UBP20_HUMAN - dbPTM
UBP20_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP20_HUMAN
UniProt AC Q9Y2K6
Protein Name Ubiquitin carboxyl-terminal hydrolase 20
Gene Name USP20
Organism Homo sapiens (Human).
Sequence Length 914
Subcellular Localization Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . According to PubMed:12865408, it localizes in the endoplasmic reticulum
however the relevance of such result is unclear.
Protein Description Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains..
Protein Sequence MGDSRDLCPHLDSIGEVTKEDLLLKSKGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTFIKLNKAFQAEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSVAQPLGPENLHGEQKIEAETRAV
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
19UbiquitinationDSIGEVTKEDLLLKS
CCCCCCCHHHHHHHC		55.1732015554
103PhosphorylationLAAPLLGSSSKFSEQ
HHHHHHCCCCCCCCC		31.2625159151
104PhosphorylationAAPLLGSSSKFSEQD
HHHHHCCCCCCCCCC		35.4330576142
105PhosphorylationAPLLGSSSKFSEQDS
HHHHCCCCCCCCCCC		39.1430576142
106UbiquitinationPLLGSSSKFSEQDSP
HHHCCCCCCCCCCCC		55.6529967540
108PhosphorylationLGSSSKFSEQDSPPP
HCCCCCCCCCCCCCC		37.7829396449
112PhosphorylationSKFSEQDSPPPSHPL
CCCCCCCCCCCCCCC		38.7129255136
116PhosphorylationEQDSPPPSHPLKAVP
CCCCCCCCCCCCCEE		43.4429396449
132PhosphorylationAVADEGESESEDDDL
EEECCCCCCCCCCCC		58.2329255136
134PhosphorylationADEGESESEDDDLKP
ECCCCCCCCCCCCCC		56.4529255136
145PhosphorylationDLKPRGLTGMKNLGN
CCCCCCCCCCHHCCC		37.7526074081
194UbiquitinationALCKSYQKLVSEVWH
HHHHHHHHHHHHHHH		42.4929967540
202UbiquitinationLVSEVWHKKRPSYVV
HHHHHHHCCCCCCCC		34.4629967540
203UbiquitinationVSEVWHKKRPSYVVP
HHHHHHCCCCCCCCC		57.5729967540
206PhosphorylationVWHKKRPSYVVPTSL
HHHCCCCCCCCCCCH		34.2925219547
207PhosphorylationWHKKRPSYVVPTSLS
HHCCCCCCCCCCCHH		14.2425219547
211PhosphorylationRPSYVVPTSLSHGIK
CCCCCCCCCHHHCHH		30.5925219547
212PhosphorylationPSYVVPTSLSHGIKL
CCCCCCCCHHHCHHH		23.0825219547
214PhosphorylationYVVPTSLSHGIKLVN
CCCCCCHHHCHHHCC		21.3125219547
227PhosphorylationVNPMFRGYAQQDTQE
CCHHHCCCCHHHHHH		9.2925884760
243UbiquitinationLRCLMDQLHEELKEP
HHHHHHHHHHHHCCC		4.8422817900
248UbiquitinationDQLHEELKEPVVATV
HHHHHHHCCCCEEEE		64.3522817900
254PhosphorylationLKEPVVATVALTEAR
HCCCCEEEEEEEECC		8.4929052541
258PhosphorylationVVATVALTEARDSDS
CEEEEEEEECCCCCC		20.1922817900
263PhosphorylationALTEARDSDSSDTDE
EEEECCCCCCCCCCH		33.5626503892
265PhosphorylationTEARDSDSSDTDEKR
EECCCCCCCCCCHHC		33.7820363803
266PhosphorylationEARDSDSSDTDEKRE
ECCCCCCCCCCHHCC		49.9020363803
268PhosphorylationRDSDSSDTDEKREGD
CCCCCCCCCHHCCCC		48.2629052541
277PhosphorylationEKREGDRSPSEDEFL
HHCCCCCCCCHHHCC		37.2023312004
279PhosphorylationREGDRSPSEDEFLSC
CCCCCCCCHHHCCCC		59.9523312004
285PhosphorylationPSEDEFLSCDSSSDR
CCHHHCCCCCCCCCC		22.6230576142
288PhosphorylationDEFLSCDSSSDRGEG
HHCCCCCCCCCCCCC		35.7530576142
289PhosphorylationEFLSCDSSSDRGEGD
HCCCCCCCCCCCCCC		24.0230108239
290PhosphorylationFLSCDSSSDRGEGDG
CCCCCCCCCCCCCCC		34.9730576142
304PhosphorylationGQGRGGGSSQAETEL
CCCCCCCCCHHEEEE		23.6625627689
305PhosphorylationQGRGGGSSQAETELL
CCCCCCCCHHEEEEE		36.3625262027
309PhosphorylationGGSSQAETELLIPDE
CCCCHHEEEEECCCH		34.6425627689
331UbiquitinationKERMKDRKFSWGQQR
HHHHCCCCCCCCCCC		54.61-
333PhosphorylationRMKDRKFSWGQQRTN
HHCCCCCCCCCCCCC		33.0723401153
339PhosphorylationFSWGQQRTNSEQVDE
CCCCCCCCCHHHCCC		38.4722817900
341PhosphorylationWGQQRTNSEQVDEDA
CCCCCCCHHHCCCCC		28.8822817900
352PhosphorylationDEDADVDTAMAALDD
CCCCCHHHHHHHHCC		20.4127251275
368PhosphorylationPAEAQPPSPRSSSPC
CCCCCCCCCCCCCCC		39.3630108239
371PhosphorylationAQPPSPRSSSPCRTP
CCCCCCCCCCCCCCC		38.2526503892
372PhosphorylationQPPSPRSSSPCRTPE
CCCCCCCCCCCCCCC		39.3130278072
373PhosphorylationPPSPRSSSPCRTPEP
CCCCCCCCCCCCCCC		29.3025159151
377PhosphorylationRSSSPCRTPEPDNDA
CCCCCCCCCCCCCCC		38.4325159151
388PhosphorylationDNDAHLRSSSRPCSP
CCCCHHHCCCCCCCC		38.7430108239
389PhosphorylationNDAHLRSSSRPCSPV
CCCHHHCCCCCCCCC		24.7530108239
390PhosphorylationDAHLRSSSRPCSPVH
CCHHHCCCCCCCCCC		41.3030576142
394PhosphorylationRSSSRPCSPVHHHEG
HCCCCCCCCCCCCCC		32.4127794612
406PhosphorylationHEGHAKLSSSPPRAS
CCCCCCCCCCCCCCC		28.2330266825
407PhosphorylationEGHAKLSSSPPRASP
CCCCCCCCCCCCCCC		58.2530266825
408PhosphorylationGHAKLSSSPPRASPV
CCCCCCCCCCCCCCC		35.2330266825
413PhosphorylationSSSPPRASPVRMAPS
CCCCCCCCCCCCCHH		25.8030266825
420PhosphorylationSPVRMAPSYVLKKAQ
CCCCCCHHHHHHHHH		20.5226074081
421PhosphorylationPVRMAPSYVLKKAQV
CCCCCHHHHHHHHHH		14.5624719451
425UbiquitinationAPSYVLKKAQVLSAG
CHHHHHHHHHHHCCC		39.6329967540
430PhosphorylationLKKAQVLSAGSRRRK
HHHHHHHCCCCHHHH		31.5621712546
482UbiquitinationLSLPIPGKEDLAKLH
HCCCCCCHHHHHHHH		42.5822817900
487UbiquitinationPGKEDLAKLHSAIYQ
CCHHHHHHHHHHHHH		54.7722817900
553MethylationFFAADELKGDNMYSC
HHHHHHCCCCCCCCH		63.27-
596PhosphorylationFRHEVMYSFKINSHV
CCCHHHHEEEECCEE		11.2828509920
803UbiquitinationIEIDTFIKLNKAFQA
CCHHHHHHHHHHHHC		41.64-
835UbiquitinationWEAFVKGKDNEPPGP
HHHHHCCCCCCCCCC		52.22-
852UbiquitinationNSRIAQVKGSGHVQL
CCCEEEEECCCEEEE		34.9729967540
854PhosphorylationRIAQVKGSGHVQLKQ
CEEEEECCCEEEEEC		21.7328348404
860UbiquitinationGSGHVQLKQGADYGQ
CCCEEEEECCCCCCC		29.6029967540
906UbiquitinationENLHGEQKIEAETRA
CCCCCHHHHHHHHCC		37.9132015554
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
333SPhosphorylationKinasePRKACAP17612
GPS
-KUbiquitinationE3 ubiquitin ligaseHERC2O95714
PMID:25355518
-KUbiquitinationE3 ubiquitin ligaseVHLP40337
PMID:12056827
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP20_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 UBP20_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IOD2_HUMANDIO2physical
12865408
ACADM_HUMANACADMphysical
19615732
APBA2_HUMANAPBA2physical
19615732
HEMH_HUMANFECHphysical
19615732
EIF3E_HUMANEIF3Ephysical
19615732
MYO1A_HUMANMYO1Aphysical
19615732
MYO1C_HUMANMYO1Cphysical
19615732
PLEC_HUMANPLECphysical
19615732
PLK1_HUMANPLK1physical
19615732
PSMD7_HUMANPSMD7physical
19615732
PSD11_HUMANPSMD11physical
19615732
PSD12_HUMANPSMD12physical
19615732
RAD17_HUMANRAD17physical
19615732
RFC2_HUMANRFC2physical
19615732
RFC3_HUMANRFC3physical
19615732
RFC4_HUMANRFC4physical
19615732
UCHL3_HUMANUCHL3physical
19615732
EIF3C_HUMANEIF3Cphysical
19615732
HERC2_HUMANHERC2physical
19615732
VAPB_HUMANVAPBphysical
19615732
VAPA_HUMANVAPAphysical
19615732
PSMD6_HUMANPSMD6physical
19615732
NU153_HUMANNUP153physical
19615732
RENR_HUMANATP6AP2physical
19615732
ECI2_HUMANECI2physical
19615732
N4BP3_HUMANN4BP3physical
19615732
SUN2_HUMANSUN2physical
19615732
ZN770_HUMANZNF770physical
19615732
LRC59_HUMANLRRC59physical
19615732
MA7D1_HUMANMAP7D1physical
19615732
ATD3B_HUMANATAD3Bphysical
19615732
RGPD5_HUMANRGPD5physical
19615732
PDIP3_HUMANPOLDIP3physical
19615732
NEUL4_HUMANNEURL4physical
19615732
ALAT2_HUMANGPT2physical
19615732
SYTL4_HUMANSYTL4physical
19615732
PKHA7_HUMANPLEKHA7physical
19615732
HIF1A_HUMANHIF1Aphysical
15776016
CP110_HUMANCCP110physical
23486064
UBP33_HUMANUSP33physical
23486064
UBP20_HUMANUSP20physical
23486064
NEUL4_HUMANNEURL4physical
23486064
RAD17_HUMANRAD17physical
24923443
PA2GA_HUMANPLA2G2Aphysical
22118674
BEND5_HUMANBEND5physical
25416956
FATE1_HUMANFATE1physical
25416956
BEND7_HUMANBEND7physical
25416956
IHO1_HUMANCCDC36physical
25416956
ARRB2_RATArrb2physical
26839314
TRAF6_HUMANTRAF6physical
21525354
CLSPN_HUMANCLSPNphysical
25355518
HERC2_HUMANHERC2physical
25355518
CLSPN_HUMANCLSPNphysical
25326330
HERC2_HUMANHERC2physical
25326330
STING_HUMANTMEM173physical
27801882
MK06_HUMANMAPK6physical
28167606
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 UBP20_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-132; SER-134 ANDSER-368, AND MASS 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-132; SER-134; SER-373;THR-377; SER-406 AND SER-413, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134; SER-407AND SER-413, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134; THR-258AND SER-263, AND MASS SPECTROMETRY.

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