GLI4_HUMAN - dbPTM
GLI4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLI4_HUMAN
UniProt AC P10075
Protein Name Zinc finger protein GLI4
Gene Name GLI4
Organism Homo sapiens (Human).
Sequence Length 376
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MAALGDIQESPSVPSPVSLSSPGTPGTQHHEPQLHLHGHQHGSPGSSPKVLSQPSDLDLQDVEEVEIGRDTFWPDSEPKPEQAPRSPGSQAPDEGAGGALRSLLRSLPRRARCSAGFGPESSAERPAGQPPGAVPCAQPRGAWRVTLVQQAAAGPEGAPERAAELGVNFGRSRQGSARGAKPHRCEACGKSFKYNSLLLKHQRIHTGEKPYACHECGKRFRGWSGFIQHHRIHTGEKPYECGQCGRAFSHSSHFTQHLRIHNGEKPYKCGECGQAFSQSSNLVRHQRLHTGEKPYACSQCGKAFIWSSVLIEHQRIHTGEKPYECSDCGKAFRGRSHFFRHLRTHTGEKPFACGACGKAFGQSSQLIQHQRVHYRE
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
86PhosphorylationKPEQAPRSPGSQAPD
CCCCCCCCCCCCCCC
32.3329255136
89PhosphorylationQAPRSPGSQAPDEGA
CCCCCCCCCCCCCCH
26.9323927012
102PhosphorylationGAGGALRSLLRSLPR
CHHHHHHHHHHHCCH
32.3828674151
106PhosphorylationALRSLLRSLPRRARC
HHHHHHHHCCHHHHC
42.5728674151
125DimethylationGPESSAERPAGQPPG
CCCCCCCCCCCCCCC
26.53-
140DimethylationAVPCAQPRGAWRVTL
CCCCCCCCCCEEEEE
35.07-
206PhosphorylationLKHQRIHTGEKPYAC
HHCCCCCCCCCCEEE
44.6728111955
234PhosphorylationIQHHRIHTGEKPYEC
CCCCCEECCCCCCCC
44.6728111955
280PhosphorylationGQAFSQSSNLVRHQR
CCCHHHCCCHHHHCC
26.9224719451
290PhosphorylationVRHQRLHTGEKPYAC
HHHCCCCCCCCCEEH
52.1821857030
318PhosphorylationIEHQRIHTGEKPYEC
EEECCCCCCCCCEEC
44.6721712546
321UbiquitinationQRIHTGEKPYECSDC
CCCCCCCCCEECCCC
55.00-
330UbiquitinationYECSDCGKAFRGRSH
EECCCCCHHHCCCCH
51.16-
344PhosphorylationHFFRHLRTHTGEKPF
HHHHHHHHCCCCCCC
30.10-
346PhosphorylationFRHLRTHTGEKPFAC
HHHHHHCCCCCCCCC
46.56-

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 GLI4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLI4_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 GLI4_HUMAN !!

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

Oops, there are no PPI records of GLI4_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 GLI4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"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-86, AND MASSSPECTROMETRY.
"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-86, 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-86, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.

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