ZN787_HUMAN - dbPTM
ZN787_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN787_HUMAN
UniProt AC Q6DD87
Protein Name Zinc finger protein 787
Gene Name ZNF787
Organism Homo sapiens (Human).
Sequence Length 382
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MELREEAWSPGPLDSEDQQMASHENPVDILIMDDDDVPSWPPTKLSPPQSAPPAGPPPRPRPPAPYICNECGKSFSHWSKLTRHQRTHTGERPNACADCGKTFSQSSHLVQHRRIHTGEKPYACLECGKRFSWSSNLMQHQRIHTGEKPYTCPDCGRSFTQSKSLAKHRRSHSGLKPFVCPRCGRGFSQPKSLARHLRLHPELSGPGVAAKVLAASVRRAKGPEEAVAADGEIAIPVGDGEGIIVVGAPGEGAAAAAAMAGAGAKAAGPRSRRAPAPKPYVCLECGKGFGHGAGLLAHQRAQHGDGLGAAGGEEPAHICVECGEGFVQGAALRRHKKIHAVGAPSVCSSCGQSYYRAGGEEEDDDDEAAGGRCPECRGGEGR
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
9PhosphorylationELREEAWSPGPLDSE
CHHHHHCCCCCCCHH		27.3325159151
15PhosphorylationWSPGPLDSEDQQMAS
CCCCCCCHHHHHHHH		51.2428348404
22PhosphorylationSEDQQMASHENPVDI
HHHHHHHHCCCCCEE		26.4528348404
46PhosphorylationSWPPTKLSPPQSAPP
CCCCCCCCCCCCCCC		35.7725849741
50PhosphorylationTKLSPPQSAPPAGPP
CCCCCCCCCCCCCCC		48.8227732954
80AcetylationKSFSHWSKLTRHQRT
CCHHHHHHHHHHHCC		49.0023236377
87PhosphorylationKLTRHQRTHTGERPN
HHHHHHCCCCCCCCC		19.7429396449
89PhosphorylationTRHQRTHTGERPNAC
HHHHCCCCCCCCCCC		39.8723401153
102PhosphorylationACADCGKTFSQSSHL
CCCCCCCCCCCCHHH		17.5023312004
104PhosphorylationADCGKTFSQSSHLVQ
CCCCCCCCCCHHHHH		34.0917525332
106PhosphorylationCGKTFSQSSHLVQHR
CCCCCCCCHHHHHCC		20.6623312004
107PhosphorylationGKTFSQSSHLVQHRR
CCCCCCCHHHHHCCC		17.1323312004
117PhosphorylationVQHRRIHTGEKPYAC
HHCCCCCCCCCCEEE		44.6726055452
120AcetylationRRIHTGEKPYACLEC
CCCCCCCCCEEEEEC		44.6826051181
122PhosphorylationIHTGEKPYACLECGK
CCCCCCCEEEEECCC		22.4828152594
132PhosphorylationLECGKRFSWSSNLMQ
EECCCCEECCCCHHH		30.0425159151
134PhosphorylationCGKRFSWSSNLMQHQ
CCCCEECCCCHHHCC		14.2428450419
135PhosphorylationGKRFSWSSNLMQHQR
CCCEECCCCHHHCCC		27.9422199227
145PhosphorylationMQHQRIHTGEKPYTC
HHCCCCCCCCCCCCC		44.6726055452
148AcetylationQRIHTGEKPYTCPDC
CCCCCCCCCCCCCCC		44.6726051181
148UbiquitinationQRIHTGEKPYTCPDC
CCCCCCCCCCCCCCC		44.6733845483
150PhosphorylationIHTGEKPYTCPDCGR
CCCCCCCCCCCCCCC		31.8522817900
151PhosphorylationHTGEKPYTCPDCGRS
CCCCCCCCCCCCCCC		26.5328387310
162PhosphorylationCGRSFTQSKSLAKHR
CCCCCCCCHHHHHHH		22.5826699800
171PhosphorylationSLAKHRRSHSGLKPF
HHHHHHHHCCCCCCE		23.2026055452
173PhosphorylationAKHRRSHSGLKPFVC
HHHHHHCCCCCCEEC		47.2526055452
191SumoylationGRGFSQPKSLARHLR
CCCCCCCHHHHHHHH		50.9228112733
204PhosphorylationLRLHPELSGPGVAAK
HHCCHHHCCHHHHHH		41.0828555341
211SumoylationSGPGVAAKVLAASVR
CCHHHHHHHHHHHHH		28.2228112733
216PhosphorylationAAKVLAASVRRAKGP
HHHHHHHHHHHHCCH		15.56-
278AcetylationSRRAPAPKPYVCLEC
CCCCCCCCCEEEEEC		51.6026051181
345PhosphorylationIHAVGAPSVCSSCGQ
EEEECCCHHHHHCCC		34.9125262027
348PhosphorylationVGAPSVCSSCGQSYY
ECCCHHHHHCCCCCC		26.8925262027
349PhosphorylationGAPSVCSSCGQSYYR
CCCHHHHHCCCCCCC		19.6925262027
353PhosphorylationVCSSCGQSYYRAGGE
HHHHCCCCCCCCCCC		14.9325262027
354PhosphorylationCSSCGQSYYRAGGEE
HHHCCCCCCCCCCCC		6.7825262027
355PhosphorylationSSCGQSYYRAGGEEE
HHCCCCCCCCCCCCC		10.1525262027
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 ZN787_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN787_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 ZN787_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IL7RA_HUMANIL7Rphysical
23151878
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 ZN787_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117; SER-171 ANDSER-173, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122 AND TYR-150, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory