UBP35_HUMAN - dbPTM
UBP35_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP35_HUMAN
UniProt AC Q9P2H5
Protein Name Ubiquitin carboxyl-terminal hydrolase 35
Gene Name USP35
Organism Homo sapiens (Human).
Sequence Length 1018
Subcellular Localization
Protein Description
Protein Sequence MDKILEAVVTSSYPVSVKQGLVRRVLEAARQPLEREQCLALLALGARLYVGGAEELPRRVGCQLLHVAGRHHPDVFAEFFSARRVLRLLQGGAGPPGPRALACVQLGLQLLPEGPAADEVFALLRREVLRTVCERPGPAACAQVARLLARHPRCVPDGPHRLLFCQQLVRCLGRFRCPAEGEEGAVEFLEQAQQVSGLLAQLWRAQPAAILPCLKELFAVISCAEEEPPSSALASVVQHLPLELMDGVVRNLSNDDSVTDSQMLTAISRMIDWVSWPLGKNIDKWIIALLKGLAAVKKFSILIEVSLTKIEKVFSKLLYPIVRGAALSVLKYMLLTFQHSHEAFHLLLPHIPPMVASLVKEDSNSGTSCLEQLAELVHCMVFRFPGFPDLYEPVMEAIKDLHVPNEDRIKQLLGQDAWTSQKSELAGFYPRLMAKSDTGKIGLINLGNTCYVNSILQALFMASDFRHCVLRLTENNSQPLMTKLQWLFGFLEHSQRPAISPENFLSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSSPSPPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAFPPPERCRRRRLGSVMRPTEDITARELPPPTSAQGPGRVGPRRQRKHCITEDTPPTSLYIEGLDSKEAGGQSSQEERIEREEEGKEERTEKEEVGEEEESTRGEGEREKEEEVEEEEEKVEKETEKEAEQEKEEDSLGAGTHPDAAIPSGERTCGSEGSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVSIPLLLRLPLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGAARPAASLGTADRPEPENQWYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYRQRPREGPEAELGSSRVRTEPTLHKDLMEAISKDNILYLQEQEKEARSRAAYISALPTSPHWGRGFDEDKDEDEGSPGGCNPAGGNGGDFHRLVF
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
275PhosphorylationSRMIDWVSWPLGKNI
HHHHHHHHCCCCCCH
20.79-
300PhosphorylationLAAVKKFSILIEVSL
HHHHHHHHEEEEEEC
25.9321712546
306PhosphorylationFSILIEVSLTKIEKV
HHEEEEEECHHHHHH
19.9621712546
357PhosphorylationHIPPMVASLVKEDSN
CCCHHHHHHHCCCCC
23.4524719451
410UbiquitinationVPNEDRIKQLLGQDA
CCCHHHHHHHHCCCC
35.4729967540
419PhosphorylationLLGQDAWTSQKSELA
HHCCCCCCCCHHHHC
24.0129083192
420PhosphorylationLGQDAWTSQKSELAG
HCCCCCCCCHHHHCC
25.5529083192
549PhosphorylationICQKLKQSSSPSPPE
HHHHHHHCCCCCCCC
31.0628348404
550PhosphorylationCQKLKQSSSPSPPEE
HHHHHHCCCCCCCCC
43.7228348404
551PhosphorylationQKLKQSSSPSPPEEP
HHHHHCCCCCCCCCC
34.3428348404
553PhosphorylationLKQSSSPSPPEEPPA
HHHCCCCCCCCCCCC
55.8428348404
612PhosphorylationRCRRRRLGSVMRPTE
HHHHHCCCCCCCCCC
19.1818669648
613PhosphorylationCRRRRLGSVMRPTED
HHHHCCCCCCCCCCC
19.8223911959
618PhosphorylationLGSVMRPTEDITARE
CCCCCCCCCCCCCCC
35.6129759185
622PhosphorylationMRPTEDITARELPPP
CCCCCCCCCCCCCCC
31.8026434776
630PhosphorylationARELPPPTSAQGPGR
CCCCCCCCCCCCCCC
42.3323312004
631PhosphorylationRELPPPTSAQGPGRV
CCCCCCCCCCCCCCC
25.1123312004
658PhosphorylationDTPPTSLYIEGLDSK
CCCCCCEEEECCCCC
9.1927642862
770PhosphorylationDLVNYFLSPEKLTAE
HHHHHHCCHHHCCCC
22.5527251275
775PhosphorylationFLSPEKLTAENRYYC
HCCHHHCCCCCCEEE
42.8927251275
780PhosphorylationKLTAENRYYCESCAS
HCCCCCCEEECCCCC
24.8524043423
781PhosphorylationLTAENRYYCESCASL
CCCCCCEEECCCCCC
6.1124043423
784PhosphorylationENRYYCESCASLQDA
CCCEEECCCCCCCCH
16.0624043423
787PhosphorylationYYCESCASLQDAEKV
EEECCCCCCCCHHHH
30.7824043423
798PhosphorylationAEKVVELSQGPCYLI
HHHHHHHHCCCHHHH
21.4230257219
803PhosphorylationELSQGPCYLILTLLR
HHHCCCHHHHHHHHH
10.4230257219
807PhosphorylationGPCYLILTLLRFSFD
CCHHHHHHHHHHHCH
19.4230257219
845PhosphorylationAGGRGQAYDLCSVVV
CCCCCHHHHHHEEEE
11.1024043423
849PhosphorylationGQAYDLCSVVVHSGV
CHHHHHHEEEEECCC
25.8324043423
854PhosphorylationLCSVVVHSGVSSESG
HHEEEEECCCCCCCC
29.3124043423
857PhosphorylationVVVHSGVSSESGHYY
EEEECCCCCCCCCEE
31.7324043423
858PhosphorylationVVHSGVSSESGHYYC
EEECCCCCCCCCEEE
33.1224043423
860PhosphorylationHSGVSSESGHYYCYA
ECCCCCCCCCEEEEE
32.5824043423
863PhosphorylationVSSESGHYYCYAREG
CCCCCCCEEEEECCC
9.9624043423
864PhosphorylationSSESGHYYCYAREGA
CCCCCCEEEEECCCC
3.5424043423
866PhosphorylationESGHYYCYAREGAAR
CCCCEEEEECCCCCC
7.8024043423
937PhosphorylationGPEAELGSSRVRTEP
CCCCCCCCCCCCCCC
27.8228122231
938PhosphorylationPEAELGSSRVRTEPT
CCCCCCCCCCCCCCC
32.7528122231
948AcetylationRTEPTLHKDLMEAIS
CCCCCCCHHHHHHHH
56.5219827047
956AcetylationDLMEAISKDNILYLQ
HHHHHHHHCCEEEHH
48.9919827057
967UbiquitinationLYLQEQEKEARSRAA
EEHHHHHHHHHHHHH
57.2629967540
971PhosphorylationEQEKEARSRAAYISA
HHHHHHHHHHHHHHH
33.0625072903
975PhosphorylationEARSRAAYISALPTS
HHHHHHHHHHHCCCC
8.4023312004
977PhosphorylationRSRAAYISALPTSPH
HHHHHHHHHCCCCCC
15.8628152594
981PhosphorylationAYISALPTSPHWGRG
HHHHHCCCCCCCCCC
56.6025159151
982PhosphorylationYISALPTSPHWGRGF
HHHHCCCCCCCCCCC
16.9028152594

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 UBP35_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP35_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 UBP35_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP35_HUMANUSP35physical
25915564
STING_HUMANTMEM173physical
27801882
TNIP2_HUMANTNIP2physical
26348204

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 UBP35_HUMAN

loading...

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-613, AND MASSSPECTROMETRY.

TOP