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UniProtKB/Swiss-Prot entry Q8R5H1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UBP15_MOUSE
Primary accession number Q8R5H1
Secondary accession number Q3UL25
Integrated into Swiss-Prot on February 22, 2003
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Ubiquitin carboxyl-terminal hydrolase 15
Synonyms EC 3.1.2.15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Deubiquitinating enzyme 15
Gene name
Name: Usp15
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6;
DOI=10.1007/s00335-002-3035-0; PubMed=12532266 [NCBI, ExPASy, EBI, Israel, Japan]
Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A., Baker R.T.;
"Isolation and characterization of the mouse ubiquitin-specific protease Usp15.";
Mamm. Genome 14:31-46(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
STRAIN=C57BL/6J;
TISSUE=Corpora quadrigemina, Testis, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF468037; AAL77418.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK046332; BAC32683.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK083303; BAC38854.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK145749; BAE26626.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_081880.2; -.
UniGene Mm.244209
3D structure databases
HSSP Q93009; 1NB8. [HSSP ENTRY / PDB]
SMR Q8R5H1; 1-120.
ModBase Q8R5H1.
Protein family/group databases
MEROPS C19.022; -.
PTM databases
PhosphoSite Q8R5H1; -.
Organism-specific databases
MGI MGI:101857; Usp15.
Gene expression databases
ArrayExpress Q8R5H1; -.
CleanEx MM_USP15; -.
GermOnline ENSMUSG00000020124; Mus musculus.
Ontologies
GO
GO:0004221; Molecular function: ubiquitin thiolesterase activity (inferred from electronic annotation from InterPro).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006615; Pept_C19_N_1.
IPR010460; Pept_C19_N_2.
IPR001394; Peptidase_C19.
Graphical view of domain structure.
Pfam PF06337; DUF1055; 1.
PF00443; UCH; 1.
Pfam graphical view of domain structure.
SMART SM00695; DUSP; 1.
SMART graphical view of domain structure.
PROSITE PS51283; DUSP; 1.
PS00972; UCH_2_1; 1.
PS00973; UCH_2_2; 1.
PS50235; UCH_2_3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8R5H1.
Genome annotation databases
Ensembl ENSMUSG00000020124; Mus musculus. [Contig view]
GeneID 14479; -.
KEGG mmu:14479; -.
Phylogenomic databases
HOGENOM Q8R5H1; -.
HOVERGEN Q8R5H1; -.
Other
NextBio 286150; -.
SOURCE Usp15; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative splicing; Hydrolase; Phosphoprotein; Protease; Thiol protease; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   981  980     Ubiquitin carboxyl-terminal hydrolase 15. PRO_0000080642
DOMAIN   7   118  112     DUSP. 
ACT_SITE   298   298        By similarity. 
ACT_SITE   883   883        By similarity. 
ACT_SITE   891   891        By similarity. 
MOD_RES   2     2        N-acetylalanine (By similarity). 
MOD_RES   229   229        Phosphoserine (By similarity). 
MOD_RES   961   961        Phosphoserine (By similarity). 
MOD_RES   965   965        Phosphoserine (By similarity). 
VAR_SEQ   18    25        TLLKTSLR -> DAWLKPRSG (in isoform 2). VSP_005262
VAR_SEQ   209   227        LVIEQKNEDGTWPRGPSTP -> PRCIQFFNFTKDLSFISIK (in isoform 4). VSP_005265
VAR_SEQ   228   981        Missing (in isoform 4). VSP_005266
VAR_SEQ   228   256        Missing (in isoform 2). VSP_005263
VAR_SEQ   229   981        Missing (in isoform 3). VSP_005264
Sequence information
Length: 981 AA [This is the length of the unprocessed precursor] Molecular weight: 112325 Da [This is the MW of the unprocessed precursor] CRC64: 6D5377C3FEA6E40A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV 

        70         80         90        100        110        120 
YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ 

       130        140        150        160        170        180 
GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFN IPDEKEARLW 

       190        200        210        220        230        240 
NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK 

       250        260        270        280        290        300 
ISPSSLSNNY NNINNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM 

       310        320        330        340        350        360 
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW SGKFSYVTPR 

       370        380        390        400        410        420 
AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR KKPYIQLKDA DGRPDKVVAE 

       430        440        450        460        470        480 
EAWENHLKRN DSIIVDIFHG LFKSTLVCPE CAKISVTFDP FCYLTLPLPM KKERSLEVYL 

       490        500        510        520        530        540 
VRMDPLAKPM QYKVIVPKIG NILDLCTALS ALSGVPADKM IVTDIYNHRF HRIFAVDENL 

       550        560        570        580        590        600 
SSIMERDDIY VFEININRAE DTEHVVIPVC LREKFRHSSY THHTGSSLFG QPFLMAIPRN 

       610        620        630        640        650        660 
NTEDKLYNLL LLRMCRYVKM STETEETDGH LRCCEDQNIN GNGPNGLHEE GSPSEMETDE 

       670        680        690        700        710        720 
PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEETC KGQLTGHKKR LFTFQFNNLG 

       730        740        750        760        770        780 
NNDINYIKDD TSHIRFDDRQ LRLDERSFLA LDWDPDLKKR YFDENAAEDF EKHESVEYKP 

       790        800        810        820        830        840 
PKRPFVKLKD CIELFTTKEK LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY 

       850        860        870        880        890        900 
SRYMRDKLDT LVDFPISDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD 

       910        920        930        940        950        960 
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG ASAATGIPLE 

       970        980 
SDEDSNDNDN DLENENCMHT N 

Q8R5H1 in FASTA format

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