K2C6A_HUMAN - dbPTM
K2C6A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C6A_HUMAN
UniProt AC P02538
Protein Name Keratin, type II cytoskeletal 6A
Gene Name KRT6A
Organism Homo sapiens (Human).
Sequence Length 564
Subcellular Localization
Protein Description Epidermis-specific type I keratin involved in wound healing. Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration. Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair..
Protein Sequence MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH
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
2Acetylation------MASTSTTIR
------CCCCCCCCC
22.86-
3Phosphorylation-----MASTSTTIRS
-----CCCCCCCCCC
22.9221955146
4Phosphorylation----MASTSTTIRSH
----CCCCCCCCCCC
22.1321955146
5Phosphorylation---MASTSTTIRSHS
---CCCCCCCCCCCC
22.5121955146
6Phosphorylation--MASTSTTIRSHSS
--CCCCCCCCCCCCC
26.7421955146
7Phosphorylation-MASTSTTIRSHSSS
-CCCCCCCCCCCCCC
17.7321955146
10PhosphorylationSTSTTIRSHSSSRRG
CCCCCCCCCCCCCCC
24.7021955146
12PhosphorylationSTTIRSHSSSRRGFS
CCCCCCCCCCCCCCC
31.1221955146
13PhosphorylationTTIRSHSSSRRGFSA
CCCCCCCCCCCCCCC
23.5721955146
14PhosphorylationTIRSHSSSRRGFSAN
CCCCCCCCCCCCCCC
29.0721955146
19PhosphorylationSSSRRGFSANSARLP
CCCCCCCCCCCCCCC
29.3925394399
22PhosphorylationRRGFSANSARLPGVS
CCCCCCCCCCCCCCC
17.9325394399
29PhosphorylationSARLPGVSRSGFSSV
CCCCCCCCCCCCEEE
27.0025247763
31PhosphorylationRLPGVSRSGFSSVSV
CCCCCCCCCCEEEEE
36.3625394399
34PhosphorylationGVSRSGFSSVSVSRS
CCCCCCCEEEEEECC
33.1025106551
35PhosphorylationVSRSGFSSVSVSRSR
CCCCCCEEEEEECCC
19.0228355574
37PhosphorylationRSGFSSVSVSRSRGS
CCCCEEEEEECCCCC
19.1428355574
39PhosphorylationGFSSVSVSRSRGSGG
CCEEEEEECCCCCCC
19.6123927012
41PhosphorylationSSVSVSRSRGSGGLG
EEEEEECCCCCCCCC
33.2226657352
42MethylationSVSVSRSRGSGGLGG
EEEEECCCCCCCCCC
42.0331122783
44PhosphorylationSVSRSRGSGGLGGAC
EEECCCCCCCCCCCC
28.6927966365
58PhosphorylationCGGAGFGSRSLYGLG
CCCCCCCCCCCCCCC
19.2125394399
60PhosphorylationGAGFGSRSLYGLGGS
CCCCCCCCCCCCCCC
27.8628355574
62PhosphorylationGFGSRSLYGLGGSKR
CCCCCCCCCCCCCCE
16.1423927012
67PhosphorylationSLYGLGGSKRISIGG
CCCCCCCCCEEEECC
19.5728355574
71PhosphorylationLGGSKRISIGGGSCA
CCCCCEEEECCCCEE
21.1525394399
76PhosphorylationRISIGGGSCAISGGY
EEEECCCCEEECCCC
12.0326356563
80PhosphorylationGGGSCAISGGYGSRA
CCCCEEECCCCCCCC
13.9825394399
83PhosphorylationSCAISGGYGSRAGGS
CEEECCCCCCCCCCC
18.5623927012
85PhosphorylationAISGGYGSRAGGSYG
EECCCCCCCCCCCCC
15.5225394399
146PhosphorylationTVNQSLLTPLNLQID
EECHHHHCCCCCCCC
30.90-
168UbiquitinationAEEREQIKTLNNKFA
HHHHHHHHHHHHHHH
46.8021906983
169PhosphorylationEEREQIKTLNNKFAS
HHHHHHHHHHHHHHH
36.0327251275
173MethylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03132999
173SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
173UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.0321906983
173SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
173AcetylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03132999
176PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH
26.3528355574
180UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.4121906983
180AcetylationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.417705595
194UbiquitinationQNKVLETKWTLLQEQ
HHHHHHHHHHHHHHH
28.89-
196PhosphorylationKVLETKWTLLQEQGT
HHHHHHHHHHHHHCC
21.1024719451
204UbiquitinationLLQEQGTKTVRQNLE
HHHHHCCHHHHHHHH
52.42-
205PhosphorylationLQEQGTKTVRQNLEP
HHHHCCHHHHHHHHH
22.2824719451
217PhosphorylationLEPLFEQYINNLRRQ
HHHHHHHHHHHHHHH
9.83-
227PhosphorylationNLRRQLDSIVGERGR
HHHHHHHHHHHHCCH
27.9728355574
237PhosphorylationGERGRLDSELRGMQD
HHCCHHHHHHHCHHH
43.0228355574
252AcetylationLVEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.0827178108
252UbiquitinationLVEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.0821906983
252MethylationLVEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.08-
253PhosphorylationVEDFKNKYEDEINKR
HHHHHHHHHHHHHHH
37.7022817900
259UbiquitinationKYEDEINKRTAAENE
HHHHHHHHHHHHHCC
57.71-
259MethylationKYEDEINKRTAAENE
HHHHHHHHHHHHHCC
57.71-
261PhosphorylationEDEINKRTAAENEFV
HHHHHHHHHHHCCCE
31.6529083192
278PhosphorylationKKDVDAAYMNKVELQ
EHHHCHHHHCHHHHH
11.7121253578
290PhosphorylationELQAKADTLTDEINF
HHHHCCCHHHHHHHH
36.1027966365
302PhosphorylationINFLRALYDAELSQM
HHHHHHHHHHHHHHC
16.4820860994
307PhosphorylationALYDAELSQMQTHIS
HHHHHHHHHCCCCCC
18.3420860994
311PhosphorylationAELSQMQTHISDTSV
HHHHHCCCCCCCCEE
18.8120860994
316PhosphorylationMQTHISDTSVVLSMD
CCCCCCCCEEEEECC
19.3420860994
332PhosphorylationNRNLDLDSIIAEVKA
CCCCCHHHHHHHHHH
24.1626657352
341PhosphorylationIAEVKAQYEEIAQRS
HHHHHHHHHHHHHHH
22.0126356563
348PhosphorylationYEEIAQRSRAEAESW
HHHHHHHHHHHHHHH
24.6224719451
356PhosphorylationRAEAESWYQTKYEEL
HHHHHHHHHHHHHHH
18.6526267517
358PhosphorylationEAESWYQTKYEELQV
HHHHHHHHHHHHHHH
21.6419060867
360PhosphorylationESWYQTKYEELQVTA
HHHHHHHHHHHHHHC
20.3022817900
366PhosphorylationKYEELQVTAGRHGDD
HHHHHHHHCCCCCCH
15.50-
393PhosphorylationRMIQRLRSEIDHVKK
HHHHHHHHHHHHHHH
43.4227251275
426AcetylationALKDAKNKLEGLEDA
HHHHHHHHHHCHHHH
47.407461939
448PhosphorylationLARLLKEYQELMNVK
HHHHHHHHHHHHCCH
13.0020068231
464PhosphorylationALDVEIATYRKLLEG
HHHHHHHHHHHHHCC
29.5329083192
465PhosphorylationLDVEIATYRKLLEGE
HHHHHHHHHHHHCCC
9.2029083192
475MethylationLLEGEECRLNGEGVG
HHCCCCCCCCCCCCC
34.17-
528PhosphorylationLGVGGGFSSSSGRAI
CCCCCCCCCCCCCEE
32.3621299198
531PhosphorylationGGGFSSSSGRAIGGG
CCCCCCCCCCEECCC
33.9624505115
540PhosphorylationRAIGGGLSSVGGGSS
CEECCCCCCCCCCCC
26.6723927012
541PhosphorylationAIGGGLSSVGGGSST
EECCCCCCCCCCCCE
29.8025394399
546PhosphorylationLSSVGGGSSTIKYTT
CCCCCCCCCEEEEEE
27.8123927012
547PhosphorylationSSVGGGSSTIKYTTT
CCCCCCCCEEEEEEC
37.1128731282
548PhosphorylationSVGGGSSTIKYTTTS
CCCCCCCEEEEEECC
24.1625394399
550MethylationGGGSSTIKYTTTSSS
CCCCCEEEEEECCCC
36.31-
551PhosphorylationGGSSTIKYTTTSSSS
CCCCEEEEEECCCCC
12.8819534553
552PhosphorylationGSSTIKYTTTSSSSR
CCCEEEEEECCCCCC
20.7019060867
553PhosphorylationSSTIKYTTTSSSSRK
CCEEEEEECCCCCCC
22.9128348404
554PhosphorylationSTIKYTTTSSSSRKS
CEEEEEECCCCCCCC
20.8628348404
555PhosphorylationTIKYTTTSSSSRKSY
EEEEEECCCCCCCCC
26.5728348404
556PhosphorylationIKYTTTSSSSRKSYK
EEEEECCCCCCCCCC
30.1824719451
557PhosphorylationKYTTTSSSSRKSYKH
EEEECCCCCCCCCCC
33.6528348404
558PhosphorylationYTTTSSSSRKSYKH-
EEECCCCCCCCCCC-
45.7528348404
561PhosphorylationTSSSSRKSYKH----
CCCCCCCCCCC----
38.0024719451

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C6A_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 K2C6A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WASC3_HUMANCCDC53physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
K1C15_HUMANKRT15physical
16189514
K1C17_HUMANKRT17physical
16189514
KDM1A_HUMANKDM1Aphysical
23455924
K1C13_HUMANKRT13physical
25416956
K1C15_HUMANKRT15physical
25416956
K1H1_HUMANKRT31physical
25416956
SGTA_HUMANSGTAphysical
25416956
KRT38_HUMANKRT38physical
25416956
HGS_HUMANHGSphysical
25416956
TFP11_HUMANTFIP11physical
25416956
TRI54_HUMANTRIM54physical
25416956
K1C40_HUMANKRT40physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615726Pachyonychia congenita 3 (PC3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C6A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62; TYR-83 AND TYR-551,AND MASS SPECTROMETRY.

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