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 23-MAR-2010, entry version 56. 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). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. 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). 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 P51168:SCNN1B; NbExp=1; IntAct=EBI-1550112, EBI-2547187; CC P51172:SCNN1D; NbExp=2; IntAct=EBI-1550112, EBI-2547114; CC P51170:SCNN1G; NbExp=1; IntAct=EBI-1550112, EBI-2547354; 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; 22. DR MINT; MINT-4140741; -. DR STRING; Q8N668; -. DR PRIDE; Q8N668; -. DR Ensembl; ENST00000311832; ENSP00000308236; ENSG00000173163; Homo sapiens. DR GeneID; 150684; -. DR KEGG; hsa:150684; -. DR UCSC; uc002sbp.1; human. DR CTD; 150684; -. DR GeneCards; GC02P062044; -. DR H-InvDB; HIX0002085; -. DR HGNC; HGNC:23024; COMMD1. DR MIM; 607238; gene. DR PharmGKB; PA134891368; -. DR HOGENOM; HBG445090; -. DR HOVERGEN; HBG051067; -. DR InParanoid; Q8N668; -. DR OMA; NQSRWDN; -. DR PhylomeDB; Q8N668; -. DR NextBio; 86500; -. DR ArrayExpress; Q8N668; -. DR Bgee; Q8N668; -. DR CleanEx; HS_COMMD1; -. DR Genevestigator; Q8N668; -. 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; Acetylation; Complete proteome; Cytoplasm; Nucleus. FT INIT_MET 1 1 Removed. FT CHAIN 2 190 COMM domain-containing protein 1. FT /FTId=PRO_0000077384. FT DOMAIN 118 186 COMM. FT MOD_RES 2 2 N-acetylalanine. FT TURN 16 19 FT HELIX 32 39 FT STRAND 41 43 FT HELIX 48 52 FT TURN 53 55 FT HELIX 59 62 FT TURN 63 65 FT TURN 69 71 FT TURN 73 75 FT HELIX 76 79 FT HELIX 88 94 FT TURN 95 101 FT STRAND 102 106 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 //