ZN507_HUMAN - dbPTM
ZN507_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN507_HUMAN
UniProt AC Q8TCN5
Protein Name Zinc finger protein 507
Gene Name ZNF507
Organism Homo sapiens (Human).
Sequence Length 953
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEESSSVAMLVPDIGEQEAILTAESIISPSLEIDEQRKTKPDPLIHVIQKLSKIVENEKSQKCLLIGKKRPRSSAATHSLETQELCEIPAKVIQSPAADTRRAEMSQTNFTPDTLAQNEGKAMSYQCSLCKFLSSSFSVLKDHIKQHGQQNEVILMCSECHITSRSQEELEAHVVNDHDNDANIHTQSKAQQCVSPSSSLCRKTTERNETIPDIPVSVDNLQTHTVQTASVAEMGRRKWYAYEQYGMYRCLFCSYTCGQQRMLKTHAWKHAGEVDCSYPIFENENEPLGLLDSSAAAAPGGVDAVVIAIGESELSIHNGPSVQVQICSSEQLSSSSPLEQSAERGVHLSQSVTLDPNEEEMLEVISDAEENLIPDSLLTSAQKIISSSPNKKGHVNVIVERLPSAEETLSQKRFLMNTEMEEGKDLSLTEAQIGREGMDDVYRADKCTVDIGGLIIGWSSSEKKDELMNKGLATDENAPPGRRRTNSESLRLHSLAAEALVTMPIRAAELTRANLGHYGDINLLDPDTSQRQVDSTLAAYSKMMSPLKNSSDGLTSLNQSNSTLVALPEGRQELSDGQVKTGISMSLLTVIEKLRERTDQNASDDDILKELQDNAQCQPNSDTSLSGNNVVEYIPNAERPYRCRLCHYTSGNKGYIKQHLRVHRQRQPYQCPICEHIADNSKDLESHMIHHCKTRIYQCKQCEESFHYKSQLRNHEREQHSLPDTLSIATSNEPRISSDTADGKCVQEGNKSSVQKQYRCDVCDYTSTTYVGVRNHRRIHNSDKPYRCSLCGYVCSHPPSLKSHMWKHASDQNYNYEQVNKAINDAISQSGRVLGKSPGKTQLKSSEESADPVTGSSENAVSSSELMSQTPSEVLGTNENEKLSPTSNTSYSLEKISSLAPPSMEYCVLLFCCCICGFESTSKENLLDHMKEHEGEIVNIILNKDHNTALNTN
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
59UbiquitinationSKIVENEKSQKCLLI
HHHHCCCCCCEEEEE		70.53-
73PhosphorylationIGKKRPRSSAATHSL
ECCCCCCCCCCCCCC		27.3225627689
74PhosphorylationGKKRPRSSAATHSLE
CCCCCCCCCCCCCCC		24.1725159151
79PhosphorylationRSSAATHSLETQELC
CCCCCCCCCCHHHHH		24.4421712546
82PhosphorylationAATHSLETQELCEIP
CCCCCCCHHHHHHCC		32.4128985074
91AcetylationELCEIPAKVIQSPAA
HHHHCCHHHHCCCCH		34.2226051181
91PhosphorylationELCEIPAKVIQSPAA
HHHHCCHHHHCCCCH		34.2218220336
95PhosphorylationIPAKVIQSPAADTRR
CCHHHHCCCCHHHCC		12.8429255136
100PhosphorylationIQSPAADTRRAEMSQ
HCCCCHHHCCHHHHH		19.8228985074
106PhosphorylationDTRRAEMSQTNFTPD
HHCCHHHHHCCCCHH		25.92-
111PhosphorylationEMSQTNFTPDTLAQN
HHHHCCCCHHHHHCC		23.4821815630
136PhosphorylationLCKFLSSSFSVLKDH
HHHHHHHHHHHHHHH		20.4028555341
195PhosphorylationSKAQQCVSPSSSLCR
HHHHHCCCCCHHHCC		27.0429255136
197PhosphorylationAQQCVSPSSSLCRKT
HHHCCCCCHHHCCHH		25.6729255136
198PhosphorylationQQCVSPSSSLCRKTT
HHCCCCCHHHCCHHC		30.6229255136
199PhosphorylationQCVSPSSSLCRKTTE
HCCCCCHHHCCHHCC		35.5129255136
238UbiquitinationVAEMGRRKWYAYEQY
HHHHHHCCCCHHHHH		43.10-
240PhosphorylationEMGRRKWYAYEQYGM
HHHHCCCCHHHHHCC		11.4423401153
242PhosphorylationGRRKWYAYEQYGMYR
HHCCCCHHHHHCCCH		6.4623401153
245PhosphorylationKWYAYEQYGMYRCLF
CCCHHHHHCCCHHHH		7.6023401153
248PhosphorylationAYEQYGMYRCLFCSY
HHHHHCCCHHHHHHC		8.2023401153
264UbiquitinationCGQQRMLKTHAWKHA
HCCHHHHHHCHHHHC		28.99-
366PhosphorylationEEMLEVISDAEENLI
HHHHHHHHHHHHHCC		35.6228464451
386PhosphorylationTSAQKIISSSPNKKG
HHHHHHHHCCCCCCC		28.3929396449
387PhosphorylationSAQKIISSSPNKKGH
HHHHHHHCCCCCCCC		39.1329396449
388PhosphorylationAQKIISSSPNKKGHV
HHHHHHCCCCCCCCE		26.2125159151
392UbiquitinationISSSPNKKGHVNVIV
HHCCCCCCCCEEEEE		61.9729967540
404PhosphorylationVIVERLPSAEETLSQ
EEEECCCCHHHHHHH		53.5625159151
408PhosphorylationRLPSAEETLSQKRFL
CCCCHHHHHHHCCHH		24.1826471730
410PhosphorylationPSAEETLSQKRFLMN
CCHHHHHHHCCHHHH		40.8718077418
412UbiquitinationAEETLSQKRFLMNTE
HHHHHHHCCHHHHCC		41.5629967540
424UbiquitinationNTEMEEGKDLSLTEA
HCCCCCCCCCCCCHH		59.79-
427PhosphorylationMEEGKDLSLTEAQIG
CCCCCCCCCCHHHHC		43.3010470851
429PhosphorylationEGKDLSLTEAQIGRE
CCCCCCCCHHHHCCC		26.3729255136
446MethylationDDVYRADKCTVDIGG
CHHHHHCCCEEEECC		30.71-
485PhosphorylationAPPGRRRTNSESLRL
CCCCCCCCCCHHHHH		41.0823312004
487PhosphorylationPGRRRTNSESLRLHS
CCCCCCCCHHHHHHH		28.1330576142
489PhosphorylationRRRTNSESLRLHSLA
CCCCCCHHHHHHHHH		20.7128102081
494PhosphorylationSESLRLHSLAAEALV
CHHHHHHHHHHHHHH		25.0526853621
502PhosphorylationLAAEALVTMPIRAAE
HHHHHHHHCCHHHHH		20.3426853621
518PhosphorylationTRANLGHYGDINLLD
HHHHCCCCCCCCCCC		18.0728796482
540PhosphorylationVDSTLAAYSKMMSPL
HHHHHHHHHHHHCCC		11.8330576142
541PhosphorylationDSTLAAYSKMMSPLK
HHHHHHHHHHHCCCC		14.8930576142
542UbiquitinationSTLAAYSKMMSPLKN
HHHHHHHHHHCCCCC		26.41-
545PhosphorylationAAYSKMMSPLKNSSD
HHHHHHHCCCCCCCC		24.4726074081
548UbiquitinationSKMMSPLKNSSDGLT
HHHHCCCCCCCCCCH		59.1629967540
550PhosphorylationMMSPLKNSSDGLTSL
HHCCCCCCCCCCHHC		28.3726074081
551PhosphorylationMSPLKNSSDGLTSLN
HCCCCCCCCCCHHCC		45.1226074081
562PhosphorylationTSLNQSNSTLVALPE
HHCCCCCCEEEECCC		28.5028555341
589PhosphorylationGISMSLLTVIEKLRE
CCCHHHHHHHHHHHH		25.40-
603PhosphorylationERTDQNASDDDILKE
HHCCCCCCHHHHHHH		49.4721815630
621PhosphorylationNAQCQPNSDTSLSGN
HCCCCCCCCCCCCCC		49.2824043423
623PhosphorylationQCQPNSDTSLSGNNV
CCCCCCCCCCCCCCC		31.2424043423
624PhosphorylationCQPNSDTSLSGNNVV
CCCCCCCCCCCCCCE		26.0624043423
626PhosphorylationPNSDTSLSGNNVVEY
CCCCCCCCCCCCEEE		38.9624043423
633PhosphorylationSGNNVVEYIPNAERP
CCCCCEEECCCCCCC		15.2924043423
641PhosphorylationIPNAERPYRCRLCHY
CCCCCCCEEEEECCC		28.6824043423
653UbiquitinationCHYTSGNKGYIKQHL
CCCCCCCCCCHHHHH		57.5329967540
657UbiquitinationSGNKGYIKQHLRVHR
CCCCCCHHHHHHHHC		24.15-
700UbiquitinationKTRIYQCKQCEESFH
CCEEEECCCCHHHHH		42.32-
721PhosphorylationNHEREQHSLPDTLSI
HHHHHHHCCCCHHHH		41.0928985074
725PhosphorylationEQHSLPDTLSIATSN
HHHCCCCHHHHCCCC		22.0629214152
744UbiquitinationSSDTADGKCVQEGNK
CCCCCCCCEECCCCH		31.60-
769PhosphorylationVCDYTSTTYVGVRNH
CCCCCCCCEEEECCC		18.90-
770PhosphorylationCDYTSTTYVGVRNHR
CCCCCCCEEEECCCC		8.69-
816PhosphorylationASDQNYNYEQVNKAI
CCCCCCCHHHHHHHH		9.44-
836UbiquitinationQSGRVLGKSPGKTQL
HHCCCCCCCCCCCCC		49.6829967540
837PhosphorylationSGRVLGKSPGKTQLK
HCCCCCCCCCCCCCC		36.7726074081
840AcetylationVLGKSPGKTQLKSSE
CCCCCCCCCCCCCCC		36.1625953088
841PhosphorylationLGKSPGKTQLKSSEE
CCCCCCCCCCCCCCC		45.0826074081
845PhosphorylationPGKTQLKSSEESADP
CCCCCCCCCCCCCCC		52.1226074081
846PhosphorylationGKTQLKSSEESADPV
CCCCCCCCCCCCCCC		43.7426074081
849PhosphorylationQLKSSEESADPVTGS
CCCCCCCCCCCCCCC		33.6426074081
884PhosphorylationTNENEKLSPTSNTSY
CCCCCCCCCCCCCCC		36.8828355574
886PhosphorylationENEKLSPTSNTSYSL
CCCCCCCCCCCCCCH		31.0922199227
887PhosphorylationNEKLSPTSNTSYSLE
CCCCCCCCCCCCCHH		41.3026074081
889PhosphorylationKLSPTSNTSYSLEKI
CCCCCCCCCCCHHHH		28.8926074081
890PhosphorylationLSPTSNTSYSLEKIS
CCCCCCCCCCHHHHH		19.5825159151
891PhosphorylationSPTSNTSYSLEKISS
CCCCCCCCCHHHHHH		18.4223312004
944UbiquitinationIVNIILNKDHNTALN
EEEEEEECCCCCCCC		57.8529967540
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 ZN507_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN507_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 ZN507_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN507_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 ZN507_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 SER-195 AND SER-884, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND MASSSPECTROMETRY.

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