ZN516_HUMAN - dbPTM
ZN516_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN516_HUMAN
UniProt AC Q92618
Protein Name Zinc finger protein 516 {ECO:0000312|HGNC:HGNC:28990}
Gene Name ZNF516 {ECO:0000312|HGNC:HGNC:28990}
Organism Homo sapiens (Human).
Sequence Length 1163
Subcellular Localization Nucleus .
Protein Description Transcriptional regulator that binds to the promoter and activates the transcription of genes promoting brown adipose tissue (BAT) differentiation. Among brown adipose tissue-specific genes, binds the proximal region of the promoter of the UCP1 gene to activate its transcription and thereby regulate thermogenesis (By similarity). May also play a role in the cellular response to replication stress. [PubMed: 23446422]
Protein Sequence MDRNREAEMELRRGPSPTRAGRGHEVDGDKATCHTCCICGKSFPFQSSLSQHMRKHTGEKPYKCPYCDHRASQKGNLKIHIRSHRTGTLIQGHEPEAGEAPLGEMRASEGLDACASPTKSASACNRLLNGASQADGARVLNGASQADSGRVLLRSSKKGAEGSACAPGEAKAAVQCSFCKSQFERKKDLELHVHQAHKPFKCRLCSYATLREESLLSHIERDHITAQGPGSGEACVENGKPELSPGEFPCEVCGQAFSQTWFLKAHMKKHRGSFDHGCHICGRRFKEPWFLKNHMKAHGPKTGSKNRPKSELDPIATINNVVQEEVIVAGLSLYEVCAKCGNLFTNLDSLNAHNAIHRRVEASRTRAPAEEGAEGPSDTKQFFLQCLNLRPSAAGDSCPGTQAGRRVAELDPVNSYQAWQLATRGKVAEPAEYLKYGAWDEALAGDVAFDKDRREYVLVSQEKRKREQDAPAAQGPPRKRASGPGDPAPAGHLDPRSAARPNRRAAATTGQGKSSECFECGKIFRTYHQMVLHSRVHRRARRERDSDGDRAARARCGSLSEGDSASQPSSPGSACAAADSPGSGLADEAAEDSGEEGAPEPAPGGQPRRCCFSEEVTSTELSSGDQSHKMGDNASERDTGESKAGIAASVSILENSSRETSRRQEQHRFSMDLKMPAFHPKQEVPVPGDGVEFPSSTGAEGQTGHPAEKLSDLHNKEHSGGGKRALAPDLMPLDLSARSTRDDPSNKETASSLQAALVVHPCPYCSHKTYYPEVLWMHKRIWHRVSCNSVAPPWIQPNGYKSIRSNLVFLSRSGRTGPPPALGGKECQPLLLARFTRTQVPGGMPGSKSGSSPLGVVTKAASMPKNKESHSGGPCALWAPGPDGYRQTKPCHGQEPHGAATQGPLAKPRQEASSKPVPAPGGGGFSRSATPTPTVIARAGAQPSANSKPVEKFGVPPAGAGFAPTNKHSAPDSLKAKFSAQPQGPPPAKGEGGAPPLPPREPPSKAAQELRTLATCAAGSRGDAALQAQPGVAGAPPVLHSIKQEPVAEGHEKRLDILNIFKTYIPKDFATLYQGWGVSGPGLEHRGTLRTQARPGEFVCIECGKSFHQPGHLRAHMRAHSVVFESDGPRGSEVHTTSADAPKQGRDHSNTGTVQTVPLRKGT
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
16PhosphorylationMELRRGPSPTRAGRG
HHHHCCCCCCCCCCC
41.5528555341
18PhosphorylationLRRGPSPTRAGRGHE
HHCCCCCCCCCCCCC
37.1728102081
42PhosphorylationTCCICGKSFPFQSSL
EEECCCCCCCCCHHH
24.36-
47PhosphorylationGKSFPFQSSLSQHMR
CCCCCCCHHHHHHHH
33.36-
57PhosphorylationSQHMRKHTGEKPYKC
HHHHHHHCCCCCCCC
50.5023532336
86PhosphorylationIHIRSHRTGTLIQGH
EEEEECCCCCEEECC
29.15-
88PhosphorylationIRSHRTGTLIQGHEP
EEECCCCCEEECCCC
21.78-
108PhosphorylationPLGEMRASEGLDACA
CCCCCHHCCCCCCCC
23.1026552605
116PhosphorylationEGLDACASPTKSASA
CCCCCCCCCCCCHHH
32.7419664994
118PhosphorylationLDACASPTKSASACN
CCCCCCCCCCHHHHH
34.8330266825
120PhosphorylationACASPTKSASACNRL
CCCCCCCCHHHHHHH
29.9023312004
122PhosphorylationASPTKSASACNRLLN
CCCCCCHHHHHHHHC
40.2123312004
132PhosphorylationNRLLNGASQADGARV
HHHHCCCCCCCCCEE
27.5726714015
144PhosphorylationARVLNGASQADSGRV
CEECCCCCCCCCCCE
27.5726714015
214PhosphorylationYATLREESLLSHIER
CHHHCHHHHHHHHHH
29.8330266825
217PhosphorylationLREESLLSHIERDHI
HCHHHHHHHHHHHCC
27.9330266825
273PhosphorylationHMKKHRGSFDHGCHI
HHHHHCCCCCCCCCC
27.7127251275
456PhosphorylationFDKDRREYVLVSQEK
ECCCCCCEEEEEHHH
9.4027642862
460PhosphorylationRREYVLVSQEKRKRE
CCCEEEEEHHHHHHH
28.58-
465UbiquitinationLVSQEKRKREQDAPA
EEEHHHHHHHCCCCH
71.94-
479UbiquitinationAAQGPPRKRASGPGD
HHHCCCCCCCCCCCC
59.08-
482PhosphorylationGPPRKRASGPGDPAP
CCCCCCCCCCCCCCC
49.9428985074
514PhosphorylationATTGQGKSSECFECG
CCCCCCCCHHHHHHH
37.89-
527PhosphorylationCGKIFRTYHQMVLHS
HHHHHHHHHHHHHHH
5.9424719451
534PhosphorylationYHQMVLHSRVHRRAR
HHHHHHHHHHHHHHH
31.6624719451
635PhosphorylationHKMGDNASERDTGES
CCCCCCHHHCCCCCC
39.14-
643SumoylationERDTGESKAGIAASV
HCCCCCCHHHHHHHH
46.4628112733
649PhosphorylationSKAGIAASVSILENS
CHHHHHHHHHHHHCC
13.8423312004
651PhosphorylationAGIAASVSILENSSR
HHHHHHHHHHHCCCH
20.9624173317
656PhosphorylationSVSILENSSRETSRR
HHHHHHCCCHHHHHH
22.7723312004
657PhosphorylationVSILENSSRETSRRQ
HHHHHCCCHHHHHHH
45.8023312004
670PhosphorylationRQEQHRFSMDLKMPA
HHHHHCHHHCCCCCC
16.0224719451
681SumoylationKMPAFHPKQEVPVPG
CCCCCCCCCCCCCCC
50.9928112733
731SulfoxidationRALAPDLMPLDLSAR
CCCCCCCCCCCCCCC
3.9521406390
736PhosphorylationDLMPLDLSARSTRDD
CCCCCCCCCCCCCCC
22.69-
779AcetylationPEVLWMHKRIWHRVS
CHHHHHHHCHHHCCC
29.4923236377
786PhosphorylationKRIWHRVSCNSVAPP
HCHHHCCCCCCCCCC
13.9226552605
789PhosphorylationWHRVSCNSVAPPWIQ
HHCCCCCCCCCCCCC
24.8026552605
800PhosphorylationPWIQPNGYKSIRSNL
CCCCCCCCHHHHHCE
14.2726552605
802PhosphorylationIQPNGYKSIRSNLVF
CCCCCCHHHHHCEEE
18.1026552605
805PhosphorylationNGYKSIRSNLVFLSR
CCCHHHHHCEEEEEC
32.6126552605
811PhosphorylationRSNLVFLSRSGRTGP
HHCEEEEECCCCCCC
16.9726552605
836PhosphorylationPLLLARFTRTQVPGG
HHHHHHEECCCCCCC
27.5326657352
838PhosphorylationLLARFTRTQVPGGMP
HHHHEECCCCCCCCC
30.7526657352
849PhosphorylationGGMPGSKSGSSPLGV
CCCCCCCCCCCCCHH
45.6723403867
851PhosphorylationMPGSKSGSSPLGVVT
CCCCCCCCCCCHHHE
35.5530266825
852PhosphorylationPGSKSGSSPLGVVTK
CCCCCCCCCCHHHEE
27.8923401153
858PhosphorylationSSPLGVVTKAASMPK
CCCCHHHEEHHHCCC
16.7424667141
862PhosphorylationGVVTKAASMPKNKES
HHHEEHHHCCCCCCC
40.2423403867
901PhosphorylationQEPHGAATQGPLAKP
CCCCCCCCCCCCCCC
33.2628348404
926PhosphorylationAPGGGGFSRSATPTP
CCCCCCCCCCCCCCC
28.7127732954
928PhosphorylationGGGGFSRSATPTPTV
CCCCCCCCCCCCCCE
34.9826657352
930PhosphorylationGGFSRSATPTPTVIA
CCCCCCCCCCCCEEE
29.0130266825
932PhosphorylationFSRSATPTPTVIARA
CCCCCCCCCCEEECC
27.5123403867
934PhosphorylationRSATPTPTVIARAGA
CCCCCCCCEEECCCC
27.3323403867
952AcetylationANSKPVEKFGVPPAG
CCCCCCHHHCCCCCC
47.8819813489
969PhosphorylationFAPTNKHSAPDSLKA
CCCCCCCCCCHHHHH
43.0122468782
973PhosphorylationNKHSAPDSLKAKFSA
CCCCCCHHHHHHCCC
30.6122468782
1043SumoylationPPVLHSIKQEPVAEG
CCCCCCCCCCCCCCC
52.1828112733
1062SumoylationLDILNIFKTYIPKDF
HHHHHHHHHHCCCHH
36.3028112733
1086DimethylationSGPGLEHRGTLRTQA
CCCCCCCCCEECCCC
30.34-
1086MethylationSGPGLEHRGTLRTQA
CCCCCCCCCEECCCC
30.3430763575
1088PhosphorylationPGLEHRGTLRTQARP
CCCCCCCEECCCCCC
17.02-
1121PhosphorylationRAHMRAHSVVFESDG
HHHHEEEEEEEECCC
20.9928450419
1137O-linked_GlycosylationRGSEVHTTSADAPKQ
CCCEEEECCCCCCCC
13.6730620550

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 ZN516_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN516_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 ZN516_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H31T_HUMANHIST3H3physical
12700765

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 ZN516_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-116; THR-118; SER-852AND THR-930, AND MASS SPECTROMETRY.
"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-116, AND MASSSPECTROMETRY.

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