ZN629_HUMAN - dbPTM
ZN629_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN629_HUMAN
UniProt AC Q9UEG4
Protein Name Zinc finger protein 629
Gene Name ZNF629
Organism Homo sapiens (Human).
Sequence Length 869
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEPETALWGPDLQGPEQSPNDAHRGAESENEEESPRQESSGEEIIMGDPAQSPESKDSTEMSLERSSQDPSVPQNPPTPLGHSNPLDHQIPLDPPAPEVVPTPSDWTKACEASWQWGALTTWNSPPVVPANEPSLRELVQGRPAGAEKPYICNECGKSFSQWSKLLRHQRIHTGERPNTCSECGKSFTQSSHLVQHQRTHTGEKPYKCPDCGKCFSWSSNLVQHQRTHTGEKPYKCTECEKAFTQSTNLIKHQRSHTGEKPYKCGECRRAFYRSSDLIQHQATHTGEKPYKCPECGKRFGQNHNLLKHQKIHAGEKPYRCTECGKSFIQSSELTQHQRTHTGEKPYECLECGKSFGHSSTLIKHQRTHLREDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNLINHQRIHRGERPYICADCGKSFIMSSTLIRHQRIHTGEKPYKCSDCGKSFIRSSHLIQHRRTHTGEKPYKCPECGKSFSQSSNLITHVRTHMDENLFVCSDCGKAFLEAHELEQHRVIHERGKTPARRAQGDSLLGLGDPSLLTPPPGAKPHKCLVCGKGFNDEGIFMQHQRIHIGENPYKNADGLIAHAAPKPPQLRSPRLPFRGNSYPGAAEGRAEAPGQPLKPPEGQEGFSQRRGLLSSKTYICSHCGESFLDRSVLLQHQLTHGNEKPFLFPDYRIGLGEGAGPSPFLSGKPFKCPECKQSFGLSSELLLHQKVHAGGKSSQKSPELGKSSSVLLEHLRSPLGARPYRCSDCRASFLDRVALTRHQETHTQEKPPNPEDPPPEAVTLSTDQEGEGETPTPTESSSHGEGQNPKTLVEEKPYLCPECGAGFTEVAALLLHRSCHPGVSL
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
5Phosphorylation---MEPETALWGPDL
---CCCCCCCCCCCC
37.4523186163
18PhosphorylationDLQGPEQSPNDAHRG
CCCCCCCCCCCCCCC
24.8225159151
28PhosphorylationDAHRGAESENEEESP
CCCCCCCCCCCCCCC
45.2323401153
34PhosphorylationESENEEESPRQESSG
CCCCCCCCCCCCCCC
28.7623927012
39PhosphorylationEESPRQESSGEEIIM
CCCCCCCCCCCCCCC
34.9928348404
40PhosphorylationESPRQESSGEEIIMG
CCCCCCCCCCCCCCC
49.8528348404
52PhosphorylationIMGDPAQSPESKDST
CCCCCCCCCCCCCCC
32.5128348404
55PhosphorylationDPAQSPESKDSTEMS
CCCCCCCCCCCCCCC
45.1829978859
58PhosphorylationQSPESKDSTEMSLER
CCCCCCCCCCCCHHH
29.9721815630
62PhosphorylationSKDSTEMSLERSSQD
CCCCCCCCHHHHCCC
22.3528674419
66PhosphorylationTEMSLERSSQDPSVP
CCCCHHHHCCCCCCC
23.9925002506
67PhosphorylationEMSLERSSQDPSVPQ
CCCHHHHCCCCCCCC
44.8425002506
71PhosphorylationERSSQDPSVPQNPPT
HHHCCCCCCCCCCCC
55.5125002506
78PhosphorylationSVPQNPPTPLGHSNP
CCCCCCCCCCCCCCC
32.1925002506
83PhosphorylationPPTPLGHSNPLDHQI
CCCCCCCCCCCCCCC
38.0425002506
120PhosphorylationSWQWGALTTWNSPPV
HEECCCCCCCCCCCC
29.2728348404
121PhosphorylationWQWGALTTWNSPPVV
EECCCCCCCCCCCCC
24.4128348404
124PhosphorylationGALTTWNSPPVVPAN
CCCCCCCCCCCCCCC
23.3428348404
148AcetylationGRPAGAEKPYICNEC
CCCCCCCCCEECCCC
42.4626051181
173PhosphorylationLRHQRIHTGERPNTC
HHHCCCCCCCCCCCH
38.0628655764
186PhosphorylationTCSECGKSFTQSSHL
CHHHCCCCHHHHHHH
20.8628555341
188PhosphorylationSECGKSFTQSSHLVQ
HHCCCCHHHHHHHHH
34.3328555341
190PhosphorylationCGKSFTQSSHLVQHQ
CCCCHHHHHHHHHCC
19.3728555341
191PhosphorylationGKSFTQSSHLVQHQR
CCCHHHHHHHHHCCC
15.8328555341
199PhosphorylationHLVQHQRTHTGEKPY
HHHHCCCCCCCCCCC
19.7428348404
201PhosphorylationVQHQRTHTGEKPYKC
HHCCCCCCCCCCCCC
46.5626270265
204UbiquitinationQRTHTGEKPYKCPDC
CCCCCCCCCCCCCCC
55.80-
227PhosphorylationNLVQHQRTHTGEKPY
CHHCCCCCCCCCCCC
19.7428348404
229PhosphorylationVQHQRTHTGEKPYKC
HCCCCCCCCCCCCCC
46.5626270265
232UbiquitinationQRTHTGEKPYKCTEC
CCCCCCCCCCCCCHH
55.80-
237UbiquitinationGEKPYKCTECEKAFT
CCCCCCCCHHHHHHH
39.2532142685
246PhosphorylationCEKAFTQSTNLIKHQ
HHHHHHHCCCHHHHC
19.0628555341
251SumoylationTQSTNLIKHQRSHTG
HHCCCHHHHCCCCCC
36.5328112733
251UbiquitinationTQSTNLIKHQRSHTG
HHCCCHHHHCCCCCC
36.5332142685
257PhosphorylationIKHQRSHTGEKPYKC
HHHCCCCCCCCCCCC
48.5624719451
274UbiquitinationCRRAFYRSSDLIQHQ
HHHHHHHCHHHHHHC
19.4733845483
283PhosphorylationDLIQHQATHTGEKPY
HHHHHCCCCCCCCCC
17.2529214152
285PhosphorylationIQHQATHTGEKPYKC
HHHCCCCCCCCCCCC
42.5625159151
288UbiquitinationQATHTGEKPYKCPEC
CCCCCCCCCCCCCCH
55.8033845483
326PhosphorylationRCTECGKSFIQSSEL
ECCCCCCHHHHHHHC
16.9328555341
339PhosphorylationELTQHQRTHTGEKPY
HCCCCCCCCCCCCCE
19.7428152594
341PhosphorylationTQHQRTHTGEKPYEC
CCCCCCCCCCCCEEH
46.5628152594
346PhosphorylationTHTGEKPYECLECGK
CCCCCCCEEHHHCCC
30.2728152594
349UbiquitinationGEKPYECLECGKSFG
CCCCEEHHHCCCCCC
4.0023000965
359PhosphorylationGKSFGHSSTLIKHQR
CCCCCCHHHHHHHHH
22.8928555341
363UbiquitinationGHSSTLIKHQRTHLR
CCHHHHHHHHHHHCC
36.4823000965
382PhosphorylationKCPVCGKTFTLSATL
CCCCCCCEEEEEHHH
13.7220068231
384PhosphorylationPVCGKTFTLSATLLR
CCCCCEEEEEHHHHH
25.6520068231
386PhosphorylationCGKTFTLSATLLRHQ
CCCEEEEEHHHHHCC
19.02-
410PhosphorylationKCPECGKSFSVSSNL
CCCCCCCEEEECCHH
14.1928555341
438PhosphorylationICADCGKSFIMSSTL
EECCCCCCHHHCHHH
12.8028555341
442PhosphorylationCGKSFIMSSTLIRHQ
CCCCHHHCHHHHHCC
18.5028555341
443PhosphorylationGKSFIMSSTLIRHQR
CCCHHHCHHHHHCCC
15.1728555341
453PhosphorylationIRHQRIHTGEKPYKC
HHCCCCCCCCCCEEC
44.6729496963
471PhosphorylationGKSFIRSSHLIQHRR
CHHHHHHHHHHHCCC
16.6828555341
479PhosphorylationHLIQHRRTHTGEKPY
HHHHCCCCCCCCCCC
24.6028348404
481PhosphorylationIQHRRTHTGEKPYKC
HHCCCCCCCCCCCCC
46.5626270265
484UbiquitinationRRTHTGEKPYKCPEC
CCCCCCCCCCCCCCC
55.80-
494PhosphorylationKCPECGKSFSQSSNL
CCCCCCCCCCCCCCH
18.5328555341
550PhosphorylationARRAQGDSLLGLGDP
HHHCCCCCCCCCCCH
32.1121712546
558PhosphorylationLLGLGDPSLLTPPPG
CCCCCCHHHCCCCCC
40.5322199227
561PhosphorylationLGDPSLLTPPPGAKP
CCCHHHCCCCCCCCC
38.7622199227
570UbiquitinationPPGAKPHKCLVCGKG
CCCCCCCEEEEECCC
37.48-
597PhosphorylationIHIGENPYKNADGLI
EECCCCCCCCCCCCC
28.58-
616PhosphorylationPKPPQLRSPRLPFRG
CCCCCCCCCCCCCCC
23.9826055452
618MethylationPPQLRSPRLPFRGNS
CCCCCCCCCCCCCCC
57.13115920545
622MethylationRSPRLPFRGNSYPGA
CCCCCCCCCCCCCCC
41.25115920549
625PhosphorylationRLPFRGNSYPGAAEG
CCCCCCCCCCCCCCC
35.2128102081
626PhosphorylationLPFRGNSYPGAAEGR
CCCCCCCCCCCCCCC
15.0829214152
628UbiquitinationFRGNSYPGAAEGRAE
CCCCCCCCCCCCCCC
29.2333845483
642UbiquitinationEAPGQPLKPPEGQEG
CCCCCCCCCCCCCCC
66.2733845483
651PhosphorylationPEGQEGFSQRRGLLS
CCCCCCCCHHHCCCC
33.3728555341
688SumoylationQLTHGNEKPFLFPDY
HCCCCCCCCCCCCCC
45.1028112733
706PhosphorylationLGEGAGPSPFLSGKP
CCCCCCCCCCCCCCC
27.6327050516
712AcetylationPSPFLSGKPFKCPEC
CCCCCCCCCCCCCHH
43.8626051181
731PhosphorylationGLSSELLLHQKVHAG
CCCHHHHHHCHHHCC
6.6833259812
741PhosphorylationKVHAGGKSSQKSPEL
HHHCCCCCCCCCCCC
41.0829396449
742PhosphorylationVHAGGKSSQKSPELG
HHCCCCCCCCCCCCC
45.1529396449
745PhosphorylationGGKSSQKSPELGKSS
CCCCCCCCCCCCCCH
18.9021955146
750SumoylationQKSPELGKSSSVLLE
CCCCCCCCCHHHHHH
60.8428112733
751PhosphorylationKSPELGKSSSVLLEH
CCCCCCCCHHHHHHH
26.5023312004
752PhosphorylationSPELGKSSSVLLEHL
CCCCCCCHHHHHHHH
28.1423312004
753PhosphorylationPELGKSSSVLLEHLR
CCCCCCHHHHHHHHC
24.7123312004
761PhosphorylationVLLEHLRSPLGARPY
HHHHHHCCCCCCCCC
30.7329978859
780MethylationCRASFLDRVALTRHQ
HHHHHHHHHHHHHCC
20.11115920553
840SumoylationPKTLVEEKPYLCPEC
CCCCCCCCCCCCCCC
26.0028112733
868PhosphorylationRSCHPGVSL------
HHCCCCCCC------
33.9925159151

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 ZN629_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN629_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 ZN629_HUMAN !!

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

Oops, there are no PPI records of ZN629_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 ZN629_HUMAN

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Related Literatures of Post-Translational Modification

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