Q8BY87 (UBP47_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1376 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair 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 mutant phenotype Ref.6. Source: UniProtKB negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from sequence or structural similarity Ref.6. Source: UniProtKB negative regulation of transcription, DNA-dependent 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_component	SCF ubiquitin ligase complex Inferred from sequence or structural similarity Ref.6. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1376	1376	Ubiquitin carboxyl-terminal hydrolase 47		PRO_0000080677
Sites
	Active site	197	1	Nucleophile By similarity
	Active site	503	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	122	1	N6-acetyllysine By similarity
	Modified residue	832	1	Phosphoserine By similarity
	Modified residue	911	1	Phosphoserine Ref.4
	Modified residue	1016	1	Phosphothreonine Ref.5
Natural variations
	Alternative sequence	14 – 33	20	Missing in isoform 2.		VSP_014416
Experimental info
	Sequence conflict	341	1	A → G in BAC38411. Ref.1
	Sequence conflict	376 – 379	4	GLRF → VRDL in BAC38411. Ref.1
	Sequence conflict	562	1	R → G in AAI08426. Ref.3
	Sequence conflict	1174	1	I → T in AAI08426. Ref.3
	Sequence conflict	1178	1	R → H in BAC27195. Ref.1
	Sequence conflict	1200 – 1203	4	DINI → IYNF in BAC40073. Ref.1
	Sequence conflict	1257	1	R → Q in BAC27195. Ref.1
	Sequence conflict	1299 – 1301	3	VST → TRP in AAH12722. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 09729C3B691C3709	FASTA	1,376	157,455
	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
	Isoform 2 [UniParc]. Checksum: 8DB6A4751B43840C	FASTA	1,356	154,841
	10 20 30 40 50 60 MVPGEENQLV PKEIENAAEE PRVLCIIQDT TNSKTVSERI TLNLPASTPV RKLFEDVANK 70 80 90 100 110 120 VGYINGTFDL TRENGVTTAD MAPLDHTSDK SLLDANFEPG KKNFLHLTDK DGEPPQMLLE 130 140 150 160 170 180 DSNNVDDSVH DRFIGPLPRE GSVASTNDYV SQNYSYSSIL NKSETGYVGL VNQAMTCYLN 190 200 210 220 230 240 SLLQTLFMTP EFRNALYKWE FEDSEEDPVT SIPYQLQRLF VLLQTSKKRA IETTDVTRSF 250 260 270 280 290 300 GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL YQGKLKDYVR CLECGYEGWR 310 320 330 340 350 360 IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN QYFCERCKKK CDARKGLRFL 370 380 390 400 410 420 HFPYLLTLQL KRFDFDYTTM HRIKLNDRMS FPEELDMSTF IDIEDEKSPQ TESCTDSGAE 430 440 450 460 470 480 NEGSCHSDQM SNDFSTDDAV DEGICLESSS GSEKISKPGL EKNSLMYELF SVMVHSGSAA 490 500 510 520 530 540 GGHYYACIKS FSDDQWYSFN DQHVSRITQE DIKKTHGGSS GSRGYYSSAF ASSTNAYMLI 550 560 570 580 590 600 YRLKDPTRNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR EIERNTCKIK LFCLHPVKQV 610 620 630 640 650 660 MMENKLEVHK DKTLKEAVEM AYKMMDLEDV IPLDCCRLVK YDEFHDYLER SYEGEEDTPM 670 680 690 700 710 720 GLLLGGVKST YMFDLLLETR KPDQIFQSYK PGEVMVKVHV VDLKAETVAA PVTVRAYLNQ 730 740 750 760 770 780 TVTEFKQLIS KATHLPADSM RIVLERCYND LRLLSMPSKT LKAEGFFRSN KVFVESSETV 790 800 810 820 830 840 DHQAAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT AYQKAGGDSG NVDDDCERVK 850 860 870 880 890 900 GPAGNLKSVD AILEESTEKL KSLSLQQQQQ DGDNGDSSKS TETSDFENIE SPLNERGSST 910 920 930 940 950 960 SVDNRELEQH IQTSDPENFQ SEERSDSDVN NDRSTSSVDS DILSSSHSSD TLCNADSAQI 970 980 990 1000 1010 1020 PLANGLDSHS ITSSRRTKAN EGKKETWDTA EEDSGTDSEY DESGKSRGDM QYMYFKADPY 1030 1040 1050 1060 1070 1080 TADEGSGEGH KWLMVHVDKR ITLAAFKQHL EPFVGVLSSH FKVFRVYTSN QEFETVRLNE 1090 1100 1110 1120 1130 1140 TLSSFSDDNK ITIRLGRALK KGEYRVKVCQ LLVNEQEPCK FLLDAVFAKG MTVRQSKEEL 1150 1160 1170 1180 1190 1200 IPQLREQCGL DLSIDRFRLR KKTWKNPGTV FLDYHIYEED INISSNWEVF LEVLDGVEKM 1210 1220 1230 1240 1250 1260 KSMSQLAILT RRWRPAEMKL DPFQELVLES NSVDELREKL SEISGIPLED IEFAKGRGTF 1270 1280 1290 1300 1310 1320 PCDISVLDIH QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD RTEEVMELTD EQRNELMKKE 1330 1340 1350 SSRLQKTGHR VTYSPRKEKA LKIYLDGAPN KDVAQD

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00420143. IPI00608091.
RefSeq	NP_598519.2. NM_133758.3. NP_796223.2. NM_177249.3.
UniGene	Mm.16974.
3D structure databases
ProteinModelPortal	Q8BY87.
SMR	Q8BY87. Positions 182-596.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000081757.
Protein family/group databases
MEROPS	C19.055.
Proteomic databases
PaxDb	Q8BY87.
PRIDE	Q8BY87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000106653; ENSMUSP00000102264; ENSMUSG00000059263.
GeneID	74996.
KEGG	mmu:74996.
UCSC	uc009jgg.2. mouse. uc009jgh.2. mouse.
Organism-specific databases
CTD	55031.
MGI	MGI:1922246. Usp47.
Phylogenomic databases
eggNOG	COG5077.
GeneTree	ENSGT00630000089581.
HOVERGEN	HBG058854.
InParanoid	Q32NY0.
KO	K11857.
OMA	NKSETGY.
OrthoDB	EOG4BRWJW.
Gene expression databases
Bgee	Q8BY87.
CleanEx	MM_USP47.
Genevestigator	Q8BY87.
GermOnline	ENSMUSG00000059263. Mus musculus.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	341978.
SOURCE	Search...

Entry information

Entry name

UBP47_MOUSE

Accession

Primary (citable) accession number: Q8BY87
Secondary accession number(s): Q32NY0 , 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:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program