ZFY_HUMAN - dbPTM
ZFY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFY_HUMAN
UniProt AC P08048
Protein Name Zinc finger Y-chromosomal protein
Gene Name ZFY
Organism Homo sapiens (Human).
Sequence Length 801
Subcellular Localization Nucleus.
Protein Description Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'..
Protein Sequence MDEDEFELQPQEPNSFFDGIGADATHMDGDQIVVEIQEAVFVSNIVDSDITVHNFVPDDPDSVVIQDVVEDVVIEEDVQCSDILEEADVSENVIIPEQVLDSDVTEEVSLPHCTVPDDVLASDITSTSMSMPEHVLTSESMHVCDIGHVEHMVHDSVVEAEIITDPLTSDIVSEEVLVADCAPEAVIDASGISVDQQDNDKASCEDYLMISLDDAGKIEHDGSTGVTIDAESEMDPCKVDSTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQQEDEDLNVAEIADEVYMEVIVGEEDAAVAAAAAAVHEQQIDEDEMKTFVPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKKRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYHCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELRKHMRIHTGEKPYQCQYCEYRSADSSNLKTHIKTKHSKEMPFKCDICLLTFSDTKEVQQHTLVHQESKTHQCLHCDHKSSNSSDLKRHVISVHTKDYPHKCEMCEKGFHRPSELKKHVAVHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQNELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP
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
253SumoylationVIKVYIFKADPGEDD
CEEEEEEECCCCCCC		42.18-
264PhosphorylationGEDDLGGTVDIVESE
CCCCCCCEEEEEECC		17.1330266825
270PhosphorylationGTVDIVESEPENDHG
CEEEEEECCCCCCCC		47.7823401153
284UbiquitinationGVELLDQNSSIRVPR
CCEEECCCCCCCCCH		37.0729967540
285PhosphorylationVELLDQNSSIRVPRE
CEEECCCCCCCCCHH		22.8530576142
286PhosphorylationELLDQNSSIRVPREK
EEECCCCCCCCCHHH		23.2026126808
398UbiquitinationKQKPKKKRRPDSRQY
CCCCCCCCCCCCCCC		65.3329967540
421PhosphorylationDGHPLTVYPCMICGK
CCCCCEEEEEEECCC		5.86-
4492-HydroxyisobutyrylationNHPEHLAKKKYHCTD
HCHHHHHHCCCCCCC		57.04-
452PhosphorylationEHLAKKKYHCTDCDY
HHHHHCCCCCCCCCC		15.82-
455PhosphorylationAKKKYHCTDCDYTTN
HHCCCCCCCCCCCCC		26.75-
459PhosphorylationYHCTDCDYTTNKKIS
CCCCCCCCCCCCEEE		23.07-
460PhosphorylationHCTDCDYTTNKKISL
CCCCCCCCCCCEEEH		15.61-
464SumoylationCDYTTNKKISLHNHL
CCCCCCCEEEHHHHH		39.33-
464UbiquitinationCDYTTNKKISLHNHL
CCCCCCCEEEHHHHH		39.33-
464SumoylationCDYTTNKKISLHNHL
CCCCCCCEEEHHHHH		39.33-
475UbiquitinationHNHLESHKLTSKAEK
HHHHHHCCCCHHHHH		63.8429967540
482AcetylationKLTSKAEKAIECDEC
CCCHHHHHHEECCCC		60.5726051181
520UbiquitinationKMHKCKFCEYETAEQ
CCCCCCCCCCHHHHH		3.1321890473
520UbiquitinationKMHKCKFCEYETAEQ
CCCCCCCCCCHHHHH		3.1321890473
539PhosphorylationRHLLAVHSKNFPHIC
HHHHHHHCCCCCCEE		23.7726055452
557PhosphorylationGKGFRHPSELRKHMR
CCCCCCHHHHHHHCE		43.0420860994
567PhosphorylationRKHMRIHTGEKPYQC
HHHCEECCCCCCCCC		44.6729496963
576PhosphorylationEKPYQCQYCEYRSAD
CCCCCCCEEECCCCC		8.55-
589PhosphorylationADSSNLKTHIKTKHS
CCCCCCCHHEECCCC		31.81-
593PhosphorylationNLKTHIKTKHSKEMP
CCCHHEECCCCCCCC		33.1326270265
593O-linked_GlycosylationNLKTHIKTKHSKEMP
CCCHHEECCCCCCCC		33.1330620550
596PhosphorylationTHIKTKHSKEMPFKC
HHEECCCCCCCCCCC		31.6926270265
596O-linked_GlycosylationTHIKTKHSKEMPFKC
HHEECCCCCCCCCCC		31.6930620550
626PhosphorylationHTLVHQESKTHQCLH
HEEEECCCCCCCCCC		35.9624275569
634UbiquitinationKTHQCLHCDHKSSNS
CCCCCCCCCCCCCCH		3.6521890473
634UbiquitinationKTHQCLHCDHKSSNS
CCCCCCCCCCCCCCH		3.6521890473
645SumoylationSSNSSDLKRHVISVH
CCCHHHHHHHEEEEE		45.51-
645SumoylationSSNSSDLKRHVISVH
CCCHHHHHHHEEEEE		45.51-
660UbiquitinationTKDYPHKCEMCEKGF
CCCCCCCCCCCCCCC		3.5121890473
674UbiquitinationFHRPSELKKHVAVHK
CCCCHHHHHHEEEEC		36.46-
685UbiquitinationAVHKGKKMHQCRHCD
EEECCCCCEECCCCC		2.7721890473
710PhosphorylationRHILSVHTKDLPFRC
CCEEEEECCCCCHHH		24.8918669648
711UbiquitinationHILSVHTKDLPFRCK
CEEEEECCCCCHHHH		42.2521890473
764PhosphorylationGFKRHVISIHTKDYP
CCCEEEEEEECCCCC		13.7627732954
767PhosphorylationRHVISIHTKDYPHRC
EEEEEEECCCCCCCC		24.7630576142
785PhosphorylationKKGFRRPSEKNQHIM
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 ZFY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFY_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 ZFY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBTB9_HUMANZBTB9physical
20211142
ZFX_HUMANZFXphysical
28514442
NSD1_HUMANNSD1physical
28514442
CACB3_HUMANCACNB3physical
28514442
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 ZFY_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory