ZNF16_HUMAN - dbPTM
ZNF16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF16_HUMAN
UniProt AC P17020
Protein Name Zinc finger protein 16
Gene Name ZNF16
Organism Homo sapiens (Human).
Sequence Length 682
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional activator. Promotes cell proliferation by facilitating the cell cycle phase transition from the S to G2/M phase. Involved in both the hemin- and phorbol myristate acetate (PMA)-induced erythroid and megakaryocytic differentiation, respectively. Plays also a role as an inhibitor of cell apoptosis..
Protein Sequence MPSLRTRREEAEMELSVPGPSPWTPAAQARVRDAPAVTHPGSAACGTPCCSDTELEAICPHYQQPDCDTRTEDKEFLHKEDIHEDLESQAEISENYAGDVSQVPELGDLCDDVSERDWGVPEGRRLPQSLSQEGDFTPAAMGLLRGPLGEKDLDCNGFDSRFSLSPNLMACQEIPTEERPHPYDMGGQSFQHSVDLTGHEGVPTAESPLICNECGKTFQGNPDLIQRQIVHTGEASFMCDDCGKTFSQNSVLKNRHRSHMSEKAYQCSECGKAFRGHSDFSRHQSHHSSERPYMCNECGKAFSQNSSLKKHQKSHMSEKPYECNECGKAFRRSSNLIQHQRIHSGEKPYVCSECGKAFRRSSNLIKHHRTHTGEKPFECGECGKAFSQSAHLRKHQRVHTGEKPYECNDCGKPFSRVSNLIKHHRVHTGEKPYKCSDCGKAFSQSSSLIQHRRIHTGEKPHVCNVCGKAFSYSSVLRKHQIIHTGEKPYRCSVCGKAFSHSSALIQHQGVHTGDKPYACHECGKTFGRSSNLILHQRVHTGEKPYECTECGKTFSQSSTLIQHQRIHNGLKPHECNQCGKAFNRSSNLIHHQKVHTGEKPYTCVECGKGFSQSSHLIQHQIIHTGERPYKCSECGKAFSQRSVLIQHQRIHTGVKPYDCAACGKAFSQRSKLIKHQLIHTRE
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
3Phosphorylation-----MPSLRTRREE
-----CCCHHHHHHH		29.2324719451
38PhosphorylationVRDAPAVTHPGSAAC
HCCCCCCCCCCCCCC		25.1830624053
42PhosphorylationPAVTHPGSAACGTPC
CCCCCCCCCCCCCCC		19.6930624053
47PhosphorylationPGSAACGTPCCSDTE
CCCCCCCCCCCCCHH		17.0330624053
51PhosphorylationACGTPCCSDTELEAI
CCCCCCCCCHHHHHH		55.0430624053
53PhosphorylationGTPCCSDTELEAICP
CCCCCCCHHHHHHCC		26.6130624053
129PhosphorylationEGRRLPQSLSQEGDF
CCCCCCCHHCCCCCC		28.2224719451
131PhosphorylationRRLPQSLSQEGDFTP
CCCCCHHCCCCCCCH		31.2822817900
253SumoylationFSQNSVLKNRHRSHM
CCHHHHHHHHHHHHH		50.18-
253SumoylationFSQNSVLKNRHRSHM
CCHHHHHHHHHHHHH		50.1828112733
278PhosphorylationGKAFRGHSDFSRHQS
HHHHCCCCCCCCCCC		43.0820860994
281PhosphorylationFRGHSDFSRHQSHHS
HCCCCCCCCCCCCCC		33.5720860994
293PhosphorylationHHSSERPYMCNECGK
CCCCCCCEEHHHHHH		22.11-
307PhosphorylationKAFSQNSSLKKHQKS
HHHHCCHHHHHHHHH		52.3225627689
319UbiquitinationQKSHMSEKPYECNEC
HHHHCCCCCCCCCHH		45.66-
333PhosphorylationCGKAFRRSSNLIQHQ
HHHHHHHHCCCCCCC		21.2328555341
334PhosphorylationGKAFRRSSNLIQHQR
HHHHHHHCCCCCCCH		33.5728555341
344PhosphorylationIQHQRIHSGEKPYVC
CCCCHHCCCCCCEEE		46.4021712546
361PhosphorylationCGKAFRRSSNLIKHH
HHHHHHHHCHHHHHC		21.2327251275
362PhosphorylationGKAFRRSSNLIKHHR
HHHHHHHCHHHHHCC		33.5728555341
370PhosphorylationNLIKHHRTHTGEKPF
HHHHHCCCCCCCCCC		21.31-
372PhosphorylationIKHHRTHTGEKPFEC
HHHCCCCCCCCCCCC		46.5628555341
387PhosphorylationGECGKAFSQSAHLRK
CCCHHHHHCHHHHHH		28.2526074081
389PhosphorylationCGKAFSQSAHLRKHQ
CHHHHHCHHHHHHHC		19.2326074081
400PhosphorylationRKHQRVHTGEKPYEC
HHHCCCCCCCCCCCC		44.1528555341
428PhosphorylationIKHHRVHTGEKPYKC
HHHCCCCCCCCCEEC		44.1529496963
431SumoylationHRVHTGEKPYKCSDC
CCCCCCCCCEECCCC		55.80-
431UbiquitinationHRVHTGEKPYKCSDC
CCCCCCCCCEECCCC		55.80-
431SumoylationHRVHTGEKPYKCSDC
CCCCCCCCCEECCCC		55.80-
436PhosphorylationGEKPYKCSDCGKAFS
CCCCEECCCCCHHHH		31.6127251275
443PhosphorylationSDCGKAFSQSSSLIQ
CCCCHHHHCCCHHHH		33.7327251275
456PhosphorylationIQHRRIHTGEKPHVC
HHCCCCCCCCCCCEE		44.67-
474PhosphorylationGKAFSYSSVLRKHQI
CCCCCHHHHHHHCCE		19.5528555341
478UbiquitinationSYSSVLRKHQIIHTG
CHHHHHHHCCEEECC		35.3829967540
484PhosphorylationRKHQIIHTGEKPYRC
HHCCEEECCCCCEEE		36.3129496963
487SumoylationQIIHTGEKPYRCSVC
CEEECCCCCEEEECC		49.0119608861
487AcetylationQIIHTGEKPYRCSVC
CEEECCCCCEEEECC		49.0119608861
487SumoylationQIIHTGEKPYRCSVC
CEEECCCCCEEEECC		49.01-
487UbiquitinationQIIHTGEKPYRCSVC
CEEECCCCCEEEECC		49.0119608861
540PhosphorylationILHQRVHTGEKPYEC
EEEEEEECCCCCEEC		44.15-
596PhosphorylationIHHQKVHTGEKPYTC
CCEEEEECCCCCEEE		50.4521857030
624PhosphorylationIQHQIIHTGERPYKC
HHEEEEECCCCCEEC		30.2624719451
642PhosphorylationGKAFSQRSVLIQHQR
CCCHHCCCHHHCCCC		17.4030631047
652PhosphorylationIQHQRIHTGVKPYDC
HCCCCCCCCCCCCCC		41.1028555341
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 ZNF16_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF16_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 ZNF16_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN101_HUMANZNF101physical
25416956
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 ZNF16_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-487, AND MASS SPECTROMETRY.

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