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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
211 | Phosphorylation | DKGNCEDYLMISLDD CCCCCCEEEEEEECC | 3.95 | 28102081 | |
215 | Phosphorylation | CEDYLMISLDDAGKI CCEEEEEEECCCCCC | 16.27 | 28102081 | |
252 | Ubiquitination | GTCPEVIKVYIFKAD CCCCCCEEEEEEECC | 33.87 | - | |
257 | Sumoylation | VIKVYIFKADPGEDD CEEEEEEECCCCCCC | 42.18 | - | |
268 | Phosphorylation | GEDDLGGTVDIVESE CCCCCCCEEEEEECC | 17.13 | 30266825 | |
274 | Phosphorylation | GTVDIVESEPENDHG CEEEEEECCCCCCCC | 47.78 | 23401153 | |
289 | Phosphorylation | VELLDQNSSIRVPRE CEEECCCCCCCCCHH | 22.85 | 30576142 | |
290 | Phosphorylation | ELLDQNSSIRVPREK EEECCCCCCCCCHHH | 23.20 | 26126808 | |
425 | Phosphorylation | DGHPLTVYPCMICGK CCCCCEEEEEEECCC | 5.86 | - | |
456 | Phosphorylation | EHLAKKKYRCTDCDY HHHHHCCCCCCCCCC | 21.57 | 29449344 | |
459 | Phosphorylation | AKKKYRCTDCDYTTN HHCCCCCCCCCCCCC | 30.57 | 29449344 | |
463 | Phosphorylation | YRCTDCDYTTNKKIS CCCCCCCCCCCCEEE | 23.07 | 29449344 | |
464 | Phosphorylation | RCTDCDYTTNKKISL CCCCCCCCCCCEEEE | 15.61 | 29449344 | |
465 | Phosphorylation | CTDCDYTTNKKISLH CCCCCCCCCCEEEEH | 38.52 | 29449344 | |
468 | Sumoylation | CDYTTNKKISLHNHL CCCCCCCEEEEHHHH | 39.33 | - | |
468 | Ubiquitination | CDYTTNKKISLHNHL CCCCCCCEEEEHHHH | 39.33 | - | |
468 | Sumoylation | CDYTTNKKISLHNHL CCCCCCCEEEEHHHH | 39.33 | - | |
479 | Ubiquitination | HNHLESHKLTSKAEK HHHHHHCCCCHHHHH | 63.84 | - | |
486 (in isoform 2) | Ubiquitination | - | 60.57 | 21890473 | |
543 | Phosphorylation | RHLLAVHSKNFPHIC HHHHHHHCCCCCCEE | 23.77 | 26055452 | |
571 | Phosphorylation | KKHMRIHTGEKPYQC HHHCEECCCCCCCCC | 44.67 | 29496963 | |
580 | Phosphorylation | EKPYQCQYCEYRSAD CCCCCCCEEECCCCC | 8.55 | - | |
592 | Ubiquitination | SADSSNLKTHVKTKH CCCCCCCCHHEECCC | 40.61 | - | |
593 | O-linked_Glycosylation | ADSSNLKTHVKTKHS CCCCCCCHHEECCCC | 34.76 | 30379171 | |
597 | Phosphorylation | NLKTHVKTKHSKEMP CCCHHEECCCCCCCC | 32.66 | 26270265 | |
600 | Phosphorylation | THVKTKHSKEMPFKC HHEECCCCCCCCCCC | 31.69 | 26270265 | |
649 | Sumoylation | SSNSSDLKRHIISVH CCCCHHHHHHEEEEE | 47.09 | - | |
649 | Sumoylation | SSNSSDLKRHIISVH CCCCHHHHHHEEEEE | 47.09 | - | |
654 | Phosphorylation | DLKRHIISVHTKDYP HHHHHEEEEECCCCC | 13.77 | 20068231 | |
657 | Phosphorylation | RHIISVHTKDYPHKC HHEEEEECCCCCCCC | 24.37 | 20068231 | |
678 | Ubiquitination | FHRPSELKKHVAAHK CCCHHHHHHHHHHHC | 36.46 | - | |
714 | Phosphorylation | RHILSVHTKDLPFRC CCEEEEECCCCCHHC | 24.89 | 18669648 | |
715 | Ubiquitination | HILSVHTKDLPFRCK CEEEEECCCCCHHCH | 42.25 | 21890473 | |
754 | Ubiquitination | YQCEYCEYSTTDASG EEEECEECCCCCCCC | 14.04 | 21890473 | |
754 (in isoform 1) | Ubiquitination | - | 14.04 | 21890473 | |
768 | Phosphorylation | GFKRHVISIHTKDYP CCCEEEEEEECCCCC | 13.76 | 27732954 | |
771 | Phosphorylation | RHVISIHTKDYPHRC EEEEEEECCCCCCCC | 24.76 | 30576142 | |
789 | Phosphorylation | KKGFRRPSEKNQHIM CCCCCCCCHHHHHHH | 60.43 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZFX_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ZFX_HUMAN !! |
Kegg Disease | ||||||
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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. |
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Phosphorylation | |
Reference | PubMed |
"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. |