dbPTM

K1C20_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K1C20_MOUSE
UniProt AC	Q9D312
Protein Name	Keratin, type I cytoskeletal 20
Gene Name	Krt20 {ECO:0000312\|EMBL:AAH57172.1, ECO:0000312\|MGI:MGI:1914059}
Organism	Mus musculus (Mouse).
Sequence Length	431
Subcellular Localization
Protein Description	Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine..
Protein Sequence	MDFSRQSFHRSLSSSSQGPALSMSGSLYRKGTVQRLGAAPSVYGGAGGHGTRISVSKAVMSYGGDLSNGSDLFGGNGKLAMQNLNDRLANYLEKVRSLEQSNSRLEAQIKQWYETNAPSTIRDYSSYYAQIKELQNQVKDAQVQNAQCVLRIDNAKLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRRQLGNNVNVEVDAAPGLNLGEIMNEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEHNILLDIKTRLEQEIATYRRLLEGEDIKTTEYQLSTLEMKDIKKTRKIKTVVEEVVDGKVVSSEVKEIEESV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MDFSRQSFHRSLSS -CCCCHHHHHHHHCC	23.16	26239621
11	Phosphorylation	SRQSFHRSLSSSSQG CHHHHHHHHCCCCCC	24.84	27087446
13	Phosphorylation	QSFHRSLSSSSQGPA HHHHHHHCCCCCCCC	29.44	27087446
14	Phosphorylation	SFHRSLSSSSQGPAL HHHHHHCCCCCCCCE	39.02	26239621
15	Phosphorylation	FHRSLSSSSQGPALS HHHHHCCCCCCCCEE	24.25	26239621
16	Phosphorylation	HRSLSSSSQGPALSM HHHHCCCCCCCCEEC	40.90	27087446
22	Phosphorylation	SSQGPALSMSGSLYR CCCCCCEECCCCCEE	17.01	26239621
23	Oxidation	SQGPALSMSGSLYRK CCCCCEECCCCCEEC	5.67	17242355
24	Phosphorylation	QGPALSMSGSLYRKG CCCCEECCCCCEECC	23.12	26239621
26	Phosphorylation	PALSMSGSLYRKGTV CCEECCCCCEECCCC	18.21	26239621
28	Phosphorylation	LSMSGSLYRKGTVQR EECCCCCEECCCCCC	16.39	26239621
41	Phosphorylation	QRLGAAPSVYGGAGG CCCCCCCCCCCCCCC	24.20	23984901
43	Phosphorylation	LGAAPSVYGGAGGHG CCCCCCCCCCCCCCC	17.74	23984901
51	Phosphorylation	GGAGGHGTRISVSKA CCCCCCCCCEEEEEH	21.10	26239621
54	Phosphorylation	GGHGTRISVSKAVMS CCCCCCEEEEEHHHH	19.63	26239621
56	Phosphorylation	HGTRISVSKAVMSYG CCCCEEEEEHHHHCC	14.22	26239621
195	Phosphorylation	DNLTLQKTDLEIQIE HHCEECCCCCHHHHH	32.62	26060331
394	Phosphorylation	KTTEYQLSTLEMKDI CCCEEECCCCCHHHH	18.54	23984901
395	Phosphorylation	TTEYQLSTLEMKDIK CCEEECCCCCHHHHH	35.02	23984901
409	Phosphorylation	KKTRKIKTVVEEVVD HHHCCCEEHHHHHHC	33.00	27180971
430	Phosphorylation	EVKEIEESV------ HHHHHHHCC------	21.97	26239621

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
13	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
13	S	Phosphorylation	Kinase	MAPKAPK2	P49138	Uniprot
13	S	Phosphorylation	Kinase	MAPKAPK3	Q3UMW7	Uniprot
13	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
13	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
13	S	Phosphorylation	16608857
Hyperphosphorylation at Ser-13 occurs during the early stages of apoptosis but becomes less prominent during the later stages (By similarity).
13	S	Phosphorylation	16608857
Phosphorylation at Ser-13 also increases in response to stress brought on by cell injury.

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 K1C20_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of K1C20_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of K1C20_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylateepithelial keratins."; Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,Seidler U., Omary M.B., Kotlyarov A., Gaestel M.; J. Biol. Chem. 285:33242-33251(2010). Cited for: PHOSPHORYLATION AT SER-13 BY MAPKAPK2 AND MAPKAPK3.	20724476 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-14, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Keratin 20 serine 13 phosphorylation is a stress and intestinalgoblet cell marker."; Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J.,Burlingame A.L., Omary M.B.; J. Biol. Chem. 281:16453-16461(2006). Cited for: FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-13.	16608857 [Abstract]