UBP22_HUMAN - dbPTM
UBP22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP22_HUMAN
UniProt AC Q9UPT9
Protein Name Ubiquitin carboxyl-terminal hydrolase 22
Gene Name USP22
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Nucleus .
Protein Description Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression..
Protein Sequence MVSRPEPEGEAMDAELAVAPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKSCICHVCGVHLNRLHSCLYCVFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIYDKDMEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSEGNVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQFLEYE
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
29UbiquitinationGCSHLGSFKVDNWKQ
CCCCCCCCCCCCHHH		9.4323000965
32UbiquitinationHLGSFKVDNWKQNLR
CCCCCCCCCHHHHHH		56.7323000965
35UbiquitinationSFKVDNWKQNLRAIY
CCCCCCHHHHHHHHH		35.2521906983
35 (in isoform 1)Ubiquitination-35.2521890473
39UbiquitinationDNWKQNLRAIYQCFV
CCHHHHHHHHHHHHH		26.8721890473
47UbiquitinationAIYQCFVWSGTAEAR
HHHHHHHCCCCHHHH		3.1922505724
54UbiquitinationWSGTAEARKRKAKSC
CCCCHHHHHHHHHHH		30.7127667366
58UbiquitinationAEARKRKAKSCICHV
HHHHHHHHHHHHHHH		17.0223000965
59UbiquitinationEARKRKAKSCICHVC
HHHHHHHHHHHHHHC		49.23-
61UbiquitinationRKRKAKSCICHVCGV
HHHHHHHHHHHHCCH		3.6623000965
95UbiquitinationKHIHEHAKAKRHNLA
HHHHHHHHHHHCCCH		57.2429967540
117 (in isoform 2)Ubiquitination-30.7021890473
125 (in isoform 2)Ubiquitination-41.1821890473
129SumoylationKDMEIIAKEEQRKAW
CCCCHHHHHHHHHHH		51.91-
129AcetylationKDMEIIAKEEQRKAW
CCCCHHHHHHHHHHH		51.9119608861
129SumoylationKDMEIIAKEEQRKAW
CCCCHHHHHHHHHHH		51.9119608861
129UbiquitinationKDMEIIAKEEQRKAW
CCCCHHHHHHHHHHH		51.9133845483
129 (in isoform 1)Ubiquitination-51.9121890473
132 (in isoform 2)Ubiquitination-53.9521890473
134AcetylationIAKEEQRKAWKMQGV
HHHHHHHHHHHCCCC		59.2925953088
134UbiquitinationIAKEEQRKAWKMQGV
HHHHHHHHHHHCCCC		59.2923000965
137SumoylationEEQRKAWKMQGVGEK
HHHHHHHHCCCCCHH		26.63-
137AcetylationEEQRKAWKMQGVGEK
HHHHHHHHCCCCCHH		26.6325953088
137SumoylationEEQRKAWKMQGVGEK
HHHHHHHHCCCCCHH		26.63-
137UbiquitinationEEQRKAWKMQGVGEK
HHHHHHHHCCCCCHH		26.6323000965
137 (in isoform 1)Ubiquitination-26.6321890473
140 (in isoform 2)Ubiquitination-26.3721890473
144AcetylationKMQGVGEKFSTWEPT
HCCCCCHHCCCCCCC		38.3925953088
144UbiquitinationKMQGVGEKFSTWEPT
HCCCCCHHCCCCCCC		38.3923000965
144 (in isoform 1)Ubiquitination-38.3921890473
146PhosphorylationQGVGEKFSTWEPTKR
CCCCHHCCCCCCCHH		43.6125159151
147PhosphorylationGVGEKFSTWEPTKRE
CCCHHCCCCCCCHHH		36.6625850435
147 (in isoform 2)Ubiquitination-36.6621890473
151PhosphorylationKFSTWEPTKRELELL
HCCCCCCCHHHHHHH		31.0825159151
152SumoylationFSTWEPTKRELELLK
CCCCCCCHHHHHHHH		55.37-
152AcetylationFSTWEPTKRELELLK
CCCCCCCHHHHHHHH		55.3725953088
152SumoylationFSTWEPTKRELELLK
CCCCCCCHHHHHHHH		55.37-
152UbiquitinationFSTWEPTKRELELLK
CCCCCCCHHHHHHHH		55.3721906983
152 (in isoform 1)Ubiquitination-55.3721890473
159AcetylationKRELELLKHNPKRRK
HHHHHHHHHCCCCCC		54.6925953088
159UbiquitinationKRELELLKHNPKRRK
HHHHHHHHHCCCCCC		54.6921906983
159 (in isoform 1)Ubiquitination-54.6921890473
163UbiquitinationELLKHNPKRRKITSN
HHHHHCCCCCCCCCC		70.8823000965
166AcetylationKHNPKRRKITSNCTI
HHCCCCCCCCCCCCE		55.1312430265
166UbiquitinationKHNPKRRKITSNCTI
HHCCCCCCCCCCCCE		55.1323000965
168PhosphorylationNPKRRKITSNCTIGL
CCCCCCCCCCCCEEH		19.5428555341
172PhosphorylationRKITSNCTIGLRGLI
CCCCCCCCEEHHHHH		23.4825690035
208MethylationRDFFLSDRHRCEMQS
HHHHCCCCCCCCCCC		18.77-
232PhosphorylationSSLFQEFYSGHRSPH
HHHHHHHHCCCCCCC		17.00-
233PhosphorylationSLFQEFYSGHRSPHI
HHHHHHHCCCCCCCC		33.1823898821
237PhosphorylationEFYSGHRSPHIPYKL
HHHCCCCCCCCCHHH		18.3730266825
242PhosphorylationHRSPHIPYKLLHLVW
CCCCCCCHHHHHHHH		17.4230266825
277UbiquitinationALDVLHRHCKGDDNG
HHHHHHHHCCCCCCC		13.5927667366
289UbiquitinationDNGKKANNPNHCNCI
CCCCCCCCCCCCCEE		43.5421963094
312UbiquitinationLQSDVTCQVCHGVST
CCCCCCHHHCCCCCC		31.3521987572
337UbiquitinationDLPGSSTPFWPLSPG
CCCCCCCCCCCCCCC		31.1121963094
342PhosphorylationSTPFWPLSPGSEGNV
CCCCCCCCCCCCCCE		24.1226074081
345PhosphorylationFWPLSPGSEGNVVNG
CCCCCCCCCCCEECC		45.7926074081
357UbiquitinationVNGESHVSGTTTLTD
ECCCCCCCCCCCHHH		25.6221963094
377PhosphorylationTRPEHLGSSAKIKCS
CCHHHCCCCCEEECC		33.2229214152
378PhosphorylationRPEHLGSSAKIKCSG
CHHHCCCCCEEECCC		31.6129214152
380AcetylationEHLGSSAKIKCSGCH
HHCCCCCEEECCCCC		44.6526051181
380UbiquitinationEHLGSSAKIKCSGCH
HHCCCCCEEECCCCC		44.6532015554
382SumoylationLGSSAKIKCSGCHSY
CCCCCEEECCCCCCC		22.95-
382SumoylationLGSSAKIKCSGCHSY
CCCCCEEECCCCCCC		22.95-
382UbiquitinationLGSSAKIKCSGCHSY
CCCCCEEECCCCCCC		22.9527667366
383UbiquitinationGSSAKIKCSGCHSYQ
CCCCEEECCCCCCCC		4.8827667366
384PhosphorylationSSAKIKCSGCHSYQE
CCCEEECCCCCCCCH		39.1821406692
388PhosphorylationIKCSGCHSYQESTKQ
EECCCCCCCCHHCCC		32.3721406692
388UbiquitinationIKCSGCHSYQESTKQ
EECCCCCCCCHHCCC		32.3721890473
389PhosphorylationKCSGCHSYQESTKQL
ECCCCCCCCHHCCCC		7.8221406692
392PhosphorylationGCHSYQESTKQLTMK
CCCCCCHHCCCCCHH		25.9421406692
393PhosphorylationCHSYQESTKQLTMKK
CCCCCHHCCCCCHHH		23.2721406692
394UbiquitinationHSYQESTKQLTMKKL
CCCCHHCCCCCHHHC		53.2221963094
396UbiquitinationYQESTKQLTMKKLPI
CCHHCCCCCHHHCCE		5.5721963094
400UbiquitinationTKQLTMKKLPIVACF
CCCCCHHHCCEEEEE		48.9921890473
410UbiquitinationIVACFHLKRFEHSAK
EEEEEEHHHCCHHHH		46.61-
417SumoylationKRFEHSAKLRRKITT
HHCCHHHHHHHHCEE		45.61-
417AcetylationKRFEHSAKLRRKITT
HHCCHHHHHHHHCEE		45.6123749302
417SumoylationKRFEHSAKLRRKITT
HHCCHHHHHHHHCEE		45.61-
417UbiquitinationKRFEHSAKLRRKITT
HHCCHHHHHHHHCEE		45.6133845483
423PhosphorylationAKLRRKITTYVSFPL
HHHHHHCEEEEECEE		18.3424719451
442UbiquitinationTPFMASSKESRMNGQ
CCCCCCCHHHHCCCC		58.1621963094
444PhosphorylationFMASSKESRMNGQYQ
CCCCCHHHHCCCCCC		40.33-
450PhosphorylationESRMNGQYQQPTDSL
HHHCCCCCCCCCCCC		15.5422817900
462SumoylationDSLNNDNKYSLFAVV
CCCCCCCCEEEEEEE		38.79-
462UbiquitinationDSLNNDNKYSLFAVV
CCCCCCCCEEEEEEE		38.7921963094
463PhosphorylationSLNNDNKYSLFAVVN
CCCCCCCEEEEEEEE		19.5026074081
464PhosphorylationLNNDNKYSLFAVVNH
CCCCCCEEEEEEEEC		20.7226074081
474PhosphorylationAVVNHQGTLESGHYT
EEEECCCEECCCCCH		22.3026074081
477PhosphorylationNHQGTLESGHYTSFI
ECCCEECCCCCHHHH		33.7026074081
480PhosphorylationGTLESGHYTSFIRQH
CEECCCCCHHHHHHC		13.9626074081
481PhosphorylationTLESGHYTSFIRQHK
EECCCCCHHHHHHCC		16.1026074081
481 (in isoform 2)Ubiquitination-16.1021890473
482PhosphorylationLESGHYTSFIRQHKD
ECCCCCHHHHHHCCC		16.1226074081
485MethylationGHYTSFIRQHKDQWF
CCCHHHHHHCCCCCE		30.46-
488UbiquitinationTSFIRQHKDQWFKCD
HHHHHHCCCCCEECC		43.1927667366
493AcetylationQHKDQWFKCDDAIIT
HCCCCCEECCCEEEE		33.5225953088
493UbiquitinationQHKDQWFKCDDAIIT
HCCCCCEECCCEEEE		33.5221963094
493 (in isoform 1)Ubiquitination-33.5221890473
493 (in isoform 2)Ubiquitination-33.5221890473
501UbiquitinationCDDAIITKASIKDVL
CCCEEEECCHHHHHH		29.7221963094
505UbiquitinationIITKASIKDVLDSEG
EEECCHHHHHHCCCC		39.0121890473
505 (in isoform 1)Ubiquitination-39.0121890473
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 UBP22_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP22_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 UBP22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HEXA_HUMANHEXAphysical
16169070
RM10_HUMANMRPL10physical
16169070
PSME1_HUMANPSME1physical
16169070
SCFD1_HUMANSCFD1physical
16169070
TRRAP_HUMANTRRAPphysical
18206972
ATX7_HUMANATXN7physical
18206972
KAT2A_HUMANKAT2Aphysical
18206972
AT7L3_HUMANATXN7L3physical
18206972
SUPT3_HUMANSUPT3Hphysical
18206972
TAF10_HUMANTAF10physical
18206972
KAT2A_HUMANKAT2Aphysical
19615732
TAF9_HUMANTAF9physical
19615732
TRRAP_HUMANTRRAPphysical
19615732
SUPT3_HUMANSUPT3Hphysical
19615732
DEDD_HUMANDEDDphysical
19615732
PPCEL_HUMANPREPLphysical
19615732
ST65G_HUMANSUPT7Lphysical
19615732
TADA3_HUMANTADA3physical
19615732
TAF6L_HUMANTAF6Lphysical
19615732
CNOT1_HUMANCNOT1physical
19615732
OFUT2_HUMANPOFUT2physical
19615732
SIR1_HUMANSIRT1physical
19615732
CNO10_HUMANCNOT10physical
19615732
SND1_HUMANSND1physical
19615732
TAF5L_HUMANTAF5Lphysical
19615732
SP20H_HUMANSUPT20Hphysical
19615732
ENY2_HUMANENY2physical
19615732
AT7L3_HUMANATXN7L3physical
19615732
ADPPT_HUMANAASDHPPTphysical
19615732
TAD2B_HUMANTADA2Bphysical
19615732
SGF29_HUMANCCDC101physical
19615732
TADA1_HUMANTADA1physical
19615732
AT7L2_HUMANATXN7L2physical
19615732
KLH23_HUMANKLHL23physical
19615732
KIF7_HUMANKIF7physical
19615732
UBP27_HUMANUSP27Xphysical
19615732
A7L3B_HUMANATXN7L3Bphysical
19615732
SIR1_HUMANSIRT1physical
22542455
ATX7_HUMANATXN7physical
19843541
H2A2C_HUMANHIST2H2ACphysical
21746879
H2B2E_HUMANHIST2H2BEphysical
21746879
SIR1_HUMANSIRT1physical
23382074
AT7L3_HUMANATXN7L3physical
23382074
NFAC2_HUMANNFATC2physical
24561192
TRRAP_HUMANTRRAPphysical
18206973
KAT2A_HUMANKAT2Aphysical
18206973
TAD2A_HUMANTADA2Aphysical
18206973
TADA3_HUMANTADA3physical
18206973
TAF9B_HUMANTAF9Bphysical
18206973
ATX7_HUMANATXN7physical
18206973
TAF10_HUMANTAF10physical
18206973
STAT3_HUMANSTAT3physical
24969755
ADPPT_HUMANAASDHPPTphysical
25416956
RCAN1_HUMANRCAN1physical
25546086
PGH2_HUMANPTGS2physical
25817787
MDM4_HUMANMDM4physical
25547493
ATX7_HUMANATXN7physical
26195632
CCNB1_HUMANCCNB1physical
27030811
CDC23_HUMANCDC23physical
27030811
UBP22_HUMANUSP22physical
27030811
STING_HUMANTMEM173physical
27801882
SIR1_HUMANSIRT1physical
28166203
MYC_HUMANMYCphysical
28160502
A7L3B_HUMANATXN7L3Bphysical
27601583
AT7L3_HUMANATXN7L3physical
27601583
ENY2_HUMANENY2physical
27601583
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 UBP22_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND MASS SPECTROMETRY.

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