UBP3_HUMAN - dbPTM
UBP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP3_HUMAN
UniProt AC Q9Y6I4
Protein Name Ubiquitin carboxyl-terminal hydrolase 3
Gene Name USP3
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Nucleus . Localizes preferentially with monoubiquitinated H2A to chromatin.
Protein Description Hydrolase that deubiquitinates monoubiquitinated target proteins such as histone H2A and H2B. Required for proper progression through S phase and subsequent mitotic entry. May regulate the DNA damage response (DDR) checkpoint through deubiquitination of H2A at DNA damage sites. Associates with the chromatin..
Protein Sequence MECPHLSSSVCIAPDSAKFPNGSPSSWCCSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQVPLTNHKKSEKQDKVQHTVCMDCSSYSTYCYRCDDFVVNDTKLGLVQKVREHLQNLENSAFTADRHKKRKLLENSTLNSKLLKVNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCCINGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHEGRWFHFNDSTVTLTDEETVVKAKAYILFYVEHQAKAGSDKL
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
1Acetylation-------MECPHLSS
-------CCCCCCCC		12.3419413330
16PhosphorylationSVCIAPDSAKFPNGS
CEEECCCCCCCCCCC		32.0923401153
23PhosphorylationSAKFPNGSPSSWCCS
CCCCCCCCCCCCCHH		28.4028985074
36AcetylationCSVCRSNKSPWVCLT
HHHHCCCCCCEEEEE		60.1725953088
37PhosphorylationSVCRSNKSPWVCLTC
HHHCCCCCCEEEEEC		28.3925159151
59UbiquitinationYVNGHAKKHYEDAQV
CCCCCHHHHCCCCCC		52.80-
61PhosphorylationNGHAKKHYEDAQVPL
CCCHHHHCCCCCCCC		25.1222817900
69PhosphorylationEDAQVPLTNHKKSEK
CCCCCCCCCCCCCCC		29.2528555341
72UbiquitinationQVPLTNHKKSEKQDK
CCCCCCCCCCCCCCC		61.13-
74PhosphorylationPLTNHKKSEKQDKVQ
CCCCCCCCCCCCCCC		55.63-
93PhosphorylationMDCSSYSTYCYRCDD
CCCCCCCCEEEECCC		14.91-
107SumoylationDFVVNDTKLGLVQKV
CEEECCCHHHHHHHH		43.34-
107UbiquitinationDFVVNDTKLGLVQKV
CEEECCCHHHHHHHH		43.34-
107SumoylationDFVVNDTKLGLVQKV
CEEECCCHHHHHHHH		43.34-
113UbiquitinationTKLGLVQKVREHLQN
CHHHHHHHHHHHHHH		35.46-
124PhosphorylationHLQNLENSAFTADRH
HHHHHHHCCCCCHHH		18.5122496350
127PhosphorylationNLENSAFTADRHKKR
HHHHCCCCCHHHHHH		27.6228555341
132UbiquitinationAFTADRHKKRKLLEN
CCCCHHHHHHHHHHC		55.99-
135UbiquitinationADRHKKRKLLENSTL
CHHHHHHHHHHCCCC		67.32-
140PhosphorylationKRKLLENSTLNSKLL
HHHHHHCCCCCCEEE		25.5428555341
141PhosphorylationRKLLENSTLNSKLLK
HHHHHCCCCCCEEEE		41.3522817900
145AcetylationENSTLNSKLLKVNGS
HCCCCCCEEEEECCC		57.6825953088
145UbiquitinationENSTLNSKLLKVNGS
HCCCCCCEEEEECCC		57.6821906983
148UbiquitinationTLNSKLLKVNGSTTA
CCCCEEEEECCCCCE		44.05-
210PhosphorylationRRTYHTRSQGDNNVS
CCCEECCCCCCCCCC		39.4029978859
217PhosphorylationSQGDNNVSLVEEFRK
CCCCCCCCHHHHHHH		28.9023186163
333UbiquitinationICGTESRKFDPFLDL
ECCCCCCCCCCCCCC		64.5021906983
350PhosphorylationDIPSQFRSKRSKNQE
CCCHHHHCCCCCCCC		33.4425627689
354MethylationQFRSKRSKNQENGPV
HHHCCCCCCCCCCCC		67.6830800147
354UbiquitinationQFRSKRSKNQENGPV
HHHCCCCCCCCCCCC		67.68-
363PhosphorylationQENGPVCSLRDCLRS
CCCCCCCCHHHHHHH		27.03-
372PhosphorylationRDCLRSFTDLEELDE
HHHHHHCCCHHHCCC		40.70-
387UbiquitinationTELYMCHKCKKKQKS
CCHHHHHHCCCCCCC		42.70-
389UbiquitinationLYMCHKCKKKQKSTK
HHHHHHCCCCCCCCC		68.74-
423UbiquitinationWTAYLRNKVDTYVEF
HHHHHHCCCCEEEEE		34.7521906983
423UbiquitinationWTAYLRNKVDTYVEF
HHHHHHCCCCEEEEE		34.7521890473
426PhosphorylationYLRNKVDTYVEFPLR
HHHCCCCEEEEEECC		32.2428152594
427PhosphorylationLRNKVDTYVEFPLRG
HHCCCCEEEEEECCC		8.1028152594
517PhosphorylationEHQAKAGSDKL----
HHHHHHCCCCC----		36.1124719451
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 UBP3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP3_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 UBP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBR3_HUMANCBR3physical
19615732
IF4G1_HUMANEIF4G1physical
19615732
GNAL_HUMANGNALphysical
19615732
LRP1_HUMANLRP1physical
19615732
KPYR_HUMANPKLRphysical
19615732
EIF3A_HUMANEIF3Aphysical
19615732
EIF3B_HUMANEIF3Bphysical
19615732
EIF3C_HUMANEIF3Cphysical
19615732
EIF3D_HUMANEIF3Dphysical
19615732
EIF3F_HUMANEIF3Fphysical
19615732
EIF3G_HUMANEIF3Gphysical
19615732
EIF3H_HUMANEIF3Hphysical
19615732
EIF3I_HUMANEIF3Iphysical
19615732
GNA13_HUMANGNA13physical
19615732
WDTC1_HUMANWDTC1physical
19615732
RIMB2_HUMANRIMBP2physical
19615732
NXN_HUMANNXNphysical
19615732
PRC2B_HUMANPRRC2Bphysical
19615732
TOIP2_HUMANTOR1AIP2physical
19615732
IFG15_HUMANTOR1AIP2physical
19615732
ZFAN6_HUMANZFAND6physical
22939629
VATH_HUMANATP6V1Hphysical
22939629
IFIH1_HUMANIFIH1physical
24366338
DDX58_HUMANDDX58physical
24366338
UBC_HUMANUBCphysical
10480896
H2B1B_HUMANHIST1H2BBphysical
17980597
RSU1_HUMANRSU1physical
26344197
STING_HUMANTMEM173physical
27801882
NHRF3_HUMANPDZK1physical
28514442
P53_HUMANTP53physical
28807825
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 UBP3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141, AND MASSSPECTROMETRY.

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