UBP5_MOUSE - dbPTM
UBP5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP5_MOUSE
UniProt AC P56399
Protein Name Ubiquitin carboxyl-terminal hydrolase 5
Gene Name Usp5
Organism Mus musculus (Mouse).
Sequence Length 858
Subcellular Localization
Protein Description Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity (By similarity)..
Protein Sequence MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRPKEEDTSAGTGDPPRKKPTRLAIGVEGGFDLTEDKFEFDEDVKIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHAFNLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRETGYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDMNQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVQVLFSIPDFQRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPALESGDGEQVPEQKEVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKVPLPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSAAESISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVVS
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
2Acetylation------MAELSEEAL
------CCCCCHHHH		26.83-
5Phosphorylation---MAELSEEALLSV
---CCCCCHHHHHHH		25.5425293948
20UbiquitinationLPTIRVPKAGDRVHK
HCCCCCCCCCCCCCC		63.24-
88PhosphorylationEEDTSAGTGDPPRKK
CCCCCCCCCCCCCCC		37.8229899451
148PhosphorylationDIVRDRVTSAVEALL
HHHHHHHHHHHHHHH		16.3228066266
149PhosphorylationIVRDRVTSAVEALLS
HHHHHHHHHHHHHHC		27.7128066266
156PhosphorylationSAVEALLSADSASRK
HHHHHHHCCCCCCCH		30.77-
159PhosphorylationEALLSADSASRKQEV
HHHHCCCCCCCHHHH		28.0629899451
161PhosphorylationLLSADSASRKQEVQA
HHCCCCCCCHHHHHH		43.92-
163UbiquitinationSADSASRKQEVQAWD
CCCCCCCHHHHHHHH		48.60-
163AcetylationSADSASRKQEVQAWD
CCCCCCCHHHHHHHH		48.607617787
184UbiquitinationSKHAFNLKQLDNPAR
HHHCCCHHHCCCCCC		50.33-
219S-nitrosylationLTDGSILCGRRYFDG
CCCCCEEECCCEECC		3.6721278135
219S-nitrosocysteineLTDGSILCGRRYFDG
CCCCCEEECCCEECC		3.67-
223PhosphorylationSILCGRRYFDGSGGN
CEEECCCEECCCCCC		12.5025195567
252PhosphorylationAVKLGTITPDGADVY
EEEECEECCCCCCEE		18.37-
291UbiquitinationLKMQKTDKTMTELEI
HHCCCCCCCCCEEEE		45.48-
292PhosphorylationKMQKTDKTMTELEID
HCCCCCCCCCEEEEE		31.9425266776
294PhosphorylationQKTDKTMTELEIDMN
CCCCCCCCEEEEECH		42.5225266776
318UbiquitinationQESGVPLKPLFGPGY
HHHCCCCCCCCCCCC		33.34-
353AcetylationSIPDFQRKYVDKLEK
CCCHHHHHHHHHHHH		38.5522826441
353UbiquitinationSIPDFQRKYVDKLEK
CCCHHHHHHHHHHHH		38.55-
357UbiquitinationFQRKYVDKLEKIFQN
HHHHHHHHHHHHHHC		48.80-
357AcetylationFQRKYVDKLEKIFQN
HHHHHHHHHHHHHHC		48.8022826441
360AcetylationKYVDKLEKIFQNAPT
HHHHHHHHHHHCCCC		60.2923954790
360UbiquitinationKYVDKLEKIFQNAPT
HHHHHHHHHHHCCCC		60.29-
379UbiquitinationDFSTQVAKLGHGLLS
CHHHHHHHHCCCHHC		57.03-
391UbiquitinationLLSGEYSKPALESGD
HHCCCCCCCHHHCCC		33.15-
396PhosphorylationYSKPALESGDGEQVP
CCCCHHHCCCCCCCC		42.9329514104
406UbiquitinationGEQVPEQKEVQDGIA
CCCCCCHHHHCCCCH		59.18-
418UbiquitinationGIAPRMFKALIGKGH
CCHHHHHHHHHCCCC		32.70-
418AcetylationGIAPRMFKALIGKGH
CCHHHHHHHHHCCCC		32.7022826441
423UbiquitinationMFKALIGKGHPEFST
HHHHHHCCCCCCCCC		47.23-
453PhosphorylationMVERNCRSSENPNEV
HHHHHCCCCCCHHHH		44.1723684622
454PhosphorylationVERNCRSSENPNEVF
HHHHCCCCCCHHHHH		23.2629899451
468UbiquitinationFRFLVEEKIKCLATE
HHHHHHHHHHHHHCC		33.68-
476UbiquitinationIKCLATEKVKYTQRV
HHHHHCCCCCCCCCC		39.41-
499UbiquitinationPMDAALNKEELLEYE
CCCHHCCHHHHHHHH		54.11-
532GlutathionylationAQVPFSSCLEAYGAP
CCCCHHHHHHHHCCC		3.7424333276
553UbiquitinationWSTALQAKSVAVKTT
HHHHHHHHCCEEECC		32.28-
558UbiquitinationQAKSVAVKTTRFASF
HHHCCEEECCEECCC		34.15-
574UbiquitinationDYLVIQIKKFTFGLD
CEEEEEEEEEEECCC		26.01-
575UbiquitinationYLVIQIKKFTFGLDW
EEEEEEEEEEECCCC		51.79-
575AcetylationYLVIQIKKFTFGLDW
EEEEEEEEEEECCCC		51.7922826441
585UbiquitinationFGLDWVPKKLDVSIE
ECCCCCCCEECEEEE		57.24-
586UbiquitinationGLDWVPKKLDVSIEM
CCCCCCCEECEEEEC		43.80-
590PhosphorylationVPKKLDVSIEMPEEL
CCCEECEEEECCCCC		16.7025338131
623PhosphorylationDIAPPLVTPDEPKGS
CCCCCCCCCCCCCCC		32.4825521595
675UbiquitinationFPMDACRKAVYYTGN
CCHHHHCEEEEECCC		41.93-
679PhosphorylationACRKAVYYTGNSGAE
HHCEEEEECCCHHHH		11.11-
743UbiquitinationFSRDQALKALRATNN
CCHHHHHHHHHHHCC		48.68-
743AcetylationFSRDQALKALRATNN
CCHHHHHHHHHHHCC		48.6822826441
743MalonylationFSRDQALKALRATNN
CCHHHHHHHHHHHCC		48.6826320211
751PhosphorylationALRATNNSLERAVDW
HHHHHCCHHHHHHHH		33.4125521595
775PhosphorylationAEAAMDISEGRSAAE
HHHHHCHHHCCHHHH		29.7222817900
779PhosphorylationMDISEGRSAAESISE
HCHHHCCHHHHHHHH		42.5625521595
783PhosphorylationEGRSAAESISESVPV
HCCHHHHHHHHCCCC		27.0425521595
785PhosphorylationRSAAESISESVPVGP
CHHHHHHHHCCCCCC		32.8525521595
787PhosphorylationAAESISESVPVGPKV
HHHHHHHCCCCCCCC		25.5725619855
793UbiquitinationESVPVGPKVRDGPGK
HCCCCCCCCCCCCCH		43.93-
813PhosphorylationFISHMGTSTMCGHYV
EEECCCCCCCCCEEE		14.39-
836UbiquitinationWVIYNDQKVCASEKP
EEEECCCEEECCCCC		41.99-
842UbiquitinationQKVCASEKPPKDLGY
CEEECCCCCCCCCCE		65.21-
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

Oops, there are no upstream regulatory protein records of UBP5_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP5_MOUSE !!
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 UBP5_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBP5_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP5_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-623, AND MASSSPECTROMETRY.

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