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E2RK09

- UBP37_CANFA

UniProt

E2RK09 - UBP37_CANFA

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Protein

Ubiquitin carboxyl-terminal hydrolase 37

Gene
USP37
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 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 cyclin-A (CCNA1 and CCNA2), 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. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-630 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2) 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 sitei352 – 3521Nucleophile By similarity
Active sitei908 – 9081Proton 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
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 37

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 981981Ubiquitin carboxyl-terminal hydrolase 37PRO_0000412645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei630 – 6301Phosphoserine; by CDK2 By similarity
Modified residuei652 – 6521Phosphoserine By similarity
Modified residuei654 – 6541Phosphoserine By similarity

Post-translational modificationi

Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1) complex during late mitosis, leading to its degradation. Able to mediate auto-deubiquitination By similarity.
Phosphorylated at Ser-630 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-630 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Interacts with FZR1/CDH1 By similarity.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini343 – 953611USPAdd
BLAST
Repeati706 – 72520UIM 1Add
BLAST
Repeati808 – 82720UIM 2Add
BLAST
Repeati830 – 84920UIM 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
Motifi223 – 2253KEN box 2 By similarity
Motifi784 – 7863KEN box 3 By similarity

Domaini

The KEN box 3 is required for interaction with FZR1/CDH1 and is essential for APC(CDH1)-mediated ubiquitination By similarity.

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00440000033542.
KOiK11850.
OMAiLQEFNNS.
OrthoDBiEOG7HMS09.

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. 4 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.

E2RK09-1 [UniParc]FASTAAdd to Basket

« Hide

MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI    50
FQLSHNIKNV VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD 100
AVHQNRLHAA MKPSQGSGSF GAILGSRTSQ KETNRQLSYS DNQASSKRGS 150
LETKDDIPFR KVLGNPGRGS IKTATGSGIT VTRTIPSLTS ASTPLRSGLL 200
ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK YLTSSREKQL 250
SLKQSEENRT SGLLPLQSSS FYGSRTGSKD YSSGSTNLDR TNVSGQTPSA 300
KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN 350
TCYMNAILQS LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC 400
NSETKKDLLK KVKNAISATA ERFSGYMQND AHEFLSQCLD QLKEDMEKLN 450
KTWKTEPVPG EENSPDISAT RVYTCPVITN LEFEVQHSII CKACGEIIPK 500
REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC EKCGGKCALV 550
RHKFNRLPRI LILHLKRYSF NVTLSLNNKI GQQVIIPRYL TLSSHCTENT 600
KPPFTLGWSA HMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKSSLALCL 650
DSDSEDELKR SVALSQRLCE MSGCEQQQDD LEKDSKPCRI EPDKSELENS 700
GFDGMSEEEL LAAVLEMSKR EASPTLSHED DDKPTSSPDT GFAEDDIQEM 750
PENQDPVETE KPKTVTEPDP ASFTEITKDC DENKENKTPE GSQGEVDWLQ 800
QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE LSLQEFNNSF 850
LDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI 900
GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY 950
MHKEIFDELL ETEKNSQALS MEVGKTTRQA L 981
Length:981
Mass (Da):110,453
Last modified:November 30, 2010 - v1
Checksum:iEBF79BF01F784AE5
GO

Sequence databases

RefSeqiXP_005640701.1. XM_005640644.1.
XP_005640702.1. XM_005640645.1.
XP_545643.2. XM_545643.4.

Genome annotation databases

EnsembliENSCAFT00000023494; ENSCAFP00000021817; ENSCAFG00000014781.
GeneIDi488523.
KEGGicfa:488523.

Cross-referencesi

Sequence databases

RefSeqi XP_005640701.1. XM_005640644.1.
XP_005640702.1. XM_005640645.1.
XP_545643.2. XM_545643.4.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000023494 ; ENSCAFP00000021817 ; ENSCAFG00000014781 .
GeneIDi 488523.
KEGGi cfa:488523.

Organism-specific databases

CTDi 57695.

Phylogenomic databases

GeneTreei ENSGT00440000033542.
KOi K11850.
OMAi LQEFNNS.
OrthoDBi EOG7HMS09.

Miscellaneous databases

NextBioi 20861854.

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. 4 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. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.

Entry informationi

Entry nameiUBP37_CANFA
AccessioniPrimary (citable) accession number: E2RK09
Secondary accession number(s): F1PGV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 26 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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