K22E_MOUSE - dbPTM
K22E_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K22E_MOUSE
UniProt AC Q3TTY5
Protein Name Keratin, type II cytoskeletal 2 epidermal
Gene Name Krt2 {ECO:0000312|EMBL:AAI20486.1}
Organism Mus musculus (Mouse).
Sequence Length 707
Subcellular Localization
Protein Description Probably contributes to terminal cornification (By similarity). Associated with keratinocyte activation, proliferation and keratinization (By similarity). Plays a role in the establishment of the epidermal barrier on plantar skin. [PubMed: 26603179]
Protein Sequence MSCQISCRSRRGGGGGGGGGFRGFSSGSAVVSGGSRRSNTSFSCISRHGGGRGGSGGGGFGSQSLVGLGGYKSISSSVAGNSGGYGGSSFGGSSGFGGGRGFGGGQGFGGSGGFGGGSGFGGGQGFGGGSRFGGGSGFGGGGFGGGSFGGGRFGGGPGGFGGPGGFPGGGIHEVSVNQSLLQPLDVKVDPEIQNVKSQEREQIKTLNNKFASFIDKVRFLEQQNQVLRTKWELLQQLDVGSRTTNLDPIFQAYIGMLKKQVDRLSAERTSQESELNNMQDLVEDFKKKYEDEINKRTSAENDFVTIKKDVDSCYMDKTELQARLDILAQEVNFLRTLYDAELSQLQQDVTDTNVILSMDNNRNLDLDSIIAEVQNQYEMIAHKSKAESEELYHSKYEELQVTAVKHGDSLKEIKMEISELNRTIQRLQGEISHVKKQCKGVQDSIADAEQRGEHAIKDARGKLTDLEEALQQCREDLARLLRDYQELMNTKLSLDVEIATYRKLLEGEECRMSGDFSDNVSVSITSSTISSSVASKTGFGSGGQSSGGRGSYGGRGGGGGGGSTYGSGGRSSGSRGSGSGSGGGGYSSGGGSRGGSGGGYGSGGGSRGGSGGGYGSGGGSGSGGGYSSGGGSRGGSGGGGVSSGGGSRGGSSSGGGSRGGSSSGGGGYSSGGGSRGGSSSGGAGSSSEKGGSGSGEGCGSGVTFSFR
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
6Phosphorylation--MSCQISCRSRRGG
--CCCEEEECCCCCC
4.2419367708
22Asymmetric dimethylarginineGGGGGGFRGFSSGSA
CCCCCCCCCCCCCCE
48.82-
22MethylationGGGGGGFRGFSSGSA
CCCCCCCCCCCCCCE
48.8224129315
25PhosphorylationGGGFRGFSSGSAVVS
CCCCCCCCCCCEEEE
36.2926643407
26PhosphorylationGGFRGFSSGSAVVSG
CCCCCCCCCCEEEEC
34.2126643407
28PhosphorylationFRGFSSGSAVVSGGS
CCCCCCCCEEEECCC
21.6026643407
32PhosphorylationSSGSAVVSGGSRRSN
CCCCEEEECCCCCCC
30.7326643407
35PhosphorylationSAVVSGGSRRSNTSF
CEEEECCCCCCCCCE
28.2226643407
38PhosphorylationVSGGSRRSNTSFSCI
EECCCCCCCCCEEEE
43.2622817900
40PhosphorylationGGSRRSNTSFSCISR
CCCCCCCCCEEEEEE
32.1822817900
41PhosphorylationGSRRSNTSFSCISRH
CCCCCCCCEEEEEEC
21.2922817900
43PhosphorylationRRSNTSFSCISRHGG
CCCCCCEEEEEECCC
15.4222817900
46PhosphorylationNTSFSCISRHGGGRG
CCCEEEEEECCCCCC
23.6622817900
52MethylationISRHGGGRGGSGGGG
EEECCCCCCCCCCCC
49.9624129315
55PhosphorylationHGGGRGGSGGGGFGS
CCCCCCCCCCCCCCC
36.7722817900
62PhosphorylationSGGGGFGSQSLVGLG
CCCCCCCCCCCEECC
17.8422817900
64PhosphorylationGGGFGSQSLVGLGGY
CCCCCCCCCEECCCC
27.0722817900
88PhosphorylationNSGGYGGSSFGGSSG
CCCCCCCCCCCCCCC
20.3822817900
89PhosphorylationSGGYGGSSFGGSSGF
CCCCCCCCCCCCCCC
31.0519367708
93PhosphorylationGGSSFGGSSGFGGGR
CCCCCCCCCCCCCCC
27.8922817900
94PhosphorylationGSSFGGSSGFGGGRG
CCCCCCCCCCCCCCC
41.2222817900
111PhosphorylationGGQGFGGSGGFGGGS
CCCCCCCCCCCCCCC
35.8022817900
118PhosphorylationSGGFGGGSGFGGGQG
CCCCCCCCCCCCCCC
33.9319367708
118O-linked_GlycosylationSGGFGGGSGFGGGQG
CCCCCCCCCCCCCCC
33.9314203875
130PhosphorylationGQGFGGGSRFGGGSG
CCCCCCCCCCCCCCC
27.93-
130O-linked_GlycosylationGQGFGGGSRFGGGSG
CCCCCCCCCCCCCCC
27.9355412377
136PhosphorylationGSRFGGGSGFGGGGF
CCCCCCCCCCCCCCC
33.9322817900
147PhosphorylationGGGFGGGSFGGGRFG
CCCCCCCCCCCCCCC
24.8022817900
193UbiquitinationVKVDPEIQNVKSQER
CCCCHHHHCCHHHHH
47.1827667366
197PhosphorylationPEIQNVKSQEREQIK
HHHHCCHHHHHHHHH
32.7519367708
205PhosphorylationQEREQIKTLNNKFAS
HHHHHHHHHHHHHHH
36.0329899451
209UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
212PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH
26.3522817900
216UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.4127667366
265PhosphorylationKKQVDRLSAERTSQE
HHHHHHHHHHHCHHH
29.0424719451
269PhosphorylationDRLSAERTSQESELN
HHHHHHHCHHHHHHH
26.6822817900
270PhosphorylationRLSAERTSQESELNN
HHHHHHCHHHHHHHH
37.8719367708
312PhosphorylationTIKKDVDSCYMDKTE
EEECCCCCCCCCHHH
13.6519367708
368PhosphorylationNRNLDLDSIIAEVQN
CCCCCHHHHHHHHHH
24.1619367708
388PhosphorylationAHKSKAESEELYHSK
HHHHHHHHHHHHHHC
41.0322817900
402PhosphorylationKYEELQVTAVKHGDS
CCCCCEEEEEECCCC
16.8721454597
480UbiquitinationCREDLARLLRDYQEL
HHHHHHHHHHHHHHH
3.7027667366
503UbiquitinationVEIATYRKLLEGEEC
HHHHHHHHHHCCCCC
47.1927667366
541PhosphorylationASKTGFGSGGQSSGG
HHCCCCCCCCCCCCC
37.1722817900
546PhosphorylationFGSGGQSSGGRGSYG
CCCCCCCCCCCCCCC
37.0622817900
551PhosphorylationQSSGGRGSYGGRGGG
CCCCCCCCCCCCCCC
21.1722817900
555MethylationGRGSYGGRGGGGGGG
CCCCCCCCCCCCCCC
35.9024129315
563PhosphorylationGGGGGGGSTYGSGGR
CCCCCCCCCCCCCCC
23.0222817900
564PhosphorylationGGGGGGSTYGSGGRS
CCCCCCCCCCCCCCC
34.8722817900
567PhosphorylationGGGSTYGSGGRSSGS
CCCCCCCCCCCCCCC
27.8819367708
571PhosphorylationTYGSGGRSSGSRGSG
CCCCCCCCCCCCCCC
42.1822817900
572PhosphorylationYGSGGRSSGSRGSGS
CCCCCCCCCCCCCCC
39.1522817900
574PhosphorylationSGGRSSGSRGSGSGS
CCCCCCCCCCCCCCC
35.1022817900
577PhosphorylationRSSGSRGSGSGSGGG
CCCCCCCCCCCCCCC
28.7725890499
579PhosphorylationSGSRGSGSGSGGGGY
CCCCCCCCCCCCCCC
31.3322817900
581PhosphorylationSRGSGSGSGGGGYSS
CCCCCCCCCCCCCCC
35.6422817900
587PhosphorylationGSGGGGYSSGGGSRG
CCCCCCCCCCCCCCC
26.2822817900
588PhosphorylationSGGGGYSSGGGSRGG
CCCCCCCCCCCCCCC
32.7322817900
592PhosphorylationGYSSGGGSRGGSGGG
CCCCCCCCCCCCCCC
30.9022817900
592O-linked_GlycosylationGYSSGGGSRGGSGGG
CCCCCCCCCCCCCCC
30.9014203815
593MethylationYSSGGGSRGGSGGGY
CCCCCCCCCCCCCCC
57.6824129315
596PhosphorylationGGGSRGGSGGGYGSG
CCCCCCCCCCCCCCC
36.7726239621
596O-linked_GlycosylationGGGSRGGSGGGYGSG
CCCCCCCCCCCCCCC
36.7714203883
600PhosphorylationRGGSGGGYGSGGGSR
CCCCCCCCCCCCCCC
16.0526239621
602PhosphorylationGSGGGYGSGGGSRGG
CCCCCCCCCCCCCCC
26.2726239621
606PhosphorylationGYGSGGGSRGGSGGG
CCCCCCCCCCCCCCC
30.9022817900
607MethylationYGSGGGSRGGSGGGY
CCCCCCCCCCCCCCC
57.68-
610PhosphorylationGGGSRGGSGGGYGSG
CCCCCCCCCCCCCCC
36.7719367708
616PhosphorylationGSGGGYGSGGGSGSG
CCCCCCCCCCCCCCC
26.2719367708
620PhosphorylationGYGSGGGSGSGGGYS
CCCCCCCCCCCCCCC
32.8219367708
622PhosphorylationGSGGGSGSGGGYSSG
CCCCCCCCCCCCCCC
35.6419367708
628PhosphorylationGSGGGYSSGGGSRGG
CCCCCCCCCCCCCCC
32.7319367708
632PhosphorylationGYSSGGGSRGGSGGG
CCCCCCCCCCCCCCC
30.90-
636PhosphorylationGGGSRGGSGGGGVSS
CCCCCCCCCCCCCCC
36.7722817900
642PhosphorylationGSGGGGVSSGGGSRG
CCCCCCCCCCCCCCC
26.9222817900
643PhosphorylationSGGGGVSSGGGSRGG
CCCCCCCCCCCCCCC
38.7719367708
647O-linked_GlycosylationGVSSGGGSRGGSSSG
CCCCCCCCCCCCCCC
30.9014203743
647PhosphorylationGVSSGGGSRGGSSSG
CCCCCCCCCCCCCCC
30.9022817900
651PhosphorylationGGGSRGGSSSGGGSR
CCCCCCCCCCCCCCC
24.9326239621
652PhosphorylationGGSRGGSSSGGGSRG
CCCCCCCCCCCCCCC
35.9626239621
653PhosphorylationGSRGGSSSGGGSRGG
CCCCCCCCCCCCCCC
43.0626239621
657PhosphorylationGSSSGGGSRGGSSSG
CCCCCCCCCCCCCCC
30.9026239621
661PhosphorylationGGGSRGGSSSGGGGY
CCCCCCCCCCCCCCC
24.9319367708
662PhosphorylationGGSRGGSSSGGGGYS
CCCCCCCCCCCCCCC
35.9625890499
663PhosphorylationGSRGGSSSGGGGYSS
CCCCCCCCCCCCCCC
43.0622817900
670PhosphorylationSGGGGYSSGGGSRGG
CCCCCCCCCCCCCCC
32.7319367708
674PhosphorylationGYSSGGGSRGGSSSG
CCCCCCCCCCCCCCC
30.9019367708
675MethylationYSSGGGSRGGSSSGG
CCCCCCCCCCCCCCC
57.68-
678PhosphorylationGGGSRGGSSSGGAGS
CCCCCCCCCCCCCCC
24.9319367708
680PhosphorylationGSRGGSSSGGAGSSS
CCCCCCCCCCCCCCC
42.8319367708
685PhosphorylationSSSGGAGSSSEKGGS
CCCCCCCCCCCCCCC
30.1122817900
686PhosphorylationSSGGAGSSSEKGGSG
CCCCCCCCCCCCCCC
41.4125890499
687PhosphorylationSGGAGSSSEKGGSGS
CCCCCCCCCCCCCCC
45.0525890499
692PhosphorylationSSSEKGGSGSGEGCG
CCCCCCCCCCCCCCC
38.1522817900
694PhosphorylationSEKGGSGSGEGCGSG
CCCCCCCCCCCCCCC
35.0522817900
700PhosphorylationGSGEGCGSGVTFSFR
CCCCCCCCCCEEEEC
33.8819367708

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 K22E_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K22E_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 K22E_MOUSE !!

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

Oops, there are no PPI records of K22E_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K22E_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-606, ANDMASS SPECTROMETRY.

TOP