ID COMD1_HUMAN Reviewed; 190 AA. AC Q8N668; Q96GS0; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 28-JUL-2009, entry version 48. 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]. 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]. 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]. 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]. 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 [5] 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 [6] 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 [7] RP INTERACTION WITH COMMD7. 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 [8] RP FUNCTION, INTERACTION WITH COMMD6 AND NFKBIB, SUBCELLULAR LOCATION, RP AND TISSUE 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). CC -!- FUNCTION: Inhibits TNF-induced NFKB1 activation. May function to CC facilitate biliary copper excretion within hepatocytes. CC -!- SUBUNIT: Interacts directly with COMMD6 and the N-terminal region CC of ATP7B. Interacts with NFKBIB and COMMD7. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-1550112, EBI-1550112; CC Q9Y6G5:COMMD10; NbExp=1; IntAct=EBI-1550112, EBI-1550310; CC Q86X83:COMMD2; NbExp=1; IntAct=EBI-1550112, EBI-1550220; CC Q9UBI1:COMMD3; NbExp=2; IntAct=EBI-1550112, EBI-714979; CC Q9H0A8:COMMD4; NbExp=1; IntAct=EBI-1550112, EBI-1550064; CC Q9GZQ3:COMMD5; NbExp=1; IntAct=EBI-1550112, EBI-1550256; CC Q7Z4G1:COMMD6; NbExp=1; IntAct=EBI-1550112, EBI-1550081; CC Q86VX2:COMMD7; NbExp=1; IntAct=EBI-1550112, EBI-1550280; CC Q9NX08:COMMD8; NbExp=1; IntAct=EBI-1550112, EBI-725694; CC Q13616:CUL1; NbExp=1; IntAct=EBI-1550112, EBI-359390; CC P19838-2:NFKB1; NbExp=1; IntAct=EBI-1550112, EBI-1452242; CC Q00653-2:NFKB2; NbExp=1; IntAct=EBI-1550112, EBI-307345; CC P25963:NFKBIA; NbExp=2; IntAct=EBI-1550112, EBI-307386; CC Q04864:REL; NbExp=1; IntAct=EBI-1550112, EBI-307352; CC Q04206:RELA; NbExp=2; IntAct=EBI-1550112, EBI-73886; CC Q01201:RELB; NbExp=1; IntAct=EBI-1550112, EBI-357837; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. CC -!- TISSUE SPECIFICITY: Highest expression in the liver, with lower CC expression in brain, lung, placenta, pancreas, small intestine, CC heart, skeletal muscle, kidney and placenta. CC -!- SIMILARITY: Contains 1 COMM domain. 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; BC009266; AAH09266.2; -; mRNA. DR EMBL; BC022046; AAH22046.1; -; mRNA. DR IPI; IPI00171117; -. DR RefSeq; NP_689729.1; -. DR UniGene; Hs.468702; -. DR PDB; 2H2M; NMR; -; A=1-108. DR PDBsum; 2H2M; -. DR IntAct; Q8N668; 19. DR PRIDE; Q8N668; -. DR Ensembl; ENST00000311832; ENSP00000308236; ENSG00000173163; Homo sapiens. DR GeneID; 150684; -. DR KEGG; hsa:150684; -. DR UCSC; uc002sbp.1; human. DR GeneCards; GC02P062044; -. DR H-InvDB; HIX0002085; -. DR HGNC; HGNC:23024; COMMD1. DR MIM; 607238; gene. DR PharmGKB; PA134891368; -. DR HOGENOM; Q8N668; -. DR HOVERGEN; Q8N668; -. DR OMA; Q8N668; QIHTPVA. DR NextBio; 86500; -. DR ArrayExpress; Q8N668; -. DR Bgee; Q8N668; -. DR CleanEx; HS_COMMD1; -. DR GermOnline; ENSG00000173163; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR InterPro; IPR017920; COMM. DR InterPro; IPR009886; HCaRG. DR Pfam; PF07258; HCaRG; 1. DR PROSITE; PS51269; COMM; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Nucleus. FT CHAIN 1 190 COMM domain-containing protein 1. FT /FTId=PRO_0000077384. FT DOMAIN 118 186 COMM. 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 //