ID UBP12_HUMAN Reviewed; 370 AA. AC O75317; A8K0X0; Q5VZV3; Q8TC49; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 07-JUL-2009, entry version 75. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 12; DE EC=3.1.2.15; DE AltName: Full=Ubiquitin thioesterase 12; DE AltName: Full=Ubiquitin-specific-processing protease 12; DE AltName: Full=Deubiquitinating enzyme 12; DE AltName: Full=Ubiquitin-hydrolyzing enzyme 1; GN Name=USP12; Synonyms=UBH1, USP12L1; 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 MEDLINE=98277453; PubMed=9615226; DOI=10.1006/geno.1998.5275; RA Hansen-Hagge T.E., Janssen J.W.G., Hameister H., Papa F.R., RA Zechner U., Seriu T., Jauch A., Becke D., Hochstrasser M., RA Bartram C.R.; RT "An evolutionarily conserved gene on human chromosome 5q33-q34, UBH1, RT encodes a novel deubiquitinating enzyme."; RL Genomics 49:411-418(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, RP INTERACTION WITH WDR48, AND MUTAGENESIS OF CYS-48. RX PubMed=19075014; DOI=10.1074/jbc.M808430200; RA Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.; RT "UAF1 is a subunit of multiple deubiquitinating enzyme complexes."; RL J. Biol. Chem. 284:5343-5351(2009). CC -!- FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating CC activity by itself and requires the interaction with WDR48 to have CC a high activity. Not involved in deubiquitination of CC monoubiquitinated FANCD2. CC -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O = CC ubiquitin + a thiol. CC -!- SUBUNIT: Interacts with WDR48. CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF022789; AAC23551.1; ALT_INIT; mRNA. DR EMBL; AK289685; BAF82374.1; -; mRNA. DR EMBL; AL158062; CAH70555.1; -; Genomic_DNA. DR EMBL; AL355473; CAH70555.1; JOINED; Genomic_DNA. DR EMBL; AL355473; CAI16331.1; -; Genomic_DNA. DR EMBL; AL158062; CAI16331.1; JOINED; Genomic_DNA. DR EMBL; CH471075; EAX08392.1; -; Genomic_DNA. DR EMBL; BC026072; AAH26072.1; -; mRNA. DR IPI; IPI00290893; -. DR RefSeq; NP_872294.1; -. DR UniGene; Hs.42400; -. DR HSSP; Q93009; 1NBF. DR MEROPS; C19.020; -. DR MEROPS; C19.062; -. DR Ensembl; ENSG00000152484; Homo sapiens. DR GeneID; 219333; -. DR GeneCards; GC13M026540; -. DR H-InvDB; HIX0011190; -. DR HGNC; HGNC:20485; USP12. DR HPA; HPA007288; -. DR MIM; 603091; gene. DR PharmGKB; PA27522; -. DR HOGENOM; O75317; -. DR HOVERGEN; O75317; -. DR OMA; O75317; QPRRKEN. DR BRENDA; 3.1.2.15; 247. DR NextBio; 90574; -. DR ArrayExpress; O75317; -. DR Bgee; O75317; -. DR CleanEx; HS_USP12; -. DR GermOnline; ENSG00000152484; Homo sapiens. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB. DR GO; GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB. DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS. DR InterPro; IPR001394; Peptidase_C19. DR Pfam; PF00443; UCH; 1. DR PROSITE; PS00972; UCH_2_1; 1. DR PROSITE; PS00973; UCH_2_2; 1. DR PROSITE; PS50235; UCH_2_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Protease; Thiol protease; KW Ubl conjugation pathway. FT CHAIN 1 370 Ubiquitin carboxyl-terminal hydrolase 12. FT /FTId=PRO_0000080634. FT ACT_SITE 48 48 Probable. FT ACT_SITE 308 308 By similarity. FT ACT_SITE 317 317 By similarity. FT MUTAGEN 48 48 C->S: Loss of activity. FT CONFLICT 173 173 H -> D (in Ref. 5; AAH26072). SQ SEQUENCE 370 AA; 42858 MW; 267EE6A3674F6440 CRC64; MEILMTVSKF ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC RPFREKVLAY KSQPRKKESL LTCLADLFHS IATQKKKVGV IPPKKFITRL RKENELFDNY MQQDAHEFLN YLLNTIADIL QEERKQEKQN GRLPNGNIDN ENNNSTPDPT WVHEIFQGTL TNETRCLTCE TISSKDEDFL DLSVDVEQNT SITHCLRGFS NTETLCSEYK YYCEECRSKQ EAHKRMKVKK LPMILALHLK RFKYMDQLHR YTKLSYRVVF PLELRLFNTS GDATNPDRMY DLVAVVVHCG SGPNRGHYIA IVKSHDFWLL FDDDIVEKID AQAIEEFYGL TSDISKNSES GYILFYQSRD //