UBP33_HUMAN - dbPTM
UBP33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP33_HUMAN
UniProt AC Q8TEY7
Protein Name Ubiquitin carboxyl-terminal hydrolase 33
Gene Name USP33
Organism Homo sapiens (Human).
Sequence Length 942
Subcellular Localization Cytoplasm, perinuclear region . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (PubMed:23486064).
Isoform 3: Golgi apparatus .
Protein Description Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and 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, 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. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains..
Protein Sequence MTGSNSHITILTLKVLPHFESLGKQEKIPNKMSAFRNHCPHLDSVGEITKEDLIQKSLGTCQDCKVQGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKTPLVAVFDDLDIEADEEDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTITTEETMEEDKSQSDVDFQSCESCSNSDRAENENGSRCFSEDNNETTMLIQDDENNSEMSKDWQKEKMCNKINKVNSEGEFDKDRDSISETVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQILPSNEGVNPRLSASPPKSGNLWPGLAPPHKKAQSASPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQKEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGNVMLRQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDILQAEEKIEVETRSL
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
2Phosphorylation------MTGSNSHIT
------CCCCCCCEE
49.6828851738
4Phosphorylation----MTGSNSHITIL
----CCCCCCCEEEE
26.4528851738
6Phosphorylation--MTGSNSHITILTL
--CCCCCCCEEEEEE
20.2628851738
9PhosphorylationTGSNSHITILTLKVL
CCCCCCEEEEEEEEH
12.4328851738
12PhosphorylationNSHITILTLKVLPHF
CCCEEEEEEEEHHHH
22.2328851738
19UbiquitinationTLKVLPHFESLGKQE
EEEEHHHHHHCCCCC
6.8721963094
31AcetylationKQEKIPNKMSAFRNH
CCCCCCCHHHHHHHH
28.9525953088
34UbiquitinationKIPNKMSAFRNHCPH
CCCCHHHHHHHHCCC
12.1532015554
50UbiquitinationDSVGEITKEDLIQKS
CCCCCCCHHHHHHHH
55.6921963094
65UbiquitinationLGTCQDCKVQGPNLW
HCCCCCCCCCCCCHH
45.9732015554
79UbiquitinationWACLENRCSYVGCGE
HHHHHCCCCCCCCCC
5.3323000965
95UbiquitinationQVDHSTIHSQETKHY
CCCCCCCCCCCCCEE
24.4229967540
120UbiquitinationWCYACSKEVFLDRKL
HHHHCCCCHHHCCCC
23.3929967540
126UbiquitinationKEVFLDRKLGTQPSL
CCHHHCCCCCCCCCC
51.4329967540
129PhosphorylationFLDRKLGTQPSLPHV
HHCCCCCCCCCCCCC
47.9828555341
132PhosphorylationRKLGTQPSLPHVRQP
CCCCCCCCCCCCCCC
44.7228348404
151UbiquitinationENSVQDFKIPSNTTL
CCCCCCCCCCCCCCC
63.0929967540
182UbiquitinationEEDELRARGLTGLKN
CHHHHHHHCCCCCCC
33.9321963094
186UbiquitinationLRARGLTGLKNIGNT
HHHHCCCCCCCCCCC
39.4321963094
188UbiquitinationARGLTGLKNIGNTCY
HHCCCCCCCCCCCHH
48.1122817900
195UbiquitinationKNIGNTCYMNAALQA
CCCCCCHHHHHHHHH
7.4333845483
199UbiquitinationNTCYMNAALQALSNC
CCHHHHHHHHHHHCC
8.6629967540
204UbiquitinationNAALQALSNCPPLTQ
HHHHHHHHCCCCCHH
39.1333845483
227UbiquitinationARTDKKPAICKSYLK
CCCCCCHHHHHHHHH
28.7923000965
227 (in isoform 2)Ubiquitination-28.79-
230UbiquitinationDKKPAICKSYLKLMT
CCCHHHHHHHHHHHH
35.7029967540
237PhosphorylationKSYLKLMTELWHKSR
HHHHHHHHHHHHHCC
38.0627762562
242AcetylationLMTELWHKSRPGSVV
HHHHHHHHCCCCCCC
36.267977275
258UbiquitinationTTLFQGIKTVNPTFR
CCHHCCCEECCCCCC
53.9323000965
267PhosphorylationVNPTFRGYSQQDAQE
CCCCCCCCCHHHHHH
10.0728152594
268PhosphorylationNPTFRGYSQQDAQEF
CCCCCCCCHHHHHHH
24.9628152594
312PhosphorylationETMEEDKSQSDVDFQ
HHHHHHCCCCCCCHH
47.43-
314PhosphorylationMEEDKSQSDVDFQSC
HHHHCCCCCCCHHHH
46.8530576142
320PhosphorylationQSDVDFQSCESCSNS
CCCCCHHHHHCCCCC
21.6130576142
323PhosphorylationVDFQSCESCSNSDRA
CCHHHHHCCCCCCCC
27.4626471730
325PhosphorylationFQSCESCSNSDRAEN
HHHHHCCCCCCCCCC
48.9628985074
327PhosphorylationSCESCSNSDRAENEN
HHHCCCCCCCCCCCC
16.5130576142
330UbiquitinationSCSNSDRAENENGSR
CCCCCCCCCCCCCCC
29.0221963094
333UbiquitinationNSDRAENENGSRCFS
CCCCCCCCCCCCCCC
55.2422817900
334UbiquitinationSDRAENENGSRCFSE
CCCCCCCCCCCCCCC
66.3821963094
336UbiquitinationRAENENGSRCFSEDN
CCCCCCCCCCCCCCC
37.1422817900
338UbiquitinationENENGSRCFSEDNNE
CCCCCCCCCCCCCCC
4.7533845483
340UbiquitinationENGSRCFSEDNNETT
CCCCCCCCCCCCCCE
47.9029967540
343UbiquitinationSRCFSEDNNETTMLI
CCCCCCCCCCCEEEE
44.1533845483
352UbiquitinationETTMLIQDDENNSEM
CCEEEEECCCCCCCC
59.1933845483
352 (in isoform 2)Ubiquitination-59.1921906983
361UbiquitinationENNSEMSKDWQKEKM
CCCCCCCHHHHHHHH
62.7721963094
365UbiquitinationEMSKDWQKEKMCNKI
CCCHHHHHHHHHHHH
55.8621963094
367UbiquitinationSKDWQKEKMCNKINK
CHHHHHHHHHHHHHH
56.6522817900
370UbiquitinationWQKEKMCNKINKVNS
HHHHHHHHHHHHCCC
44.7529967540
371UbiquitinationQKEKMCNKINKVNSE
HHHHHHHHHHHCCCC
42.6129967540
374UbiquitinationKMCNKINKVNSEGEF
HHHHHHHHCCCCCCC
46.3933845483
377PhosphorylationNKINKVNSEGEFDKD
HHHHHCCCCCCCCCC
50.3825159151
383UbiquitinationNSEGEFDKDRDSISE
CCCCCCCCCCCCCCE
61.0421906983
383 (in isoform 1)Ubiquitination-61.0421906983
383 (in isoform 3)Ubiquitination-61.0421906983
387PhosphorylationEFDKDRDSISETVDL
CCCCCCCCCCEEEEC
28.9830576142
389PhosphorylationDKDRDSISETVDLNN
CCCCCCCCEEEECCC
31.0325159151
391PhosphorylationDRDSISETVDLNNQE
CCCCCCEEEECCCCC
16.7227690223
401UbiquitinationLNNQETVKVQIHSRA
CCCCCEEEEEEEECC
35.5229967540
404UbiquitinationQETVKVQIHSRASEY
CCEEEEEEEECCHHH
3.4021963094
409PhosphorylationVQIHSRASEYITDVH
EEEEECCHHHEEECC
29.8028796482
411PhosphorylationIHSRASEYITDVHSN
EEECCHHHEEECCCC
13.4628796482
411UbiquitinationIHSRASEYITDVHSN
EEECCHHHEEECCCC
13.4629967540
413PhosphorylationSRASEYITDVHSNDL
ECCHHHEEECCCCCC
30.9428796482
417PhosphorylationEYITDVHSNDLSTPQ
HHEEECCCCCCCCCC
31.7128796482
421PhosphorylationDVHSNDLSTPQILPS
ECCCCCCCCCCCCCC
40.6928555341
422PhosphorylationVHSNDLSTPQILPSN
CCCCCCCCCCCCCCC
26.8928555341
437PhosphorylationEGVNPRLSASPPKSG
CCCCCCCCCCCCCCC
28.1630266825
439PhosphorylationVNPRLSASPPKSGNL
CCCCCCCCCCCCCCC
38.0610470851
442UbiquitinationRLSASPPKSGNLWPG
CCCCCCCCCCCCCCC
74.5129967540
443PhosphorylationLSASPPKSGNLWPGL
CCCCCCCCCCCCCCC
38.3925159151
461PhosphorylationHKKAQSASPKRKKQH
CCCCCCCCHHHHHHH
35.88-
481UbiquitinationVISDIFDGTIISSVQ
HHHHHCCCCCEEEEE
14.2022817900
481 (in isoform 2)Ubiquitination-14.2021906983
486UbiquitinationFDGTIISSVQCLTCD
CCCCCEEEEEEECCC
13.0533845483
512UbiquitinationLSLPIPGKEDLAKLH
CCCCCCCHHHHHHHH
42.5822817900
512 (in isoform 1)Ubiquitination-42.5821906983
512 (in isoform 3)Ubiquitination-42.5821906983
517UbiquitinationPGKEDLAKLHSSSHP
CCHHHHHHHHCCCCC
54.7733845483
544UbiquitinationYAPQGWIAFFMEYVK
CCCCCHHHHHHHHHH
5.7721963094
552UbiquitinationFFMEYVKRFVVSCVP
HHHHHHHHHHHHHCC
21.3921963094
575UbiquitinationTLQDCLAAFFARDEL
EHHHHHHHHHHCHHH
6.2721963094
583UbiquitinationFFARDELKGDNMYSC
HHHCHHHCCCCCCCH
63.2721963094
588PhosphorylationELKGDNMYSCEKCKK
HHCCCCCCCHHHHHH
19.20-
617UbiquitinationEILCIHLKRFRHELM
CCEEEEHHHHCHHHH
35.02-
668PhosphorylationSVICHHGTASSGHYI
HHHCCCCCCCCCCCE
21.00-
670PhosphorylationICHHGTASSGHYIAY
HCCCCCCCCCCCEEE
36.37-
671PhosphorylationCHHGTASSGHYIAYC
CCCCCCCCCCCEEEE
27.42-
684UbiquitinationYCRNNLNNLWYEFDD
EECCCCCCEEEEECC
34.8132142685
686UbiquitinationRNNLNNLWYEFDDQS
CCCCCCEEEEECCCC
7.8523503661
698UbiquitinationDQSVTEVSESTVQNA
CCCEEEECHHHHHCE
21.4322817900
703UbiquitinationEVSESTVQNAEAYVL
EECHHHHHCEEEEEE
43.4321963094
714AcetylationAYVLFYRKSSEEAQK
EEEEEEECCHHHHHH
47.13155477
725UbiquitinationEAQKERRRISNLLNI
HHHHHHHHHHHHHHH
42.8032142685
727PhosphorylationQKERRRISNLLNIME
HHHHHHHHHHHHHHC
21.4424719451
727UbiquitinationQKERRRISNLLNIME
HHHHHHHHHHHHHHC
21.4423503661
733UbiquitinationISNLLNIMEPSLLQF
HHHHHHHHCHHHHHH
6.3632142685
735UbiquitinationNLLNIMEPSLLQFYI
HHHHHHCHHHHHHHH
16.9423503661
736PhosphorylationLLNIMEPSLLQFYIS
HHHHHCHHHHHHHHH
28.5324719451
739UbiquitinationIMEPSLLQFYISRQW
HHCHHHHHHHHHHHH
34.1022817900
741PhosphorylationEPSLLQFYISRQWLN
CHHHHHHHHHHHHHH
5.75-
743PhosphorylationSLLQFYISRQWLNKF
HHHHHHHHHHHHHHC
13.6724719451
744UbiquitinationLLQFYISRQWLNKFK
HHHHHHHHHHHHHCC
23.3321963094
747UbiquitinationFYISRQWLNKFKTFA
HHHHHHHHHHCCCCC
3.6522817900
752UbiquitinationQWLNKFKTFAEPGPI
HHHHHCCCCCCCCCC
31.0721963094
764UbiquitinationGPISNNDFLCIHGGV
CCCCCCCEEEEECCC
6.9632142685
766UbiquitinationISNNDFLCIHGGVPP
CCCCCEEEEECCCCC
1.8723503661
778UbiquitinationVPPRKAGYIEDLVLM
CCCCCCCHHHHHHHH
13.1422817900
783UbiquitinationAGYIEDLVLMLPQNI
CCHHHHHHHHCCHHH
4.5821963094
796PhosphorylationNIWDNLYSRYGGGPA
HHHHHHHHHHCCCCC
23.3824719451
824UbiquitinationAEKIEKRRKTELEIF
HHHHHHHHHHHHHHH
62.4132142685
826UbiquitinationKIEKRRKTELEIFIR
HHHHHHHHHHHHHHH
43.9523503661
832UbiquitinationKTELEIFIRLNRAFQ
HHHHHHHHHHHHHHH
6.3432142685
832 (in isoform 2)Ubiquitination-6.34-
834UbiquitinationELEIFIRLNRAFQKE
HHHHHHHHHHHHHCC
4.3223503661
838UbiquitinationFIRLNRAFQKEDSPA
HHHHHHHHHCCCCCC
10.8722817900
843UbiquitinationRAFQKEDSPATFYCI
HHHHCCCCCCEEEEE
19.9521963094
846UbiquitinationQKEDSPATFYCISMQ
HCCCCCCEEEEEEHH
20.6522817900
851UbiquitinationPATFYCISMQWFREW
CCEEEEEEHHHHHHH
11.0221963094
855UbiquitinationYCISMQWFREWESFV
EEEEHHHHHHHHHHH
2.6032142685
857UbiquitinationISMQWFREWESFVKG
EEHHHHHHHHHHHCC
46.2323503661
863UbiquitinationREWESFVKGKDGDPP
HHHHHHHCCCCCCCC
59.2332142685
865UbiquitinationWESFVKGKDGDPPGP
HHHHHCCCCCCCCCC
53.4723503661
869UbiquitinationVKGKDGDPPGPIDNT
HCCCCCCCCCCCCCC
41.0822817900
874UbiquitinationGDPPGPIDNTKIAVT
CCCCCCCCCCEEEEE
60.9421963094
877UbiquitinationPGPIDNTKIAVTKCG
CCCCCCCEEEEEECC
34.6222817900
882UbiquitinationNTKIAVTKCGNVMLR
CCEEEEEECCCEEEE
33.2821963094
907PhosphorylationETWNFLQSIYGGGPE
HHHHHHHHHHCCCCE
21.67-
909PhosphorylationWNFLQSIYGGGPEVI
HHHHHHHHCCCCEEE
18.24-
941PhosphorylationKIEVETRSL------
HHEEEECCC------
45.9429514088

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 ligaseVHLP40337
PMID:11739384

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP33_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 UBP33_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IOD2_HUMANDIO2physical
12865408
SBP1_HUMANSELENBP1physical
19118533
KRR1_HUMANKRR1physical
19615732
IFIT5_HUMANIFIT5physical
19615732
ZFR_HUMANZFRphysical
19615732
PR38B_HUMANPRPF38Bphysical
19615732
ARRB2_HUMANARRB2physical
19363159
ARRB1_HUMANARRB1physical
19363159
ROBO1_HUMANROBO1physical
19706539
CP110_HUMANCCP110physical
23486064
UBP20_HUMANUSP20physical
23486064
NEUL4_HUMANNEURL4physical
23486064
RALA_HUMANRALAphysical
24056301
RALB_HUMANRALBphysical
24056301
UBC_HUMANUBCphysical
24377933
ARRB2_HUMANARRB2physical
24377933
TRAF6_HUMANTRAF6physical
21525354
ARRB2_HUMANARRB2physical
27835898

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 UBP33_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-439, AND MASSSPECTROMETRY.

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