UBP13_HUMAN - dbPTM
UBP13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP13_HUMAN
UniProt AC Q92995
Protein Name Ubiquitin carboxyl-terminal hydrolase 13
Gene Name USP13
Organism Homo sapiens (Human).
Sequence Length 863
Subcellular Localization
Protein Description Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data..
Protein Sequence MQRRGALFGMPGGSGGRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKIFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDMGYPLAVKLGTITPDGADVYSFQEEEPVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKLRVSEWEVIQESGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAEANRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSIDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMNQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIIVHMEEPDFAEPLTMPGYGGAASAGASVFGASGLDNQPPEEIVAIITSMGFQRNQAIQALRATNNNLERALDWIFSHPEFEEDSDFVIEMENNANANIISEAKPEGPRVKDGSGTYELFAFISHMGTSTMSGHYICHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS
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
4Methylation----MQRRGALFGMP
----CCCCCCCCCCC		20.1854560483
14PhosphorylationLFGMPGGSGGRKMAA
CCCCCCCCCCCCCCC		43.9521815630
18UbiquitinationPGGSGGRKMAAGDIG
CCCCCCCCCCCCCHH		35.8421906983
34PhosphorylationLLVPHMPTIRVPRSG
HHCCCCCEEECCCCC		17.53-
53PhosphorylationKNECAFSYDSPNSEG
CCCEEEECCCCCCCC		17.6222817900
63PhosphorylationPNSEGGLYVCMNTFL
CCCCCCEEEEHHHHH		8.5522817900
84PhosphorylationVERHFRKTGQSVYMH
HHHHHHHHCCHHHHH		35.8827080861
87PhosphorylationHFRKTGQSVYMHLKR
HHHHHCCHHHHHHHH		19.2927080861
89PhosphorylationRKTGQSVYMHLKRHV
HHHCCHHHHHHHHHH		5.5322210691
93UbiquitinationQSVYMHLKRHVREKV
CHHHHHHHHHHHHHH		26.27-
101MethylationRHVREKVRGASGGAL
HHHHHHHCCCCCCCC		46.13115919589
104PhosphorylationREKVRGASGGALPKR
HHHHCCCCCCCCCCC		40.3523403867
110UbiquitinationASGGALPKRRNSKIF
CCCCCCCCCCCCCEE		65.91-
114PhosphorylationALPKRRNSKIFLDLD
CCCCCCCCCEEEECC		25.8927422710
122PhosphorylationKIFLDLDTDDDLNSD
CEEEECCCCCCCCCC		48.9321659512
125UbiquitinationLDLDTDDDLNSDDYE
EECCCCCCCCCCCCC		51.0321890473
128PhosphorylationDTDDDLNSDDYEYED
CCCCCCCCCCCCCCC		38.8723403867
131PhosphorylationDDLNSDDYEYEDEAK
CCCCCCCCCCCCCCC		25.9623403867
133PhosphorylationLNSDDYEYEDEAKLV
CCCCCCCCCCCCCEE		23.5823403867
176UbiquitinationSSKSPYRKQDPDTWE
CCCCCCCCCCCCCCC		53.8921906983
181PhosphorylationYRKQDPDTWENELPV
CCCCCCCCCCCCCCH		39.8130624053
190UbiquitinationENELPVSKYANNLTQ
CCCCCHHHHCCCCEE		48.9221890473
190UbiquitinationENELPVSKYANNLTQ
CCCCCHHHHCCCCEE		48.9221906983
210UbiquitinationRIPPSGWKCARCDLR
ECCCCCCCCCCCCCC		22.88-
225PhosphorylationENLWLNLTDGSVLCG
CCEEEECCCCCEEEC		36.9220068231
228PhosphorylationWLNLTDGSVLCGKWF
EEECCCCCEEECEEE		18.0920068231
259UbiquitinationMGYPLAVKLGTITPD
CCCCEEEEECEECCC		35.2821906983
263UbiquitinationLAVKLGTITPDGADV
EEEEECEECCCCCCE		5.0921890473
311SumoylationGLQDNDIKLRVSEWE
CCCCCCEEEEHHHHH		32.8628112733
326UbiquitinationVIQESGTKLKPMYGP
HHHCCCCCCCCCCCC		59.0221906983
328UbiquitinationQESGTKLKPMYGPGY
HCCCCCCCCCCCCCC		29.3321906983
328UbiquitinationQESGTKLKPMYGPGY
HCCCCCCCCCCCCCC		29.3321890473
336PhosphorylationPMYGPGYTGLKNLGN
CCCCCCCCCHHHCCC		41.7924719451
339UbiquitinationGPGYTGLKNLGNSCY
CCCCCCHHHCCCCHH		52.01-
356PhosphorylationSVMQAIFSIPEFQRA
HHHHHHHCCHHHHHH		30.9926852163
380PhosphorylationDYSPLDPTQDFNTQM
CCCCCCCCCCCCHHH		40.20-
385PhosphorylationDPTQDFNTQMTKLGH
CCCCCCCHHHHHHCC		21.51-
388PhosphorylationQDFNTQMTKLGHGLL
CCCCHHHHHHCCCHH		17.19-
389UbiquitinationDFNTQMTKLGHGLLS
CCCHHHHHHCCCHHC		47.32-
396PhosphorylationKLGHGLLSGQYSKPP
HHCCCHHCCCCCCCC		28.97-
399PhosphorylationHGLLSGQYSKPPVKS
CCHHCCCCCCCCHHH		23.37-
401UbiquitinationLLSGQYSKPPVKSEL
HHCCCCCCCCHHHHH		48.7021906983
405UbiquitinationQYSKPPVKSELIEQV
CCCCCCHHHHHHHHH		43.9421906983
405SumoylationQYSKPPVKSELIEQV
CCCCCCHHHHHHHHH		43.94-
405SumoylationQYSKPPVKSELIEQV
CCCCCCHHHHHHHHH		43.9428112733
414UbiquitinationELIEQVMKEEHKPQQ
HHHHHHHHHHCCCCC		62.18-
425PhosphorylationKPQQNGISPRMFKAF
CCCCCCCCHHHHHHH		14.0925159151
430UbiquitinationGISPRMFKAFVSKSH
CCCHHHHHHHHCCCC		31.4121906983
435UbiquitinationMFKAFVSKSHPEFSS
HHHHHHCCCCCCCCC		47.7021906983
511UbiquitinationAMEAATNKDELIAYE
HHHHHCCHHHHHHHH		48.5021906983
532UbiquitinationEANRRPLPELVRAKI
HHHCCCCHHHHHCCC		35.2421890473
565UbiquitinationWSSALQAKSAGVKTS
HHHHHHHHHCCCCCC		28.07-
586UbiquitinationEYLVVQIKKFTFGLD
CEEEEEEEEEEECCC		25.4121906983
587UbiquitinationYLVVQIKKFTFGLDW
EEEEEEEEEEECCCC		51.7921906983
597UbiquitinationFGLDWVPKKFDVSID
ECCCCCCCCCCEECC		57.3521890473
597UbiquitinationFGLDWVPKKFDVSID
ECCCCCCCCCCEECC		57.3521906983
598UbiquitinationGLDWVPKKFDVSIDM
CCCCCCCCCCEECCC		40.50-
630PhosphorylationEEELPDISPPIVIPD
CCCCCCCCCCEECCC		31.8123401153
639PhosphorylationPIVIPDDSKDRLMNQ
CEECCCCCCCHHHHH		43.7827080861
640SumoylationIVIPDDSKDRLMNQL
EECCCCCCCHHHHHC		54.59-
640UbiquitinationIVIPDDSKDRLMNQL
EECCCCCCCHHHHHC		54.5921906983
708PhosphorylationEPLTMPGYGGAASAG
CCCCCCCCCCCCCCC		13.40-
830UbiquitinationHYICHIKKEGRWVIY
EEEEEEEECCEEEEE		65.87-
841UbiquitinationWVIYNDHKVCASERP
EEEECCCCEECCCCC		41.70-
850UbiquitinationCASERPPKDLGYMYF
ECCCCCCCCCCCCEE		69.16-
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
708YPhosphorylationKinaseCLK3P49761
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP13_HUMAN !!
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 UBP13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DVL1_HUMANDVL1physical
16169070
FUND2_HUMANFUNDC2physical
16169070
MYO15_HUMANMYO15Aphysical
16169070
RM20_HUMANMRPL20physical
16169070
FBP1L_HUMANFNBP1Lphysical
16169070
TRI55_HUMANTRIM55physical
11927605
TRI63_HUMANTRIM63physical
11927605
CYLD_HUMANCYLDphysical
19615732
ODO2_HUMANDLSTphysical
19615732
NEDD8_HUMANNEDD8physical
19615732
ODO1_HUMANOGDHphysical
19615732
UFD1_HUMANUFD1Lphysical
19615732
SMC1A_HUMANSMC1Aphysical
19615732
UBL4A_HUMANUBL4Aphysical
19615732
SMC3_HUMANSMC3physical
19615732
TCAF1_HUMANFAM115Aphysical
19615732
FAF2_HUMANFAF2physical
19615732
CYBP_HUMANCACYBPphysical
19615732
KCTD3_HUMANKCTD3physical
19615732
NPL4_HUMANNPLOC4physical
19615732
DBLOH_HUMANDIABLOphysical
19615732
ITCH_HUMANITCHphysical
19615732
BACD3_HUMANKCTD10physical
19615732
UBC_HUMANUBCphysical
22216260
STAT1_HUMANSTAT1physical
23940278
PTEN_HUMANPTENphysical
24270891
TERA_HUMANVCPphysical
24424410
AMFR_HUMANAMFRphysical
24424410
BAG6_HUMANBAG6physical
24424410
UBL4A_HUMANUBL4Aphysical
24424410
GET4_HUMANGET4physical
24424410
YTHD2_HUMANYTHDF2physical
26344197
PTEN_HUMANPTENphysical
26453058
PTEN_HUMANPTENphysical
26280536
ACLY_HUMANACLYphysical
27892457
ODO1_HUMANOGDHphysical
27892457
STING_HUMANTMEM173physical
27801882
ZEB1_HUMANZEB1physical
29119051
UIMC1_HUMANUIMC1physical
28569838
MDC1_HUMANMDC1physical
28569838
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP13_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-122, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND MASSSPECTROMETRY.

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