UBP37_MOUSE - dbPTM
UBP37_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP37_MOUSE
UniProt AC Q8C0R0
Protein Name Ubiquitin carboxyl-terminal hydrolase 37
Gene Name Usp37 {ECO:0000312|MGI:MGI:2442483}
Organism Mus musculus (Mouse).
Sequence Length 979
Subcellular Localization
Protein Description 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). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1..
Protein Sequence MSPLKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGIPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLHAAMKASQGSGSFGTILGSRTSQKETNRQLSYSDNQASSKRGSLETKDEIPFRKVLGSPGRGPIKTVTGGGMAVTRTIPSLTLTSTPLRSGLLENRTEKRKRMLSGSELTEDYPKENDSSSNNKAMTDPSRKYLTSCREKQLSLKQAEENRTSGLLPLQSSSFYGSRAGSKDYSSGVTNLDRCNVSSQTPSAKRSLGFLPQPTPLSVKKLRCNQDYAGWNRPRVPLSSHQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQSIPWKKIPFNALIRRFANLLIKKDICNSETKKELLKKVKNAISATAERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVLGEENLPDTSATKVFTCPVITNLEFEVQHSIICKACGETIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKLGQQVIIPRFLTLASHCTESTKPPVTLGWSAPVAISRPLRACQMMNSCITSPSAPSKKFTFKSKSSVTSCLDSDSEDELKRSVVLSQRLCDLPGNEQYQEDVEKDLKLCRLEPGKAELENSGFDRMSEEEVLAAVLEISRREASPVLSPEDDDKPTSSPDTGFAEDDIPEMPENPDAMEIEKSKTITEPGPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDVDREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFLDSLGSDEDSGNEDVFDMEYTEAEAEELKRNAETGALPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKTSQALSMEVGRAARQAS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSPLKIYGP
------CCCCCCCCC		38.6524719451
7Phosphorylation-MSPLKIYGPIRIRS
-CCCCCCCCCEEEEE		18.4324719451
26PhosphorylationITKWKEGSFEIVEKD
CCCCCCCCEEEEECC		22.3122817900
150PhosphorylationQASSKRGSLETKDEI
CHHHCCCCCCCCCCC		27.3725338131
165PhosphorylationPFRKVLGSPGRGPIK
CHHHHCCCCCCCCCE		21.7426824392
175PhosphorylationRGPIKTVTGGGMAVT
CCCCEEEECCCEEEE		35.0329895711
187PhosphorylationAVTRTIPSLTLTSTP
EEEEECCCCEEECCC		30.0929895711
189PhosphorylationTRTIPSLTLTSTPLR
EEECCCCEEECCCCC		32.1229895711
191PhosphorylationTIPSLTLTSTPLRSG
ECCCCEEECCCCCCC		25.8930482847
192PhosphorylationIPSLTLTSTPLRSGL
CCCCEEECCCCCCCC		31.0126643407
193PhosphorylationPSLTLTSTPLRSGLL
CCCEEECCCCCCCCC		22.5526643407
208AcetylationENRTEKRKRMLSGSE
CCCHHHHHHHCCCCC		53.9130988483
210OxidationRTEKRKRMLSGSELT
CHHHHHHHCCCCCCC		3.8117203969
212PhosphorylationEKRKRMLSGSELTED
HHHHHHCCCCCCCCC		30.8125619855
214PhosphorylationRKRMLSGSELTEDYP
HHHHCCCCCCCCCCC		26.5125619855
217PhosphorylationMLSGSELTEDYPKEN
HCCCCCCCCCCCCCC		23.8217203969
222AcetylationELTEDYPKENDSSSN
CCCCCCCCCCCCCCC		64.0230988489
226PhosphorylationDYPKENDSSSNNKAM
CCCCCCCCCCCCCCC		47.4419854140
231AcetylationNDSSSNNKAMTDPSR
CCCCCCCCCCCCHHH		43.7330988495
234PhosphorylationSSNNKAMTDPSRKYL
CCCCCCCCCHHHHHH		50.0119854140
302PhosphorylationQTPSAKRSLGFLPQP
CCCCCCHHCCCCCCC		31.9425619855
310PhosphorylationLGFLPQPTPLSVKKL
CCCCCCCCCCEEEEC		31.4525619855
313PhosphorylationLPQPTPLSVKKLRCN
CCCCCCCEEEECCCC		32.8525619855
415PhosphorylationKKVKNAISATAERFS
HHHHHHHHHHHHHHH		19.70-
417PhosphorylationVKNAISATAERFSGY
HHHHHHHHHHHHHHH		23.43-
627PhosphorylationQMMNSCITSPSAPSK
HHHHHHCCCCCCCCC		38.6223567750
628PhosphorylationMMNSCITSPSAPSKK
HHHHHCCCCCCCCCC		9.2823567750
630PhosphorylationNSCITSPSAPSKKFT
HHHCCCCCCCCCCEE		53.2123567750
646PhosphorylationKSKSSVTSCLDSDSE
CCCCCCCCCCCCCCH		15.5525619855
650PhosphorylationSVTSCLDSDSEDELK
CCCCCCCCCCHHHHH		30.0427149854
652PhosphorylationTSCLDSDSEDELKRS
CCCCCCCCHHHHHHH		51.3927149854
663PhosphorylationLKRSVVLSQRLCDLP
HHHHHHHHHHHHCCC		11.1422006019
698PhosphorylationGKAELENSGFDRMSE
CCHHHHCCCCCCCCH		31.3128066266
770PhosphorylationITEPGPASFTEITKD
CCCCCCCCHHEEECC		35.5226643407
772PhosphorylationEPGPASFTEITKDCD
CCCCCCHHEEECCCC		24.7926643407
775PhosphorylationPASFTEITKDCDENK
CCCHHEEECCCCCCC		18.0126643407
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
628SPhosphorylationKinaseCDK2P97377
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
628SPhosphorylation

-
628Subiquitylation

-
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UBP37_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBP37_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP37_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND THR-217, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory