ZKSC2_HUMAN - dbPTM
ZKSC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZKSC2_HUMAN
UniProt AC Q63HK3
Protein Name Zinc finger protein with KRAB and SCAN domains 2
Gene Name ZKSCAN2
Organism Homo sapiens (Human).
Sequence Length 967
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAVALDSQIDAPLEVEGCLIMKVEKDPEWASEPILEGSDSSETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALVVHLEKETGRLRQQVSSPVHREKHSPLGAAWEVADFQPEQVETQPRAVSREEPGSLHSGHQEQLNRKRERRPLPKNARPSPWVPALADEWNTLDQEVTTTRLPAGSQEPVKDVHVARGFSYRKSVHQIPAQRDLYRDFRKENVGNVVSLGSAVSTSNKITRLEQRKEPWTLGLHSSNKRSILRSNYVKEKSVHAIQVPARSAGKTWREQQQWGLEDEKIAGVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGHMLEPCAFFEDMDALLNPAARAPSTDKPKEMIPVPRLKRIAISAKEHISLVEEEEAAEDSDDDEIGIEFIRKSEIHGAPVLFQNLSGVHWGYEETKTFLDILRETRFYEALQACHRKSKLYGAVAEQLRECGFLRTPEQCRTKFKSLQKSYRKVKNGHVLESCAFYKEMDALINSRASAPSPSTPEEVPSPSRQERGGIEVEPQEPTGWEPEETSQEAVIEDSCSERMSEEEIVQEPEFQGPPGLLQSPNDFEIGSSIKEDPTQIVYKDMEQHRALIEKSKRVVSQSTDPSKYRKRECISGRQWENLQGIRQGKPMSQPRDLGKAVVHQRPFVGKRPYRLLKYGESFGRSTRLMCRMTHHKENPYKCGVCGKCFGRSRSLIRHQRIHTGEKPFKCLDCGKSFNDSSNFGAHQRIHTGEKPYRCGECGKCFSQSSSLIIHQRTHTGEKPYQCGECGKSFTNSSHFSAHRRVHTGENPYKCVDCEKSFNNCTRFREHRRIHTGEKPYGCAQCGKRFSKSSVLTKHREVHVREKPLPHPPSLYCPENPHKGKTDEFRKTF
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
22SumoylationVEGCLIMKVEKDPEW
EECEEEEEEECCCHH
40.0028112733
31PhosphorylationEKDPEWASEPILEGS
ECCCHHHCCCCCCCC
45.00-
38PhosphorylationSEPILEGSDSSETFR
CCCCCCCCCCHHHHH
25.58-
40PhosphorylationPILEGSDSSETFRKC
CCCCCCCCHHHHHHH
31.60-
43PhosphorylationEGSDSSETFRKCFRQ
CCCCCHHHHHHHHHH
30.59-
135PhosphorylationGRLRQQVSSPVHREK
CCHHHHCCCCCHHCC
25.2922210691
136PhosphorylationRLRQQVSSPVHREKH
CHHHHCCCCCHHCCC
31.8928985074
144PhosphorylationPVHREKHSPLGAAWE
CCHHCCCCCCCHHHH
32.6525159151
242SumoylationARGFSYRKSVHQIPA
ECCCCCCCCHHHCCC
48.9028112733
242SumoylationARGFSYRKSVHQIPA
ECCCCCCCCHHHCCC
48.90-
259SumoylationDLYRDFRKENVGNVV
HHHHHHHHHCCCCEE
54.3428112733
277SumoylationSAVSTSNKITRLEQR
HHHCCCCCCCHHHHC
45.2628112733
289PhosphorylationEQRKEPWTLGLHSSN
HHCCCCCCCCCCCCC
22.97-
297UbiquitinationLGLHSSNKRSILRSN
CCCCCCCCHHHHHHC
49.85-
337SumoylationQWGLEDEKIAGVHWS
HHCCCCCCCCCCCCC
50.6128112733
371O-linked_GlycosylationLQACPRNSQVYGAVA
HHHCCCCCHHHHHHH
23.4630379171
434PhosphorylationNPAARAPSTDKPKEM
CHHHCCCCCCCCHHH
48.53-
435PhosphorylationPAARAPSTDKPKEMI
HHHCCCCCCCCHHHC
47.16-
482SumoylationIGIEFIRKSEIHGAP
CHHHHHHHHHCCCCC
47.8528112733
529SumoylationQACHRKSKLYGAVAE
HHHHHHCHHHHHHHH
49.0828112733
529SumoylationQACHRKSKLYGAVAE
HHHHHHCHHHHHHHH
49.08-
531PhosphorylationCHRKSKLYGAVAEQL
HHHHCHHHHHHHHHH
13.53-
585PhosphorylationEMDALINSRASAPSP
HHHHHHHCCCCCCCC
23.41-
588PhosphorylationALINSRASAPSPSTP
HHHHCCCCCCCCCCC
39.3325850435
591PhosphorylationNSRASAPSPSTPEEV
HCCCCCCCCCCCCCC
31.0621712546
593PhosphorylationRASAPSPSTPEEVPS
CCCCCCCCCCCCCCC
62.0129255136
594PhosphorylationASAPSPSTPEEVPSP
CCCCCCCCCCCCCCC
37.8029255136
600PhosphorylationSTPEEVPSPSRQERG
CCCCCCCCCCCCCCC
40.4630266825
602PhosphorylationPEEVPSPSRQERGGI
CCCCCCCCCCCCCCE
51.4330266825
658PhosphorylationGPPGLLQSPNDFEIG
CCCCCCCCCCCCCCC
26.16-
724SumoylationLQGIRQGKPMSQPRD
HCCHHCCCCCCCCCC
29.25-
724SumoylationLQGIRQGKPMSQPRD
HCCHHCCCCCCCCCC
29.25-
727PhosphorylationIRQGKPMSQPRDLGK
HHCCCCCCCCCCCCC
45.63-
734SumoylationSQPRDLGKAVVHQRP
CCCCCCCCCCHHCCC
45.3528112733
745SumoylationHQRPFVGKRPYRLLK
HCCCCCCCCCEEEHH
44.9228112733
752SumoylationKRPYRLLKYGESFGR
CCCEEEHHCHHHCCH
56.6628112733
753PhosphorylationRPYRLLKYGESFGRS
CCEEEHHCHHHCCHH
26.54-
761PhosphorylationGESFGRSTRLMCRMT
HHHCCHHHHHHHHHH
26.85-
787PhosphorylationCGKCFGRSRSLIRHQ
CHHHHCCCHHHHHCC
26.9723532336
789PhosphorylationKCFGRSRSLIRHQRI
HHHCCCHHHHHCCCC
29.4223532336
798PhosphorylationIRHQRIHTGEKPFKC
HHCCCCCCCCCCEEE
44.6718669648
815PhosphorylationCGKSFNDSSNFGAHQ
CCCCCCCCCCCCCCC
28.4328555341
816PhosphorylationGKSFNDSSNFGAHQR
CCCCCCCCCCCCCCC
38.7628985074
826PhosphorylationGAHQRIHTGEKPYRC
CCCCCCCCCCCCEEC
44.6729496963
829SumoylationQRIHTGEKPYRCGEC
CCCCCCCCCEECCCC
49.01-
829SumoylationQRIHTGEKPYRCGEC
CCCCCCCCCEECCCC
49.01-
829UbiquitinationQRIHTGEKPYRCGEC
CCCCCCCCCEECCCC
49.01-
843PhosphorylationCGKCFSQSSSLIIHQ
CHHHCCCCCCEEEEE
22.2423186163
844PhosphorylationGKCFSQSSSLIIHQR
HHHCCCCCCEEEEEC
22.8723186163
845PhosphorylationKCFSQSSSLIIHQRT
HHCCCCCCEEEEECC
28.9125106551
852PhosphorylationSLIIHQRTHTGEKPY
CEEEEECCCCCCCCE
19.74-
854PhosphorylationIIHQRTHTGEKPYQC
EEEECCCCCCCCEEC
46.56-
857AcetylationQRTHTGEKPYQCGEC
ECCCCCCCCEECCCC
50.827428793
894UbiquitinationYKCVDCEKSFNNCTR
CCEECCHHHCCCCCH
67.68-
910PhosphorylationREHRRIHTGEKPYGC
HHHCCCCCCCCCCCC
44.6728111955
925PhosphorylationAQCGKRFSKSSVLTK
CCCCCCCCCHHHHHC
35.3429396449
927PhosphorylationCGKRFSKSSVLTKHR
CCCCCCCHHHHHCCC
25.2029396449
928PhosphorylationGKRFSKSSVLTKHRE
CCCCCCHHHHHCCCE
25.5329396449
931PhosphorylationFSKSSVLTKHREVHV
CCCHHHHHCCCEEEC
23.7329396449
966PhosphorylationKTDEFRKTF------
CCHHHHHCC------
30.2627134283

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 ZKSC2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZKSC2_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 ZKSC2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZKSC2_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 ZKSC2_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-591; THR-594 ANDSER-600, AND MASS SPECTROMETRY.

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