K2C75_HUMAN - dbPTM
K2C75_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C75_HUMAN
UniProt AC O95678
Protein Name Keratin, type II cytoskeletal 75
Gene Name KRT75
Organism Homo sapiens (Human).
Sequence Length 551
Subcellular Localization
Protein Description Plays a central role in hair and nail formation. Essential component of keratin intermediate filaments in the companion layer of the hair follicle..
Protein Sequence MSRQSSITFQSGSRRGFSTTSAITPAAGRSRFSSVSVARSAAGSGGLGRISSAGASFGSRSLYNLGGAKRVSINGCGSSCRSGFGGRASNRFGVNSGFGYGGGVGGGFSGPSFPVCPPGGIQEVTVNQSLLTPLHLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGSRTVRQNLEPLFDSYTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEECRLSGEGVSPVNISVVTSTLSSGYGSGSSIGGGNLGLGGGSGYSFTTSGGHSLGAGLGGSGFSATSNRGLGGSGSSVKFVSTTSSSQKSYTH
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
5Phosphorylation---MSRQSSITFQSG
---CCCCCCEEECCC		23.6923403867
6Phosphorylation--MSRQSSITFQSGS
--CCCCCCEEECCCC		19.8023403867
8PhosphorylationMSRQSSITFQSGSRR
CCCCCCEEECCCCCC		19.9823403867
11PhosphorylationQSSITFQSGSRRGFS
CCCEEECCCCCCCCC		34.2523403867
13PhosphorylationSITFQSGSRRGFSTT
CEEECCCCCCCCCCC		24.8522210691
18PhosphorylationSGSRRGFSTTSAITP
CCCCCCCCCCCCCCC		33.3324719451
19PhosphorylationGSRRGFSTTSAITPA
CCCCCCCCCCCCCCC		23.6224245541
20PhosphorylationSRRGFSTTSAITPAA
CCCCCCCCCCCCCCC		18.2428348404
21PhosphorylationRRGFSTTSAITPAAG
CCCCCCCCCCCCCCC		20.1224245541
33PhosphorylationAAGRSRFSSVSVARS
CCCCCCCCCHHHHHH		28.8124719451
34PhosphorylationAGRSRFSSVSVARSA
CCCCCCCCHHHHHHC		18.72-
36PhosphorylationRSRFSSVSVARSAAG
CCCCCCHHHHHHCCC		16.41-
40PhosphorylationSSVSVARSAAGSGGL
CCHHHHHHCCCCCCC		16.8420860994
44PhosphorylationVARSAAGSGGLGRIS
HHHHCCCCCCCCCCC		25.5920860994
51PhosphorylationSGGLGRISSAGASFG
CCCCCCCCCCCCCCC		16.8720860994
52PhosphorylationGGLGRISSAGASFGS
CCCCCCCCCCCCCCC		28.4920860994
56PhosphorylationRISSAGASFGSRSLY
CCCCCCCCCCCCCCC		29.2620860994
59PhosphorylationSAGASFGSRSLYNLG
CCCCCCCCCCCCCCC		19.3820860994
61PhosphorylationGASFGSRSLYNLGGA
CCCCCCCCCCCCCCC		36.5824245541
69AcetylationLYNLGGAKRVSINGC
CCCCCCCCEEEECCC		57.527960381
72PhosphorylationLGGAKRVSINGCGSS
CCCCCEEEECCCCCC		17.8619060867
78PhosphorylationVSINGCGSSCRSGFG
EEECCCCCCCCCCCC		30.2724719451
154UbiquitinationAEEREQIKTLNNKFA
HHHHHHHHHHHHHHH		46.8021906983
155PhosphorylationEEREQIKTLNNKFAS
HHHHHHHHHHHHHHH		36.0327251275
159UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0321963094
159SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
159SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
159AcetylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0327178108
159NeddylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0332015554
159MalonylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0321908771
159MethylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.037212395
162PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH		26.3528355574
166AcetylationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4119608861
166UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4121963094
175UbiquitinationRFLEQQNKVLETKWA
HHHHHHHHHHHHHHH		43.8116196087
191PhosphorylationLQEQGSRTVRQNLEP
HHHCCCHHHHHHCHH		23.0327251275
215PhosphorylationRRQLESITTERGRLE
HHHHHHHHHHHHHHH		31.7022985185
216PhosphorylationRQLESITTERGRLEA
HHHHHHHHHHHHHHH		23.2422985185
264PhosphorylationKKDVDAAYMNKVELE
ECCCCHHHHCHHHHH		11.7122817900
297PhosphorylationAELSQLQTQVGDTSV
HHHHHHHHHCCCCEE		33.54-
302PhosphorylationLQTQVGDTSVVLSMD
HHHHCCCCEEEEEEC		19.93-
318PhosphorylationNRNLDLDSIIAEVKA
CCCCCHHHHHHHHHH		24.1626657352
324UbiquitinationDSIIAEVKAQYEDIA
HHHHHHHHHHHHHHH		22.6822817900
327PhosphorylationIAEVKAQYEDIANRS
HHHHHHHHHHHHHHH		22.0427273156
334PhosphorylationYEDIANRSRAEAESW
HHHHHHHHHHHHHHH		35.3328355574
342PhosphorylationRAEAESWYQTKYEEL
HHHHHHHHHHHHHHH		18.6522817900
344PhosphorylationEAESWYQTKYEELQV
HHHHHHHHHHHHHHH		21.6419060867
346PhosphorylationESWYQTKYEELQVTA
HHHHHHHHHHHHHHC		20.3022817900
352PhosphorylationKYEELQVTAGRHGDD
HHHHHHHHCCCCCHH		15.50-
383PhosphorylationRLRAEIDSVKKQCSS
HHHHHHHHHHHHHHH		41.3120068231
407UbiquitinationQRGELALKDARAKLV
HHHHHHHHHHHHHCC		43.6721963094
412UbiquitinationALKDARAKLVDLEEA
HHHHHHHHCCCHHHH		43.4122817900
424SumoylationEEALQKAKQDMARLL
HHHHHHHHHHHHHHH		54.59-
424SumoylationEEALQKAKQDMARLL
HHHHHHHHHHHHHHH		54.59-
434PhosphorylationMARLLREYQELMNIK
HHHHHHHHHHHHCHH		10.80-
453UbiquitinationVEIATYRKLLEGEEC
HHHHHHHHHHCCCCC		47.1922817900
461MethylationLLEGEECRLSGEGVS
HHCCCCCCCCCCCCC		34.86-
532PhosphorylationSNRGLGGSGSSVKFV
CCCCCCCCCCCEEEE		33.4327251275
534PhosphorylationRGLGGSGSSVKFVST
CCCCCCCCCEEEEEC		33.3927251275
535PhosphorylationGLGGSGSSVKFVSTT
CCCCCCCCEEEEECC		32.6227251275
545PhosphorylationFVSTTSSSQKSYTH-
EEECCCCCCCCCCC-		41.20-
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 K2C75_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C75_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 K2C75_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of K2C75_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600628Loose anagen hair syndrome (LAHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C75_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory