ZN768_HUMAN - dbPTM
ZN768_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN768_HUMAN
UniProt AC Q9H5H4
Protein Name Zinc finger protein 768
Gene Name ZNF768
Organism Homo sapiens (Human).
Sequence Length 540
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEREALPWGLEPQDVQSSDEMRSPEGYLRGNMSENEEEEISQQEGSGDYEVEEIPFGLEPQSPGFEPQSPEFEPQSPRFEPESPGFESRSPGLVPPSPEFAPRSPESDSQSPEFESQSPRYEPQSPGYEPRSPGYEPRSPGYESESSRYESQNTELKTQSPEFEAQSSKFQEGAEMLLNPEEKSPLNISVGVHPLDSFTQGFGEQPTGDLPIGPPFEMPTGALLSTPQFEMLQNPLGLTGALRGPGRRGGRARGGQGPRPNICGICGKSFGRGSTLIQHQRIHTGEKPYKCEVCSKAFSQSSDLIKHQRTHTGERPYKCPRCGKAFADSSYLLRHQRTHSGQKPYKCPHCGKAFGDSSYLLRHQRTHSHERPYSCTECGKCYSQNSSLRSHQRVHTGQRPFSCGICGKSFSQRSALIPHARSHAREKPFKCPECGKRFGQSSVLAIHARTHLPGRTYSCPDCGKTFNRSSTLIQHQRSHTGERPYRCAVCGKGFCRSSTLLQHHRVHSGERPYKCDDCGKAFSQSSDLIRHQRTHAAGRR
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
17PhosphorylationLEPQDVQSSDEMRSP
CCHHHCCCCHHHCCC		39.3423401153
18PhosphorylationEPQDVQSSDEMRSPE
CHHHCCCCHHHCCCC		22.0922115753
23PhosphorylationQSSDEMRSPEGYLRG
CCCHHHCCCCCHHHC		26.4522617229
27PhosphorylationEMRSPEGYLRGNMSE
HHCCCCCHHHCCCCC		7.4928450419
33PhosphorylationGYLRGNMSENEEEEI
CHHHCCCCCCHHHHH		41.0725921289
62PhosphorylationPFGLEPQSPGFEPQS
CCCCCCCCCCCCCCC		37.3921552520
69PhosphorylationSPGFEPQSPEFEPQS
CCCCCCCCCCCCCCC		36.7921552520
76PhosphorylationSPEFEPQSPRFEPES
CCCCCCCCCCCCCCC		28.8521552520
83PhosphorylationSPRFEPESPGFESRS
CCCCCCCCCCCCCCC		40.8319664994
88PhosphorylationPESPGFESRSPGLVP
CCCCCCCCCCCCCCC		35.4823927012
90PhosphorylationSPGFESRSPGLVPPS
CCCCCCCCCCCCCCC		32.3829255136
97PhosphorylationSPGLVPPSPEFAPRS
CCCCCCCCCCCCCCC		30.8719664994
104PhosphorylationSPEFAPRSPESDSQS
CCCCCCCCCCCCCCC		31.7722617229
107PhosphorylationFAPRSPESDSQSPEF
CCCCCCCCCCCCCCC		46.0425022875
109PhosphorylationPRSPESDSQSPEFES
CCCCCCCCCCCCCHH		41.6623663014
111PhosphorylationSPESDSQSPEFESQS
CCCCCCCCCCCHHCC		30.2825849741
116PhosphorylationSQSPEFESQSPRYEP
CCCCCCHHCCCCCCC		41.0825849741
118PhosphorylationSPEFESQSPRYEPQS
CCCCHHCCCCCCCCC		22.1825022875
121PhosphorylationFESQSPRYEPQSPGY
CHHCCCCCCCCCCCC		35.0322167270
125PhosphorylationSPRYEPQSPGYEPRS
CCCCCCCCCCCCCCC		30.8919664994
128PhosphorylationYEPQSPGYEPRSPGY
CCCCCCCCCCCCCCC		26.5830278072
132PhosphorylationSPGYEPRSPGYEPRS
CCCCCCCCCCCCCCC		33.1323401153
135PhosphorylationYEPRSPGYEPRSPGY
CCCCCCCCCCCCCCC		26.5828450419
139PhosphorylationSPGYEPRSPGYESES
CCCCCCCCCCCCCCH		33.1329255136
142PhosphorylationYEPRSPGYESESSRY
CCCCCCCCCCCHHHC		21.4823927012
144PhosphorylationPRSPGYESESSRYES
CCCCCCCCCHHHCHH		34.0023401153
146PhosphorylationSPGYESESSRYESQN
CCCCCCCHHHCHHCC		29.4223927012
147PhosphorylationPGYESESSRYESQNT
CCCCCCHHHCHHCCC		34.5323927012
149PhosphorylationYESESSRYESQNTEL
CCCCHHHCHHCCCCC		23.1428450419
151PhosphorylationSESSRYESQNTELKT
CCHHHCHHCCCCCCC		21.5730108239
154PhosphorylationSRYESQNTELKTQSP
HHCHHCCCCCCCCCH		34.7530108239
157UbiquitinationESQNTELKTQSPEFE
HHCCCCCCCCCHHHH		37.9821906983
158PhosphorylationSQNTELKTQSPEFEA
HCCCCCCCCCHHHHH		47.0729255136
160PhosphorylationNTELKTQSPEFEAQS
CCCCCCCCHHHHHHH		31.4619664994
167PhosphorylationSPEFEAQSSKFQEGA
CHHHHHHHHHHHHHH		42.4123403867
168PhosphorylationPEFEAQSSKFQEGAE
HHHHHHHHHHHHHHH		25.9623403867
253MethylationGRRGGRARGGQGPRP
CCCCCCCCCCCCCCC		48.7154560901
269PhosphorylationICGICGKSFGRGSTL
CCCCCCCCCCCCCCE		20.4420068231
272MethylationICGKSFGRGSTLIQH
CCCCCCCCCCCEEEE		33.6012020271
274PhosphorylationGKSFGRGSTLIQHQR
CCCCCCCCCEEEECC		20.7620068231
275PhosphorylationKSFGRGSTLIQHQRI
CCCCCCCCEEEECCC		30.6120068231
284PhosphorylationIQHQRIHTGEKPYKC
EEECCCCCCCCCCCC		44.6729496963
289PhosphorylationIHTGEKPYKCEVCSK
CCCCCCCCCCEECCH		39.06-
295PhosphorylationPYKCEVCSKAFSQSS
CCCCEECCHHHHCCH		31.9917525332
299PhosphorylationEVCSKAFSQSSDLIK
EECCHHHHCCHHHHH		33.7317525332
306UbiquitinationSQSSDLIKHQRTHTG
HCCHHHHHHCCCCCC		40.77-
329PhosphorylationCGKAFADSSYLLRHQ
CCCCCCCHHHHHHCC		19.9028152594
330PhosphorylationGKAFADSSYLLRHQR
CCCCCCHHHHHHCCC		21.9828152594
331PhosphorylationKAFADSSYLLRHQRT
CCCCCHHHHHHCCCC		17.4428152594
357PhosphorylationCGKAFGDSSYLLRHQ
CCCCCCCHHHHHHCC		22.6628555341
366PhosphorylationYLLRHQRTHSHERPY
HHHHCCCCCCCCCCC		22.5929449344
368PhosphorylationLRHQRTHSHERPYSC
HHCCCCCCCCCCCEE		26.8228555341
373PhosphorylationTHSHERPYSCTECGK
CCCCCCCCEECCCCC		23.6929449344
374PhosphorylationHSHERPYSCTECGKC
CCCCCCCEECCCCCC		19.7629449344
396PhosphorylationRSHQRVHTGQRPFSC
CCCCCCCCCCCCCCC		31.9529214152
414PhosphorylationGKSFSQRSALIPHAR
CCCHHHHHHHHHHHH		21.5728555341
430SumoylationHAREKPFKCPECGKR
HHHCCCCCCCCHHHH		58.36-
430SumoylationHAREKPFKCPECGKR
HHHCCCCCCCCHHHH		58.36-
442PhosphorylationGKRFGQSSVLAIHAR
HHHHCCCCEEEEEEE		17.17-
464UbiquitinationYSCPDCGKTFNRSST
EECCCCCCCCCCCCC		57.16-
469PhosphorylationCGKTFNRSSTLIQHQ
CCCCCCCCCCHHHHC		28.8728555341
480PhosphorylationIQHQRSHTGERPYRC
HHHCHHCCCCCCEEE		41.8229496963
499PhosphorylationKGFCRSSTLLQHHRV
CCCCCCCHHHHHCCC		32.5028555341
508PhosphorylationLQHHRVHSGERPYKC
HHHCCCCCCCCCEEC		39.2221857030
513PhosphorylationVHSGERPYKCDDCGK
CCCCCCCEECCCCHH		30.39-
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
139SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN768_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 ZN768_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN768_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 ZN768_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-83; SER-125; SER-139;SER-144; THR-158 AND SER-160, AND MASS SPECTROMETRY.
"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 SER-17; SER-18 AND SER-83,AND MASS 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-97 AND SER-125, AND MASSSPECTROMETRY.
"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-295 AND SER-299, ANDMASS SPECTROMETRY.

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