dbPTM

K1C20_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K1C20_HUMAN
UniProt AC	P35900
Protein Name	Keratin, type I cytoskeletal 20
Gene Name	KRT20
Organism	Homo sapiens (Human).
Sequence Length	424
Subcellular Localization	Cytoplasm .
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 (By similarity)..
Protein Sequence	MDFSRRSFHRSLSSSLQAPVVSTVGMQRLGTTPSVYGGAGGRGIRISNSRHTVNYGSDLTGGGDLFVGNEKMAMQNLNDRLASYLEKVRTLEQSNSKLEVQIKQWYETNAPRAGRDYSAYYRQIEELRSQIKDAQLQNARCVLQIDNAKLAAEDFRLKYETERGIRLTVEADLQGLNKVFDDLTLHKTDLEIQIEELNKDLALLKKEHQEEVDGLHKHLGNTVNVEVDAAPGLNLGVIMNEMRQKYEVMAQKNLQEAKEQFERQTAVLQQQVTVNTEELKGTEVQLTELRRTSQSLEIELQSHLSMKESLEHTLEETKARYSSQLANLQSLLSSLEAQLMQIRSNMERQNNEYHILLDIKTRLEQEIATYRRLLEGEDVKTTEYQLSTLEERDIKKTRKIKTVVQEVVDGKVVSSEVKEVEENI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	SRRSFHRSLSSSLQA CHHHHHHHHHHCCCC	24.84	26657352
13	Phosphorylation	RSFHRSLSSSLQAPV HHHHHHHHHCCCCCE	21.08	21248752
14	Phosphorylation	SFHRSLSSSLQAPVV HHHHHHHHCCCCCEE	40.12	26657352
15	Phosphorylation	FHRSLSSSLQAPVVS HHHHHHHCCCCCEEE	22.56	26657352
31	Phosphorylation	VGMQRLGTTPSVYGG CCCCCCCCCCCCCCC	39.88	23312004
32	Phosphorylation	GMQRLGTTPSVYGGA CCCCCCCCCCCCCCC	16.27	23312004
34	Phosphorylation	QRLGTTPSVYGGAGG CCCCCCCCCCCCCCC	26.36	21082442
36	Phosphorylation	LGTTPSVYGGAGGRG CCCCCCCCCCCCCCC	17.74	23312004
42	Methylation	VYGGAGGRGIRISNS CCCCCCCCCEEECCC	36.13	54556931
52	Phosphorylation	RISNSRHTVNYGSDL EECCCCCEEECCCCC	14.88	23312004
55	Phosphorylation	NSRHTVNYGSDLTGG CCCCEEECCCCCCCC	17.42	23312004
57	Phosphorylation	RHTVNYGSDLTGGGD CCEEECCCCCCCCCC	21.06	23312004
60	Phosphorylation	VNYGSDLTGGGDLFV EECCCCCCCCCCEEE	38.48	23312004
83	Phosphorylation	NLNDRLASYLEKVRT HHHHHHHHHHHHHHH	34.54	20068231
84	Phosphorylation	LNDRLASYLEKVRTL HHHHHHHHHHHHHHH	17.17	20068231
90	Phosphorylation	SYLEKVRTLEQSNSK HHHHHHHHHHHCCCC	37.32	28509920
94	Phosphorylation	KVRTLEQSNSKLEVQ HHHHHHHCCCCEEEH	33.42	20068231
96	Phosphorylation	RTLEQSNSKLEVQIK HHHHHCCCCEEEHHH	43.81	28509920
117	Phosphorylation	APRAGRDYSAYYRQI CCCCCCCHHHHHHHH	8.21	20860994
118	Phosphorylation	PRAGRDYSAYYRQIE CCCCCCHHHHHHHHH	17.68	20860994
120	Phosphorylation	AGRDYSAYYRQIEEL CCCCHHHHHHHHHHH	8.01	23312004
121	Phosphorylation	GRDYSAYYRQIEELR CCCHHHHHHHHHHHH	8.85	20860994
149	Ubiquitination	VLQIDNAKLAAEDFR EEEECCHHHHHHHHH	44.93	-
168	Phosphorylation	TERGIRLTVEADLQG CCCCEEEEEEECCCH	13.37	30576142
205	Acetylation	NKDLALLKKEHQEEV HHHHHHHHHHHHHHH	57.89	27178108
292	Phosphorylation	QLTELRRTSQSLEIE EHHHHHHHCCCHHHH	25.37	20068231
293	Phosphorylation	LTELRRTSQSLEIEL HHHHHHHCCCHHHHH	18.89	20068231
295	Phosphorylation	ELRRTSQSLEIELQS HHHHHCCCHHHHHHH	27.95	20068231
369	Phosphorylation	RLEQEIATYRRLLEG HHHHHHHHHHHHHCC	24.19	-
370	Phosphorylation	LEQEIATYRRLLEGE HHHHHHHHHHHHCCC	5.68	21253578
384	Phosphorylation	EDVKTTEYQLSTLEE CCCCCCCCCCCCHHH	16.80	22817900
387	Phosphorylation	KTTEYQLSTLEERDI CCCCCCCCCHHHHHH	18.54	26657352
388	Phosphorylation	TTEYQLSTLEERDIK CCCCCCCCHHHHHHH	46.94	26657352
402	Phosphorylation	KKTRKIKTVVQEVVD HHHHCHHHHHHHHHC	29.40	23312004

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	PRKCA	P17252	GPS
13	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
13	S	Phosphorylation	Kinase	MAPKAPK3	Q16644	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.
13	S	Phosphorylation	16608857
Phosphorylation at Ser-13 also increases in response to stress brought on by cell injury (By similarity).

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EXOC8_HUMAN	EXOC8	physical	16189514
K1C20_HUMAN	KRT20	physical	16189514
COASY_HUMAN	COASY	physical	16189514
ZC3HE_HUMAN	ZC3H14	physical	16189514
ZC21C_HUMAN	ZC2HC1C	physical	16189514
CI016_HUMAN	C9orf16	physical	16189514
CI016_HUMAN	C9orf16	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
K2C80_HUMAN	KRT80	physical	25416956
TXLNA_HUMAN	TXLNA	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956

Drug and Disease Associations

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

Regulatory Network of K1C20_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASSSPECTROMETRY.	16083285 [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: PROTEIN SEQUENCE OF 11-28, FUNCTION, INTERACTION WITH KRT8,PHOSPHORYLATION AT SER-13, CLEAVAGE AT ASP-228, AND MUTAGENESIS OFSER-13 AND SER-14.	16608857 [Abstract]

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