dbPTM

K1C19_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K1C19_HUMAN
UniProt AC	P08727
Protein Name	Keratin, type I cytoskeletal 19
Gene Name	KRT19
Organism	Homo sapiens (Human).
Sequence Length	400
Subcellular Localization
Protein Description	Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle..
Protein Sequence	MTSYSYRQSSATSSFGGLGGGSVRFGPGVAFRAPSIHGGSGGRGVSVSSARFVSSSSSGAYGGGYGGVLTASDGLLAGNEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLSASKVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTSYSYRQS ------CCCCCCCCC	36.05	24719451
3	Phosphorylation	-----MTSYSYRQSS -----CCCCCCCCCC	15.69	28857561
4	Phosphorylation	----MTSYSYRQSSA ----CCCCCCCCCCC	10.68	28857561
5	Phosphorylation	---MTSYSYRQSSAT ---CCCCCCCCCCCC	17.38	24719451
6	Phosphorylation	--MTSYSYRQSSATS --CCCCCCCCCCCCC	12.39	28857561
7	Dimethylation	-MTSYSYRQSSATSS -CCCCCCCCCCCCCC	24.78	-
7	Methylation	-MTSYSYRQSSATSS -CCCCCCCCCCCCCC	24.78	24129315
9	Phosphorylation	TSYSYRQSSATSSFG CCCCCCCCCCCCCCC	16.97	23911959
10	Phosphorylation	SYSYRQSSATSSFGG CCCCCCCCCCCCCCC	27.51	23911959
12	Phosphorylation	SYRQSSATSSFGGLG CCCCCCCCCCCCCCC	27.18	30278072
13	Phosphorylation	YRQSSATSSFGGLGG CCCCCCCCCCCCCCC	24.32	28355574
14	Phosphorylation	RQSSATSSFGGLGGG CCCCCCCCCCCCCCC	24.45	28355574
22	Phosphorylation	FGGLGGGSVRFGPGV CCCCCCCCCEECCCE	17.25	28355574
24	Asymmetric dimethylarginine	GLGGGSVRFGPGVAF CCCCCCCEECCCEEE	32.28	-
24	Methylation	GLGGGSVRFGPGVAF CCCCCCCEECCCEEE	32.28	24129315
32	Methylation	FGPGVAFRAPSIHGG ECCCEEEECCCCCCC	35.53	24129315
35	Phosphorylation	GVAFRAPSIHGGSGG CEEEECCCCCCCCCC	26.66	27273156
40	Phosphorylation	APSIHGGSGGRGVSV CCCCCCCCCCCCCCC	42.54	28355574
43	Dimethylation	IHGGSGGRGVSVSSA CCCCCCCCCCCCCCE	45.96	-
43	Methylation	IHGGSGGRGVSVSSA CCCCCCCCCCCCCCE	45.96	24129315
46	Phosphorylation	GSGGRGVSVSSARFV CCCCCCCCCCCEEEE	21.07	28355574
48	Phosphorylation	GGRGVSVSSARFVSS CCCCCCCCCEEEEEC	15.69	28857561
49	Phosphorylation	GRGVSVSSARFVSSS CCCCCCCCEEEEECC	22.70	28857561
51	Methylation	GVSVSSARFVSSSSS CCCCCCEEEEECCCC	34.15	24129315
54	Phosphorylation	VSSARFVSSSSSGAY CCCEEEEECCCCCCC	23.07	28152594
55	Phosphorylation	SSARFVSSSSSGAYG CCEEEEECCCCCCCC	29.01	27273156
56	Phosphorylation	SARFVSSSSSGAYGG CEEEEECCCCCCCCC	22.48	28152594
57	Phosphorylation	ARFVSSSSSGAYGGG EEEEECCCCCCCCCC	34.44	26657352
58	Phosphorylation	RFVSSSSSGAYGGGY EEEECCCCCCCCCCC	29.41	28152594
61	Phosphorylation	SSSSSGAYGGGYGGV ECCCCCCCCCCCCCE	21.59	28152594
65	Phosphorylation	SGAYGGGYGGVLTAS CCCCCCCCCCEEECC	17.62	28152594
70	Phosphorylation	GGYGGVLTASDGLLA CCCCCEEECCCCCCC	23.00	28152594
72	Phosphorylation	YGGVLTASDGLLAGN CCCEEECCCCCCCCC	27.29	26657352
81	Ubiquitination	GLLAGNEKLTMQNLN CCCCCCCCCCCCCHH	53.94	21906983
93	Phosphorylation	NLNDRLASYLDKVRA CHHHHHHHHHHHHHH	30.71	25106551
94	Phosphorylation	LNDRLASYLDKVRAL HHHHHHHHHHHHHHH	17.20	26356563
97	Acetylation	RLASYLDKVRALEAA HHHHHHHHHHHHHHC	30.90	24786549
97	Ubiquitination	RLASYLDKVRALEAA HHHHHHHHHHHHHHC	30.90	21906983
111	Ubiquitination	ANGELEVKIRDWYQK CCCCEEEEEEHHHHH	23.73	21906983
116	Phosphorylation	EVKIRDWYQKQGPGP EEEEEHHHHHCCCCC	15.32	22817900
118	Methylation	KIRDWYQKQGPGPSR EEEHHHHHCCCCCCC	41.34	24583695
118	Ubiquitination	KIRDWYQKQGPGPSR EEEHHHHHCCCCCCC	41.34	21906983
124	Phosphorylation	QKQGPGPSRDYSHYY HHCCCCCCCCCHHHE	43.64	28348404
127	Phosphorylation	GPGPSRDYSHYYTTI CCCCCCCCHHHEEEH	9.02	28857561
128	Phosphorylation	PGPSRDYSHYYTTIQ CCCCCCCHHHEEEHH	14.87	28857561
130	Phosphorylation	PSRDYSHYYTTIQDL CCCCCHHHEEEHHHH	9.14	28857561
131	Phosphorylation	SRDYSHYYTTIQDLR CCCCHHHEEEHHHHH	7.62	28857561
132	Phosphorylation	RDYSHYYTTIQDLRD CCCHHHEEEHHHHHH	15.40	23312004
133	Phosphorylation	DYSHYYTTIQDLRDK CCHHHEEEHHHHHHH	10.66	27251275
140	Ubiquitination	TIQDLRDKILGATIE EHHHHHHHHHCCEEE	33.14	22817900
145	Phosphorylation	RDKILGATIENSRIV HHHHHCCEEECCEEE	27.33	23312004
149	Phosphorylation	LGATIENSRIVLQID HCCEEECCEEEEEEE	15.59	22985185
167	Phosphorylation	LAADDFRTKFETEQA CCHHHHHHHHHHHHH	39.83	21406692
168	Sumoylation	AADDFRTKFETEQAL CHHHHHHHHHHHHHH	36.63	-
168	Acetylation	AADDFRTKFETEQAL CHHHHHHHHHHHHHH	36.63	27178108
168	Methylation	AADDFRTKFETEQAL CHHHHHHHHHHHHHH	36.63	72594069
168	Sumoylation	AADDFRTKFETEQAL CHHHHHHHHHHHHHH	36.63	-
168	Ubiquitination	AADDFRTKFETEQAL CHHHHHHHHHHHHHH	36.63	21906983
171	Phosphorylation	DFRTKFETEQALRMS HHHHHHHHHHHHHHH	36.21	21406692
178	Phosphorylation	TEQALRMSVEADING HHHHHHHHHHHCHHH	15.46	24719451
194	Phosphorylation	RRVLDELTLARTDLE HHHHHHHHHHCCCHH	19.14	24719451
198	Phosphorylation	DELTLARTDLEMQIE HHHHHHCCCHHHHHH	39.05	20068231
208	Sumoylation	EMQIEGLKEELAYLK HHHHHHHHHHHHHHH	61.06	-
208	Sumoylation	EMQIEGLKEELAYLK HHHHHHHHHHHHHHH	61.06	-
208	Ubiquitination	EMQIEGLKEELAYLK HHHHHHHHHHHHHHH	61.06	21906983
213	Phosphorylation	GLKEELAYLKKNHEE HHHHHHHHHHHCCHH	31.51	21118733
215	Sumoylation	KEELAYLKKNHEEEI HHHHHHHHHCCHHHH	38.56	-
215	Sumoylation	KEELAYLKKNHEEEI HHHHHHHHHCCHHHH	38.56	-
215	Ubiquitination	KEELAYLKKNHEEEI HHHHHHHHHCCHHHH	38.56	21906983
216	Ubiquitination	EELAYLKKNHEEEIS HHHHHHHHCCHHHHH	62.02	21906983
223	Phosphorylation	KNHEEEISTLRGQVG HCCHHHHHHHCCCCC	25.35	24719451
224	Phosphorylation	NHEEEISTLRGQVGG CCHHHHHHHCCCCCC	26.57	23312004
234	Phosphorylation	GQVGGQVSVEVDSAP CCCCCEEEEEEECCC	12.50	26657352
239	Phosphorylation	QVSVEVDSAPGTDLA EEEEEEECCCCCCHH	41.35	28348404
243	Phosphorylation	EVDSAPGTDLAKILS EEECCCCCCHHHHHH	27.12	22468782
247	Ubiquitination	APGTDLAKILSDMRS CCCCCHHHHHHHHHH	52.02	21906983
250	Phosphorylation	TDLAKILSDMRSQYE CCHHHHHHHHHHHHH	32.60	24719451
254	Phosphorylation	KILSDMRSQYEVMAE HHHHHHHHHHHHHHH	30.40	26356563
256	Phosphorylation	LSDMRSQYEVMAEQN HHHHHHHHHHHHHHH	16.25	26356563
265	Ubiquitination	VMAEQNRKDAEAWFT HHHHHHHHHHHHHHH	69.69	21906983
272	Phosphorylation	KDAEAWFTSRTEELN HHHHHHHHHHHHHHH	13.44	28348404
273	Phosphorylation	DAEAWFTSRTEELNR HHHHHHHHHHHHHHH	27.94	27251275
275	Phosphorylation	EAWFTSRTEELNREV HHHHHHHHHHHHHHH	33.31	27251275
286	Phosphorylation	NREVAGHTEQLQMSR HHHHCCCHHHHHCCH	25.22	23312004
292	Phosphorylation	HTEQLQMSRSEVTDL CHHHHHCCHHHHHHH	21.50	23312004
294	Phosphorylation	EQLQMSRSEVTDLRR HHHHCCHHHHHHHHH	29.16	24719451
302	Phosphorylation	EVTDLRRTLQGLEIE HHHHHHHHHHHHHHH	19.59	20068231
312	Phosphorylation	GLEIELQSQLSMKAA HHHHHHHHHHHHHHH	45.79	20068231
315	Phosphorylation	IELQSQLSMKAALED HHHHHHHHHHHHHHH	15.59	30278072
317	Ubiquitination	LQSQLSMKAALEDTL HHHHHHHHHHHHHHH	27.42	21906983
323	Phosphorylation	MKAALEDTLAETEAR HHHHHHHHHHHHHHH	20.63	28355574
327	Phosphorylation	LEDTLAETEARFGAQ HHHHHHHHHHHHHHH	29.36	20860994
343	Phosphorylation	AHIQALISGIEAQLG HHHHHHHHCHHHHHC	34.27	24719451
370	Ubiquitination	YQRLMDIKSRLEQEI HHHHHHHHHHHHHHH	25.84	22817900
371	Phosphorylation	QRLMDIKSRLEQEIA HHHHHHHHHHHHHHH	42.29	30087585
379	Phosphorylation	RLEQEIATYRSLLEG HHHHHHHHHHHHHCC	25.73	-
380	Phosphorylation	LEQEIATYRSLLEGQ HHHHHHHHHHHHCCC	6.81	-
382	Phosphorylation	QEIATYRSLLEGQED HHHHHHHHHHCCCHH	27.22	26356563
391	Phosphorylation	LEGQEDHYNNLSASK HCCCHHHCCCCCHHH	20.33	30278072
395	Phosphorylation	EDHYNNLSASKVL-- HHHCCCCCHHHCC--	32.40	24670416
397	Phosphorylation	HYNNLSASKVL---- HCCCCCHHHCC----	21.66	30278072
398	Ubiquitination	YNNLSASKVL----- CCCCCHHHCC-----	47.47	21906983

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
35	S	Phosphorylation	Kinase	AKT1	P31749	PSP
391	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of K1C19_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 K1C19_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HGS_HUMAN	HGS	physical	16189514
DGC6L_HUMAN	DGCR6L	physical	16189514
SFI1_HUMAN	SFI1	physical	16189514
ABI2_HUMAN	ABI2	physical	16189514
PCM1_HUMAN	PCM1	physical	16189514
DEPP_HUMAN	C10orf10	physical	16189514
EXOC8_HUMAN	EXOC8	physical	16189514
ZN638_HUMAN	ZNF638	physical	16189514
USBP1_HUMAN	USHBP1	physical	16189514
F107A_HUMAN	FAM107A	physical	16189514
KDM1A_HUMAN	KDM1A	physical	23455924
K1C19_HUMAN	KRT19	physical	25416956
UBC9_HUMAN	UBE2I	physical	25416956
IF4E2_HUMAN	EIF4E2	physical	25416956
RPAC1_HUMAN	POLR1C	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
TFPT_HUMAN	TFPT	physical	25416956
TBCD7_HUMAN	TBC1D7	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
CA109_HUMAN	C1orf109	physical	25416956
4ET_HUMAN	EIF4ENIF1	physical	25416956
CC146_HUMAN	CCDC146	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
F124B_HUMAN	FAM124B	physical	25416956
HAUS1_HUMAN	HAUS1	physical	25416956
PPR18_HUMAN	PPP1R18	physical	25416956
CE57L_HUMAN	CEP57L1	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 K1C19_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-40, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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-35 AND SER-46, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Characterization of the major physiologic phosphorylation site ofhuman keratin 19 and its role in filament organization."; Zhou X., Liao J., Hu L., Feng L., Omary M.B.; J. Biol. Chem. 274:12861-12866(1999). Cited for: PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF SER-10 AND SER-35.	10212274 [Abstract]
"Characterization of in vivo keratin 19 phosphorylation on tyrosine-391."; Zhou Q., Snider N.T., Liao J., Li D.H., Hong A., Ku N.O.,Cartwright C.A., Omary M.B.; PLoS ONE 5:E13538-E13538(2010). Cited for: PHOSPHORYLATION AT TYR-391.	21049038 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-130, AND MASSSPECTROMETRY.	18083107 [Abstract]