dbPTM

K1C17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K1C17_HUMAN
UniProt AC	Q04695
Protein Name	Keratin, type I cytoskeletal 17
Gene Name	KRT17
Organism	Homo sapiens (Human).
Sequence Length	432
Subcellular Localization	Cytoplasm .
Protein Description	Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair (By similarity). Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state (By similarity). Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway (By similarity). Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial "stem cells". Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors (By similarity). May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation..
Protein Sequence	MTTSIRQFTSSSSIKGSSGLGGGSSRTSCRLSGGLGAGSCRLGSAGGLGSTLGGSSYSSCYSFGSGGGYGSSFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPARDYSQYYRTIEELQNKILTATVDNANILLQIDNARLAADDFRTKFETEQALRLSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGNLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTTSIRQFT ------CCCCCHHCC	29.29	30619164
3	Phosphorylation	-----MTTSIRQFTS -----CCCCCHHCCC	22.36	30619164
4	Phosphorylation	----MTTSIRQFTSS ----CCCCCHHCCCC	13.45	30619164
9	O-linked_Glycosylation	TTSIRQFTSSSSIKG CCCCHHCCCCCCCCC	21.25	30059200
9	Phosphorylation	TTSIRQFTSSSSIKG CCCCHHCCCCCCCCC	21.25	23927012
10	O-linked_Glycosylation	TSIRQFTSSSSIKGS CCCHHCCCCCCCCCC	29.52	30059200
10	Phosphorylation	TSIRQFTSSSSIKGS CCCHHCCCCCCCCCC	29.52	23927012
11	Phosphorylation	SIRQFTSSSSIKGSS CCHHCCCCCCCCCCC	25.66	23927012
12	Phosphorylation	IRQFTSSSSIKGSSG CHHCCCCCCCCCCCC	35.53	28731282
13	Phosphorylation	RQFTSSSSIKGSSGL HHCCCCCCCCCCCCC	30.21	28355574
15	Sumoylation	FTSSSSIKGSSGLGG CCCCCCCCCCCCCCC	55.47	-
15	Methylation	FTSSSSIKGSSGLGG CCCCCCCCCCCCCCC	55.47	30782239
15	Sumoylation	FTSSSSIKGSSGLGG CCCCCCCCCCCCCCC	55.47	25114211
15	Ubiquitination	FTSSSSIKGSSGLGG CCCCCCCCCCCCCCC	55.47	-
17	Phosphorylation	SSSSIKGSSGLGGGS CCCCCCCCCCCCCCC	19.07	23927012
18	Phosphorylation	SSSIKGSSGLGGGSS CCCCCCCCCCCCCCC	46.86	23927012
24	Phosphorylation	SSGLGGGSSRTSCRL CCCCCCCCCCCEEEC	21.66	23927012
25	Phosphorylation	SGLGGGSSRTSCRLS CCCCCCCCCCEEECC	42.74	29632367
27	Phosphorylation	LGGGSSRTSCRLSGG CCCCCCCCEEECCCC	33.84	23927012
28	Phosphorylation	GGGSSRTSCRLSGGL CCCCCCCEEECCCCC	8.98	23927012
32	Phosphorylation	SRTSCRLSGGLGAGS CCCEEECCCCCCCCC	16.09	20201521
39	Phosphorylation	SGGLGAGSCRLGSAG CCCCCCCCCCCCCCC	8.77	23927012
44	O-linked_Glycosylation	AGSCRLGSAGGLGST CCCCCCCCCCCCCCC	28.47	30059200
44	Phosphorylation	AGSCRLGSAGGLGST CCCCCCCCCCCCCCC	28.47	22006917
50	Phosphorylation	GSAGGLGSTLGGSSY CCCCCCCCCCCCCCC	26.04	22210691
51	Phosphorylation	SAGGLGSTLGGSSYS CCCCCCCCCCCCCCC	27.85	22210691
55	Phosphorylation	LGSTLGGSSYSSCYS CCCCCCCCCCCCCCC	25.06	28348404
56	Phosphorylation	GSTLGGSSYSSCYSF CCCCCCCCCCCCCCC	32.10	28348404
57	Phosphorylation	STLGGSSYSSCYSFG CCCCCCCCCCCCCCC	13.29	28348404
58	Phosphorylation	TLGGSSYSSCYSFGS CCCCCCCCCCCCCCC	18.84	28348404
59	Phosphorylation	LGGSSYSSCYSFGSG CCCCCCCCCCCCCCC	14.61	28348404
61	Phosphorylation	GSSYSSCYSFGSGGG CCCCCCCCCCCCCCC	14.69	28348404
62	Phosphorylation	SSYSSCYSFGSGGGY CCCCCCCCCCCCCCC	27.71	28348404
65	Phosphorylation	SSCYSFGSGGGYGSS CCCCCCCCCCCCCCC	32.05	28348404
69	Phosphorylation	SFGSGGGYGSSFGGV CCCCCCCCCCCCCCC	19.67	27966365
71	Phosphorylation	GSGGGYGSSFGGVDG CCCCCCCCCCCCCCC	17.63	28348404
72	Phosphorylation	SGGGYGSSFGGVDGL CCCCCCCCCCCCCCE	24.44	28348404
87	Phosphorylation	LAGGEKATMQNLNDR ECCCCHHHHHHHHHH	30.29	26330541
97	Phosphorylation	NLNDRLASYLDKVRA HHHHHHHHHHHHHHH	30.71	25106551
98	Phosphorylation	LNDRLASYLDKVRAL HHHHHHHHHHHHHHH	17.20	21082442
101	Acetylation	RLASYLDKVRALEEA HHHHHHHHHHHHHHH	30.90	24788583
101	Ubiquitination	RLASYLDKVRALEEA HHHHHHHHHHHHHHH	30.90	21906983
110	Phosphorylation	RALEEANTELEVKIR HHHHHHCCCHHHHHH	49.33	21815630
115	Sumoylation	ANTELEVKIRDWYQR HCCCHHHHHHHHHHH	23.73	-
115	Ubiquitination	ANTELEVKIRDWYQR HCCCHHHHHHHHHHH	23.73	-
120	Phosphorylation	EVKIRDWYQRQAPGP HHHHHHHHHHCCCCC	9.71	-
131	Phosphorylation	APGPARDYSQYYRTI CCCCCCCHHHHHHHH	7.66	24043423
132	Phosphorylation	PGPARDYSQYYRTIE CCCCCCHHHHHHHHH	18.92	21815630
134	Phosphorylation	PARDYSQYYRTIEEL CCCCHHHHHHHHHHH	6.75	19060867
135	Phosphorylation	ARDYSQYYRTIEELQ CCCHHHHHHHHHHHH	8.14	18083107
137	Phosphorylation	DYSQYYRTIEELQNK CHHHHHHHHHHHHHH	19.33	21815630
171	Phosphorylation	LAADDFRTKFETEQA HCCHHHHHHHHHHHH	39.83	20068231
172	Sumoylation	AADDFRTKFETEQAL CCHHHHHHHHHHHHH	36.63	-
172	Methylation	AADDFRTKFETEQAL CCHHHHHHHHHHHHH	36.63	72594075
172	Sumoylation	AADDFRTKFETEQAL CCHHHHHHHHHHHHH	36.63	-
172	Ubiquitination	AADDFRTKFETEQAL CCHHHHHHHHHHHHH	36.63	2190698
175	Phosphorylation	DFRTKFETEQALRLS HHHHHHHHHHHHHHH	36.21	20068231
182	Phosphorylation	TEQALRLSVEADING HHHHHHHHHHHCHHH	16.10	28674419
198	Phosphorylation	RRVLDELTLARADLE HHHHHHHHHHHHHHH	19.14	24719451
206	Sulfoxidation	LARADLEMQIENLKE HHHHHHHHHHHHHHH	6.72	28183972
217	Phosphorylation	NLKEELAYLKKNHEE HHHHHHHHHHHCCHH	31.51	-
219	Sumoylation	KEELAYLKKNHEEEM HHHHHHHHHCCHHHH	38.56	-
219	Sumoylation	KEELAYLKKNHEEEM HHHHHHHHHCCHHHH	38.56	-
219	Ubiquitination	KEELAYLKKNHEEEM HHHHHHHHHCCHHHH	38.56	-
220	Ubiquitination	EELAYLKKNHEEEMN HHHHHHHHCCHHHHH	62.02	-
241	Sulfoxidation	GGEINVEMDAAPGVD CCEEEEECCCCCCCC	3.56	28183972
250	Phosphorylation	AAPGVDLSRILNEMR CCCCCCHHHHHHHHH	16.89	22468782
260	Phosphorylation	LNEMRDQYEKMAEKN HHHHHHHHHHHHHHH	23.08	21253578
262	Ubiquitination	EMRDQYEKMAEKNRK HHHHHHHHHHHHHHH	38.18	-
269	Ubiquitination	KMAEKNRKDAEDWFF HHHHHHHHCHHHHHC	71.35	-
277	Phosphorylation	DAEDWFFSKTEELNR CHHHHHCCCHHHHCH	29.24	21815630
278	Sumoylation	AEDWFFSKTEELNRE HHHHHCCCHHHHCHH	55.59	-
278	Methylation	AEDWFFSKTEELNRE HHHHHCCCHHHHCHH	55.59	30782233
278	Sumoylation	AEDWFFSKTEELNRE HHHHHCCCHHHHCHH	55.59	28112733
278	Ubiquitination	AEDWFFSKTEELNRE HHHHHCCCHHHHCHH	55.59	-
279	Phosphorylation	EDWFFSKTEELNREV HHHHCCCHHHHCHHH	33.23	-
288	Phosphorylation	ELNREVATNSELVQS HHCHHHHCCHHHHHC	44.44	21712546
290	Phosphorylation	NREVATNSELVQSGK CHHHHCCHHHHHCCH	28.14	21815630
295	Phosphorylation	TNSELVQSGKSEISE CCHHHHHCCHHHHHH	40.48	21815630
297	Ubiquitination	SELVQSGKSEISELR HHHHHCCHHHHHHHH	50.60	-
298	Phosphorylation	ELVQSGKSEISELRR HHHHCCHHHHHHHHH	43.62	21815630
301	Phosphorylation	QSGKSEISELRRTMQ HCCHHHHHHHHHHHH	26.90	24719451
306	Phosphorylation	EISELRRTMQALEIE HHHHHHHHHHHHHHH	13.75	22468782
316	Phosphorylation	ALEIELQSQLSMKAS HHHHHHHHHHHHHHH	45.79	22468782
319	Phosphorylation	IELQSQLSMKASLEG HHHHHHHHHHHHHHC	15.59	21082442
323	Phosphorylation	SQLSMKASLEGNLAE HHHHHHHHHHCCHHH	22.80	23927012
348	Phosphorylation	QIQGLIGSVEEQLAQ HHHHHHHCHHHHHHH	21.25	24043423
367	Phosphorylation	MEQQNQEYKILLDVK HHHHCHHEEEEHHHH	8.12	29978859
368	Ubiquitination	EQQNQEYKILLDVKT HHHCHHEEEEHHHHH	26.56	-
374	Ubiquitination	YKILLDVKTRLEQEI EEEEHHHHHHHHHHH	27.82	-
383	Phosphorylation	RLEQEIATYRRLLEG HHHHHHHHHHHHHCC	24.19	-
384	Phosphorylation	LEQEIATYRRLLEGE HHHHHHHHHHHHCCC	5.68	21253578
396	Phosphorylation	EGEDAHLTQYKKEPV CCCCCCHHCCCCCCC	21.71	26356563
398	Phosphorylation	EDAHLTQYKKEPVTT CCCCHHCCCCCCCCH	20.84	25394399
399	Sumoylation	DAHLTQYKKEPVTTR CCCHHCCCCCCCCHH	40.62	-
399	Sumoylation	DAHLTQYKKEPVTTR CCCHHCCCCCCCCHH	40.62	25114211
399	Ubiquitination	DAHLTQYKKEPVTTR CCCHHCCCCCCCCHH	40.62	-
400	Sumoylation	AHLTQYKKEPVTTRQ CCHHCCCCCCCCHHH	63.42	25114211
400	Ubiquitination	AHLTQYKKEPVTTRQ CCHHCCCCCCCCHHH	63.42	-
410	Phosphorylation	VTTRQVRTIVEEVQD CCHHHHHHHHHHHHC	30.44	21815630
419	Sumoylation	VEEVQDGKVISSREQ HHHHHCCCEECCHHH	44.69	-
419	Sumoylation	VEEVQDGKVISSREQ HHHHHCCCEECCHHH	44.69	25114211
419	Ubiquitination	VEEVQDGKVISSREQ HHHHHCCCEECCHHH	44.69	-
422	Phosphorylation	VQDGKVISSREQVHQ HHCCCEECCHHHHCC	26.74	23927012
423	Phosphorylation	QDGKVISSREQVHQT HCCCEECCHHHHCCC	28.81	24719451
431	O-linked_Glycosylation	REQVHQTTR------ HHHHCCCCC------	28.01	30059200

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
44	S	Phosphorylation	Kinase	RPS6KA1	Q15418	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
44	S	Phosphorylation		22006917
Phosphorylation at Ser-44 occurs in a growth- and stress-dependent fashion in skin keratinocytes, it has no effect on filament organization.

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 K1C17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC85B_HUMAN	CCDC85B	physical	16189514
K2C72_HUMAN	KRT72	physical	9630597
K2C8_HUMAN	KRT8	physical	9630597
KDM1A_HUMAN	KDM1A	physical	23455924
QOR_HUMAN	CRYZ	physical	22863883
PA2G4_HUMAN	PA2G4	physical	22863883
TRI69_HUMAN	TRIM69	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
167210	Pachyonychia congenita 2 (PC2)
184500	Steatocystoma multiplex (SM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of K1C17_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-12; SER-13 SER-32 ANDSER-39, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-32, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-39, AND MASSSPECTROMETRY.	19007248 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.	16964243 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-398, AND MASSSPECTROMETRY.	19534553 [Abstract]

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