ZN358_HUMAN - dbPTM
ZN358_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN358_HUMAN
UniProt AC Q9NW07
Protein Name Zinc finger protein 358
Gene Name ZNF358
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MRRSVLVRNPGHKGLRPVYEELDSDSEDLDPNPEDLDPVSEDPEPDPEDLNTVPEDVDPSYEDLEPVSEDLDPDAEAPGSEPQDPDPMSSSFDLDPDVIGPVPLILDPNSDTLSPGDPKVDPISSGLTATPQVLATSPAVLPAPASPPRPFSCPDCGRAFRRSSGLSQHRRTHSGEKPYRCPDCGKSFSHGATLAQHRGIHTGARPYQCAACGKAFGWRSTLLKHRSSHSGEKPHHCPVCGKAFGHGSLLAQHLRTHGGPRPHKCPVCAKGFGQGSALLKHLRTHTGERPYPCPQCGKAFGQSSALLQHQRTHTAERPYRCPHCGKAFGQSSNLQHHLRIHTGERPYACPHCSKAFGQSSALLQHLHVHSGERPYRCQLCGKAFGQASSLTKHKRVHEGAAAAAAAAAAAAAAAAAGLGLGPGLSPASMMRPGQVSLLGPDAVSVLGSGLGLSPGTSSGRNPDPGSGPGTLPDPSSKPLPGSRSTPSPTPVESSDPKAGHDAGPDLVPSPDLDPVPSPDPDPVPSPDPNPVSCPDPCSPTRGTVSPALPTGESPEWVQEQGALLGPDG
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
4Phosphorylation----MRRSVLVRNPG
----CCCCEEECCCC		14.9419664994
124PhosphorylationDPKVDPISSGLTATP
CCCCCCCCCCCCCCC		24.6025002506
125PhosphorylationPKVDPISSGLTATPQ
CCCCCCCCCCCCCCC		38.2425002506
128PhosphorylationDPISSGLTATPQVLA
CCCCCCCCCCCCCCC		31.8225002506
130PhosphorylationISSGLTATPQVLATS
CCCCCCCCCCCCCCC		14.7125002506
136PhosphorylationATPQVLATSPAVLPA
CCCCCCCCCCCCCCC		30.9625002506
137PhosphorylationTPQVLATSPAVLPAP
CCCCCCCCCCCCCCC		12.7825002506
146PhosphorylationAVLPAPASPPRPFSC
CCCCCCCCCCCCCCC		34.0826657352
152PhosphorylationASPPRPFSCPDCGRA
CCCCCCCCCCCHHHH		27.6722210691
187PhosphorylationRCPDCGKSFSHGATL
ECCCCCCCCCCCCHH		19.7728555341
202PhosphorylationAQHRGIHTGARPYQC
HHHCCCCCCCCCCCC		30.5328555341
280UbiquitinationGQGSALLKHLRTHTG
CCHHHHHHHHHHCCC		41.2522817900
286PhosphorylationLKHLRTHTGERPYPC
HHHHHHCCCCCCCCC		39.8725159151
299UbiquitinationPCPQCGKAFGQSSAL
CCCCHHHHHCCHHHH		10.0921890473
312PhosphorylationALLQHQRTHTAERPY
HHHHHCCCCCCCCCC		19.6024719451
314PhosphorylationLQHQRTHTAERPYRC
HHHCCCCCCCCCCCC		29.6021857030
342PhosphorylationQHHLRIHTGERPYAC
CCEEEECCCCCCCCC		38.0628555341
359PhosphorylationCSKAFGQSSALLQHL
HHHHHCCHHHHHHHH		20.2520068231
360PhosphorylationSKAFGQSSALLQHLH
HHHHCCHHHHHHHHH		18.3020068231
370PhosphorylationLQHLHVHSGERPYRC
HHHHHHCCCCCCEEC		41.0620068231
375PhosphorylationVHSGERPYRCQLCGK
HCCCCCCEECCCCHH		30.1820068231
388PhosphorylationGKAFGQASSLTKHKR
HHHHCCCHHHCCCCH		20.2826270265
389PhosphorylationKAFGQASSLTKHKRV
HHHCCCHHHCCCCHH		42.9725159151
391PhosphorylationFGQASSLTKHKRVHE
HCCCHHHCCCCHHHH		32.8126270265
436PhosphorylationMMRPGQVSLLGPDAV
HCCCCCEEEECCCHH		15.2520068231
444PhosphorylationLLGPDAVSVLGSGLG
EECCCHHHHCCCCCC		17.2220068231
448PhosphorylationDAVSVLGSGLGLSPG
CHHHHCCCCCCCCCC		27.0427732954
453PhosphorylationLGSGLGLSPGTSSGR
CCCCCCCCCCCCCCC		21.3420068231
456PhosphorylationGLGLSPGTSSGRNPD
CCCCCCCCCCCCCCC		24.0927732954
457PhosphorylationLGLSPGTSSGRNPDP
CCCCCCCCCCCCCCC		36.3927732954
458PhosphorylationGLSPGTSSGRNPDPG
CCCCCCCCCCCCCCC		41.4327732954
466PhosphorylationGRNPDPGSGPGTLPD
CCCCCCCCCCCCCCC		47.4025002506
470PhosphorylationDPGSGPGTLPDPSSK
CCCCCCCCCCCCCCC		37.9525002506
475PhosphorylationPGTLPDPSSKPLPGS
CCCCCCCCCCCCCCC		59.3730177828
476PhosphorylationGTLPDPSSKPLPGSR
CCCCCCCCCCCCCCC		43.6224719451
482PhosphorylationSSKPLPGSRSTPSPT
CCCCCCCCCCCCCCC		22.5522199227
484PhosphorylationKPLPGSRSTPSPTPV
CCCCCCCCCCCCCCC		46.5029255136
485PhosphorylationPLPGSRSTPSPTPVE
CCCCCCCCCCCCCCC		27.0329255136
487PhosphorylationPGSRSTPSPTPVESS
CCCCCCCCCCCCCCC		41.3029255136
489PhosphorylationSRSTPSPTPVESSDP
CCCCCCCCCCCCCCC		44.2829255136
493PhosphorylationPSPTPVESSDPKAGH
CCCCCCCCCCCCCCC		40.0323403867
494PhosphorylationSPTPVESSDPKAGHD
CCCCCCCCCCCCCCC		44.4123403867
543PhosphorylationPCSPTRGTVSPALPT
CCCCCCCCCCCCCCC		17.9629449344
545PhosphorylationSPTRGTVSPALPTGE
CCCCCCCCCCCCCCC		12.3225002506
550PhosphorylationTVSPALPTGESPEWV
CCCCCCCCCCCHHHH		55.2025002506
553PhosphorylationPALPTGESPEWVQEQ
CCCCCCCCHHHHHHC		29.4822496350
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 ZN358_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN358_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 ZN358_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN358_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 ZN358_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485 AND SER-487, ANDMASS SPECTROMETRY.

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