protein expression."; RL Cell. Mol. Life Sci. 69:149-163(2012). RN [29] RP FUNCTION, AND INTERACTION WITH SLC12A2. RX PubMed=23515529; DOI=10.1152/ajpcell.00394.2012; RA Smith L., Litman P., Liedtke C.M.; RT "COMMD1 interacts with the COOH terminus of NKCC1 in Calu-3 airway RT epithelial cells to modulate NKCC1 ubiquitination."; RL Am. J. Physiol. 305:C133-C146(2013). RN [30] 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 RT sodium channel."; RL Am. J. Physiol. 305:F80-F89(2013). RN [31] RP INTERACTION WITH CCDC22; CUL2 AND TCEB1. RX PubMed=23563313; DOI=10.1172/JCI66466; RA Starokadomskyy P., Gluck N., Li H., Chen B., Wallis M., Maine G.N., RA Mao X., Zaidi I.W., Hein M.Y., McDonald F.J., Lenzner S., Zecha A., RA Ropers H.H., Kuss A.W., McGaughran J., Gecz J., Burstein E.; RT "CCDC22 deficiency in humans blunts activation of proinflammatory NF- RT kappaB signaling."; RL J. Clin. Invest. 123:2244-2256(2013). RN [32] RP ACETYLATION BY EP300, AND INTERACTION WITH RELA. RX PubMed=25074812; DOI=10.1242/jcs.149328; RA O'Hara A., Simpson J., Morin P., Loveridge C.J., Williams A.C., RA Novo S.M., Stark L.A.; RT "p300-mediated acetylation of COMMD1 regulates its stability, and the RT ubiquitylation and nucleolar translocation of the RelA NF-kappaB RT subunit."; RL J. Cell Sci. 127:3659-3665(2014). RN [33] RP FUNCTION, IDENTIFICATION IN THE CCC COMPLEX, SUBCELLULAR LOCATION, AND RP SUBUNIT. 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 RT trafficking of the copper transporter ATP7A."; RL Mol. Biol. Cell 26:91-103(2015). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [35] RP STRUCTURE BY NMR OF 1-108. RX PubMed=17097678; DOI=10.1016/j.jmb.2006.10.030; RA Sommerhalter M., Zhang Y., Rosenzweig A.C.; RT "Solution structure of the COMMD1 N-terminal domain."; RL J. Mol. Biol. 365:715-721(2007). CC -!- FUNCTION: Proposed scaffold protein that is implicated in diverse CC physiological processes and whose function may be in part linked CC to its ability to regulate ubiquitination of specific cellular CC proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase CC (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 CC activity and dissociates CAND1 from CUL1 and CUL2 CC (PubMed:21778237). Promotes ubiquitination of NF-kappa-B subunit CC RELA and its subsequent proteasomal degradation. Down-regulates CC NF-kappa-B activity (PubMed:15799966, PubMed:17183367, CC PubMed:20048074). Involved in the regulation of membrane CC expression and ubiquitination of SLC12A2 (PubMed:23515529). CC Modulates Na(+) transport in epithelial cells by regulation of CC apical cell surface expression of amiloride-sensitive sodium CC channel (ENaC) subunits and by promoting their ubiquitination CC presumably involving NEDD4L. Promotes the localization of SCNN1D CC to recycling endosomes (PubMed:14645214, PubMed:20237237, CC PubMed:21741370). Promotes CFTR cell surface expression through CC regulation of its ubiquitination (PubMed:21483833). Down-regulates CC SOD1 activity by interfering with its homodimerization CC (PubMed:20595380). Plays a role in copper ion homeostasis. CC Involved in copper-dependent ATP7A trafficking between the trans- CC Golgi network and vesicles in the cell periphery; the function is CC proposed to depend on its association within the CCC complex and CC cooperation with the WASH complex on early endosomes CC (PubMed:25355947). Can bind one copper ion per monomer CC (PubMed:17309234). May function to facilitate biliary copper CC excretion within hepatocytes. Binds to phosphatidylinositol 4,5- CC bisphosphate (PtdIns(4,5)P2) (PubMed:18940794). Involved in the CC regulation of HIF1A-mediated transcription; competes with CC ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA CC binding and impaired transcriptional activation by HIF-1 CC (PubMed:20458141). {ECO:0000269|PubMed:14645214, CC ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:15799966, CC ECO:0000269|PubMed:16573520, ECO:0000269|PubMed:17183367, CC ECO:0000269|PubMed:17309234, ECO:0000269|PubMed:20048074, CC ECO:0000269|PubMed:20237237, ECO:0000269|PubMed:20458141, CC ECO:0000269|PubMed:20595380, ECO:0000269|PubMed:21483833, CC ECO:0000269|PubMed:21741370, ECO:0000269|PubMed:21778237, CC ECO:0000269|PubMed:23515529, ECO:0000269|PubMed:25355947}. CC -!- SUBUNIT: Monomer, homodimer. Can form heterodimers with other COMM CC domain-containing proteins but only certain combinations may exist CC in vivo (PubMed:23563313). Interacts (via COMM domain) with CC COMMD2, COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8 and COMMD10 CC (via COMM domain). Identified in a complex with an E3 ubiquitin CC ligase complex composed of TCEB1/elongin C, CUL2, SOCS1 and RBX1; CC in the complex interacts directly with SOCS1 and CUL2. Interacts CC directly with ATP7B (via the N-terminal region). Interacts with CC CCS, CDKN2A, RELA, REL, RELB, NFKB1/p105, NFKB2/p100, NFKBIB, CC SCNN1D, SCNN1B, CFTR, CLU, SGK1, AKT1, CUL1, CUL2, CUL3, CUL4A, CC CUL4B, CUL5, CUL7, HIF1A. Identified in a complex with NF-kappa-B. CC Interacts directly with SLC12A2. Interacts with CCDC22, CCDC93 and CC C16orf62; proposed to be a component of the CCC CC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and CC possibly other COMM domain-containing proteins), CCDC22, CCDC93 CC and C16orf62 (PubMed:25355947). Interacts with ATP7A CC (PubMed:21667063). {ECO:0000269|PubMed:12547404, CC ECO:0000269|PubMed:12968035, ECO:0000269|PubMed:14645214, CC ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:15799966, CC ECO:0000269|PubMed:16573520, ECO:0000269|PubMed:17183367, CC ECO:0000269|PubMed:17309234, ECO:0000269|PubMed:17919502, CC ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:20068069, CC ECO:0000269|PubMed:20237237, ECO:0000269|PubMed:20458141, CC ECO:0000269|PubMed:20595380, ECO:0000269|PubMed:21667063, CC ECO:0000269|PubMed:21778237, ECO:0000269|PubMed:23515529, CC ECO:0000269|PubMed:23563313, ECO:0000269|PubMed:23637203, CC ECO:0000269|PubMed:25355947, ECO:0000305|PubMed:23563313, CC ECO:0000305|PubMed:25355947}. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-1550112, EBI-1550112; CC P35670:ATP7B; NbExp=6; IntAct=EBI-1550112, EBI-11668501; CC O60826:CCDC22; NbExp=14; IntAct=EBI-1550112, EBI-3943153; CC Q9UBI1:COMMD3; NbExp=4; IntAct=EBI-1550112, EBI-714979; CC Q9H0A8:COMMD4; NbExp=3; IntAct=EBI-1550112, EBI-1550064; CC Q7Z4G1:COMMD6; NbExp=16; IntAct=EBI-1550112, EBI-1550081; CC Q9NX08:COMMD8; NbExp=2; IntAct=EBI-1550112, EBI-725694; CC Q13617:CUL2; NbExp=6; IntAct=EBI-1550112, EBI-456179; CC Q15369:ELOC; NbExp=2; IntAct=EBI-1550112, EBI-301231; CC P25963:NFKBIA; NbExp=3; IntAct=EBI-1550112, EBI-307386; CC Q04864:REL; NbExp=3; IntAct=EBI-1550112, EBI-307352; CC Q04206:RELA; NbExp=7; IntAct=EBI-1550112, EBI-73886; CC Q01201:RELB; NbExp=2; IntAct=EBI-1550112, EBI-357837; CC P51172:SCNN1D; NbExp=3; IntAct=EBI-1550112, EBI-2547114; CC O15524:SOCS1; NbExp=3; IntAct=EBI-1550112, EBI-968198; CC Q96BW1:UPRT; NbExp=4; IntAct=EBI-1550112, EBI-742943; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21778237}. CC Cytoplasm {ECO:0000269|PubMed:21778237}. Endosome membrane CC {ECO:0000269|PubMed:18940794}. Cytoplasmic vesicle CC {ECO:0000269|PubMed:18940794}. Early endosome CC {ECO:0000269|PubMed:21483833, ECO:0000269|PubMed:25355947}. CC Recycling endosome {ECO:0000269|PubMed:21483833, CC ECO:0000269|PubMed:21741370}. Note=Shuttles between nucleus and CC cytosol. Detected in perinuclear foci that may be aggresomes CC containing misfolded, ubiquitinated proteins. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N668-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N668-2; Sequence=VSP_055532; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in the liver, CC with lower expression in brain, lung, placenta, pancreas, small CC intestine, heart, skeletal muscle, kidney and placenta. Down- CC regulated in cancer tissues. {ECO:0000269|PubMed:11809725, CC ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:16573520, CC ECO:0000269|PubMed:20458141}. CC -!- PTM: Acetylated by EP300 ina stimuli-specific manner; protecting CC it from XIAP-mediated proteasomal degradation and required for CC interaction with RElA in response to stress. CC {ECO:0000269|PubMed:25074812}. CC -!- PTM: Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked CC polyubiquitination. Ubiquitinated by XIAP, leading to its CC proteasomal degradation. {ECO:0000269|PubMed:14685266, CC ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:20068069}. 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; AB178811; BAD18972.1; -; mRNA. DR EMBL; AK294203; BAG57515.1; -; mRNA. DR EMBL; AC018462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107081; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116652; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009266; AAH09266.2; -; mRNA. DR EMBL; BC022046; AAH22046.1; -; mRNA. DR CCDS; CCDS1869.1; -. [Q8N668-1] DR RefSeq; NP_689729.1; NM_152516.3. [Q8N668-1] DR UniGene; Hs.468702; -. DR PDB; 2H2M; NMR; -; A=1-108. DR PDBsum; 2H2M; -. DR ProteinModelPortal; Q8N668; -. DR SMR; Q8N668; -. DR BioGrid; 127317; 76. DR CORUM; Q8N668; -. DR IntAct; Q8N668; 34. DR MINT; Q8N668; -. DR STRING; 9606.ENSP00000308236; -. DR iPTMnet; Q8N668; -. DR PhosphoSitePlus; Q8N668; -. DR BioMuta; COMMD1; -. DR DMDM; 51316026; -. DR EPD; Q8N668; -. DR MaxQB; Q8N668; -. DR PaxDb; Q8N668; -. DR PeptideAtlas; Q8N668; -. DR PRIDE; Q8N668; -. DR DNASU; 150684; -. DR Ensembl; ENST00000311832; ENSP00000308236; ENSG00000173163. [Q8N668-1] DR GeneID; 150684; -. DR KEGG; hsa:150684; -. DR UCSC; uc002sbp.4; human. [Q8N668-1] DR CTD; 150684; -. DR DisGeNET; 150684; -. DR EuPathDB; HostDB:ENSG00000173163.10; -. DR GeneCards; COMMD1; -. DR HGNC; HGNC:23024; COMMD1. DR HPA; HPA034633; -. DR HPA; HPA049223; -. DR MIM; 607238; gene. DR neXtProt; NX_Q8N668; -. DR OpenTargets; ENSG00000173163; -. DR PharmGKB; PA134891368; -. DR eggNOG; ENOG410IWFF; Eukaryota. DR eggNOG; ENOG4111IWI; LUCA. DR GeneTree; ENSGT00390000012029; -. DR HOGENOM; HOG000236295; -. DR HOVERGEN; HBG051067; -. DR InParanoid; Q8N668; -. DR OMA; SRWDSGL; -. DR OrthoDB; EOG091G0XWL; -. DR PhylomeDB; Q8N668; -. DR TreeFam; TF332823; -. DR Reactome; R-HSA-8951664; Neddylation. DR ChiTaRS; COMMD1; human. DR EvolutionaryTrace; Q8N668; -. DR GeneWiki; COMMD1; -. DR GenomeRNAi; 150684; -. DR PRO; PR:Q8N668; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000173163; -. DR CleanEx; HS_COMMD1; -. DR ExpressionAtlas; Q8N668; baseline and differential. DR Genevisible; Q8N668; HS. DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0055070; P:copper ion homeostasis; IDA:UniProtKB. DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB. DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB. DR GO; GO:1902306; P:negative regulation of sodium ion transmembrane transport; IDA:UniProtKB. DR GO; GO:0048227; P:plasma membrane to endosome transport; IDA:UniProtKB. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0016567; P:protein ubiquitination; TAS:Reactome. DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR CDD; cd04749; Commd1_MURR1; 1. DR InterPro; IPR017920; COMM. DR InterPro; IPR033776; COMMD1_N. DR InterPro; IPR037351; Murr1. DR PANTHER; PTHR21199; PTHR21199; 1. DR Pfam; PF07258; COMM_domain; 1. DR Pfam; PF17221; COMMD1_N; 1. DR PROSITE; PS51269; COMM; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Copper; Cytoplasm; Cytoplasmic vesicle; Endosome; Lipid-binding; KW Membrane; Metal-binding; Nucleus; Protein transport; KW Reference proteome; Transcription; Transcription regulation; KW Transport; Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}. FT CHAIN 2 190 COMM domain-containing protein 1. FT /FTId=PRO_0000077384. FT DOMAIN 118 186 COMM. {ECO:0000255|PROSITE- FT ProRule:PRU00602}. FT REGION 2 123 Sufficient for interaction with SLC12A2. FT {ECO:0000269|PubMed:23515529}. FT REGION 125 190 Required for binding to PtdIns(4,5)P2. FT {ECO:0000269|PubMed:18940794}. FT METAL 101 101 Copper. {ECO:0000255}. FT METAL 110 110 Copper. {ECO:0000255}. FT METAL 134 134 Copper. {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330}. FT VAR_SEQ 155 190 ESEFLCLEFDEVKVNQILKTLSEVEESISTLISQPN -> V FT HCNQ (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055532. FT MUTAGEN 110 110 M->A: Reduces copper-induced fluorescence FT change. {ECO:0000269|PubMed:17309234}. FT MUTAGEN 134 134 H->A: Reduces copper-induced fluorescence FT change. {ECO:0000269|PubMed:17309234}. FT STRAND 3 5 {ECO:0000244|PDB:2H2M}. FT HELIX 9 13 {ECO:0000244|PDB:2H2M}. FT HELIX 15 18 {ECO:0000244|PDB:2H2M}. FT STRAND 23 25 {ECO:0000244|PDB:2H2M}. FT HELIX 32 39 {ECO:0000244|PDB:2H2M}. FT STRAND 41 43 {ECO:0000244|PDB:2H2M}. FT HELIX 48 52 {ECO:0000244|PDB:2H2M}. FT TURN 53 55 {ECO:0000244|PDB:2H2M}. FT HELIX 59 62 {ECO:0000244|PDB:2H2M}. FT TURN 63 65 {ECO:0000244|PDB:2H2M}. FT TURN 69 71 {ECO:0000244|PDB:2H2M}. FT TURN 73 75 {ECO:0000244|PDB:2H2M}. FT HELIX 76 79 {ECO:0000244|PDB:2H2M}. FT STRAND 82 84 {ECO:0000244|PDB:2H2M}. FT HELIX 88 94 {ECO:0000244|PDB:2H2M}. FT TURN 95 101 {ECO:0000244|PDB:2H2M}. FT STRAND 102 106 {ECO:0000244|PDB:2H2M}. SQ SEQUENCE 190 AA; 21178 MW; 9C810AECA67011DC CRC64; MAAGELEGGK PLSGLLNALA QDTFHGYPGI TEELLRSQLY PEVPPEEFRP FLAKMRGILK SIASADMDFN QLEAFLTAQT KKQGGITSDQ AAVISKFWKS HKTKIRESLM NQSRWNSGLR GLSWRVDGKS QSRHSAQIHT PVAIIELELG KYGQESEFLC LEFDEVKVNQ ILKTLSEVEE SISTLISQPN //