K1C17_MOUSE - dbPTM
K1C17_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K1C17_MOUSE
UniProt AC Q9QWL7
Protein Name Keratin, type I cytoskeletal 17
Gene Name Krt17
Organism Mus musculus (Mouse).
Sequence Length 433
Subcellular Localization Cytoplasm .
Protein Description Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair. [PubMed: 14714564]
Protein Sequence MTTTIRQFTSSSSIKGSSGLGGGSSRTSCRLSGSLGAGSCRLGSASGLGSALGSNSYSSCYSFGTGSGYGGNFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPARDYSAYYHTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKPKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR
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------MTTTIRQFT
------CCCCCHHHC
32.4230635358
3Phosphorylation-----MTTTIRQFTS
-----CCCCCHHHCC
20.9430635358
4Phosphorylation----MTTTIRQFTSS
----CCCCCHHHCCC
12.6630635358
9PhosphorylationTTTIRQFTSSSSIKG
CCCCHHHCCCCCCCC
21.2522817900
10PhosphorylationTTIRQFTSSSSIKGS
CCCHHHCCCCCCCCC
29.5230635358
11PhosphorylationTIRQFTSSSSIKGSS
CCHHHCCCCCCCCCC
25.6622006019
12PhosphorylationIRQFTSSSSIKGSSG
CHHHCCCCCCCCCCC
35.5322817900
13PhosphorylationRQFTSSSSIKGSSGL
HHHCCCCCCCCCCCC
30.2122817900
17PhosphorylationSSSSIKGSSGLGGGS
CCCCCCCCCCCCCCC
19.0730635358
18PhosphorylationSSSIKGSSGLGGGSS
CCCCCCCCCCCCCCC
46.8630635358
24PhosphorylationSSGLGGGSSRTSCRL
CCCCCCCCCCCCEEC
21.6630635358
25PhosphorylationSGLGGGSSRTSCRLS
CCCCCCCCCCCEECC
42.7430635358
32PhosphorylationSRTSCRLSGSLGAGS
CCCCEECCCCCCCCC
13.6422817900
34PhosphorylationTSCRLSGSLGAGSCR
CCEECCCCCCCCCCC
21.9122817900
39PhosphorylationSGSLGAGSCRLGSAS
CCCCCCCCCCCCCCC
8.7722817900
44PhosphorylationAGSCRLGSASGLGSA
CCCCCCCCCCCCCHH
24.6922006917
97PhosphorylationNLNDRLASYLDKVRA
HHHHHHHHHHHHHHH
30.71-
110PhosphorylationRALEEANTELEVKIR
HHHHHHCCCHHHHHH
49.33-
142UbiquitinationYHTIEDLKNKILVAT
CCCHHHHCCCEEEEE
69.39-
172UbiquitinationAADDFRTKFETEQAL
CCHHHHHHHHHHHHH
36.63-
182PhosphorylationTEQALRMSVEADING
HHHHHHHHHHHCHHH
15.46-
279PhosphorylationEDWFFSKTEELNREV
HHHHCCCHHHHCHHH
33.23-
307OxidationISELRRTMQALEIEL
HHHHHHHHHHHHHHH
1.7617203969
319PhosphorylationIELQSQLSMKASLEG
HHHHHHHHHHHHHCC
15.5917203969
320OxidationELQSQLSMKASLEGS
HHHHHHHHHHHHCCC
5.9717203969
323PhosphorylationSQLSMKASLEGSLAE
HHHHHHHHHCCCHHH
22.80-
401UbiquitinationHLTQYKPKEPVTTRQ
CCCCCCCCCCCCHHH
71.18-

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
44SPhosphorylationKinaseRPS6KA1Q15418
GPS
44SPhosphorylationKinaseP90RSKP18653
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
44SPhosphorylation

16710422

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 K1C17_MOUSE !!

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

Oops, there are no PPI records of K1C17_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K1C17_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASSSPECTROMETRY.

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