CRNN_HUMAN - dbPTM
CRNN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRNN_HUMAN
UniProt AC Q9UBG3
Protein Name Cornulin
Gene Name CRNN
Organism Homo sapiens (Human).
Sequence Length 495
Subcellular Localization Cytoplasm . Does not colocalize with TGM1.
Protein Description Survival factor that participates in the clonogenicity of squamous esophageal epithelium cell lines, attenuates deoxycholic acid (DCA)-induced apoptotic cell death and release of calcium. When overexpressed in oral squamous carcinom cell lines, regulates negatively cell proliferation by the induction of G1 arrest..
Protein Sequence MPQLLQNINGIIEAFRRYARTEGNCTALTRGELKRLLEQEFADVIVKPHDPATVDEVLRLLDEDHTGTVEFKEFLVLVFKVAQACFKTLSESAEGACGSQESGSLHSGASQELGEGQRSGTEVGRAGKGQHYEGSSHRQSQQGSRGQNRPGVQTQGQATGSAWVSSYDRQAESQSQERISPQIQLSGQTEQTQKAGEGKRNQTTEMRPERQPQTREQDRAHQTGETVTGSGTQTQAGATQTVEQDSSHQTGRTSKQTQEATNDQNRGTETHGQGRSQTSQAVTGGHAQIQAGTHTQTPTQTVEQDSSHQTGSTSTQTQESTNGQNRGTEIHGQGRSQTSQAVTGGHTQIQAGSHTETVEQDRSQTVSHGGAREQGQTQTQPGSGQRWMQVSNPEAGETVPGGQAQTGASTESGRQEWSSTHPRRCVTEGQGDRQPTVVGEEWVDDHSRETVILRLDQGNLHTSVSSAQGQDAAQSEEKRGITARELYSYLRSTKP
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
26PhosphorylationARTEGNCTALTRGEL
HHCCCCCEECCHHHH
28.80-
132PhosphorylationRAGKGQHYEGSSHRQ
CCCCCCCCCCCCCCC
17.69-
180PhosphorylationSQSQERISPQIQLSG
HHCCCCCCCCEECCC
19.5729759185
203PhosphorylationGEGKRNQTTEMRPER
CCCCCCCCCCCCCCC
28.4227174698
204PhosphorylationEGKRNQTTEMRPERQ
CCCCCCCCCCCCCCC
20.3027174698
336PhosphorylationEIHGQGRSQTSQAVT
EEECCCCCCCCCCCC
44.6323532336
357PhosphorylationQAGSHTETVEQDRSQ
ECCCCCCEEECCHHH
30.4222468782
363PhosphorylationETVEQDRSQTVSHGG
CEEECCHHHCCCCCC
38.1922468782
365PhosphorylationVEQDRSQTVSHGGAR
EECCHHHCCCCCCCH
25.8122468782
398PhosphorylationSNPEAGETVPGGQAQ
CCCCCCCCCCCCCCC
30.9622817900
406PhosphorylationVPGGQAQTGASTESG
CCCCCCCCCCCCCCC
37.4222817900
462PhosphorylationLDQGNLHTSVSSAQG
EECCCCCCCCHHHCC
33.7129978859
463PhosphorylationDQGNLHTSVSSAQGQ
ECCCCCCCCHHHCCC
14.8429978859
465PhosphorylationGNLHTSVSSAQGQDA
CCCCCCCHHHCCCCH
21.5229978859
466PhosphorylationNLHTSVSSAQGQDAA
CCCCCCHHHCCCCHH
23.5829978859
475PhosphorylationQGQDAAQSEEKRGIT
CCCCHHHCHHHHCCC
42.8929978859
482PhosphorylationSEEKRGITARELYSY
CHHHHCCCHHHHHHH
23.61-
487PhosphorylationGITARELYSYLRSTK
CCCHHHHHHHHHCCC
7.19-
489PhosphorylationTARELYSYLRSTKP-
CHHHHHHHHHCCCC-
7.80-
492PhosphorylationELYSYLRSTKP----
HHHHHHHCCCC----
37.88-
493PhosphorylationLYSYLRSTKP-----
HHHHHHCCCC-----
40.68-

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 CRNN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRNN_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 CRNN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADIP_HUMANSSX2IPphysical
28514442
SLMAP_HUMANSLMAPphysical
28514442
TRAP1_HUMANTRAP1physical
27173435
IF2P_HUMANEIF5Bphysical
27173435
G6PI_HUMANGPIphysical
27173435
PDIA3_HUMANPDIA3physical
27173435

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 CRNN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-398 AND THR-406, ANDMASS SPECTROMETRY.

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