E2RK09 (UBP37_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

USP37

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	981 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 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 FZR1/CDH1 By similarity.
Domain	The KEN box 3 is required for interaction with FZR1/CDH1 and is essential for APC(CDH1)-mediated ubiquitination By similarity.
Post-translational modification	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.
Sequence similarities	Belongs to the peptidase C19 family. Contains 3 UIM (ubiquitin-interacting motif) repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Domain	Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein K11-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB protein K48-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 981	981	Ubiquitin carboxyl-terminal hydrolase 37		PRO_0000412645
Regions
	Repeat	706 – 725	20	UIM 1
	Repeat	808 – 827	20	UIM 2
	Repeat	830 – 849	20	UIM 3
	Motif	32 – 34	3	KEN box 1 By similarity
	Motif	71 – 79	9	D-box 1 By similarity
	Motif	96 – 105	10	D-box 2 By similarity
	Motif	160 – 168	9	D-box 3 By similarity
	Motif	223 – 225	3	KEN box 2 By similarity
	Motif	784 – 786	3	KEN box 3 By similarity
Sites
	Active site	352	1	Nucleophile By similarity
	Active site	908	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	215	1	Phosphoserine By similarity
	Modified residue	630	1	Phosphoserine; by CDK2 By similarity
	Modified residue	652	1	Phosphoserine By similarity
	Modified residue	654	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	E2RK09 [UniParc]. Last modified November 30, 2010. Version 1. Checksum: EBF79BF01F784AE5	FASTA	981	110,453
	10 20 30 40 50 60 MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV 70 80 90 100 110 120 VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLHAA MKPSQGSGSF 130 140 150 160 170 180 GAILGSRTSQ KETNRQLSYS DNQASSKRGS LETKDDIPFR KVLGNPGRGS IKTATGSGIT 190 200 210 220 230 240 VTRTIPSLTS ASTPLRSGLL ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK 250 260 270 280 290 300 YLTSSREKQL SLKQSEENRT SGLLPLQSSS FYGSRTGSKD YSSGSTNLDR TNVSGQTPSA 310 320 330 340 350 360 KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN TCYMNAILQS 370 380 390 400 410 420 LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC NSETKKDLLK KVKNAISATA 430 440 450 460 470 480 ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKTEPVPG EENSPDISAT RVYTCPVITN 490 500 510 520 530 540 LEFEVQHSII CKACGEIIPK REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC 550 560 570 580 590 600 EKCGGKCALV RHKFNRLPRI LILHLKRYSF NVTLSLNNKI GQQVIIPRYL TLSSHCTENT 610 620 630 640 650 660 KPPFTLGWSA HMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKSSLALCL DSDSEDELKR 670 680 690 700 710 720 SVALSQRLCE MSGCEQQQDD LEKDSKPCRI EPDKSELENS GFDGMSEEEL LAAVLEMSKR 730 740 750 760 770 780 EASPTLSHED DDKPTSSPDT GFAEDDIQEM PENQDPVETE KPKTVTEPDP ASFTEITKDC 790 800 810 820 830 840 DENKENKTPE GSQGEVDWLQ QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE 850 860 870 880 890 900 LSLQEFNNSF LDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI 910 920 930 940 950 960 GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY MHKEIFDELL 970 980 ETEKNSQALS MEVGKTTRQA L

References

[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.

Cross-references

Sequence databases
RefSeq	XP_545643.2. XM_545643.3.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCAFT00000023494; ENSCAFP00000021817; ENSCAFG00000014781.
GeneID	488523.
KEGG	cfa:488523.
Organism-specific databases
CTD	57695.
Phylogenomic databases
GeneTree	ENSGT00440000033542.
KO	K11850.
OMA	LQEFNNS.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR003903. Ubiquitin-int_motif. [Graphical view]
Pfam	PF00443. UCH. 1 hit. PF02809. UIM. 3 hits. [Graphical view]
SMART	SM00726. UIM. 4 hits. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50330. UIM. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	20861854.

Entry information

Entry name

UBP37_CANFA

Accession

Primary (citable) accession number: E2RK09
Secondary accession number(s): F1PGV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	November 30, 2010
Last modified:	October 3, 2012
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program