K22E_HUMAN - dbPTM
K22E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K22E_HUMAN
UniProt AC P35908
Protein Name Keratin, type II cytoskeletal 2 epidermal
Gene Name KRT2
Organism Homo sapiens (Human).
Sequence Length 639
Subcellular Localization
Protein Description Probably contributes to terminal cornification. [PubMed: 1380918 Associated with keratinocyte activation, proliferation and keratinization]
Protein Sequence MSCQISCKSRGRGGGGGGFRGFSSGSAVVSGGSRRSTSSFSCLSRHGGGGGGFGGGGFGSRSLVGLGGTKSISISVAGGGGGFGAAGGFGGRGGGFGGGSSFGGGSGFSGGGFGGGGFGGGRFGGFGGPGGVGGLGGPGGFGPGGYPGGIHEVSVNQSLLQPLNVKVDPEIQNVKAQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNVGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECRMSGDLSSNVTVSVTSSTISSNVASKAAFGGSGGRGSSSGGGYSSGSSSYGSGGRQSGSRGGSGGGGSISGGGYGSGGGSGGRYGSGGGSKGGSISGGGYGSGGGKHSSGGGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR
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
12MethylationISCKSRGRGGGGGGF
EEECCCCCCCCCCCC		39.20-
20Asymmetric dimethylarginineGGGGGGFRGFSSGSA
CCCCCCCCCCCCCCE		48.82-
20MethylationGGGGGGFRGFSSGSA
CCCCCCCCCCCCCCE		48.82-
23PhosphorylationGGGFRGFSSGSAVVS
CCCCCCCCCCCEEEE		36.29-
24PhosphorylationGGFRGFSSGSAVVSG
CCCCCCCCCCEEEEC		34.2124719451
26PhosphorylationFRGFSSGSAVVSGGS
CCCCCCCCEEEECCC		21.6030087585
42GlutathionylationRSTSSFSCLSRHGGG
CCCCCCCCCCCCCCC		3.6324333276
62PhosphorylationGGGFGSRSLVGLGGT
CCCCCCCCEEECCCC		29.168077693
71PhosphorylationVGLGGTKSISISVAG
EECCCCEEEEEEEEC		22.7720860994
73PhosphorylationLGGTKSISISVAGGG
CCCCEEEEEEEECCC		18.8520860994
75PhosphorylationGTKSISISVAGGGGG
CCEEEEEEEECCCCC		10.10-
183UbiquitinationAQEREQIKTLNNKFA
HHHHHHHHHHHHHHH		46.8022817900
184PhosphorylationQEREQIKTLNNKFAS
HHHHHHHHHHHHHHH		36.0324719451
188NeddylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0332015554
188UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0321963094
188SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
188MethylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03132985
188SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
188AcetylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03132985
189UbiquitinationIKTLNNKFASFIDKV
HHHHHHHHHHHHHHH		8.1721890473
191PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH		26.3528355574
194UbiquitinationNKFASFIDKVRFLEQ
HHHHHHHHHHHHHHH		41.1921890473
195UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4121963094
195AcetylationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.417705745
201UbiquitinationDKVRFLEQQNQVLQT
HHHHHHHHHHHHHHH		50.0721890473
264PhosphorylationMQDLVEDYKKKYEDE
HHHHHHHHHHHHHHH		15.94-
265AcetylationQDLVEDYKKKYEDEI
HHHHHHHHHHHHHHH		55.937481293
267UbiquitinationLVEDYKKKYEDEINK
HHHHHHHHHHHHHHH		50.1220972266
267NeddylationLVEDYKKKYEDEINK
HHHHHHHHHHHHHHH		50.1232015554
347PhosphorylationSRNLDLDSIIAEVKA
CCCCCHHHHHHHHHH		24.1626657352
356PhosphorylationIAEVKAQYEEIAQRS
HHHHHHHHHHHHHHC		22.0126356563
418UbiquitinationAHVKKQCKNVQDAIA
HHHHHHHCCHHHHHH		58.6321853274
463PhosphorylationLARLLRDYQELMNVK
HHHHHHHHHHHHCHH		9.4620068231
482UbiquitinationVEIATYRKLLEGEEC
HHHHHHHHHHCCCCC		47.1922817900
490MethylationLLEGEECRMSGDLSS
HHCCCCCCCCCCCCC		26.11-
496PhosphorylationCRMSGDLSSNVTVSV
CCCCCCCCCCEEEEE		25.3023532336
524MethylationAFGGSGGRGSSSGGG
CCCCCCCCCCCCCCC		45.40115385381
526PhosphorylationGGSGGRGSSSGGGYS
CCCCCCCCCCCCCCC		21.7028857561
527PhosphorylationGSGGRGSSSGGGYSS
CCCCCCCCCCCCCCC		35.5128857561
528PhosphorylationSGGRGSSSGGGYSSG
CCCCCCCCCCCCCCC		43.06-
536PhosphorylationGGGYSSGSSSYGSGG
CCCCCCCCCCCCCCC		20.3317192257
546PhosphorylationYGSGGRQSGSRGGSG
CCCCCCCCCCCCCCC		37.06-
548PhosphorylationSGGRQSGSRGGSGGG
CCCCCCCCCCCCCCC		32.76-
552PhosphorylationQSGSRGGSGGGGSIS
CCCCCCCCCCCCCCC		36.7720860994
557PhosphorylationGGSGGGGSISGGGYG
CCCCCCCCCCCCCCC		19.4917192257
557O-linked_GlycosylationGGSGGGGSISGGGYG
CCCCCCCCCCCCCCC		19.4926853435
563PhosphorylationGSISGGGYGSGGGSG
CCCCCCCCCCCCCCC		16.05-
565PhosphorylationISGGGYGSGGGSGGR
CCCCCCCCCCCCCCC		26.2722817900
569PhosphorylationGYGSGGGSGGRYGSG
CCCCCCCCCCCCCCC		41.1520860994
569O-linked_GlycosylationGYGSGGGSGGRYGSG
CCCCCCCCCCCCCCC		41.1526853435
573PhosphorylationGGGSGGRYGSGGGSK
CCCCCCCCCCCCCCC		20.9330576142
579O-linked_GlycosylationRYGSGGGSKGGSISG
CCCCCCCCCCCCCCC		31.2526853435
579PhosphorylationRYGSGGGSKGGSISG
CCCCCCCCCCCCCCC		31.2524275569
589PhosphorylationGSISGGGYGSGGGKH
CCCCCCCCCCCCCCC		16.0528857561
591PhosphorylationISGGGYGSGGGKHSS
CCCCCCCCCCCCCCC		26.2728857561
597PhosphorylationGSGGGKHSSGGGSRG
CCCCCCCCCCCCCCC		33.8825954137
598PhosphorylationSGGGKHSSGGGSRGG
CCCCCCCCCCCCCCC		40.9724275569
602PhosphorylationKHSSGGGSRGGSSSG
CCCCCCCCCCCCCCC		30.9025954137
606PhosphorylationGGGSRGGSSSGGGYG
CCCCCCCCCCCCCCC		24.9325954137
607PhosphorylationGGSRGGSSSGGGYGS
CCCCCCCCCCCCCCC		35.9620562096
608PhosphorylationGSRGGSSSGGGYGSG
CCCCCCCCCCCCCCC		43.0622817900
614PhosphorylationSSGGGYGSGGGGSSS
CCCCCCCCCCCCCCC		26.2722817900
620PhosphorylationGSGGGGSSSVKGSSG
CCCCCCCCCCCCCCC		42.28-
621PhosphorylationSGGGGSSSVKGSSGE
CCCCCCCCCCCCCCC		29.55-
635PhosphorylationEAFGSSVTFSFR---
CCCCCCEEEEEC---		18.6020562096
637PhosphorylationFGSSVTFSFR-----
CCCCEEEEEC-----		15.6725954137
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K22E_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 K22E_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K2C1_HUMANKRT1physical
22939629
K1C13_HUMANKRT13physical
25416956
K1C19_HUMANKRT19physical
25416956
K1H1_HUMANKRT31physical
25416956
KRT38_HUMANKRT38physical
25416956
K1C40_HUMANKRT40physical
25416956
K1C10_HUMANKRT10physical
26344197
K2C5_HUMANKRT5physical
26344197
K2C1B_HUMANKRT77physical
26344197
TRY1_HUMANPRSS1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
146800Ichthyosis bullosa of Siemens (IBS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K22E_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-536 AND SER-557,AND MASS SPECTROMETRY.

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