ID Q59GH5_HUMAN Unreviewed; 276 AA. AC Q59GH5; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 02-SEP-2026, entry version 77. DE RecName: Full=COP9 signalosome complex subunit 5 {ECO:0000256|ARBA:ARBA00014880}; DE AltName: Full=Jun activation domain-binding protein 1 {ECO:0000256|ARBA:ARBA00076748}; DE Flags: Fragment; 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 {ECO:0000313|EMBL:BAD92371.1}; RN [1] {ECO:0000313|EMBL:BAD92371.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:BAD92371.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|ARBA:ARBA00001968}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily. CC {ECO:0000256|ARBA:ARBA00006008}. 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; AB209134; BAD92371.1; -; mRNA. DR AlphaFoldDB; Q59GH5; -. DR MEROPS; M67.002; -. DR PeptideAtlas; Q59GH5; -. DR GO; GO:0008180; C:COP9 signalosome; IEA:UniProtKB-ARBA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:UniProtKB-ARBA. DR CDD; cd08069; MPN_RPN11_CSN5; 1. DR FunFam; 3.40.140.10:FF:000203; COP9 signalosome complex subunit 5; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1. DR InterPro; IPR040961; CSN5_C. DR InterPro; IPR000555; JAMM/MPN+_dom. DR InterPro; IPR050242; JAMM_MPN+_peptidase_M67A. DR InterPro; IPR037518; MPN. DR PANTHER; PTHR10410; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 -RELATED; 1. DR Pfam; PF18323; CSN5_C; 1. DR Pfam; PF01398; JAB; 1. DR SMART; SM00232; JAB_MPN; 1. DR SUPFAM; SSF102712; JAB1/MPN domain; 1. DR PROSITE; PS50249; MPN; 1. PE 2: Evidence at transcript level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01182}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU01182}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE- KW ProRule:PRU01182}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU01182}; Signalosome {ECO:0000256|ARBA:ARBA00022790}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01182}. FT DOMAIN 24..161 FT /note="MPN" FT /evidence="ECO:0000259|PROSITE:PS50249" FT MOTIF 107..120 FT /note="JAMM motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01182" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01182" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01182" FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01182" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD92371.1" SQ SEQUENCE 276 AA; 31259 MW; 1928491F16FC794E CRC64; NFTLYKEFNY IVILFCSHHY FKYCKISALA LLKMVMHARS GGNLEVMGLM LGKVDGETMI IMDSFALPVE GTETRVNAQA AAYEYMAAYI ENAKQVGRLE NAIGWYHSHP GYGCWLSGID VSTQMLNQQF QEPFVAVVID PTRTISAGKV NLGAFRTYPK GYKPPDEGPS EYQTIPLNKI EDFGVHCKQY YALEVSYFKS SLDRKLLELL WNKYWVNTLS SSSLLTNADY TTGQVFDLSE KLEQSEAQLG RGSFMLGLET HDRKSEDKLA KATRDR //