UBP5_HUMAN - dbPTM
UBP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP5_HUMAN
UniProt AC P45974
Protein Name Ubiquitin carboxyl-terminal hydrolase 5
Gene Name USP5
Organism Homo sapiens (Human).
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. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition..
Protein Sequence MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRPKEEDPATGTGDPPRKKPTRLAIGVEGGFDLSEEKFELDEDVKIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHAFSLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRETGYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDMNQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVQVLFSIPDFQRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESGDGERVPEQKEVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKMALPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSAADSISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVAS
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		26.8322223895
5Phosphorylation---MAELSEEALLSV
---CCCCCHHHHHHH		25.5425867546
11PhosphorylationLSEEALLSVLPTIRV
CCHHHHHHHHCCCCC		23.5825867546
15PhosphorylationALLSVLPTIRVPKAG
HHHHHHCCCCCCCCC		19.7725867546
20UbiquitinationLPTIRVPKAGDRVHK
HCCCCCCCCCCCCCC		63.2421906983
20 (in isoform 1)Ubiquitination-63.2421890473
20 (in isoform 2)Ubiquitination-63.2421890473
27UbiquitinationKAGDRVHKDECAFSF
CCCCCCCCCCEEEEC		52.9821906983
27 (in isoform 1)Ubiquitination-52.9821890473
27 (in isoform 2)Ubiquitination-52.9821890473
57PhosphorylationFLGFGKQYVERHFNK
CCCCCHHHHHHHHCC		14.0424719451
64UbiquitinationYVERHFNKTGQRVYL
HHHHHHCCCCCEEEE		53.7621906983
64 (in isoform 1)Ubiquitination-53.7621890473
64 (in isoform 2)Ubiquitination-53.7621890473
65PhosphorylationVERHFNKTGQRVYLH
HHHHHCCCCCEEEEE		39.3824719451
80UbiquitinationLRRTRRPKEEDPATG
EECCCCCCCCCCCCC		72.43-
121SumoylationFELDEDVKIVILPDY
CCCCCCCEEEECCCH		43.51-
128PhosphorylationKIVILPDYLEIARDG
EEEECCCHHHHHHHC		12.3228796482
148PhosphorylationDIVRDRVTSAVEALL
HHHHHHHHHHHHHHH		16.3229255136
149PhosphorylationIVRDRVTSAVEALLS
HHHHHHHHHHHHHHC		27.7129255136
156PhosphorylationSAVEALLSADSASRK
HHHHHHHCCCCCCCH		30.7720068231
159PhosphorylationEALLSADSASRKQEV
HHHHCCCCCCCHHHH		28.0620068231
161PhosphorylationLLSADSASRKQEVQA
HHCCCCCCCHHHHHH		43.9220068231
163AcetylationSADSASRKQEVQAWD
CCCCCCCHHHHHHHH		48.607617791
163SumoylationSADSASRKQEVQAWD
CCCCCCCHHHHHHHH		48.60-
163UbiquitinationSADSASRKQEVQAWD
CCCCCCCHHHHHHHH		48.6021906983
163 (in isoform 1)Ubiquitination-48.6021890473
163 (in isoform 2)Ubiquitination-48.6021890473
178AcetylationGEVRQVSKHAFSLKQ
HHHHHHHHHCCCHHH		39.8419822935
178UbiquitinationGEVRQVSKHAFSLKQ
HHHHHHHHHCCCHHH		39.84-
182PhosphorylationQVSKHAFSLKQLDNP
HHHHHCCCHHHCCCC		35.1324719451
1842-HydroxyisobutyrylationSKHAFSLKQLDNPAR
HHHCCCHHHCCCCCC		47.84-
184AcetylationSKHAFSLKQLDNPAR
HHHCCCHHHCCCCCC		47.8423236377
184UbiquitinationSKHAFSLKQLDNPAR
HHHCCCHHHCCCCCC		47.8421890473
184 (in isoform 1)Ubiquitination-47.8421890473
184 (in isoform 2)Ubiquitination-47.8421890473
198UbiquitinationRIPPCGWKCSKCDMR
CCCCCCCCCCCCCCC		17.57-
213PhosphorylationENLWLNLTDGSILCG
CCEEEECCCCCEEEC		36.9220068231
216PhosphorylationWLNLTDGSILCGRRY
EEECCCCCEEECCCE		18.3920068231
223PhosphorylationSILCGRRYFDGSGGN
CEEECCCEECCCCCC		12.5028442448
247UbiquitinationTGYPLAVKLGTITPD
HCCCEEEEECEECCC		35.28-
247 (in isoform 2)Ubiquitination-35.28-
289PhosphorylationDMLKMQKTDKTMTEL
CHHHCCCCCCCCCEE		26.3229978859
291UbiquitinationLKMQKTDKTMTELEI
HHCCCCCCCCCEEEE		45.48-
292PhosphorylationKMQKTDKTMTELEID
HCCCCCCCCCEEEEE		31.9421815630
294PhosphorylationQKTDKTMTELEIDMN
CCCCCCCCEEEEECH		42.5221815630
318UbiquitinationQESGVPLKPLFGPGY
HHHCCCCCCCCCCCC		33.3421890473
318 (in isoform 1)Ubiquitination-33.3421890473
318 (in isoform 2)Ubiquitination-33.3421890473
353AcetylationSIPDFQRKYVDKLEK
CCCHHHHHHHHHHHH		38.5523749302
353UbiquitinationSIPDFQRKYVDKLEK
CCCHHHHHHHHHHHH		38.5521906983
353 (in isoform 1)Ubiquitination-38.5521890473
353 (in isoform 2)Ubiquitination-38.5521890473
354PhosphorylationIPDFQRKYVDKLEKI
CCHHHHHHHHHHHHH		18.9728152594
3572-HydroxyisobutyrylationFQRKYVDKLEKIFQN
HHHHHHHHHHHHHHC		48.80-
357AcetylationFQRKYVDKLEKIFQN
HHHHHHHHHHHHHHC		48.8022424773
357UbiquitinationFQRKYVDKLEKIFQN
HHHHHHHHHHHHHHC		48.8021890473
357 (in isoform 1)Ubiquitination-48.8021890473
357 (in isoform 2)Ubiquitination-48.8021890473
360AcetylationKYVDKLEKIFQNAPT
HHHHHHHHHHHCCCC		60.2926051181
360SumoylationKYVDKLEKIFQNAPT
HHHHHHHHHHHCCCC		60.29-
360UbiquitinationKYVDKLEKIFQNAPT
HHHHHHHHHHHCCCC		60.2922053931
360 (in isoform 1)Ubiquitination-60.2921890473
360 (in isoform 2)Ubiquitination-60.2921890473
379UbiquitinationDFSTQVAKLGHGLLS
CHHHHHHHHCCCCCC		57.03-
379 (in isoform 2)Ubiquitination-57.03-
386PhosphorylationKLGHGLLSGEYSKPV
HHCCCCCCCCCCCCC		34.3223312004
389PhosphorylationHGLLSGEYSKPVPES
CCCCCCCCCCCCCCC		26.0628796482
390PhosphorylationGLLSGEYSKPVPESG
CCCCCCCCCCCCCCC		26.6128857561
391UbiquitinationLLSGEYSKPVPESGD
CCCCCCCCCCCCCCC		49.4821906983
391 (in isoform 1)Ubiquitination-49.4821890473
391 (in isoform 2)Ubiquitination-49.4821890473
396PhosphorylationYSKPVPESGDGERVP
CCCCCCCCCCCCCCC		35.7928555341
406UbiquitinationGERVPEQKEVQDGIA
CCCCCCHHHHHCCCC		59.1821906983
406 (in isoform 1)Ubiquitination-59.1821890473
406 (in isoform 2)Ubiquitination-59.1821890473
418UbiquitinationGIAPRMFKALIGKGH
CCCHHHHHHHHCCCC		32.7021906983
418 (in isoform 1)Ubiquitination-32.7021890473
418 (in isoform 2)Ubiquitination-32.7021890473
423MalonylationMFKALIGKGHPEFST
HHHHHHCCCCCCCCC		47.2330639696
423UbiquitinationMFKALIGKGHPEFST
HHHHHHCCCCCCCCC		47.2321890473
423 (in isoform 1)Ubiquitination-47.2321890473
423 (in isoform 2)Ubiquitination-47.2321890473
453PhosphorylationMVERNCRSSENPNEV
HHHHHCCCCCCHHHH		44.1728348404
468AcetylationFRFLVEEKIKCLATE
HHHHHHHHHHHHHCC		33.6826051181
468UbiquitinationFRFLVEEKIKCLATE
HHHHHHHHHHHHHCC		33.6821906983
468 (in isoform 1)Ubiquitination-33.6821890473
468 (in isoform 2)Ubiquitination-33.6821890473
470UbiquitinationFLVEEKIKCLATEKV
HHHHHHHHHHHCCCC		33.9721890473
470 (in isoform 1)Ubiquitination-33.9721890473
470 (in isoform 2)Ubiquitination-33.9721890473
476UbiquitinationIKCLATEKVKYTQRV
HHHHHCCCCCCCCCC		39.4121906983
476 (in isoform 1)Ubiquitination-39.4121890473
476 (in isoform 2)Ubiquitination-39.4121890473
478UbiquitinationCLATEKVKYTQRVDY
HHHCCCCCCCCCCCE		54.36-
479PhosphorylationLATEKVKYTQRVDYI
HHCCCCCCCCCCCEE		15.87-
485PhosphorylationKYTQRVDYIMQLPVP
CCCCCCCEEECCCCC		8.7420068231
499UbiquitinationPMDAALNKEELLEYE
CCCHHCCHHHHHHHH		54.1121906983
499 (in isoform 1)Ubiquitination-54.1121890473
499 (in isoform 2)Ubiquitination-54.1121890473
505PhosphorylationNKEELLEYEEKKRQA
CHHHHHHHHHHHHHH		29.3820068231
508UbiquitinationELLEYEEKKRQAEEE
HHHHHHHHHHHHHHH		41.12-
516UbiquitinationKRQAEEEKMALPELV
HHHHHHHHHHHHHHH		32.52-
553UbiquitinationWSTALQAKSVAVKTT
HHHHHHHHCCEEECC		32.28-
558UbiquitinationQAKSVAVKTTRFASF
HHHCCEEECCEECCC		34.1521906983
558 (in isoform 1)Ubiquitination-34.1521890473
558 (in isoform 2)Ubiquitination-34.1521890473
559PhosphorylationAKSVAVKTTRFASFP
HHCCEEECCEECCCC		19.32-
5742-HydroxyisobutyrylationDYLVIQIKKFTFGLD
CEEEEEEEEEEECCC		26.01-
574UbiquitinationDYLVIQIKKFTFGLD
CEEEEEEEEEEECCC		26.0121890473
574 (in isoform 1)Ubiquitination-26.0121890473
574 (in isoform 2)Ubiquitination-26.0121890473
575UbiquitinationYLVIQIKKFTFGLDW
EEEEEEEEEEECCCC		51.7921890473
575 (in isoform 1)Ubiquitination-51.7921890473
575 (in isoform 2)Ubiquitination-51.7921890473
585UbiquitinationFGLDWVPKKLDVSIE
ECCCCCCCEECEEEE		57.24-
585 (in isoform 1)Ubiquitination-57.2421890473
585 (in isoform 2)Ubiquitination-57.2421890473
586UbiquitinationGLDWVPKKLDVSIEM
CCCCCCCEECEEEEC		43.8021906983
586 (in isoform 1)Ubiquitination-43.8021890473
586 (in isoform 2)Ubiquitination-43.8021890473
593SulfoxidationKLDVSIEMPEELDIS
EECEEEECCCCCCHH		4.8930846556
623PhosphorylationDIAPPLVTPDEPKGS
CCCCCCCCCCCCCCC		32.4830266825
623 (in isoform 2)Phosphorylation-32.4825849741
635 (in isoform 2)Phosphorylation-28.8722199227
651PhosphorylationSPHFSSPTSPMLDES
CCCCCCCCCCCCCHH		47.6226074081
652PhosphorylationPHFSSPTSPMLDESV
CCCCCCCCCCCCHHH		16.2326074081
658PhosphorylationTSPMLDESVIIQLVE
CCCCCCHHHHHHHHH		20.48-
680PhosphorylationCRKAVYYTGNSGAEA
HCEEEEECCCHHHHH		16.5220860994
683PhosphorylationAVYYTGNSGAEAAMN
EEEECCCHHHHHHHH		40.5020860994
694PhosphorylationAAMNWVMSHMDDPDF
HHHHHHHHCCCCCCC		13.1720860994
715PhosphorylationPGSSGPGSTSAAADP
CCCCCCCCCCCCCCC		23.4826074081
716PhosphorylationGSSGPGSTSAAADPP
CCCCCCCCCCCCCCC		28.4426074081
717PhosphorylationSSGPGSTSAAADPPP
CCCCCCCCCCCCCCC		20.0126074081
720 (in isoform 2)Ubiquitination-29.5621890473
737PhosphorylationTIVSMGFSRDQALKA
HHHHCCCCHHHHHHH		29.2620860994
743AcetylationFSRDQALKALRATNN
CCHHHHHHHHHHHCC		48.6825953088
743UbiquitinationFSRDQALKALRATNN
CCHHHHHHHHHHHCC		48.6822053931
743 (in isoform 1)Ubiquitination-48.6821890473
751PhosphorylationALRATNNSLERAVDW
HHHHHCCHHHHHHHH		33.4124719451
770 (in isoform 2)Ubiquitination-15.1421890473
779PhosphorylationMDISEGRSAADSISE
HHHHCCCCHHHHHCC		38.3729255136
783PhosphorylationEGRSAADSISESVPV
CCCCHHHHHCCCCCC		24.2429255136
785PhosphorylationRSAADSISESVPVGP
CCHHHHHCCCCCCCC		27.9830266825
787PhosphorylationAADSISESVPVGPKV
HHHHHCCCCCCCCCC		25.5730266825
793UbiquitinationESVPVGPKVRDGPGK
CCCCCCCCCCCCCCH		43.9322053931
793 (in isoform 1)Ubiquitination-43.9321890473
813 (in isoform 2)Ubiquitination-14.3921890473
822 (in isoform 2)Ubiquitination-25.5121890473
832PhosphorylationKEGRWVIYNDQKVCA
ECCEEEEECCCEEEC		11.7627642862
836UbiquitinationWVIYNDQKVCASEKP
EEEECCCEEECCCCC		41.9921890473
836 (in isoform 1)Ubiquitination-41.9921890473
840PhosphorylationNDQKVCASEKPPKDL
CCCEEECCCCCCCCC		40.8130622161
842UbiquitinationQKVCASEKPPKDLGY
CEEECCCCCCCCCCE		65.21-
845UbiquitinationCASEKPPKDLGYIYF
ECCCCCCCCCCEEEE		74.2921890473
845 (in isoform 1)Ubiquitination-74.2921890473
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP5_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 UBP5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TADA3_HUMANTADA3physical
16189514
UBC_HUMANUBCphysical
18482987
UBP13_HUMANUSP13physical
19615732
UBC_HUMANUBCphysical
22216260
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
TRAF6_HUMANTRAF6physical
20622874
UBC_HUMANUBCphysical
19373254
TRIML_HUMANTRIML1physical
19156909
UBC_HUMANUBCphysical
8841133
UBC_HUMANUBCphysical
16007098
A4_HUMANAPPphysical
21832049
UBR1_HUMANUBR1physical
22939629
ZN593_HUMANZNF593physical
22939629
ZFP91_HUMANZFP91physical
22939629
URM1_HUMANURM1physical
22939629
XIAP_HUMANXIAPphysical
22939629
UCHL3_HUMANUCHL3physical
22939629
VATA_HUMANATP6V1Aphysical
22939629
TRI26_HUMANTRIM26physical
23105109
TRI39_HUMANTRIM39physical
23105109
TRIM5_HUMANTRIM5physical
23105109
UBC_HUMANUBCphysical
23287719
UB2R1_HUMANCDC34physical
22863883
GNPI1_HUMANGNPDA1physical
22863883
HERC4_HUMANHERC4physical
22863883
IPO9_HUMANIPO9physical
22863883
PDIA1_HUMANP4HBphysical
22863883
PCNA_HUMANPCNAphysical
22863883
RD23A_HUMANRAD23Aphysical
22863883
TCAL4_HUMANTCEAL4physical
22863883
SYWC_HUMANWARSphysical
22863883
RAD18_HUMANRAD18physical
24454762
UBA1_HUMANUBA1physical
25207809
UBTD2_HUMANUBTD2physical
25207809
PA2GA_HUMANPLA2G2Aphysical
22118674
UBC_HUMANUBCphysical
16564012
DAZP2_HUMANDAZAP2physical
25416956
TM239_HUMANTMEM239physical
25416956
UBC_HUMANUBCphysical
24424410
GDE_HUMANAGLphysical
26344197
LAGE3_HUMANLAGE3physical
26344197
TMOD3_HUMANTMOD3physical
26344197
YTHD1_HUMANYTHDF1physical
26344197
YTHD2_HUMANYTHDF2physical
26344197
UBC_HUMANUBCphysical
25970461
UBC_HUMANUBCphysical
27066941
SMUF1_HUMANSMURF1physical
27133717
UBC_HUMANUBCphysical
26876099
FOXM1_HUMANFOXM1physical
26912724
FOXM1_HUMANFOXM1physical
28807830
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 UBP5_HUMAN

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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 ALA-2, AND MASS SPECTROMETRY.
"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-184, AND MASS SPECTROMETRY.
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-783, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-623, AND MASSSPECTROMETRY.

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