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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).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 – 3521NucleophilePROSITE-ProRule annotation
Active sitei908 – 9081Proton acceptorPROSITE-ProRule annotation

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

Protein family/group databases

MEROPSiC19.053.

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 CDK2By similarity
Modified residuei652 – 6521PhosphoserineBy similarity
Modified residuei654 – 6541PhosphoserineBy 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).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).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 1By similarity
Motifi71 – 799D-box 1By similarity
Motifi96 – 10510D-box 2By similarity
Motifi160 – 1689D-box 3By similarity
Motifi223 – 2253KEN box 2By similarity
Motifi784 – 7863KEN box 3By 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.Curated
Contains 3 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00440000033542.
InParanoidiE2RK09.
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

        10         20         30         40         50
MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI
60 70 80 90 100
FQLSHNIKNV VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD
110 120 130 140 150
AVHQNRLHAA MKPSQGSGSF GAILGSRTSQ KETNRQLSYS DNQASSKRGS
160 170 180 190 200
LETKDDIPFR KVLGNPGRGS IKTATGSGIT VTRTIPSLTS ASTPLRSGLL
210 220 230 240 250
ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK YLTSSREKQL
260 270 280 290 300
SLKQSEENRT SGLLPLQSSS FYGSRTGSKD YSSGSTNLDR TNVSGQTPSA
310 320 330 340 350
KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN
360 370 380 390 400
TCYMNAILQS LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC
410 420 430 440 450
NSETKKDLLK KVKNAISATA ERFSGYMQND AHEFLSQCLD QLKEDMEKLN
460 470 480 490 500
KTWKTEPVPG EENSPDISAT RVYTCPVITN LEFEVQHSII CKACGEIIPK
510 520 530 540 550
REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC EKCGGKCALV
560 570 580 590 600
RHKFNRLPRI LILHLKRYSF NVTLSLNNKI GQQVIIPRYL TLSSHCTENT
610 620 630 640 650
KPPFTLGWSA HMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKSSLALCL
660 670 680 690 700
DSDSEDELKR SVALSQRLCE MSGCEQQQDD LEKDSKPCRI EPDKSELENS
710 720 730 740 750
GFDGMSEEEL LAAVLEMSKR EASPTLSHED DDKPTSSPDT GFAEDDIQEM
760 770 780 790 800
PENQDPVETE KPKTVTEPDP ASFTEITKDC DENKENKTPE GSQGEVDWLQ
810 820 830 840 850
QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE LSLQEFNNSF
860 870 880 890 900
LDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI
910 920 930 940 950
GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY
960 970 980
MHKEIFDELL ETEKNSQALS MEVGKTTRQA L
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...

Protein family/group databases

MEROPSi C19.053.

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.
InParanoidi E2RK09.
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: October 29, 2014
This is version 28 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