E1C213 (UBP37_CHICK) 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

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	986 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 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 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).
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
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 – 986	986	Ubiquitin carboxyl-terminal hydrolase 37		PRO_0000412647
Regions
	Repeat	712 – 731	20	UIM 1
	Repeat	813 – 832	20	UIM 2
	Repeat	835 – 854	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	224 – 226	3	KEN box 2 By similarity
	Motif	789 – 791	3	KEN box 3 By similarity
Sites
	Active site	353	1	Nucleophile By similarity
	Active site	913	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	E1C213 [UniParc]. Last modified November 2, 2010. Version 1. Checksum: A1780CFB799F5970	FASTA	986	110,863
	10 20 30 40 50 60 MAPLKVHGPV RMRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNVGGIPKT FQLSHNIKSV 70 80 90 100 110 120 TLRPNGRKLC CLMLTLKDTS FLTIDKVPLK DANEMRMYLD AVHQDRVHTA GKPSQGSGSF 130 140 150 160 170 180 GGVLGSRTTQ KEANRQFSYI ENQAPPKRVT VESKDETPFR KVLGTPARAS VKNSSGTGAP 190 200 210 220 230 240 SNRVNVAASP TSSVPHRTGL LESRSEKRKR AQPPSSEMSE DYPKENDSST NNTAMSDPAW 250 260 270 280 290 300 KYLNSSREKQ LKLKQEEENR TSGVLPLQSS SYYGSRSSSK EYSTSSSTLD RSSVSSQTTS 310 320 330 340 350 360 AKRSLGFLSQ PAPLSVKKMR SNQDYTGWNK PRVPLSTHPQ QQLQGFSNLG NTCYMNAILQ 370 380 390 400 410 420 SLFSIQSFAN DLLKQGIPWK KIPLNALIRR FAHLLAKKDV SSPEVKKELL KKVKSAISAT 430 440 450 460 470 480 AERFSGYMQN DAHEFLSQCL DQLKEDMEKL NKTWKSEPVP NDDSSPGRAS DDLSATKVYT 490 500 510 520 530 540 CPVISNLEFE VQHSIICKTC GETVTKREQF NDLSIDLPRR KKLFPSRSIQ DSLDLFFRAE 550 560 570 580 590 600 EIEYSCEKCN GKSAVVTHKF NRLPRVLILH LKRYSFNVAL SLNHKVGQQV VIPRYLTLLS 610 620 630 640 650 660 HCTESTRLPL TLGWSAHSAI SRPLKASQMV NSCTISTSTP CRKGRFLRKE GLSELRSSTG 670 680 690 700 710 720 RKNLNRVHVF KEDVQDINSS LQVQRGIRKS SKRSKMEGDK PELGNAGFDG MSEDELLAAV 730 740 750 760 770 780 LEISKREASL SLSHDEDKPT SSPDTGFGDD EIQELPENLE TMETEKPKAP LESGPANFTE 790 800 810 820 830 840 ITKDFDENKE NKTPEGSQGE VDWLQQYDME REREEQELQQ ALAQSLQEQE AREQKEDDDL 850 860 870 880 890 900 KRATELSLQE FNSSLLDSVG SDEDSGNEDV LDMEYSEAEA EELKRNAETG ELPHSYRLIS 910 920 930 940 950 960 IVSHIGSTSS SGHYISDVYD IKKQSWFTYN DLEVSRTLET TVQCDRDRSG YIFFYMHKDI 970 980 FDELLETEKN AQPLSMEVGR SIRQPL

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AADN02016788 Genomic DNA. No translation available. AADN02016789 Genomic DNA. No translation available.
IPI	IPI00819033.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000038204; ENSGALP00000037410; ENSGALG00000011427.
Phylogenomic databases
GeneTree	ENSGT00440000033542.
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. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP37_CHICK

Accession

Primary (citable) accession number: E1C213
Secondary accession number(s): E1BU11

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	November 2, 2010
Last modified:	May 16, 2012
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program