UBP16_HUMAN - dbPTM
UBP16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP16_HUMAN
UniProt AC Q9Y5T5
Protein Name Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000255|HAMAP-Rule:MF_03062}
Gene Name USP16 {ECO:0000255|HAMAP-Rule:MF_03062}
Organism Homo sapiens (Human).
Sequence Length 823
Subcellular Localization Nucleus .
Protein Description Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B..
Protein Sequence MGKKRTKGKTVPIDDSSETLEPVCRHIRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKAEEETEEKPSVWLCLKCGHQGCGRNSQEQHALKHYLTPRSEPHCLVLSLDNWSVWCYVCDNEVQYCSSNQLGQVVDYVRKQASITTPKPAEKDNGNIELENKKLEKESKNEQEREKKENMAKENPPMNSPCQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPDLALTEPLEINLEPPGPLTLAMSQFLNEMQETKKGVVTPKELFSQVCKKAVRFKGYQQQDSQELLRYLLDGMRAEEHQRVSKGILKAFGNSTEKLDEELKNKVKDYEKKKSMPSFVDRIFGGELTSMIMCDQCRTVSLVHESFLDLSLPVLDDQSGKKSVNDKNLKKTVEDEDQDSEEEKDNDSYIKERSDIPSGTSKHLQKKAKKQAKKQAKNQRRQQKIQGKVLHLNDICTIDHPEDSEYEAEMSLQGEVNIKSNHISQEGVMHKEYCVNQKDLNGQAKMIESVTDNQKSTEEVDMKNINMDNDLEVLTSSPTRNLNGAYLTEGSNGEVDISNGFKNLNLNAALHPDEINIEILNDSHTPGTKVYEVVNEDPETAFCTLANREVFNTDECSIQHCLYQFTRNEKLRDANKLLCEVCTRRQCNGPKANIKGERKHVYTNAKKQMLISLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILDLAPFCTLKCKNVAEENTRVLYSLYGVVEHSGTMRSGHYTAYAKARTANSHLSNLVLHGDIPQDFEMESKGQWFHISDTHVQAVPTTKVLNSQAYLLFYERIL
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
4Ubiquitination----MGKKRTKGKTV
----CCCCCCCCCEE		60.6222817900
7Ubiquitination-MGKKRTKGKTVPID
-CCCCCCCCCEECCC		63.5422817900
9UbiquitinationGKKRTKGKTVPIDDS
CCCCCCCCEECCCCC		48.1521963094
10PhosphorylationKKRTKGKTVPIDDSS
CCCCCCCEECCCCCC		39.9323403867
16PhosphorylationKTVPIDDSSETLEPV
CEECCCCCCCCHHHH		26.7328985074
17PhosphorylationTVPIDDSSETLEPVC
EECCCCCCCCHHHHH		41.4121815630
19PhosphorylationPIDDSSETLEPVCRH
CCCCCCCCHHHHHHH		38.0728857561
23 (in isoform 3)Ubiquitination-3.0621890473
29AcetylationPVCRHIRKGLEQGNL
HHHHHHHHHHHHCCH		68.2112439435
29UbiquitinationPVCRHIRKGLEQGNL
HHHHHHHHHHHHCCH		68.2129967540
37AcetylationGLEQGNLKKALVNVE
HHHHCCHHHHHEECE		39.7523749302
37UbiquitinationGLEQGNLKKALVNVE
HHHHCCHHHHHEECE		39.7521906983
37 (in isoform 1)Ubiquitination-39.7521890473
37 (in isoform 2)Ubiquitination-39.7521890473
37 (in isoform 5)Ubiquitination-39.7521890473
38UbiquitinationLEQGNLKKALVNVEW
HHHCCHHHHHEECEE		50.5533845483
116UbiquitinationLDNWSVWCYVCDNEV
CCCCEEEEEECCCEE		1.3822817900
116 (in isoform 4)Ubiquitination-1.3821906983
131 (in isoform 3)Phosphorylation-6.4020068231
140SumoylationQVVDYVRKQASITTP
HHHHHHHHHCCCCCC		39.9228112733
143PhosphorylationDYVRKQASITTPKPA
HHHHHHCCCCCCCCC		20.2720068231
145PhosphorylationVRKQASITTPKPAEK
HHHHCCCCCCCCCCC		34.2520068231
145 (in isoform 2)Phosphorylation-34.2520068231
146PhosphorylationRKQASITTPKPAEKD
HHHCCCCCCCCCCCC		27.8720068231
181UbiquitinationREKKENMAKENPPMN
HHHHHHHHHHCCCCC		27.8233845483
182UbiquitinationEKKENMAKENPPMNS
HHHHHHHHHCCCCCC		47.4533845483
189PhosphorylationKENPPMNSPCQITVK
HHCCCCCCCCEEEEE		22.3221815630
196UbiquitinationSPCQITVKGLSNLGN
CCCEEEEECHHHCCC		45.5521963094
199PhosphorylationQITVKGLSNLGNTCF
EEEEECHHHCCCCHH		38.3822817900
203UbiquitinationKGLSNLGNTCFFNAV
ECHHHCCCCHHHHHH		36.5221963094
204PhosphorylationGLSNLGNTCFFNAVM
CHHHCCCCHHHHHHH		14.6419690332
210UbiquitinationNTCFFNAVMQNLSQT
CCHHHHHHHHCCCCC		4.2123503661
215PhosphorylationNAVMQNLSQTPVLRE
HHHHHCCCCCHHHHH		39.2919690332
217PhosphorylationVMQNLSQTPVLRELL
HHHCCCCCHHHHHHH		16.4019690332
228UbiquitinationRELLKEVKMSGTIVK
HHHHHHHCCCCEEEE		28.5623503661
230PhosphorylationLLKEVKMSGTIVKIE
HHHHHCCCCEEEEEC		27.37-
277PhosphorylationETKKGVVTPKELFSQ
HHCCCCCCHHHHHHH		26.6629396449
278UbiquitinationTKKGVVTPKELFSQV
HCCCCCCHHHHHHHH		19.2632015554
278 (in isoform 3)Ubiquitination-19.2621890473
279UbiquitinationKKGVVTPKELFSQVC
CCCCCCHHHHHHHHH		58.6532015554
286UbiquitinationKELFSQVCKKAVRFK
HHHHHHHHHHHHHCC		2.6523000965
287UbiquitinationELFSQVCKKAVRFKG
HHHHHHHHHHHHCCC		44.9323000965
288UbiquitinationLFSQVCKKAVRFKGY
HHHHHHHHHHHCCCC		47.1623000965
292UbiquitinationVCKKAVRFKGYQQQD
HHHHHHHCCCCCCCC		6.0623000965
292 (in isoform 2)Ubiquitination-6.0621890473
293UbiquitinationCKKAVRFKGYQQQDS
HHHHHHCCCCCCCCH		46.2623000965
293 (in isoform 1)Ubiquitination-46.2621890473
293 (in isoform 5)Ubiquitination-46.2621890473
300PhosphorylationKGYQQQDSQELLRYL
CCCCCCCHHHHHHHH		22.6330624053
330PhosphorylationILKAFGNSTEKLDEE
HHHHHCCCHHHHHHH		38.02-
332UbiquitinationKAFGNSTEKLDEELK
HHHCCCHHHHHHHHH		51.9833845483
333UbiquitinationAFGNSTEKLDEELKN
HHCCCHHHHHHHHHH		62.4233845483
341UbiquitinationLDEELKNKVKDYEKK
HHHHHHHHHHHHHHH		49.4224816145
353PhosphorylationEKKKSMPSFVDRIFG
HHHHCCCHHHHHHHC		29.30-
356UbiquitinationKSMPSFVDRIFGGEL
HCCCHHHHHHHCCCE		35.6324816145
386PhosphorylationHESFLDLSLPVLDDQ
CHHHHCCCCCEEECC		30.23-
407PhosphorylationNDKNLKKTVEDEDQD
CCCCHHHHCCCCCCC		27.7823927012
411 (in isoform 3)Ubiquitination-44.0321890473
415PhosphorylationVEDEDQDSEEEKDND
CCCCCCCCHHHHCCC		41.0722167270
423PhosphorylationEEEKDNDSYIKERSD
HHHHCCCHHHHHHCC		34.7023927012
424PhosphorylationEEKDNDSYIKERSDI
HHHCCCHHHHHHCCC		20.9023927012
425UbiquitinationEKDNDSYIKERSDIP
HHCCCHHHHHHCCCC		4.2932015554
425 (in isoform 2)Ubiquitination-4.2921890473
426UbiquitinationKDNDSYIKERSDIPS
HCCCHHHHHHCCCCC		38.5522817900
426 (in isoform 1)Ubiquitination-38.5521890473
436UbiquitinationSDIPSGTSKHLQKKA
CCCCCCHHHHHHHHH		22.9233845483
437UbiquitinationDIPSGTSKHLQKKAK
CCCCCHHHHHHHHHH		48.4433845483
447UbiquitinationQKKAKKQAKKQAKNQ
HHHHHHHHHHHHHHH		29.8730230243
448UbiquitinationKKAKKQAKKQAKNQR
HHHHHHHHHHHHHHH		42.8130230243
479PhosphorylationTIDHPEDSEYEAEMS
CCCCCCCCCCEEEEE		40.1827642862
481PhosphorylationDHPEDSEYEAEMSLQ
CCCCCCCCEEEEEEE		25.1327642862
486PhosphorylationSEYEAEMSLQGEVNI
CCCEEEEEEECEEEE		14.73-
505UbiquitinationISQEGVMHKEYCVNQ
CCCCCCCCHHHCCCH		19.8621963094
506UbiquitinationSQEGVMHKEYCVNQK
CCCCCCCHHHCCCHH		32.0821963094
512UbiquitinationHKEYCVNQKDLNGQA
CHHHCCCHHCCCCCE		21.9021963094
513UbiquitinationKEYCVNQKDLNGQAK
HHHCCCHHCCCCCEE		60.0021963094
519UbiquitinationQKDLNGQAKMIESVT
HHCCCCCEEEEECCC		12.5532015554
519 (in isoform 2)Ubiquitination-12.55-
520UbiquitinationKDLNGQAKMIESVTD
HCCCCCEEEEECCCC		32.3032015554
524PhosphorylationGQAKMIESVTDNQKS
CCEEEEECCCCCCCC		21.2825159151
526PhosphorylationAKMIESVTDNQKSTE
EEEEECCCCCCCCCC		38.2129759185
529UbiquitinationIESVTDNQKSTEEVD
EECCCCCCCCCCEEC		43.8432015554
530UbiquitinationESVTDNQKSTEEVDM
ECCCCCCCCCCEECH		66.6532015554
531PhosphorylationSVTDNQKSTEEVDMK
CCCCCCCCCCEECHH		31.15-
537UbiquitinationKSTEEVDMKNINMDN
CCCCEECHHHCCCCC		4.2923503661
537 (in isoform 2)Ubiquitination-4.29-
538UbiquitinationSTEEVDMKNINMDND
CCCEECHHHCCCCCC		50.6523503661
550PhosphorylationDNDLEVLTSSPTRNL
CCCCCHHCCCCCCCC		32.1330266825
551PhosphorylationNDLEVLTSSPTRNLN
CCCCHHCCCCCCCCC		30.1129255136
552PhosphorylationDLEVLTSSPTRNLNG
CCCHHCCCCCCCCCC		25.6719664994
554PhosphorylationEVLTSSPTRNLNGAY
CHHCCCCCCCCCCCE		33.8529255136
561PhosphorylationTRNLNGAYLTEGSNG
CCCCCCCEECCCCCC		18.6326074081
563PhosphorylationNLNGAYLTEGSNGEV
CCCCCEECCCCCCEE		26.1428348404
566PhosphorylationGAYLTEGSNGEVDIS
CCEECCCCCCEEECC		35.1128348404
598PhosphorylationNIEILNDSHTPGTKV
EEEEECCCCCCCCEE		28.3420068231
600PhosphorylationEILNDSHTPGTKVYE
EEECCCCCCCCEEEE		27.6320068231
603PhosphorylationNDSHTPGTKVYEVVN
CCCCCCCCEEEEEEC		20.6720068231
606PhosphorylationHTPGTKVYEVVNEDP
CCCCCEEEEEECCCC		12.4528796482
615PhosphorylationVVNEDPETAFCTLAN
EECCCCCCCEEEECC		30.3528796482
618GlutathionylationEDPETAFCTLANREV
CCCCCCEEEECCCCC		2.5622555962
619PhosphorylationDPETAFCTLANREVF
CCCCCEEEECCCCCC		23.5828796482
638PhosphorylationCSIQHCLYQFTRNEK
CHHHHHHHHHHCCHH		13.6327642862
650UbiquitinationNEKLRDANKLLCEVC
CHHHHHHHHHHHHHH		39.5324816145
651UbiquitinationEKLRDANKLLCEVCT
HHHHHHHHHHHHHHH		44.5524816145
665UbiquitinationTRRQCNGPKANIKGE
HHHCCCCCCCCCCCC		20.7024816145
666UbiquitinationRRQCNGPKANIKGER
HHCCCCCCCCCCCCC		56.3024816145
677PhosphorylationKGERKHVYTNAKKQM
CCCCCEEECCHHHHH		8.2624532841
728UbiquitinationDLAPFCTLKCKNVAE
HHHCCCEEEECCHHH		6.8832015554
729UbiquitinationLAPFCTLKCKNVAEE
HHCCCEEEECCHHHH		25.6332015554
738PhosphorylationKNVAEENTRVLYSLY
CCHHHHHHHHHHEEE		25.9922210691
742PhosphorylationEENTRVLYSLYGVVE
HHHHHHHHEEEEEEE		8.1824719451
743PhosphorylationENTRVLYSLYGVVEH
HHHHHHHEEEEEEEC		15.7924719451
751PhosphorylationLYGVVEHSGTMRSGH
EEEEEECCCCCCCCC		23.5822210691
762PhosphorylationRSGHYTAYAKARTAN
CCCCEEEEEEECCCC		10.8030257219
764UbiquitinationGHYTAYAKARTANSH
CCEEEEEEECCCCHH		26.23-
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
330SPhosphorylationKinasePLK1P53350
PSP
386SPhosphorylationKinasePLK1P53350
PSP
415SPhosphorylationKinaseTTKP33981
PSP
486SPhosphorylationKinasePLK1P53350
PSP
552SPhosphorylationKinaseCDK1P06493
PSP
552SPhosphorylationKinaseTTKP33981
PSP
554TPhosphorylationKinaseTTKP33981
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP16_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 UBP16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
17512543
ODB2_HUMANDBTphysical
19615732
H2B1L_HUMANHIST1H2BLphysical
19615732
HERC2_HUMANHERC2physical
19615732
FBX11_HUMANFBXO11physical
21090589
PTOV1_HUMANPTOV1physical
21090589
UBD_HUMANUBDphysical
21090589
UBC_HUMANUBCphysical
22195557
UBC_HUMANUBCphysical
15171253
UBC_HUMANUBCphysical
23287719
H2A2C_HUMANHIST2H2ACphysical
17914355
H2A2A_HUMANHIST2H2AA3physical
17914355
UBP16_HUMANUSP16physical
24013421
H2B1B_HUMANHIST1H2BBphysical
24013421
HERC2_HUMANHERC2physical
25305019
RNF8_HUMANRNF8physical
25305019
PLK1_HUMANPLK1physical
26323689
H2AZ_HUMANH2AFZphysical
21245042
H2A2C_HUMANHIST2H2ACphysical
21245042
NEUL4_HUMANNEURL4physical
28514442
HERC2_HUMANHERC2physical
28514442
WDR54_HUMANWDR54physical
28514442
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 UBP16_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-552, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-554, 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 SER-415 AND SER-552, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND MASSSPECTROMETRY.

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