ZN395_HUMAN - dbPTM
ZN395_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN395_HUMAN
UniProt AC Q9H8N7
Protein Name Zinc finger protein 395
Gene Name ZNF395
Organism Homo sapiens (Human).
Sequence Length 513
Subcellular Localization Cytoplasm. Nucleus. May shuttle between nucleus and cytoplasm.
Protein Description Plays a role in papillomavirus genes transcription..
Protein Sequence MASVLSRRLGKRSLLGARVLGPSASEGPSAAPPSEPLLEGAAPQPFTTSDDTPCQEQPKEVLKAPSTSGLQQVAFQPGQKVYVWYGGQECTGLVEQHSWMEGQVTVWLLEQKLQVCCRVEEVWLAELQGPCPQAPPLEPGAQALAYRPVSRNIDVPKRKSDAVEMDEMMAAMVLTSLSCSPVVQSPPGTEANFSASRAACDPWKESGDISDSGSSTTSGHWSGSSGVSTPSPPHPQASPKYLGDAFGSPQTDHGFETDPDPFLLDEPAPRKRKNSVKVMYKCLWPNCGKVLRSIVGIKRHVKALHLGDTVDSDQFKREEDFYYTEVQLKEESAAAAAAAAAGTPVPGTPTSEPAPTPSMTGLPLSALPPPLHKAQSSGPEHPGPESSLPSGALSKSAPGSFWHIQADHAYQALPSFQIPVSPHIYTSVSWAAAPSAACSLSPVRSRSLSFSEPQQPAPAMKSHLIVTSPPRAQSGARKARGEAKKCRKVYGIEHRDQWCTACRWKKACQRFLD
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
13PhosphorylationSRRLGKRSLLGARVL
HHHHCCHHHCCCEEC
31.2824719451
63UbiquitinationEQPKEVLKAPSTSGL
CCCHHHHCCCCCCCC
64.52-
66PhosphorylationKEVLKAPSTSGLQQV
HHHHCCCCCCCCCEE
39.8128348404
67PhosphorylationEVLKAPSTSGLQQVA
HHHCCCCCCCCCEEE
26.2528348404
68PhosphorylationVLKAPSTSGLQQVAF
HHCCCCCCCCCEEEE
41.6728348404
160PhosphorylationIDVPKRKSDAVEMDE
CCCCCCHHCCCCHHH
34.5323401153
175PhosphorylationMMAAMVLTSLSCSPV
HHHHHHHHHHCCCCC
19.0623401153
178PhosphorylationAMVLTSLSCSPVVQS
HHHHHHHCCCCCCCC
16.5923401153
180PhosphorylationVLTSLSCSPVVQSPP
HHHHHCCCCCCCCCC
19.8423401153
238PhosphorylationSPPHPQASPKYLGDA
CCCCCCCCCCCCHHH
19.3725159151
241PhosphorylationHPQASPKYLGDAFGS
CCCCCCCCCHHHCCC
21.2128464451
248PhosphorylationYLGDAFGSPQTDHGF
CCHHHCCCCCCCCCC
13.8425159151
251PhosphorylationDAFGSPQTDHGFETD
HHCCCCCCCCCCCCC
33.0928450419
257PhosphorylationQTDHGFETDPDPFLL
CCCCCCCCCCCCCCC
51.0428464451
275PhosphorylationAPRKRKNSVKVMYKC
CCCCCCCHHHHHHHH
26.7524719451
289UbiquitinationCLWPNCGKVLRSIVG
HHCCCHHHHHHHHHH
40.05-
309PhosphorylationKALHLGDTVDSDQFK
HHECCCCCCCHHHHH
25.1428122231
322PhosphorylationFKREEDFYYTEVQLK
HHHHHCCEEEEEECC
23.0727642862
323PhosphorylationKREEDFYYTEVQLKE
HHHHCCEEEEEECCH
9.0927642862
324PhosphorylationREEDFYYTEVQLKEE
HHHCCEEEEEECCHH
20.5027642862
332PhosphorylationEVQLKEESAAAAAAA
EEECCHHHHHHHHHH
25.05-
376PhosphorylationPPLHKAQSSGPEHPG
CCCCCCCCCCCCCCC
41.9623401153
377PhosphorylationPLHKAQSSGPEHPGP
CCCCCCCCCCCCCCC
46.4125394399
386PhosphorylationPEHPGPESSLPSGAL
CCCCCCCCCCCCCCC
40.0725627689
387PhosphorylationEHPGPESSLPSGALS
CCCCCCCCCCCCCCC
42.5125627689
445PhosphorylationCSLSPVRSRSLSFSE
CCCCCCCCCCCCCCC
26.8428857561
447PhosphorylationLSPVRSRSLSFSEPQ
CCCCCCCCCCCCCCC
29.6130266825
449PhosphorylationPVRSRSLSFSEPQQP
CCCCCCCCCCCCCCC
28.1523401153
451PhosphorylationRSRSLSFSEPQQPAP
CCCCCCCCCCCCCCC
45.0230266825
462PhosphorylationQPAPAMKSHLIVTSP
CCCCCCCCEEEEECC
15.5028509920
467PhosphorylationMKSHLIVTSPPRAQS
CCCEEEEECCCHHHC
28.6430266825
468PhosphorylationKSHLIVTSPPRAQSG
CCEEEEECCCHHHCC
23.2430266825
474PhosphorylationTSPPRAQSGARKARG
ECCCHHHCCHHHHCC
33.1722617229

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
447SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN395_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 ZN395_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAP30_HUMANSAP30physical
17897615
HDAC1_HUMANHDAC1physical
17897615

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 ZN395_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-248, AND MASSSPECTROMETRY.

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