Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8BY87 (UBP47_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 47

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 47
Ubiquitin thioesterase 47
Ubiquitin-specific-processing protease 47
Gene names
Name:Usp47
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER) By similarity. Acts as a regulator of cell growth and genome integrity. May also indirectly regulates CDC25A expression at a transcriptional level. Ref.6

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Subunit structure

Interacts with BTRC and FBXW11. Interacts with POLB By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP47 subfamily.

Contains 1 USP domain.

Sequence caution

The sequence BAC27179.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC27195.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC38411.1 differs from that shown. Reason: Frameshift at position 109.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to UV

Inferred from mutant phenotype Ref.6. Source: UniProtKB

monoubiquitinated protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of G2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype Ref.6. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentSCF ubiquitin ligase complex

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BY87-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BY87-2)

The sequence of this isoform differs from the canonical sequence as follows:
     14-33: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13761376Ubiquitin carboxyl-terminal hydrolase 47
PRO_0000080677

Regions

Domain188 – 564377USP

Sites

Active site1971Nucleophile By similarity
Active site5031Proton acceptor By similarity

Amino acid modifications

Modified residue1221N6-acetyllysine By similarity
Modified residue8321Phosphoserine By similarity
Modified residue9111Phosphoserine Ref.4
Modified residue10161Phosphothreonine Ref.5

Natural variations

Alternative sequence14 – 3320Missing in isoform 2.
VSP_014416

Experimental info

Sequence conflict3411A → G in BAC38411. Ref.1
Sequence conflict376 – 3794GLRF → VRDL in BAC38411. Ref.1
Sequence conflict5621R → G in AAI08426. Ref.3
Sequence conflict11741I → T in AAI08426. Ref.3
Sequence conflict11781R → H in BAC27195. Ref.1
Sequence conflict1200 – 12034DINI → IYNF in BAC40073. Ref.1
Sequence conflict12571R → Q in BAC27195. Ref.1
Sequence conflict1299 – 13013VST → TRP in AAH12722. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 09729C3B691C3709

FASTA1,376157,455
        10         20         30         40         50         60 
MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVSERI 

        70         80         90        100        110        120 
TLNLPASTPV RKLFEDVANK VGYINGTFDL TRENGVTTAD MAPLDHTSDK SLLDANFEPG 

       130        140        150        160        170        180 
KKNFLHLTDK DGEPPQMLLE DSNNVDDSVH DRFIGPLPRE GSVASTNDYV SQNYSYSSIL 

       190        200        210        220        230        240 
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEDSEEDPVT SIPYQLQRLF 

       250        260        270        280        290        300 
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL 

       310        320        330        340        350        360 
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN 

       370        380        390        400        410        420 
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMS FPEELDMSTF 

       430        440        450        460        470        480 
IDIEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSTDDAV DEGICLESSS GSEKISKPGL 

       490        500        510        520        530        540 
EKNSLMYELF SVMVHSGSAA GGHYYACIKS FSDDQWYSFN DQHVSRITQE DIKKTHGGSS 

       550        560        570        580        590        600 
GSRGYYSSAF ASSTNAYMLI YRLKDPTRNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR 

       610        620        630        640        650        660 
EIERNTCKIK LFCLHPVKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEDV IPLDCCRLVK 

       670        680        690        700        710        720 
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQIFQSYK PGEVMVKVHV 

       730        740        750        760        770        780 
VDLKAETVAA PVTVRAYLNQ TVTEFKQLIS KATHLPADSM RIVLERCYND LRLLSMPSKT 

       790        800        810        820        830        840 
LKAEGFFRSN KVFVESSETV DHQAAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT 

       850        860        870        880        890        900 
AYQKAGGDSG NVDDDCERVK GPAGNLKSVD AILEESTEKL KSLSLQQQQQ DGDNGDSSKS 

       910        920        930        940        950        960 
TETSDFENIE SPLNERGSST SVDNRELEQH IQTSDPENFQ SEERSDSDVN NDRSTSSVDS 

       970        980        990       1000       1010       1020 
DILSSSHSSD TLCNADSAQI PLANGLDSHS ITSSRRTKAN EGKKETWDTA EEDSGTDSEY 

      1030       1040       1050       1060       1070       1080 
DESGKSRGDM QYMYFKADPY TADEGSGEGH KWLMVHVDKR ITLAAFKQHL EPFVGVLSSH 

      1090       1100       1110       1120       1130       1140 
FKVFRVYTSN QEFETVRLNE TLSSFSDDNK ITIRLGRALK KGEYRVKVCQ LLVNEQEPCK 

      1150       1160       1170       1180       1190       1200 
FLLDAVFAKG MTVRQSKEEL IPQLREQCGL DLSIDRFRLR KKTWKNPGTV FLDYHIYEED 

      1210       1220       1230       1240       1250       1260 
INISSNWEVF LEVLDGVEKM KSMSQLAILT RRWRPAEMKL DPFQELVLES NSVDELREKL 

      1270       1280       1290       1300       1310       1320 
SEISGIPLED IEFAKGRGTF PCDISVLDIH QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD 

      1330       1340       1350       1360       1370 
RTEEVMELTD EQRNELMKKE SSRLQKTGHR VTYSPRKEKA LKIYLDGAPN KDVAQD 

« Hide

Isoform 2 [UniParc].

Checksum: 8DB6A4751B43840C
Show »

FASTA1,356154,841

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-379 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-591 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-1376 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Cerebellum and Thymus.
[2]"Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1376.
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C3H/He and Czech II.
Tissue: Brain, Liver, Mammary gland and Mesenchymal stem cell.
[4]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival."
Peschiaroli A., Skaar J.R., Pagano M., Melino G.
Oncogene 29:1384-1393(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK030909 mRNA. Translation: BAC27179.1. Different initiation.
AK030963 mRNA. Translation: BAC27195.1. Different initiation.
AK041541 mRNA. Translation: BAC30979.1.
AK082114 mRNA. Translation: BAC38411.1. Frameshift.
AK087981 mRNA. Translation: BAC40073.1.
AK131138 mRNA. Translation: BAD21388.1.
BC012722 mRNA. Translation: AAH12722.1.
BC024117 mRNA. Translation: AAH24117.1.
BC089364 mRNA. Translation: AAH89364.1.
BC108425 mRNA. Translation: AAI08426.1.
CCDSCCDS40089.1. [Q8BY87-2]
RefSeqNP_598519.2. NM_133758.3. [Q8BY87-2]
NP_796223.2. NM_177249.3. [Q8BY87-1]
UniGeneMm.16974.

3D structure databases

ProteinModelPortalQ8BY87.
SMRQ8BY87. Positions 182-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BY87. 1 interaction.
MINTMINT-4110662.
STRING10090.ENSMUSP00000081757.

Protein family/group databases

MEROPSC19.055.

Proteomic databases

MaxQBQ8BY87.
PaxDbQ8BY87.
PRIDEQ8BY87.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000106653; ENSMUSP00000102264; ENSMUSG00000059263. [Q8BY87-2]
GeneID74996.
KEGGmmu:74996.
UCSCuc009jgg.2. mouse. [Q8BY87-2]
uc009jgh.2. mouse. [Q8BY87-1]

Organism-specific databases

CTD55031.
MGIMGI:1922246. Usp47.

Phylogenomic databases

eggNOGCOG5077.
GeneTreeENSGT00740000115066.
HOVERGENHBG058854.
InParanoidQ32NY0.
KOK11857.
OMALCEISGI.
OrthoDBEOG7M3HZD.
PhylomeDBQ8BY87.
TreeFamTF314142.

Gene expression databases

BgeeQ8BY87.
CleanExMM_USP47.
GenevestigatorQ8BY87.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF14560. Ubiquitin_2. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio341978.
PROQ8BY87.
SOURCESearch...

Entry information

Entry nameUBP47_MOUSE
AccessionPrimary (citable) accession number: Q8BY87
Secondary accession number(s): Q32NY0 expand/collapse secondary AC list , Q5EBP2, Q6KAR9, Q80V06, Q8BHU1, Q8BI15, Q8BI16, Q8BUW4, Q91X25
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot