ZFX_HUMAN - dbPTM
ZFX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFX_HUMAN
UniProt AC P17010
Protein Name Zinc finger X-chromosomal protein
Gene Name ZFX
Organism Homo sapiens (Human).
Sequence Length 805
Subcellular Localization Nucleus.
Protein Description Probable transcriptional activator..
Protein Sequence MDEDGLELQQEPNSFFDATGADGTHMDGDQIVVEVQETVFVSDVVDSDITVHNFVPDDPDSVVIQDVIEDVVIEDVQCPDIMEEADVSETVIIPEQVLDSDVTEEVSLAHCTVPDDVLASDITSASMSMPEHVLTGDSIHVSDVGHVGHVGHVEHVVHDSVVEAEIVTDPLTTDVVSEEVLVADCASEAVIDANGIPVDQQDDDKGNCEDYLMISLDDAGKIEHDGSSGMTMDTESEIDPCKVDGTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQPEDEDLNVAEIADEVYMEVIVGEEDAAAAAAAAAVHEQQMDDNEIKTFMPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKRRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYRCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHVKTKHSKEMPFKCDICLLTFSDTKEVQQHALIHQESKTHQCLHCDHKSSNSSDLKRHIISVHTKDYPHKCDMCDKGFHRPSELKKHVAAHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQSELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP
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
211PhosphorylationDKGNCEDYLMISLDD
CCCCCCEEEEEEECC
3.9528102081
215PhosphorylationCEDYLMISLDDAGKI
CCEEEEEEECCCCCC
16.2728102081
252UbiquitinationGTCPEVIKVYIFKAD
CCCCCCEEEEEEECC
33.87-
257SumoylationVIKVYIFKADPGEDD
CEEEEEEECCCCCCC
42.18-
268PhosphorylationGEDDLGGTVDIVESE
CCCCCCCEEEEEECC
17.1330266825
274PhosphorylationGTVDIVESEPENDHG
CEEEEEECCCCCCCC
47.7823401153
289PhosphorylationVELLDQNSSIRVPRE
CEEECCCCCCCCCHH
22.8530576142
290PhosphorylationELLDQNSSIRVPREK
EEECCCCCCCCCHHH
23.2026126808
425PhosphorylationDGHPLTVYPCMICGK
CCCCCEEEEEEECCC
5.86-
456PhosphorylationEHLAKKKYRCTDCDY
HHHHHCCCCCCCCCC
21.5729449344
459PhosphorylationAKKKYRCTDCDYTTN
HHCCCCCCCCCCCCC
30.5729449344
463PhosphorylationYRCTDCDYTTNKKIS
CCCCCCCCCCCCEEE
23.0729449344
464PhosphorylationRCTDCDYTTNKKISL
CCCCCCCCCCCEEEE
15.6129449344
465PhosphorylationCTDCDYTTNKKISLH
CCCCCCCCCCEEEEH
38.5229449344
468SumoylationCDYTTNKKISLHNHL
CCCCCCCEEEEHHHH
39.33-
468UbiquitinationCDYTTNKKISLHNHL
CCCCCCCEEEEHHHH
39.33-
468SumoylationCDYTTNKKISLHNHL
CCCCCCCEEEEHHHH
39.33-
479UbiquitinationHNHLESHKLTSKAEK
HHHHHHCCCCHHHHH
63.84-
486 (in isoform 2)Ubiquitination-60.5721890473
543PhosphorylationRHLLAVHSKNFPHIC
HHHHHHHCCCCCCEE
23.7726055452
571PhosphorylationKKHMRIHTGEKPYQC
HHHCEECCCCCCCCC
44.6729496963
580PhosphorylationEKPYQCQYCEYRSAD
CCCCCCCEEECCCCC
8.55-
592UbiquitinationSADSSNLKTHVKTKH
CCCCCCCCHHEECCC
40.61-
593O-linked_GlycosylationADSSNLKTHVKTKHS
CCCCCCCHHEECCCC
34.7630379171
597PhosphorylationNLKTHVKTKHSKEMP
CCCHHEECCCCCCCC
32.6626270265
600PhosphorylationTHVKTKHSKEMPFKC
HHEECCCCCCCCCCC
31.6926270265
649SumoylationSSNSSDLKRHIISVH
CCCCHHHHHHEEEEE
47.09-
649SumoylationSSNSSDLKRHIISVH
CCCCHHHHHHEEEEE
47.09-
654PhosphorylationDLKRHIISVHTKDYP
HHHHHEEEEECCCCC
13.7720068231
657PhosphorylationRHIISVHTKDYPHKC
HHEEEEECCCCCCCC
24.3720068231
678UbiquitinationFHRPSELKKHVAAHK
CCCHHHHHHHHHHHC
36.46-
714PhosphorylationRHILSVHTKDLPFRC
CCEEEEECCCCCHHC
24.8918669648
715UbiquitinationHILSVHTKDLPFRCK
CEEEEECCCCCHHCH
42.2521890473
754UbiquitinationYQCEYCEYSTTDASG
EEEECEECCCCCCCC
14.0421890473
754 (in isoform 1)Ubiquitination-14.0421890473
768PhosphorylationGFKRHVISIHTKDYP
CCCEEEEEEECCCCC
13.7627732954
771PhosphorylationRHVISIHTKDYPHRC
EEEEEEECCCCCCCC
24.7630576142
789PhosphorylationKKGFRRPSEKNQHIM
CCCCCCCCHHHHHHH
60.43-

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 ZFX_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFX_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 ZFX_HUMAN !!

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

Oops, there are no PPI records of ZFX_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 ZFX_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASSSPECTROMETRY.
"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-274, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASSSPECTROMETRY.

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