ZN316_HUMAN - dbPTM
ZN316_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN316_HUMAN
UniProt AC A6NFI3
Protein Name Zinc finger protein 316
Gene Name ZNF316
Organism Homo sapiens (Human).
Sequence Length 1004
Subcellular Localization Nucleus.
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAALHTTPDSPAAQLERAEDGSECDPDQEEEEEEEEKGEEVQEVEEEEEEIVVEEEEEGVAEVVQDAQVEAVAEVEVEADVEEEDVKEVLAEEECPALGTQERLSRGGDAKSPVLQEKGLQASRAPATPRDEDLEEEEEEEEDEDEDDLLTAGCQELVTFEDVAVYFSLEEWERLEADQRGLYQEVMQENYGILVSLGYPIPKPDLIFRLEQGEEPWVPDSPRPEEGDIVTGVYTGAWFWTDDIEDHEEEDDEDFLAEVAEEENEPPGLWSAAYGVGDVPGTWGPDDSDSAQTPEGWGPDPGGLGVLADGSEAKPFLPGREPGANLLSPWAFPAAVAPPAGRPETTCDVCGKVFPHRSRLAKHQRYHAAVKPFGCEECGKGFVYRSHLAIHQRTHTGEKPFPCPDCGKRFVYKSHLVTHRRIHTGERPYRCAFCGAGFGRRSYLVTHQRTHTGERPYPCSHCGRSFSQSSALARHQAVHTADRPHCCPDCGQAFRLRADFQRHRRGGGCAEAGGDGPRREPGETAAAAGPEDTDPGPEGSEVGEADGEAEAAAEEREEAAVAAPTPSGKVDPAPERRFLELGNGLGEGEGPSSHPLGFHFPVHPKSWLHPDSFPILGLPDFRERLPVDGRPLPAPLGGPLSLVEGTGLACDPFGGGGAAGGGGGLRAFGPAIGGLLAEPAPAALAEEESPWICSDCGKTFGRRAALAKHQRYHAGERPHRCADCGKSFVYGSHLARHRRTHTGERPFPCPECGARFARGSHLAAHVRGHTGEKPFVCGVCGAGFSRRAHLTAHGRAHTGERPYACGECGRRFGQSAALTRHQWAHAEEKPHRCPDCGKGFGHSSDFKRHRRTHTGEKPFRCADCGRGFAQRSNLAKHRRGHTGERPFPCPECGKRFSQRSVLVTHQRTHTGERPYACANCGRRFSQSSHLLTHMKTHRGATAAPGSGSAPAPAPKPEAAAKGPSSAGPGERGSALLEFAGGTSFGSEHQAAFAGPSGAYREGVL
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
2Acetylation------MAALHTTPD
------CCCCCCCCC
29.9919369195
6Phosphorylation--MAALHTTPDSPAA
--CCCCCCCCCCHHH
40.6530266825
7Phosphorylation-MAALHTTPDSPAAQ
-CCCCCCCCCCHHHH
17.8530266825
10PhosphorylationALHTTPDSPAAQLER
CCCCCCCCHHHHHHC
20.0329255136
22PhosphorylationLERAEDGSECDPDQE
HHCCCCCCCCCCCHH
47.5827732954
100PhosphorylationEECPALGTQERLSRG
HCCCCCCCHHHHHCC
28.2725849741
105PhosphorylationLGTQERLSRGGDAKS
CCCHHHHHCCCCCCC
34.7925849741
112PhosphorylationSRGGDAKSPVLQEKG
HCCCCCCCHHHHHHC
23.2029255136
123PhosphorylationQEKGLQASRAPATPR
HHHCCCCCCCCCCCC
18.9326074081
128PhosphorylationQASRAPATPRDEDLE
CCCCCCCCCCCCCHH
20.1427362937
328PhosphorylationEPGANLLSPWAFPAA
CCCCCCCCCCCCCCC
22.8925159151
371AcetylationQRYHAAVKPFGCEEC
HHHCEECCCCCCCCC
29.8726051181
394PhosphorylationHLAIHQRTHTGEKPF
EEEEECCCCCCCCCC
19.74-
396PhosphorylationAIHQRTHTGEKPFPC
EEECCCCCCCCCCCC
46.5629214152
399AcetylationQRTHTGEKPFPCPDC
CCCCCCCCCCCCCCC
53.997428687
424PhosphorylationVTHRRIHTGERPYRC
EECCEECCCCCCEEE
38.0621857030
429PhosphorylationIHTGERPYRCAFCGA
ECCCCCCEEECCCCC
25.2528555341
442PhosphorylationGAGFGRRSYLVTHQR
CCCCCCCEEEEEECC
22.8128555341
467PhosphorylationSHCGRSFSQSSALAR
CCCCCCCCHHHHHHH
30.3328857561
480PhosphorylationARHQAVHTADRPHCC
HHHHHHHHCCCCCCC
24.5328555341
533PhosphorylationAAAGPEDTDPGPEGS
HHCCCCCCCCCCCCC
42.2929255136
540PhosphorylationTDPGPEGSEVGEADG
CCCCCCCCCCCCCCC
27.7025849741
565PhosphorylationEAAVAAPTPSGKVDP
HHHHHCCCCCCCCCC
25.9229255136
567PhosphorylationAVAAPTPSGKVDPAP
HHHCCCCCCCCCCCC
54.4429255136
727PhosphorylationRCADCGKSFVYGSHL
CCCCCCCCHHCCHHH
12.7728555341
732PhosphorylationGKSFVYGSHLARHRR
CCCHHCCHHHHHCCC
9.5328555341
740PhosphorylationHLARHRRTHTGERPF
HHHHCCCCCCCCCCC
24.6023532336
742PhosphorylationARHRRTHTGERPFPC
HHCCCCCCCCCCCCC
39.8729214152
760PhosphorylationGARFARGSHLAAHVR
CCCCCCCCCHHHHHC
15.1328555341
770PhosphorylationAAHVRGHTGEKPFVC
HHHHCCCCCCCCEEE
50.2729214152
798PhosphorylationTAHGRAHTGERPYAC
ECCCCCCCCCCCCCC
39.4928985074
829SumoylationQWAHAEEKPHRCPDC
HHHHHHCCCCCCCCC
37.3128112733
844PhosphorylationGKGFGHSSDFKRHRR
CCCCCCCHHHHHHCC
41.2028555341
852PhosphorylationDFKRHRRTHTGEKPF
HHHHHCCCCCCCCCC
24.60-
854PhosphorylationKRHRRTHTGEKPFRC
HHHCCCCCCCCCCCC
46.5629496963
857UbiquitinationRRTHTGEKPFRCADC
CCCCCCCCCCCCCCC
51.29-
882PhosphorylationAKHRRGHTGERPFPC
HHHCCCCCCCCCCCC
43.4925159151
908PhosphorylationVLVTHQRTHTGERPY
EEEEECCCCCCCCCE
19.7429759185
910PhosphorylationVTHQRTHTGERPYAC
EEECCCCCCCCCEEE
39.8729759185
925PhosphorylationANCGRRFSQSSHLLT
CCCCCCCCHHHHHHH
27.6023312004
927PhosphorylationCGRRFSQSSHLLTHM
CCCCCCHHHHHHHHC
20.6623312004
928PhosphorylationGRRFSQSSHLLTHMK
CCCCCHHHHHHHHCH
15.5423312004
946PhosphorylationGATAAPGSGSAPAPA
CCCCCCCCCCCCCCC
28.6323532336
948PhosphorylationTAAPGSGSAPAPAPK
CCCCCCCCCCCCCCC
32.5423532336
955AcetylationSAPAPAPKPEAAAKG
CCCCCCCCHHHHHCC
58.5626051181
955SumoylationSAPAPAPKPEAAAKG
CCCCCCCCHHHHHCC
58.5628112733

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 ZN316_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN316_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 ZN316_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN316_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 ZN316_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.
"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-112, AND MASSSPECTROMETRY.

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