Q8C0R0 (UBP37_MOUSE) 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
Synonyms:	Kiaa1594

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	979 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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-628 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-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 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
Coding sequence diversity	Alternative splicing
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
Cellular_component	nucleus Inferred from electronic annotation. Source: Compara
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q8C0R0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 Ref.1 Ref.3 (identifier: Q8C0R0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     612-634: ISRPLRACQMMNSCITSPSAPSK → M

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 979	979	Ubiquitin carboxyl-terminal hydrolase 37		PRO_0000259610
Regions
	Repeat	704 – 723	20	UIM 1
	Repeat	806 – 825	20	UIM 2
	Repeat	828 – 847	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	222 – 224	3	KEN box 2 By similarity
	Motif	782 – 784	3	KEN box 3 By similarity
Sites
	Active site	350	1	Nucleophile By similarity
	Active site	906	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	214	1	Phosphoserine Ref.4
	Modified residue	217	1	Phosphothreonine Ref.4
	Modified residue	628	1	Phosphoserine; by CDK2 By similarity
	Modified residue	650	1	Phosphoserine By similarity
	Modified residue	652	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	612 – 634	23	ISRPL…SAPSK → M in isoform 2. Ref.1 Ref.3		VSP_052196
Experimental info
	Sequence conflict	622	1	M → V in AAI39092. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: FF11DB673C1CA902	FASTA	979	110,063
	10 20 30 40 50 60 MSPLKIYGPI RIRSMQTGIT KWKEGSFEIV EKDNRVSLLV HYNTGGIPRV FQLSHNIKNV 70 80 90 100 110 120 VLRPSGIKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLHAA MKASQGSGSF 130 140 150 160 170 180 GTILGSRTSQ KETNRQLSYS DNQASSKRGS LETKDEIPFR KVLGSPGRGP IKTVTGGGMA 190 200 210 220 230 240 VTRTIPSLTL TSTPLRSGLL ENRTEKRKRM LSGSELTEDY PKENDSSSNN KAMTDPSRKY 250 260 270 280 290 300 LTSCREKQLS LKQAEENRTS GLLPLQSSSF YGSRAGSKDY SSGVTNLDRC NVSSQTPSAK 310 320 330 340 350 360 RSLGFLPQPT PLSVKKLRCN QDYAGWNRPR VPLSSHQQQL QGFSNLGNTC YMNAILQSLF 370 380 390 400 410 420 SLQSFANDLL KQSIPWKKIP FNALIRRFAN LLIKKDICNS ETKKELLKKV KNAISATAER 430 440 450 460 470 480 FSGYVQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVLGEE NLPDTSATKV FTCPVITNLE 490 500 510 520 530 540 FEVQHSIICK ACGETIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK 550 560 570 580 590 600 CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKLGQ QVIIPRFLTL ASHCTESTKP 610 620 630 640 650 660 PVTLGWSAPV AISRPLRACQ MMNSCITSPS APSKKFTFKS KSSVTSCLDS DSEDELKRSV 670 680 690 700 710 720 VLSQRLCDLP GNEQYQEDVE KDLKLCRLEP GKAELENSGF DRMSEEEVLA AVLEISRREA 730 740 750 760 770 780 SPVLSPEDDD KPTSSPDTGF AEDDIPEMPE NPDAMEIEKS KTITEPGPAS FTEITKDCDE 790 800 810 820 830 840 NKENKTPEGS QGEVDWLQQY DVDREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS 850 860 870 880 890 900 LQEFNNSFLD SLGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGALPHSYR LISVVSHIGS 910 920 930 940 950 960 TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH KEIFDELLET 970 EKTSQALSME VGRAARQAS
	Isoform 2 [UniParc]. Checksum: 1ACD5A844FBCB4D3	FASTA	957	107,733
	10 20 30 40 50 60 MSPLKIYGPI RIRSMQTGIT KWKEGSFEIV EKDNRVSLLV HYNTGGIPRV FQLSHNIKNV 70 80 90 100 110 120 VLRPSGIKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLHAA MKASQGSGSF 130 140 150 160 170 180 GTILGSRTSQ KETNRQLSYS DNQASSKRGS LETKDEIPFR KVLGSPGRGP IKTVTGGGMA 190 200 210 220 230 240 VTRTIPSLTL TSTPLRSGLL ENRTEKRKRM LSGSELTEDY PKENDSSSNN KAMTDPSRKY 250 260 270 280 290 300 LTSCREKQLS LKQAEENRTS GLLPLQSSSF YGSRAGSKDY SSGVTNLDRC NVSSQTPSAK 310 320 330 340 350 360 RSLGFLPQPT PLSVKKLRCN QDYAGWNRPR VPLSSHQQQL QGFSNLGNTC YMNAILQSLF 370 380 390 400 410 420 SLQSFANDLL KQSIPWKKIP FNALIRRFAN LLIKKDICNS ETKKELLKKV KNAISATAER 430 440 450 460 470 480 FSGYVQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVLGEE NLPDTSATKV FTCPVITNLE 490 500 510 520 530 540 FEVQHSIICK ACGETIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK 550 560 570 580 590 600 CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKLGQ QVIIPRFLTL ASHCTESTKP 610 620 630 640 650 660 PVTLGWSAPV AMKFTFKSKS SVTSCLDSDS EDELKRSVVL SQRLCDLPGN EQYQEDVEKD 670 680 690 700 710 720 LKLCRLEPGK AELENSGFDR MSEEEVLAAV LEISRREASP VLSPEDDDKP TSSPDTGFAE 730 740 750 760 770 780 DDIPEMPENP DAMEIEKSKT ITEPGPASFT EITKDCDENK ENKTPEGSQG EVDWLQQYDV 790 800 810 820 830 840 DREREEQELQ QALAQSLQEQ EAWEQKEDDD LKRATELSLQ EFNNSFLDSL GSDEDSGNED 850 860 870 880 890 900 VFDMEYTEAE AEELKRNAET GALPHSYRLI SVVSHIGSTS SSGHYISDVY DIKKQAWFTY 910 920 930 940 950 NDLEVSKIQE AAVQSDRDRS GYIFFYMHKE IFDELLETEK TSQALSMEVG RAARQAS

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-779 (ISOFORM 2). Strain: C57BL/6J. Tissue: Testis and Urinary bladder.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-979 (ISOFORM 2). Tissue: Pancreatic islet.
[4]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND THR-217, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK030013 mRNA. Translation: BAC26734.1. AK035640 mRNA. Translation: BAC29135.1. AK173210 mRNA. Translation: BAD32488.1. BC139091 mRNA. Translation: AAI39092.1.
IPI	IPI00223928. IPI00269743.
RefSeq	NP_795946.2. NM_176972.4.
UniGene	Mm.471601. Mm.66568.
3D structure databases
HSSP	HSSP built from PDB template 1VJV based on UniProtKB P43593.
ProteinModelPortal	Q8C0R0.
SMR	Q8C0R0. Positions 4-106, 331-601.
ModBase	Search...
Protein family/group databases
MEROPS	C19.053.
PTM databases
PhosphoSite	Q8C0R0.
Proteomic databases
PaxDb	Q8C0R0.
PRIDE	Q8C0R0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000044260; ENSMUSP00000035445; ENSMUSG00000033364.
GeneID	319651.
KEGG	mmu:319651.
UCSC	uc007bmc.2. mouse.
Organism-specific databases
CTD	57695.
MGI	MGI:2442483. Usp37.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG279142.
GeneTree	ENSGT00440000033542.
HOGENOM	HOG000060197.
HOVERGEN	HBG055893.
InParanoid	B2RT12.
KO	K11850.
OrthoDB	EOG4S4PFQ.
Gene expression databases
Bgee	Q8C0R0.
CleanEx	MM_USP37.
Genevestigator	Q8C0R0.
GermOnline	ENSMUSG00000033364. Mus musculus.
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. 3 hits. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50330. UIM. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	USP37. mouse.
NextBio	395152.
SOURCE	Search...

Entry information

Entry name

UBP37_MOUSE

Accession

Primary (citable) accession number: Q8C0R0
Secondary accession number(s): B2RT12, Q69ZF6, Q8BZE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program