K2C5_HUMAN - dbPTM
K2C5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C5_HUMAN
UniProt AC P13647
Protein Name Keratin, type II cytoskeletal 5
Gene Name KRT5
Organism Homo sapiens (Human).
Sequence Length 590
Subcellular Localization
Protein Description
Protein Sequence MSRQSSVSFRSGGSRSFSTASAITPSVSRTSFTSVSRSGGGGGGGFGRVSLAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGYGFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTSSVSSGYGSGSGYGGGLGGGLGGGLGGGLAGGSSGSYYSSSSGGVGLGGGLSVGGSGFSASSGRGLGVGFGSGGGSSSSVKFVSTTSSSRKSFKS
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------MSRQSSVSF
------CCCCCCEEE
38.7428355574
5Phosphorylation---MSRQSSVSFRSG
---CCCCCCEEECCC
31.4328355574
6Phosphorylation--MSRQSSVSFRSGG
--CCCCCCEEECCCC
17.2828355574
8PhosphorylationMSRQSSVSFRSGGSR
CCCCCCEEECCCCCC
19.5225394399
11PhosphorylationQSSVSFRSGGSRSFS
CCCEEECCCCCCCCE
45.5625394399
14PhosphorylationVSFRSGGSRSFSTAS
EEECCCCCCCCEECC
28.4223927012
16PhosphorylationFRSGGSRSFSTASAI
ECCCCCCCCEECCEE
25.8328355574
18PhosphorylationSGGSRSFSTASAITP
CCCCCCCEECCEECC
25.0628355574
19PhosphorylationGGSRSFSTASAITPS
CCCCCCEECCEECCC
23.7128355574
21PhosphorylationSRSFSTASAITPSVS
CCCCEECCEECCCCC
21.9428355574
24PhosphorylationFSTASAITPSVSRTS
CEECCEECCCCCCCE
14.8228355574
26PhosphorylationTASAITPSVSRTSFT
ECCEECCCCCCCEEE
24.8723927012
28PhosphorylationSAITPSVSRTSFTSV
CEECCCCCCCEEEEE
33.8925394399
30PhosphorylationITPSVSRTSFTSVSR
ECCCCCCCEEEEECC
22.2323927012
31PhosphorylationTPSVSRTSFTSVSRS
CCCCCCCEEEEECCC
25.9725394399
33PhosphorylationSVSRTSFTSVSRSGG
CCCCCEEEEECCCCC
28.1723927012
34PhosphorylationVSRTSFTSVSRSGGG
CCCCEEEEECCCCCC
18.9828355574
36PhosphorylationRTSFTSVSRSGGGGG
CCEEEEECCCCCCCC
22.0928355574
38PhosphorylationSFTSVSRSGGGGGGG
EEEEECCCCCCCCCC
33.9925106551
50PhosphorylationGGGFGRVSLAGACGV
CCCCCCCCCCCCCCC
15.9023927012
60PhosphorylationGACGVGGYGSRSLYN
CCCCCCCCCCCEEEE
13.1423927012
62PhosphorylationCGVGGYGSRSLYNLG
CCCCCCCCCEEEECC
15.3723927012
64PhosphorylationVGGYGSRSLYNLGGS
CCCCCCCEEEECCCC
36.5828355574
66PhosphorylationGYGSRSLYNLGGSKR
CCCCCEEEECCCCCC
15.0223927012
71PhosphorylationSLYNLGGSKRISIST
EEEECCCCCCEEEEE
19.5728355574
72MethylationLYNLGGSKRISISTS
EEECCCCCCEEEEEC
57.967379933
72AcetylationLYNLGGSKRISISTS
EEECCCCCCEEEEEC
57.967379933
75PhosphorylationLGGSKRISISTSGGS
CCCCCCEEEEECCCC
17.9628355574
77PhosphorylationGSKRISISTSGGSFR
CCCCEEEEECCCCCC
15.1028355574
78PhosphorylationSKRISISTSGGSFRN
CCCEEEEECCCCCCC
29.7123927012
79PhosphorylationKRISISTSGGSFRNR
CCEEEEECCCCCCCC
34.0725394399
82PhosphorylationSISTSGGSFRNRFGA
EEEECCCCCCCCCCC
25.2628355574
151PhosphorylationTVNQSLLTPLNLQID
EECHHHHCCCCCCCC
30.90-
173UbiquitinationTEEREQIKTLNNKFA
HHHHHHHHHHHHHHH
46.8022817900
174PhosphorylationEEREQIKTLNNKFAS
HHHHHHHHHHHHHHH
36.0324719451
178MethylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03132991
178SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
178SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
178UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.0321963094
178NeddylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.0332015554
178AcetylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03132991
181PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH
26.3528355574
185AcetylationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.417705685
185UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.4121963094
194UbiquitinationRFLEQQNKVLDTKWT
HHHHHHHCHHHHHHH
39.5816196087
199MethylationQNKVLDTKWTLLQEQ
HHCHHHHHHHHHHHH
37.5472616219
201PhosphorylationKVLDTKWTLLQEQGT
CHHHHHHHHHHHHCC
21.1024719451
210PhosphorylationLQEQGTKTVRQNLEP
HHHHCCHHHHHHHHH
22.2824719451
222PhosphorylationLEPLFEQYINNLRRQ
HHHHHHHHHHHHHHH
9.83-
232PhosphorylationNLRRQLDSIVGERGR
HHHHHHHHHHCHHHH
27.9728355574
242PhosphorylationGERGRLDSELRNMQD
CHHHHHHHHHHHHHH
43.0228355574
255NeddylationQDLVEDFKNKYEDEI
HHHHHHHHHHHHHHH
65.9232015554
255UbiquitinationQDLVEDFKNKYEDEI
HHHHHHHHHHHHHHH
65.9222817900
257NeddylationLVEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.0832015554
257UbiquitinationLVEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.0821906983
257MethylationLVEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.0855169325
258PhosphorylationVEDFKNKYEDEINKR
HHHHHHHHHHHHHHC
37.7020736484
264MethylationKYEDEINKRTTAENE
HHHHHHHHCCCCCCE
57.70-
264UbiquitinationKYEDEINKRTTAENE
HHHHHHHHCCCCCCE
57.7029901268
283PhosphorylationKKDVDAAYMNKVELE
ECCCCHHHHCCHHHH
11.7118083107
316PhosphorylationAELSQMQTHVSDTSV
HHHHHCCCCCCCCEE
20.9220068231
319PhosphorylationSQMQTHVSDTSVVLS
HHCCCCCCCCEEEEE
27.8020068231
321PhosphorylationMQTHVSDTSVVLSMD
CCCCCCCCEEEEECC
18.8620068231
322PhosphorylationQTHVSDTSVVLSMDN
CCCCCCCEEEEECCC
18.4120068231
326PhosphorylationSDTSVVLSMDNNRNL
CCCEEEEECCCCCCC
16.6920068231
337PhosphorylationNRNLDLDSIIAEVKA
CCCCCHHHHHHHHHH
24.1626657352
346PhosphorylationIAEVKAQYEEIANRS
HHHHHHHHHHHHHCC
22.0126356563
353PhosphorylationYEEIANRSRTEAESW
HHHHHHCCHHHHHHH
43.2824719451
355PhosphorylationEIANRSRTEAESWYQ
HHHHCCHHHHHHHHH
40.57-
359PhosphorylationRSRTEAESWYQTKYE
CCHHHHHHHHHHHHH
37.8218452278
361PhosphorylationRTEAESWYQTKYEEL
HHHHHHHHHHHHHHH
18.6519060867
363PhosphorylationEAESWYQTKYEELQQ
HHHHHHHHHHHHHHH
21.6419060867
365PhosphorylationESWYQTKYEELQQTA
HHHHHHHHHHHHHHH
20.3022817900
426UbiquitinationQRGELALKDARNKLA
HHHHHHHHHHHHHHH
43.6733845483
443SumoylationEEALQKAKQDMARLL
HHHHHHHHHHHHHHH
54.59-
443SumoylationEEALQKAKQDMARLL
HHHHHHHHHHHHHHH
54.59-
453PhosphorylationMARLLREYQELMNTK
HHHHHHHHHHHHCCC
10.80-
472UbiquitinationVEIATYRKLLEGEEC
HHHHHHHHHHCCCCC
47.1922817900
480MethylationLLEGEECRLSGEGVG
HHCCCCCCCCCCCCC
34.86-
567PhosphorylationGLGVGFGSGGGSSSS
CCCCCCCCCCCCCCC
31.8128731282
571PhosphorylationGFGSGGGSSSSVKFV
CCCCCCCCCCCEEEE
30.2623927012
572PhosphorylationFGSGGGSSSSVKFVS
CCCCCCCCCCEEEEE
29.8823927012
573PhosphorylationGSGGGSSSSVKFVST
CCCCCCCCCEEEEEC
40.6325394399
574PhosphorylationSGGGSSSSVKFVSTT
CCCCCCCCEEEEECC
31.1325394399
579PhosphorylationSSSVKFVSTTSSSRK
CCCEEEEECCCCCCC
29.1523927012
580PhosphorylationSSVKFVSTTSSSRKS
CCEEEEECCCCCCCC
25.9523927012
581PhosphorylationSVKFVSTTSSSRKSF
CEEEEECCCCCCCCC
21.0723927012
582PhosphorylationVKFVSTTSSSRKSFK
EEEEECCCCCCCCCC
26.8023927012
583PhosphorylationKFVSTTSSSRKSFKS
EEEECCCCCCCCCCC
31.8828731282
584PhosphorylationFVSTTSSSRKSFKS-
EEECCCCCCCCCCC-
43.4225247763
587PhosphorylationTTSSSRKSFKS----
CCCCCCCCCCC----
36.4825106551
590PhosphorylationSSRKSFKS-------
CCCCCCCC-------
43.3624719451

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 K2C5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C5_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 K2C5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C18_HUMANKRT18physical
9786957
K1C15_HUMANKRT15physical
25416956
K1H1_HUMANKRT31physical
25416956
KRT38_HUMANKRT38physical
25416956
K1C40_HUMANKRT40physical
25416956
K1C10_HUMANKRT10physical
26344197
K1C16_HUMANKRT16physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
131760Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS)
609352Epidermolysis bullosa simplex, with migratory circinate erythema (EBSMCE)
131800Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS)
131900Epidermolysis bullosa simplex, Koebner type (K-EBS)
131960Epidermolysis bullosa simplex, with mottled pigmentation (MP-EBS)
179850Dowling-Degos disease 1 (DDD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C5_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-60 AND TYR-66, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60 AND TYR-66, AND MASSSPECTROMETRY.

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