Primary Information |
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BoMiProt ID | Bomi10219 |
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Protein Name | Ubiquitin carboxyl-terminal hydrolase 37/Deubiquitinating enzyme 37/Ubiquitin thioesterase 37/Ubiquitin-specific-processing protease 37 |
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Organism | Bos taurus |
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Uniprot ID | F1N5V1 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001258921.1 |
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Aminoacid Length | 981 |
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Molecular Weight | 110398 |
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FASTA Sequence |
Download |
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Gene Name | USP37 |
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Gene ID | 407168 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | remove mono-ubiquitin or ubiquitin chains from substrate proteins.USP37 directly binds, deubiquitinates, and stabilizes SNAI1. which is an epithelial-mesenchymal transition (EMT)-inducing transcription factor, promotes tumor metastasis and resistance to apoptosis and chemotherapy.deubiquitinates Cdt1 and contributes to regulate DNA replication.USP37 is a DUB that associates with and antago-
nizes APCCDH1 following E2F-mediated USP37 transcription in G1. |
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Biochemical Properties | 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). |
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PTMs | Ubiquitination.Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|F1N5V1|UBP37_BOVIN Ubiquitin carboxyl-terminal hydrolase 37 OS=Bos taurus OX=9913 GN=USP37 PE=3 SV=1
MSPLKIHGPIRIRSMQTGITKWKEGSFEVVEKENKVSLVVHYNTGGIPRIFQLSHNIKNV
VLRPSGAKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLNAAMKPSQGSGSF
GAILGSRTSQKETNRQLSYSDNQVSSKRGSLETKDDTPFRKVLGNPSRGS*170IKAAAGNGVT
PARTIPSLTSTSTPLRSGLLENRTEKRKRMLS*212SGSELNEDYPKENDSSSNNKAMTDPSRK
YLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRTAAKDYSPGSTNLDRTNISSQTPSA
KRSLGFLPQPAPLSVKKLRCNQDYTGWNKPRVPLSSHQQQQLQGFSNLGNTCYMNAILQS
LFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATA
ERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKIEPVPGEENSPDISATRVYTCPVITN
LEFEVQHSIICKVCGEIIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSC
EKCGGKCALVRHKFNRLPRILILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENT
KPPFNLGWSAQMAVSRPLKASQMVNSCITS*630PSTPSKNFTFKSKTSLALSLDS*652DS*654EDELKR
SVALSHRLCEMSGSEQQQEDLEKDSKSCRIEPDKSELENSGFDGMSEEELLAAVLEISKR
EASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDSVETEKPKTITEPDPAS*772FTEITKDC
DENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATE
LSLQEFNNSFVDSLGSDEDSGNEDVLDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHI
GSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEASVQSDRDRSGYIFFYMHKEIFDELL
ETEKNSQALNLEVGKTTRQVS
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Predicted Disorder Regions | 115-191, 213-233, 259-282, 666-885 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | USP37 is a substrate of ubiquitination k11 by the APC/CCdh1 and its regulated during the cell cycle as USP37 levels increase at the G1/S boundary, and remain high during S and G2 phases.phosphoryla-tion of Ser-628 contributing to USP37 activation.Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis. |
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Bibliography | 1.Xiao Z, Chang L, Kim J, Zhang P, Hang Q, Yap S, Guo Y, Zhou Z, Zeng L, Hu X, Siverly A, Sun Y, Ma L. USP37 is a SNAI1 deubiquitinase. Am J Cancer Res. 2019 Dec 1;9(12):2749-2759. PMID: 31911859; PMCID: PMC6943346. 2.Hernández-Pérez S, Cabrera E, Amoedo H, Rodríguez-Acebes S, Koundrioukoff S, Debatisse M, Méndez J, Freire R. USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication. Mol Oncol. 2016 Oct;10(8):1196-206. doi: 10.1016/j.molonc.2016.05.008. Epub 2016 Jun 3. PMID: 27296872; PMCID: PMC5423201. 3.Huang X, Summers MK, Pham V, Lill JR, Liu J, Lee G, Kirkpatrick DS, Jackson PK, Fang G, Dixit VM. Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry. Mol Cell. 2011 May 20;42(4):511-23. doi: 10.1016/j.molcel.2011.03.027. PMID: 21596315. |