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E1C1R4

- UBP47_CHICK

UniProt

E1C1R4 - UBP47_CHICK

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Protein
Ubiquitin carboxyl-terminal hydrolase 47
Gene
USP47
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER) By similarity.

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei196 – 1961Nucleophile By similarity
Active sitei502 – 5021Proton acceptor By similarity

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. monoubiquitinated protein deubiquitination Source: UniProtKB
  4. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
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 namesi
Name:USP47
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13751375Ubiquitin carboxyl-terminal hydrolase 47
PRO_0000408357Add
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 563377USP
Add
BLAST

Sequence similaritiesi

Contains 1 USP domain.

Phylogenomic databases

OMAiLCEISGI.
OrthoDBiEOG7M3HZD.
PhylomeDBiE1C1R4.
TreeFamiTF314142.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF14560. Ubiquitin_2. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E1C1R4-1 [UniParc]FASTAAdd to Basket

« Hide

MKEFVSMRLL PEDMFWSCRQ STLAEMKKKF AQVESAAEEP RVLCIIQDTT     50
NSKTVNERVT LNVPASTPLK KLFEDVASKV GYVNGTFDLV WGNGDNVTDM 100
TPIDQNSDKT ILDAGFEPGK KNFLHLTDKD GEQPHIMQEE SGTTEDSAQD 150
RFIGPLPREG SVGCTNDYVS QSYSYSSVLS KSETGYVGLV NQAMTCYLNS 200
LLQTLFMTPE FRNALYKWEF EESEEDPVTS IPYQLQRLFV LLQTSKKRAI 250
ETTDVTRSFG WDSSEAWQQH DVQELCRVMF DALEQKWKQT EQADLINQLY 300
QGKLKDYVRC LECGYEGWRI DTYLDIPLVI RPYGSNQAFA SVEEALHAFI 350
QPEILDGPNQ YFCERCKKKC DARKGLRFLH FPYLLTLQLK RFDFDYTTMH 400
RIKLNDRMTF PEELDMSIFI DVEDEKSPQT ESCTDSGAEN EGSCHSDQMS 450
NDFSNDDGVD EGICLESNSA AERIAKVGSE KNSLLYELFS VMVHSGSAAG 500
GHYYACIKSF SDDQWYSFND QHVSKITQED IKKTYGGSSG SRGYYSSAFA 550
SSTNAYMLIY RLKDPARNAK FLESHEYPDH IKQLVQKERE LEEQEKRQRE 600
IERNTCKIKL FCMHPTKQIM MENKLEVHKD RTLKEAVGIA YKLMDLEEAV 650
PLDCCRLVKY DEFHDYLERS YEGEEDTPMG LLLGGVKSTY MFDLLLETRR 700
PDQIFQCYKP GEVMVKVHVV DLKTESVAPP ISVRAYLNQT VSEFKQLISK 750
ATHLPAETMR VVLERCYNDL RLLTVSSKTL KAEGFFRSNK VFIESSESLD 800
RHVAYTDSHL WKLLDRHANT IRLYVSLPEQ SPGSQFRRSI YQKPSGDLGN 850
LDEACERVKG PAGNMKSVEA ILEESTEKLK SLSLQQQQQE GDNGDSSKST 900
EASDFENIES PSNEIDSSAS VENRELENQI QISDPENLQS EERSDSDVNN 950
DRSTSSVDSD ILSSSHSSDT LCNVDNAPIP LANGLDSHSI TSSRRSKANQ 1000
GKKETWDTAE EDSGTDSEYD ESGKSRGETQ YMYFKSEPYT ADEGSGEGQK 1050
WLMVHVDKRI TLSAFKQQLE PFVGVPSSHF KVFRVYASNQ EFESVRLNET 1100
LSSFSDDNKI TIRLGRALKK GEYRVKVYQL LVNEPEPCKF LLDAVFAKGM 1150
TVRQSKEELL PQLREQCGLD LTIDRFRLRK KTWKNPGTVF LDYHIYEEDI 1200
NISSNWEVFL EILDGVEKMK SMSQLAVLSR RWRPSEMKLD SFQEVVLESS 1250
SVEELKEKLS ELSGIPLENI EFAKGRGTFP CDISVLEIHQ DLDWNPKVST 1300
LNVWPLYICD DGAVIFYRDK TEELMELTDE QRNELMKKES SRLQKTGHRV 1350
TYSPRKEKAL KIYLDGAPNK DLTQD 1375
Length:1,375
Mass (Da):157,247
Last modified:November 2, 2010 - v1
Checksum:iE5929D1809146267
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AADN02030606 Genomic DNA. No translation available.
AADN02030607 Genomic DNA. No translation available.
UniGeneiGga.5374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AADN02030606 Genomic DNA. No translation available.
AADN02030607 Genomic DNA. No translation available.
UniGenei Gga.5374.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OMAi LCEISGI.
OrthoDBi EOG7M3HZD.
PhylomeDBi E1C1R4.
TreeFami TF314142.

Miscellaneous databases

PROi E1C1R4.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF14560. Ubiquitin_2. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiUBP47_CHICK
AccessioniPrimary (citable) accession number: E1C1R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: November 2, 2010
Last modified: May 14, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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