ZFP62_HUMAN - dbPTM
ZFP62_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFP62_HUMAN
UniProt AC Q8NB50
Protein Name Zinc finger protein 62 homolog
Gene Name ZFP62
Organism Homo sapiens (Human).
Sequence Length 900
Subcellular Localization Nucleus .
Protein Description May play a role in differentiating skeletal muscle..
Protein Sequence MSHLKTSTEDEEPTEEYENVGNAASKWPKVEDPMPESKVGDTCVWDSKVENQQKKPVENRMKEDKSSIREAISKAKSTANIKTEQEGEASEKSLHLSPQHITHQTMPIGQRGSEQGKRVENINGTSYPSLQQKTNAVKKLHKCDECGKSFKYNSRLVQHKIMHTGEKRYECDDCGGTFRSSSSLRVHKRIHTGEKPYKCEECGKAYMSYSSLINHKSTHSGEKNCKCDECGKSFNYSSVLDQHKRIHTGEKPYECGECGKAFRNSSGLRVHKRIHTGEKPYECDICGKTFSNSSGLRVHKRIHTGEKPYECDECGKAFITCRTLLNHKSIHFGDKPYKCDECEKSFNYSSLLIQHKVIHTGEKPYECDECGKAFRNSSGLIVHKRIHTGEKPYKCDVCGKAFSYSSGLAVHKSIHPGKKAHECKECGKSFSYNSLLLQHRTIHTGERPYVCDVCGKTFRNNAGLKVHRRLHTGEKPYKCDVCGKAYISRSSLKNHKGIHLGEKPYKCSYCEKSFNYSSALEQHKRIHTREKPFGCDECGKAFRNNSGLKVHKRIHTGERPYKCEECGKAYISLSSLINHKSVHPGEKPFKCDECEKAFITYRTLTNHKKVHLGEKPYKCDVCEKSFNYTSLLSQHRRVHTREKPYECDRCEKVFRNNSSLKVHKRIHTGERPYECDVCGKAYISHSSLINHKSTHPGRTPHTCDECGKAFFSSRTLISHKRVHLGEKPFKCVECGKSFSYSSLLSQHKRIHTGEKPYVCDRCGKAFRNSSGLTVHKRIHTGEKPYECDECGKAYISHSSLINHKSVHQGKQPYNCECGKSFNYRSVLDQHKRIHTGKKPYRCNECGKAFNIRSNLTKHKRTHTGEESLNVIYVGSYSGTSQKRTYEGGNALDGGRMRMPL
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
5Sumoylation---MSHLKTSTEDEE
---CCCCCCCCCCCC		34.7028112733
17PhosphorylationDEEPTEEYENVGNAA
CCCCCHHHCCCHHHH		13.4327642862
25PhosphorylationENVGNAASKWPKVED
CCCHHHHHHCCCCCC		32.61-
48SumoylationDTCVWDSKVENQQKK
CCCEECHHCCCCCCC		51.6128112733
62SumoylationKPVENRMKEDKSSIR
CCCCHHHHHCHHHHH		60.5728112733
65SumoylationENRMKEDKSSIREAI
CHHHHHCHHHHHHHH		47.39-
65SumoylationENRMKEDKSSIREAI
CHHHHHCHHHHHHHH		47.3928112733
66PhosphorylationNRMKEDKSSIREAIS
HHHHHCHHHHHHHHH		43.23-
67PhosphorylationRMKEDKSSIREAISK
HHHHCHHHHHHHHHH		31.26-
73PhosphorylationSSIREAISKAKSTAN
HHHHHHHHHHHHHCC		33.34-
82SumoylationAKSTANIKTEQEGEA
HHHHCCCCCHHCCHH		45.90-
82SumoylationAKSTANIKTEQEGEA
HHHHCCCCCHHCCHH		45.9028112733
92SumoylationQEGEASEKSLHLSPQ
HCCHHCCCCCCCCCH		56.6828112733
93PhosphorylationEGEASEKSLHLSPQH
CCHHCCCCCCCCCHH		19.5730576142
97PhosphorylationSEKSLHLSPQHITHQ
CCCCCCCCCHHCCCC		16.2725159151
102PhosphorylationHLSPQHITHQTMPIG
CCCCHHCCCCCCCCC		13.0525850435
105PhosphorylationPQHITHQTMPIGQRG
CHHCCCCCCCCCCCC		19.8125850435
125PhosphorylationRVENINGTSYPSLQQ
EEECCCCCCCHHHHH		22.16-
126PhosphorylationVENINGTSYPSLQQK
EECCCCCCCHHHHHH		36.12-
127PhosphorylationENINGTSYPSLQQKT
ECCCCCCCHHHHHHH		9.18-
129PhosphorylationINGTSYPSLQQKTNA
CCCCCCHHHHHHHHH		30.49-
160SumoylationNSRLVQHKIMHTGEK
CHHHHEEEEECCCCC		25.32-
160SumoylationNSRLVQHKIMHTGEK
CHHHHEEEEECCCCC		25.32-
192PhosphorylationRVHKRIHTGEKPYKC
EEEEEEECCCCCEEC		44.6729496963
195UbiquitinationKRIHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
197PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
198UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
198SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
198SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
211PhosphorylationKAYMSYSSLINHKST
CEEECHHHHCCCCCC		25.6519664995
233PhosphorylationKCDECGKSFNYSSVL
EECCCCCCCCHHHHH		12.1925159151
237PhosphorylationCGKSFNYSSVLDQHK
CCCCCCHHHHHHHCC		18.3128555341
244SumoylationSSVLDQHKRIHTGEK
HHHHHHCCCCCCCCC		47.62-
244SumoylationSSVLDQHKRIHTGEK
HHHHHHCCCCCCCCC		47.62-
248PhosphorylationDQHKRIHTGEKPYEC
HHCCCCCCCCCCCCC		44.6720736484
260SumoylationYECGECGKAFRNSSG
CCCCCCHHHHCCCCC		56.88-
260SumoylationYECGECGKAFRNSSG
CCCCCCHHHHCCCCC		56.88-
265PhosphorylationCGKAFRNSSGLRVHK
CHHHHCCCCCCEEEE		22.8724719451
266PhosphorylationGKAFRNSSGLRVHKR
HHHHCCCCCCEEEEE		45.4524719451
276PhosphorylationRVHKRIHTGEKPYEC
EEEEEEECCCCCEEC		44.6720736484
304PhosphorylationRVHKRIHTGEKPYEC
EEECEEECCCCCEEC		44.6725159151
307AcetylationKRIHTGEKPYECDEC
CEEECCCCCEECCCC		55.0019817411
316SumoylationYECDECGKAFITCRT
EECCCCCCEEEHHHH		52.35-
316SumoylationYECDECGKAFITCRT
EECCCCCCEEEHHHH		52.35-
345PhosphorylationKCDECEKSFNYSSLL
CCCCCCCCCCHHHHE		9.0925159151
349PhosphorylationCEKSFNYSSLLIQHK
CCCCCCHHHHEEEEE		18.6628555341
350PhosphorylationEKSFNYSSLLIQHKV
CCCCCHHHHEEEEEE		19.4827251275
360PhosphorylationIQHKVIHTGEKPYEC
EEEEEEECCCCCCCC		35.5921857030
377PhosphorylationCGKAFRNSSGLIVHK
HHHHHCCCCCEEEEE		22.8728555341
388PhosphorylationIVHKRIHTGEKPYKC
EEEEEEECCCCCEEC		44.6729496963
428SumoylationHECKECGKSFSYNSL
HCCCHHCCCCCHHHE		61.05-
428SumoylationHECKECGKSFSYNSL
HCCCHHCCCCCHHHE		61.05-
442UbiquitinationLLLQHRTIHTGERPY
EEEEECEECCCCCCE		2.4921890473
472PhosphorylationKVHRRLHTGEKPYKC
CEEEECCCCCCCCCC		52.1827422710
475UbiquitinationRRLHTGEKPYKCDVC
EECCCCCCCCCCCCC		55.8021890473
475SumoylationRRLHTGEKPYKCDVC
EECCCCCCCCCCCCC		55.80-
475SumoylationRRLHTGEKPYKCDVC
EECCCCCCCCCCCCC		55.80-
492UbiquitinationAYISRSSLKNHKGIH
EEECHHHHCCCCCEE		7.3021890473
506SumoylationHLGEKPYKCSYCEKS
ECCCCCCCCCCCCCC		25.82-
506SumoylationHLGEKPYKCSYCEKS
ECCCCCCCCCCCCCC		25.82-
518PhosphorylationEKSFNYSSALEQHKR
CCCCCCHHHHHHHHC		26.89-
540SumoylationFGCDECGKAFRNNSG
CCCCHHHHHHHCCCC		56.88-
540SumoylationFGCDECGKAFRNNSG
CCCCHHHHHHHCCCC		56.88-
556PhosphorylationKVHKRIHTGERPYKC
EEEEECCCCCCCEEC		38.0624719451
562SumoylationHTGERPYKCEECGKA
CCCCCCEECCCCCCE		37.54-
562SumoylationHTGERPYKCEECGKA
CCCCCCEECCCCCCE		37.54-
562UbiquitinationHTGERPYKCEECGKA
CCCCCCEECCCCCCE		37.54-
587SumoylationKSVHPGEKPFKCDEC
CCCCCCCCCCCCCHH		62.76-
587SumoylationKSVHPGEKPFKCDEC
CCCCCCCCCCCCCHH		62.7628112733
590SumoylationHPGEKPFKCDECEKA
CCCCCCCCCCHHHEE		49.67-
590SumoylationHPGEKPFKCDECEKA
CCCCCCCCCCHHHEE		49.67-
600PhosphorylationECEKAFITYRTLTNH
HHHEEEEEEEECCCC		10.6620860994
601PhosphorylationCEKAFITYRTLTNHK
HHEEEEEEEECCCCC		9.2220860994
603PhosphorylationKAFITYRTLTNHKKV
EEEEEEEECCCCCCE		27.7620860994
618SumoylationHLGEKPYKCDVCEKS
ECCCCCCCCCCCCCC		32.27-
618SumoylationHLGEKPYKCDVCEKS
ECCCCCCCCCCCCCC		32.27-
625PhosphorylationKCDVCEKSFNYTSLL
CCCCCCCCCCHHHHH		9.0928555341
668PhosphorylationKVHKRIHTGERPYEC
EEEEEEECCCCCEEC		38.0625159151
673PhosphorylationIHTGERPYECDVCGK
EECCCCCEECCCCCC		35.10-
718PhosphorylationFSSRTLISHKRVHLG
HCCCEEECCCEEECC		26.5225690035
727SumoylationKRVHLGEKPFKCVEC
CEEECCCCCEEEEEC		54.69-
727SumoylationKRVHLGEKPFKCVEC
CEEECCCCCEEEEEC		54.69-
730SumoylationHLGEKPFKCVECGKS
ECCCCCEEEEECCCC		45.99-
730SumoylationHLGEKPFKCVECGKS
ECCCCCEEEEECCCC		45.99-
739PhosphorylationVECGKSFSYSSLLSQ
EECCCCCCHHHHHHH		31.06-
748SumoylationSSLLSQHKRIHTGEK
HHHHHHCCCCCCCCC		45.4728112733
748SumoylationSSLLSQHKRIHTGEK
HHHHHHCCCCCCCCC		45.47-
752PhosphorylationSQHKRIHTGEKPYVC
HHCCCCCCCCCCEEE		44.6720736484
769PhosphorylationCGKAFRNSSGLTVHK
CCCCHHCCCCCEEEC		22.8720860994
770PhosphorylationGKAFRNSSGLTVHKR
CCCHHCCCCCEEECE		41.1728555341
780PhosphorylationTVHKRIHTGEKPYEC
EEECEEECCCCCCCC		44.6721857030
792SumoylationYECDECGKAYISHSS
CCCCCCCCEEECHHH		50.07-
792SumoylationYECDECGKAYISHSS
CCCCCCCCEEECHHH		50.07-
861PhosphorylationNLTKHKRTHTGEESL
CCCCCCCCCCCCCCE		28.7027461979
863PhosphorylationTKHKRTHTGEESLNV
CCCCCCCCCCCCEEE		45.7527461979
867PhosphorylationRTHTGEESLNVIYVG
CCCCCCCCEEEEEEE		22.4227461979
872PhosphorylationEESLNVIYVGSYSGT
CCCEEEEEEECCCCC		8.4227461979
882SumoylationSYSGTSQKRTYEGGN
CCCCCCCCEEECCCC		46.6128112733
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 ZFP62_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFP62_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 ZFP62_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZFP62_HUMAN !!
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 ZFP62_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-472, AND MASSSPECTROMETRY.

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