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E1C213

- UBP37_CHICK

UniProt

E1C213 - UBP37_CHICK

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Protein

Ubiquitin carboxyl-terminal hydrolase 37

Gene
USP37
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of APC/C target proteins, thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex 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 sitei353 – 3531Nucleophile By similarity
Active sitei913 – 9131Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: UniProtKB
  2. mitotic nuclear division Source: UniProtKB-KW
  3. protein K11-linked deubiquitination Source: UniProtKB
  4. protein K48-linked deubiquitination Source: UniProtKB
  5. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 37 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 37
Ubiquitin thioesterase 37
Ubiquitin-specific-processing protease 37
Gene namesi
Name:USP37
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 986986Ubiquitin carboxyl-terminal hydrolase 37PRO_0000412647Add
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 958615USPAdd
BLAST
Repeati712 – 73120UIM 1Add
BLAST
Repeati813 – 83220UIM 2Add
BLAST
Repeati835 – 85420UIM 3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 343KEN box 1 By similarity
Motifi71 – 799D-box 1 By similarity
Motifi96 – 10510D-box 2 By similarity
Motifi160 – 1689D-box 3 By similarity
Motifi224 – 2263KEN box 2 By similarity
Motifi789 – 7913KEN box 3 By similarity

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 USP domain.

Keywords - Domaini

Repeat

Phylogenomic databases

OrthoDBiEOG7HMS09.
PhylomeDBiE1C213.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR003903. Ubiquitin-int_motif.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02809. UIM. 3 hits.
[Graphical view]
SMARTiSM00726. UIM. 3 hits.
[Graphical view]
PROSITEiPS50330. UIM. 3 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E1C213-1 [UniParc]FASTAAdd to Basket

« Hide

MAPLKVHGPV RMRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNVGGIPKT    50
FQLSHNIKSV TLRPNGRKLC CLMLTLKDTS FLTIDKVPLK DANEMRMYLD 100
AVHQDRVHTA GKPSQGSGSF GGVLGSRTTQ KEANRQFSYI ENQAPPKRVT 150
VESKDETPFR KVLGTPARAS VKNSSGTGAP SNRVNVAASP TSSVPHRTGL 200
LESRSEKRKR AQPPSSEMSE DYPKENDSST NNTAMSDPAW KYLNSSREKQ 250
LKLKQEEENR TSGVLPLQSS SYYGSRSSSK EYSTSSSTLD RSSVSSQTTS 300
AKRSLGFLSQ PAPLSVKKMR SNQDYTGWNK PRVPLSTHPQ QQLQGFSNLG 350
NTCYMNAILQ SLFSIQSFAN DLLKQGIPWK KIPLNALIRR FAHLLAKKDV 400
SSPEVKKELL KKVKSAISAT AERFSGYMQN DAHEFLSQCL DQLKEDMEKL 450
NKTWKSEPVP NDDSSPGRAS DDLSATKVYT CPVISNLEFE VQHSIICKTC 500
GETVTKREQF NDLSIDLPRR KKLFPSRSIQ DSLDLFFRAE EIEYSCEKCN 550
GKSAVVTHKF NRLPRVLILH LKRYSFNVAL SLNHKVGQQV VIPRYLTLLS 600
HCTESTRLPL TLGWSAHSAI SRPLKASQMV NSCTISTSTP CRKGRFLRKE 650
GLSELRSSTG RKNLNRVHVF KEDVQDINSS LQVQRGIRKS SKRSKMEGDK 700
PELGNAGFDG MSEDELLAAV LEISKREASL SLSHDEDKPT SSPDTGFGDD 750
EIQELPENLE TMETEKPKAP LESGPANFTE ITKDFDENKE NKTPEGSQGE 800
VDWLQQYDME REREEQELQQ ALAQSLQEQE AREQKEDDDL KRATELSLQE 850
FNSSLLDSVG SDEDSGNEDV LDMEYSEAEA EELKRNAETG ELPHSYRLIS 900
IVSHIGSTSS SGHYISDVYD IKKQSWFTYN DLEVSRTLET TVQCDRDRSG 950
YIFFYMHKDI FDELLETEKN AQPLSMEVGR SIRQPL 986
Length:986
Mass (Da):110,863
Last modified:November 2, 2010 - v1
Checksum:iA1780CFB799F5970
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AADN02016788 Genomic DNA. No translation available.
AADN02016789 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AADN02016788 Genomic DNA. No translation available.
AADN02016789 Genomic DNA. No translation available.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OrthoDBi EOG7HMS09.
PhylomeDBi E1C213.

Miscellaneous databases

PROi E1C213.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR003903. Ubiquitin-int_motif.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02809. UIM. 3 hits.
[Graphical view ]
SMARTi SM00726. UIM. 3 hits.
[Graphical view ]
PROSITEi PS50330. UIM. 3 hits.
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 nameiUBP37_CHICK
AccessioniPrimary (citable) accession number: E1C213
Secondary accession number(s): E1BU11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: November 2, 2010
Last modified: September 3, 2014
This is version 21 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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