UBP33_MOUSE - dbPTM
UBP33_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP33_MOUSE
UniProt AC Q8R5K2
Protein Name Ubiquitin carboxyl-terminal hydrolase 33
Gene Name Usp33
Organism Mus musculus (Mouse).
Sequence Length 909
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 (By similarity).
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 MTTFRNHCPHLDSVGEITKEDLIQKSLGACQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTPPSLPHVRQPQQTQENSVQDFKIPSNPALKTPMVAVSEDLDIEVEEEDELKARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEMEEEPQTLTSEETVEEEKSQSDVDFQSCESCSSSEKAENESGSKGFPEDSNETTMLIQDEDDLEMAKDWQKEKVCNKINKANADVELDKDRDTVCETVDLNSQETVKVQIHGRASESITDVHLNDLATSQILPSNESVSPRLSASPPKLGSLWPGLSPPHKKAQSTSAKRKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAKLHSSSHPTIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGIPPRKASYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIELEKIEKRRKTELEIFIRLNRAFQEEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGSVMLKQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDVLQAEEKIEVETRSL
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
34UbiquitinationLGACQDCKVRGPNLW
CCCCCCCCCCCCCHH		43.1722790023
98PhosphorylationFLDRKLGTPPSLPHV
HHHCCCCCCCCCCCC		42.3226643407
101PhosphorylationRKLGTPPSLPHVRQP
CCCCCCCCCCCCCCC		56.5926643407
227UbiquitinationANLFQGIKTVNPTFR
CHHHCCCCCCCCCCC		53.9322790023
247S-nitrosocysteineDAQEFLRCLMDLLHE
HHHHHHHHHHHHHHH		3.92-
247S-nitrosylationDAQEFLRCLMDLLHE
HHHHHHHHHHHHHHH		3.9220925432
281PhosphorylationETVEEEKSQSDVDFQ
HHHHHHHHCCCCCHH		37.8929899451
283PhosphorylationVEEEKSQSDVDFQSC
HHHHHHCCCCCHHHH		46.8525521595
342UbiquitinationKVCNKINKANADVEL
HHHHHHHHHCCCCCC		46.6322790023
377PhosphorylationVQIHGRASESITDVH
EEEECCCCCCCCEEE		30.4323984901
379PhosphorylationIHGRASESITDVHLN
EECCCCCCCCEEEHH		28.4423984901
381PhosphorylationGRASESITDVHLNDL
CCCCCCCCEEEHHHH		41.0523984901
390PhosphorylationVHLNDLATSQILPSN
EEHHHHHHCCCCCCC		28.5823984901
391PhosphorylationHLNDLATSQILPSNE
EHHHHHHCCCCCCCC		15.0423984901
396PhosphorylationATSQILPSNESVSPR
HHCCCCCCCCCCCCC		50.1923984901
399PhosphorylationQILPSNESVSPRLSA
CCCCCCCCCCCCCCC		31.9523984901
401PhosphorylationLPSNESVSPRLSASP
CCCCCCCCCCCCCCC		17.3730352176
405PhosphorylationESVSPRLSASPPKLG
CCCCCCCCCCCCCCC		28.1623984901
407PhosphorylationVSPRLSASPPKLGSL
CCCCCCCCCCCCCCC		38.0626643407
413PhosphorylationASPPKLGSLWPGLSP
CCCCCCCCCCCCCCC		37.3826643407
419PhosphorylationGSLWPGLSPPHKKAQ
CCCCCCCCCCCHHCC		42.1526643407
429PhosphorylationHKKAQSTSAKRKKQH
CHHCCCCCHHHHHHH		36.7228059163
441PhosphorylationKQHKKYRSVISDIFD
HHHHHHHHHHHHHCC		22.2525367039
444PhosphorylationKKYRSVISDIFDGTV
HHHHHHHHHHCCCCE		23.6225367039
450PhosphorylationISDIFDGTVISSVQC
HHHHCCCCEEEEEEE		19.2625367039
453PhosphorylationIFDGTVISSVQCLTC
HCCCCEEEEEEEECC		21.8125367039
454PhosphorylationFDGTVISSVQCLTCD
CCCCEEEEEEEECCC		12.7025367039
459PhosphorylationISSVQCLTCDRVSIT
EEEEEEECCCCEEEE		21.7125367039
464PhosphorylationCLTCDRVSITLETFQ
EECCCCEEEEEEEEC		15.6825367039
466PhosphorylationTCDRVSITLETFQDL
CCCCEEEEEEEECCC		15.8425367039
469PhosphorylationRVSITLETFQDLSLP
CEEEEEEEECCCCCC		29.7025367039
474PhosphorylationLETFQDLSLPIPGKE
EEEECCCCCCCCCHH		40.1522006019
488PhosphorylationEDLAKLHSSSHPTIV
HHHHHHHHCCCCEEE		43.9328066266
489PhosphorylationDLAKLHSSSHPTIVK
HHHHHHHCCCCEEEE		23.1728066266
490PhosphorylationLAKLHSSSHPTIVKA
HHHHHHCCCCEEEEC		36.1828066266
493PhosphorylationLHSSSHPTIVKAGSC
HHHCCCCEEEECCCC		32.7428066266
561AcetylationMYSCEKCKKLRNGVK
CCCHHHHHHHHCCCC		66.958275909
571AcetylationRNGVKFCKVQKFPEI
HCCCCEEECCCCCCC		51.328275919
849UbiquitinationNTKIAVTKCGSVMLK
CCEEEEEECCCEEEE		29.9622790023
906PhosphorylationEEKIEVETRSL----
HHCEEEEECCC----		30.6322324799
908PhosphorylationKIEVETRSL------
CEEEEECCC------		45.9422324799
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 UBP33_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP33_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROBO1_MOUSERobo1physical
19684588
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP33_MOUSE

loading...

Related Literatures of Post-Translational Modification

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