K1C25_HUMAN - dbPTM
K1C25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K1C25_HUMAN
UniProt AC Q7Z3Z0
Protein Name Keratin, type I cytoskeletal 25
Gene Name KRT25 {ECO:0000312|HGNC:HGNC:30839}
Organism Homo sapiens (Human).
Sequence Length 450
Subcellular Localization Cytoplasm .
Protein Description Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs) (By similarity). Plays a role in the cytoskeleton organization. [PubMed: 26902920]
Protein Sequence MSLRLSSASRRSCPRPTTGSLRLYGGGTSFGTGNSCGISGIGSGFSSAFGGSSSGGNTGGGNPCAGFTVNERGLLSGNEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIDDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDDGACKSGGYKSKDYGSGNVGSQVKDPAKAIVVKKVLEEVDQRSKILTTRLHSLEEKSQSN
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
2Phosphorylation------MSLRLSSAS
------CCCCCCCCC
23.3829978859
6Phosphorylation--MSLRLSSASRRSC
--CCCCCCCCCCCCC
19.8829978859
7Phosphorylation-MSLRLSSASRRSCP
-CCCCCCCCCCCCCC
34.5529978859
9PhosphorylationSLRLSSASRRSCPRP
CCCCCCCCCCCCCCC
30.1229978859
115PhosphorylationEQKIKGWYEKFGPGS
HHHHHHHHHHHCCCC
20.22-
147PhosphorylationLKNQIIASTTSNANA
HHCCEEEECCCCCCC
23.08-
148PhosphorylationKNQIIASTTSNANAV
HCCEEEECCCCCCCE
25.81-
149PhosphorylationNQIIASTTSNANAVL
CCEEEECCCCCCCEE
19.93-
150PhosphorylationQIIASTTSNANAVLQ
CEEEECCCCCCCEEE
33.75-
197PhosphorylationRRVLDEITLCRTDLE
HHHHHHHHEECCCCH
20.12-
207PhosphorylationRTDLEIQYETLSEEM
CCCCHHHHHHHHHHH
19.2826657352
209PhosphorylationDLEIQYETLSEEMTY
CCHHHHHHHHHHHHH
30.5626657352
433PhosphorylationLEEVDQRSKILTTRL
HHHHHHHHHHHHHHH
20.5818669648
437PhosphorylationDQRSKILTTRLHSLE
HHHHHHHHHHHHHHH
17.2218669648
438PhosphorylationQRSKILTTRLHSLEE
HHHHHHHHHHHHHHH
27.9929978859
442PhosphorylationILTTRLHSLEEKSQS
HHHHHHHHHHHHHHC
41.9126160856

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 K1C25_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K1C25_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 K1C25_HUMAN !!

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

Oops, there are no PPI records of K1C25_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 K1C25_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-433; THR-437 ANDSER-442, AND MASS SPECTROMETRY.

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