K2C6A_MOUSE - dbPTM
K2C6A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C6A_MOUSE
UniProt AC P50446
Protein Name Keratin, type II cytoskeletal 6A
Gene Name Krt6a
Organism Mus musculus (Mouse).
Sequence Length 553
Subcellular Localization
Protein Description Epidermis-specific type I keratin involved in wound healing. [PubMed: 10866680 Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration]
Protein Sequence MSTKTTIKSQTSHRGYSASSARVPGLNRSGFSSVSVCRSRGSGGSSAMCGGAGFGSRSLYGVGSSKRISIGGGSCGIGGGYGSRFGGSFGIGGGAGSGFGFGGGAGFGGGYGGAGFPVCPPGGIQEVTINQSLLTPLNLQIDPTIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRQNLEPMFEQYISNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADSLTDDINFLRALYEAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQDMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGPVNISVVQSTVSSGYGSAGGASSSLGLGGGSSYSYSSSHGLGGGFSAGSGRAIGGGLSSSGGLSSSTIKYTTTSSSKKSYRQ
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
9PhosphorylationSTKTTIKSQTSHRGY
CCCCEECCCCCCCCC
34.54-
17PhosphorylationQTSHRGYSASSARVP
CCCCCCCCCCCCCCC
25.2119367708
19PhosphorylationSHRGYSASSARVPGL
CCCCCCCCCCCCCCC
20.7021082442
20PhosphorylationHRGYSASSARVPGLN
CCCCCCCCCCCCCCC
21.5819367708
29PhosphorylationRVPGLNRSGFSSVSV
CCCCCCCCCCCEEEE
43.0219367708
35PhosphorylationRSGFSSVSVCRSRGS
CCCCCEEEEEECCCC
19.9022817900
39PhosphorylationSSVSVCRSRGSGGSS
CEEEEEECCCCCCCC
35.5522817900
40MethylationSVSVCRSRGSGGSSA
EEEEEECCCCCCCCC
24.7631122779
42PhosphorylationSVCRSRGSGGSSAMC
EEEECCCCCCCCCCC
38.5819367708
58PhosphorylationGAGFGSRSLYGVGSS
CCCCCCCCEECCCCC
27.8622817900
69PhosphorylationVGSSKRISIGGGSCG
CCCCCEEEECCCCCC
21.1522817900
74PhosphorylationRISIGGGSCGIGGGY
EEEECCCCCCCCCCC
16.6719367708
150PhosphorylationPTIQRVRTEEREQIK
CCHHHHCHHHHHHHH
39.06-
158PhosphorylationEEREQIKTLNNKFAS
HHHHHHHHHHHHHHH
36.0329899451
162UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
165PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH
26.3522817900
169UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.4127667366
178UbiquitinationRFLEQQNKVLDTKWA
HHHHHHHCHHHHHHH
39.58-
183UbiquitinationQNKVLDTKWALLQEQ
HHCHHHHHHHHHHHH
30.09-
226PhosphorylationGERGRLDSELRNMQD
CCCCHHHHHHHHCHH
43.0222817900
258PhosphorylationAAENEFVTLKKDVDA
HHHCCCEEEEHHHCH
37.8721659604
316PhosphorylationLSMDNNRSLDLDSII
EECCCCCCCCHHHHH
28.4922817900
321PhosphorylationNRSLDLDSIIAEVKA
CCCCCHHHHHHHHHH
24.1622817900
358DimethylationELQVTAGRHGDDLRN
HHHHHCCCCCCHHHH
28.31-
415AcetylationALKDARGKLEGLEDA
HHHHHHHHHCCHHHH
37.507461943
435AcetylationQDMARLLKEYQELMN
HHHHHHHHHHHHHHC
59.997612025
456UbiquitinationVEIATYRKLLEGEEC
HHHHHHHHHHCCCCC
47.1927667366

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 K2C6A_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C6A_MOUSE !!

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 K2C6A_MOUSE !!

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

Oops, there are no PPI records of K2C6A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C6A_MOUSE

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Related Literatures of Post-Translational Modification

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