ZN483_HUMAN - dbPTM
ZN483_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN483_HUMAN
UniProt AC Q8TF39
Protein Name Zinc finger protein 483
Gene Name ZNF483
Organism Homo sapiens (Human).
Sequence Length 744
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MQAVVPLNKMTAISPEPQTLASTEQNEVPRVVTSGEQEAILRGNAADAESFRQRFRWFCYSEVAGPRKALSQLWELCNQWLRPDIHTKEQILELLVFEQFLTILPGEIRIWVKSQHPESSEEVVTLIEDLTQMLEEKDPVSQDSTVSQEENSKEDKMVTVCPNTESCESITLKDVAVNFSRGEWKKLEPFQKELYKEVLLENLRNLEFLDFPVSKLELISQLKWVELPWLLEEVSKSSRLDESALDKIIERCLRDDDHGLMEESQQYCGSSEEDHGNQGNSKGRVAQNKTLGSGSRGKKFDPDKSPFGHNFKETSDLIKHLRVYLRKKSRRYNESKKPFSFHSDLVLNRKEKTAGEKSRKSNDGGKVLSHSSALTEHQKRQKIHLGDRSQKCSKCGIIFIRRSTLSRRKTPMCEKCRKDSCQEAALNKDEGNESGEKTHKCSKCGKAFGYSASLTKHRRIHTGEKPYMCNECGKAFSDSSSLTPHHRTHSGEKPFKCDDCGKGFTLSAHLIKHQRIHTGEKPYKCKDCGRPFSDSSSLIQHQRIHTGEKPYTCSNCGKSFSHSSSLSKHQRIHTGEKPYKCGECGKAFRQNSCLTRHQRIHTGEKPYLCNDCGMTFSHFTSVIYHQRLHSGEKPYKCNQCEKAFPTHSLLSRHQRIHTGVKPYKCKECGKSFSQSSSLNEHHRIHTGEKPYECNYCGATFSRSSILVEHLKIHTGRREYECNECEKTFKSNSGLIRHRGFHSAE
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
11PhosphorylationVVPLNKMTAISPEPQ
EEECCCCEECCCCCC		23.5821406692
14PhosphorylationLNKMTAISPEPQTLA
CCCCEECCCCCCCCC		22.2827050516
19PhosphorylationAISPEPQTLASTEQN
ECCCCCCCCCCCCCC		34.7021406692
22PhosphorylationPEPQTLASTEQNEVP
CCCCCCCCCCCCCCC		35.2721406692
23PhosphorylationEPQTLASTEQNEVPR
CCCCCCCCCCCCCCC		35.6621406692
159PhosphorylationSKEDKMVTVCPNTES
CCCCCEEEECCCCCC		16.94-
164PhosphorylationMVTVCPNTESCESIT
EEEECCCCCCCCEEE		17.89-
166PhosphorylationTVCPNTESCESITLK
EECCCCCCCCEEEHH		22.58-
195PhosphorylationEPFQKELYKEVLLEN
HHHHHHHHHHHHHHH		13.2428387310
215UbiquitinationFLDFPVSKLELISQL
CCCCCHHHHHHHHHC		46.33-
220PhosphorylationVSKLELISQLKWVEL
HHHHHHHHHCCCCCH		41.9324719451
236UbiquitinationWLLEEVSKSSRLDES
HHHHHHHHCCCCCHH		58.59-
247UbiquitinationLDESALDKIIERCLR
CCHHHHHHHHHHHHC		46.57-
264PhosphorylationDHGLMEESQQYCGSS
CCCHHHHHHHHCCCC		14.8521406692
267PhosphorylationLMEESQQYCGSSEED
HHHHHHHHCCCCCCC		7.3721406692
270PhosphorylationESQQYCGSSEEDHGN
HHHHHCCCCCCCCCC		30.8921406692
271PhosphorylationSQQYCGSSEEDHGNQ
HHHHCCCCCCCCCCC		30.2321406692
281PhosphorylationDHGNQGNSKGRVAQN
CCCCCCCCCCCCCCC		43.2221406692
305PhosphorylationKKFDPDKSPFGHNFK
CCCCCCCCCCCCCCH		32.6126074081
336"N6,N6-dimethyllysine"SRRYNESKKPFSFHS
CCCCCCCCCCCCCCH		59.28-
336MethylationSRRYNESKKPFSFHS
CCCCCCCCCCCCCCH		59.2823644510
337MethylationRRYNESKKPFSFHSD
CCCCCCCCCCCCCHH		61.6523644510
350MethylationSDLVLNRKEKTAGEK
HHHHCCCCCCCCCHH		63.5923644510
352UbiquitinationLVLNRKEKTAGEKSR
HHCCCCCCCCCHHHC		46.86-
352MethylationLVLNRKEKTAGEKSR
HHCCCCCCCCCHHHC		46.8623644510
360UbiquitinationTAGEKSRKSNDGGKV
CCCHHHCCCCCCCCE		61.78-
391UbiquitinationHLGDRSQKCSKCGII
CCCCHHHHCCCCEEE		41.54-
434PhosphorylationNKDEGNESGEKTHKC
CCCCCCCCCCCCEEC		57.1428985074
450PhosphorylationKCGKAFGYSASLTKH
CCCCCCCCCCCCCCC		8.4622461510
451PhosphorylationCGKAFGYSASLTKHR
CCCCCCCCCCCCCCC		16.2622461510
462PhosphorylationTKHRRIHTGEKPYMC
CCCCCCCCCCCCEEC		44.6728111955
518PhosphorylationIKHQRIHTGEKPYKC
HCCCCCCCCCCCCCC		44.6729496963
546PhosphorylationIQHQRIHTGEKPYTC
HCCCCCCCCCCCEEC		44.6726055452
574PhosphorylationSKHQRIHTGEKPYKC
CCCCCCCCCCCCCCC		44.6729496963
580SumoylationHTGEKPYKCGECGKA
CCCCCCCCCCCHHHH		44.27-
580SumoylationHTGEKPYKCGECGKA
CCCCCCCCCCCHHHH		44.27-
602PhosphorylationTRHQRIHTGEKPYLC
CCCHHHHCCCCCEEC		44.6728111955
630PhosphorylationIYHQRLHSGEKPYKC
HHHHHCCCCCCCCCC		53.9227794612
648PhosphorylationEKAFPTHSLLSRHQR
HHHCCCHHHHHHHHH		33.2224719451
651PhosphorylationFPTHSLLSRHQRIHT
CCCHHHHHHHHHHHC		32.7724719451
671PhosphorylationKCKECGKSFSQSSSL
ECCCCCCCCCCCCCC		18.5328555341
686PhosphorylationNEHHRIHTGEKPYEC
CCCCCCCCCCCCEEC		44.6728111955
695PhosphorylationEKPYECNYCGATFSR
CCCEECCCCCCEECC		12.15-
699PhosphorylationECNYCGATFSRSSIL
ECCCCCCEECCHHHH		13.87-
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 ZN483_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN483_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 ZN483_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECM29_HUMANKIAA0368physical
20682791
A4_HUMANAPPphysical
21832049
ZSC22_HUMANZSCAN22physical
25416956
ZY11A_HUMANZYG11Aphysical
28514442
TIF1A_HUMANTRIM24physical
28514442
ZKSC3_HUMANZKSCAN3physical
28514442
ZKSC4_HUMANZKSCAN4physical
28514442
ZN174_HUMANZNF174physical
28514442
ZN197_HUMANZNF197physical
28514442
SCND1_HUMANSCAND1physical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
ZN446_HUMANZNF446physical
28514442
ZN445_HUMANZNF445physical
28514442
ZN397_HUMANZNF397physical
28514442
ZNF24_HUMANZNF24physical
28514442
ZKSC8_HUMANZKSCAN8physical
28514442
ZSC25_HUMANZSCAN25physical
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 ZN483_HUMAN

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Related Literatures of Post-Translational Modification

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