dbPTM

K1C18_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K1C18_HUMAN
UniProt AC	P05783
Protein Name	Keratin, type I cytoskeletal 18
Gene Name	KRT18
Organism	Homo sapiens (Human).
Sequence Length	430
Subcellular Localization	Cytoplasm, perinuclear region. Nucleus, nucleolus.
Protein Description	Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection..
Protein Sequence	MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSNSMQTIQKTTTRRIVDGKVVSETNDTKVLRH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSFTTRSTF ------CCCCCCCCC	31.16	32155916
2	Phosphorylation	------MSFTTRSTF ------CCCCCCCCC	31.16	27696853
4	Phosphorylation	----MSFTTRSTFST ----CCCCCCCCCCC	17.62	25849741
5	Phosphorylation	---MSFTTRSTFSTN ---CCCCCCCCCCCC	22.17	22199227
7	O-linked_Glycosylation	-MSFTTRSTFSTNYR -CCCCCCCCCCCCCC	31.54	32574038
7	Phosphorylation	-MSFTTRSTFSTNYR -CCCCCCCCCCCCCC	31.54	22167270
8	Phosphorylation	MSFTTRSTFSTNYRS CCCCCCCCCCCCCCC	20.51	22167270
10	O-linked_Glycosylation	FTTRSTFSTNYRSLG CCCCCCCCCCCCCCC	18.81	32574038
10	Phosphorylation	FTTRSTFSTNYRSLG CCCCCCCCCCCCCCC	18.81	22167270
11	Phosphorylation	TTRSTFSTNYRSLGS CCCCCCCCCCCCCCC	31.88	21945579
13	Phosphorylation	RSTFSTNYRSLGSVQ CCCCCCCCCCCCCEE	11.15	21945579
15	O-linked_Glycosylation	TFSTNYRSLGSVQAP CCCCCCCCCCCEECC	27.07	32574038
15	Phosphorylation	TFSTNYRSLGSVQAP CCCCCCCCCCCEECC	27.07	22167270
18	O-linked_Glycosylation	TNYRSLGSVQAPSYG CCCCCCCCEECCCCC	19.15	32574038
18	Phosphorylation	TNYRSLGSVQAPSYG CCCCCCCCEECCCCC	19.15	19664994
23	O-linked_Glycosylation	LGSVQAPSYGARPVS CCCEECCCCCCCCCC	38.93	32574038
23	Phosphorylation	LGSVQAPSYGARPVS CCCEECCCCCCCCCC	38.93	21945579
24	Phosphorylation	GSVQAPSYGARPVSS CCEECCCCCCCCCCC	17.47	21945579
27	Methylation	QAPSYGARPVSSAAS ECCCCCCCCCCCCCE	27.99	16188883
30	O-linked_Glycosylation	SYGARPVSSAASVYA CCCCCCCCCCCEEEC	19.55	32574038
30	O-linked_Glycosylation	SYGARPVSSAASVYA CCCCCCCCCCCEEEC	19.55	20729549
30	Phosphorylation	SYGARPVSSAASVYA CCCCCCCCCCCEEEC	19.55	25159151
31	O-linked_Glycosylation	YGARPVSSAASVYAG CCCCCCCCCCEEECC	28.26	32574038
31	O-linked_Glycosylation	YGARPVSSAASVYAG CCCCCCCCCCEEECC	28.26	18669648
31	Phosphorylation	YGARPVSSAASVYAG CCCCCCCCCCEEECC	28.26	23927012
34	O-linked_Glycosylation	RPVSSAASVYAGAGG CCCCCCCEEECCCCC	18.51	32574038
34	Phosphorylation	RPVSSAASVYAGAGG CCCCCCCEEECCCCC	18.51	20201521
36	Phosphorylation	VSSAASVYAGAGGSG CCCCCEEECCCCCCC	9.23	21945579
42	O-linked_Glycosylation	VYAGAGGSGSRISVS EECCCCCCCCCEEEC	32.45	32574038
42	Phosphorylation	VYAGAGGSGSRISVS EECCCCCCCCCEEEC	32.45	22167270
44	Phosphorylation	AGAGGSGSRISVSRS CCCCCCCCCEEECCC	28.30	21945579
45	Dimethylation	GAGGSGSRISVSRST CCCCCCCCEEECCCC	28.82	-
45	Methylation	GAGGSGSRISVSRST CCCCCCCCEEECCCC	28.82	24129315
47	O-linked_Glycosylation	GGSGSRISVSRSTSF CCCCCCEEECCCCCC	16.96	32574038
47	Phosphorylation	GGSGSRISVSRSTSF CCCCCCEEECCCCCC	16.96	27696853
49	O-linked_Glycosylation	SGSRISVSRSTSFRG CCCCEEECCCCCCCC	17.45	32574038
49	O-linked_Glycosylation	SGSRISVSRSTSFRG CCCCEEECCCCCCCC	17.45	32645325
49	Phosphorylation	SGSRISVSRSTSFRG CCCCEEECCCCCCCC	17.45	27696853
50	Methylation	GSRISVSRSTSFRGG CCCEEECCCCCCCCC	41.62	30760147
51	Phosphorylation	SRISVSRSTSFRGGM CCEEECCCCCCCCCC	22.39	20201521
52	Phosphorylation	RISVSRSTSFRGGMG CEEECCCCCCCCCCC	30.67	20201521
53	Phosphorylation	ISVSRSTSFRGGMGS EEECCCCCCCCCCCC	17.75	20201521
55	Dimethylation	VSRSTSFRGGMGSGG ECCCCCCCCCCCCCH	40.29	-
55	Methylation	VSRSTSFRGGMGSGG ECCCCCCCCCCCCCH	40.29	24129315
58	Sulfoxidation	STSFRGGMGSGGLAT CCCCCCCCCCCHHHH	4.26	28183972
60	Phosphorylation	SFRGGMGSGGLATGI CCCCCCCCCHHHHHH	22.31	22167270
65	Phosphorylation	MGSGGLATGIAGGLA CCCCHHHHHHHHHHH	33.88	22167270
74	Sulfoxidation	IAGGLAGMGGIQNEK HHHHHHCCCCCCCHH	3.55	28183972
81	2-Hydroxyisobutyrylation	MGGIQNEKETMQSLN CCCCCCHHHHHHHHH	67.06	-
81	Acetylation	MGGIQNEKETMQSLN CCCCCCHHHHHHHHH	67.06	88109
81	Sumoylation	MGGIQNEKETMQSLN CCCCCCHHHHHHHHH	67.06	28112733
81	Ubiquitination	MGGIQNEKETMQSLN CCCCCCHHHHHHHHH	67.06	21890473
83	Phosphorylation	GIQNEKETMQSLNDR CCCCHHHHHHHHHHH	31.42	24732914
84	Sulfoxidation	IQNEKETMQSLNDRL CCCHHHHHHHHHHHH	2.39	28183972
86	Phosphorylation	NEKETMQSLNDRLAS CHHHHHHHHHHHHHH	20.51	28176443
90	Methylation	TMQSLNDRLASYLDR HHHHHHHHHHHHHHH	30.95	115480773
93	Phosphorylation	SLNDRLASYLDRVRS HHHHHHHHHHHHHHH	30.71	30266825
94	Phosphorylation	LNDRLASYLDRVRSL HHHHHHHHHHHHHHH	13.65	30266825
97	Methylation	RLASYLDRVRSLETE HHHHHHHHHHHHHHH	24.13	54390289
100	Phosphorylation	SYLDRVRSLETENRR HHHHHHHHHHHHHHH	27.92	28355574
103	Phosphorylation	DRVRSLETENRRLES HHHHHHHHHHHHHHH	43.80	23403867
110	Phosphorylation	TENRRLESKIREHLE HHHHHHHHHHHHHHH	37.66	28857561
111	Acetylation	ENRRLESKIREHLEK HHHHHHHHHHHHHHH	36.09	19608861
118	Methylation	KIREHLEKKGPQVRD HHHHHHHHHCCCCCC	70.19	72626689
118	Ubiquitination	KIREHLEKKGPQVRD HHHHHHHHHCCCCCC	70.19	-
127	Phosphorylation	GPQVRDWSHYFKIIE CCCCCCHHHHHHHHH	16.76	28355574
129	Phosphorylation	QVRDWSHYFKIIEDL CCCCHHHHHHHHHHH	10.89	28152594
131	Acetylation	RDWSHYFKIIEDLRA CCHHHHHHHHHHHHH	35.29	19608861
131	Methylation	RDWSHYFKIIEDLRA CCHHHHHHHHHHHHH	35.29	19608861
131	Ubiquitination	RDWSHYFKIIEDLRA CCHHHHHHHHHHHHH	35.29	21906983
167	Sumoylation	AADDFRVKYETELAM CCCCCHHHHHHHHHH	32.87	-
167	2-Hydroxyisobutyrylation	AADDFRVKYETELAM CCCCCHHHHHHHHHH	32.87	-
167	Acetylation	AADDFRVKYETELAM CCCCCHHHHHHHHHH	32.87	19608861
167	Methylation	AADDFRVKYETELAM CCCCCHHHHHHHHHH	32.87	22640197
167	Sumoylation	AADDFRVKYETELAM CCCCCHHHHHHHHHH	32.87	19608861
167	Ubiquitination	AADDFRVKYETELAM CCCCCHHHHHHHHHH	32.87	21906983
168	Phosphorylation	ADDFRVKYETELAMR CCCCHHHHHHHHHHH	25.81	28152594
170	Phosphorylation	DFRVKYETELAMRQS CCHHHHHHHHHHHHH	32.96	28152594
177	Phosphorylation	TELAMRQSVENDIHG HHHHHHHHHHHCHHH	22.49	30266825
187	Sumoylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	-
187	2-Hydroxyisobutyrylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	-
187	Acetylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	23954790
187	Malonylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	26320211
187	Methylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	3967011
187	Succinylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	23954790
187	Sumoylation	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	-
187	Ubiquitination	NDIHGLRKVIDDTNI HCHHHHHHHHCCCCC	48.89	-
192	Phosphorylation	LRKVIDDTNITRLQL HHHHHCCCCCCEEEH	25.44	20860994
195	Phosphorylation	VIDDTNITRLQLETE HHCCCCCCEEEHHHH	27.65	21815630
201	Phosphorylation	ITRLQLETEIEALKE CCEEEHHHHHHHHHH	51.35	-
207	Sumoylation	ETEIEALKEELLFMK HHHHHHHHHHHHHHH	57.07	-
207	Sumoylation	ETEIEALKEELLFMK HHHHHHHHHHHHHHH	57.07	-
207	Ubiquitination	ETEIEALKEELLFMK HHHHHHHHHHHHHHH	57.07	-
214	2-Hydroxyisobutyrylation	KEELLFMKKNHEEEV HHHHHHHHHCCHHHH	42.99	-
214	Acetylation	KEELLFMKKNHEEEV HHHHHHHHHCCHHHH	42.99	19608861
214	Ubiquitination	KEELLFMKKNHEEEV HHHHHHHHHCCHHHH	42.99	21890473
215	Ubiquitination	EELLFMKKNHEEEVK HHHHHHHHCCHHHHH	52.31	-
222	2-Hydroxyisobutyrylation	KNHEEEVKGLQAQIA HCCHHHHHHHHHHHH	58.12	-
222	Acetylation	KNHEEEVKGLQAQIA HCCHHHHHHHHHHHH	58.12	23954790
230	Phosphorylation	GLQAQIASSGLTVEV HHHHHHHHCCCEEEE	26.94	24275569
241	Ubiquitination	TVEVDAPKSQDLAKI EEEEECCCCHHHHHH	63.57	21890473
242	Phosphorylation	VEVDAPKSQDLAKIM EEEECCCCHHHHHHH	28.06	24719451
247	Sumoylation	PKSQDLAKIMADIRA CCCHHHHHHHHHHHH	40.07	-
247	2-Hydroxyisobutyrylation	PKSQDLAKIMADIRA CCCHHHHHHHHHHHH	40.07	-
247	Acetylation	PKSQDLAKIMADIRA CCCHHHHHHHHHHHH	40.07	23954790
247	Sumoylation	PKSQDLAKIMADIRA CCCHHHHHHHHHHHH	40.07	28112733
247	Ubiquitination	PKSQDLAKIMADIRA CCCHHHHHHHHHHHH	40.07	21890473
256	Phosphorylation	MADIRAQYDELARKN HHHHHHHHHHHHHHC	15.48	28152594
262	Ubiquitination	QYDELARKNREELDK HHHHHHHHCHHHHHH	55.54	-
269	Sumoylation	KNREELDKYWSQQIE HCHHHHHHHHHHHHH	62.33	-
270	Phosphorylation	NREELDKYWSQQIEE CHHHHHHHHHHHHHH	15.23	24043423
272	Phosphorylation	EELDKYWSQQIEEST HHHHHHHHHHHHHCC	14.76	28348404
278	Phosphorylation	WSQQIEESTTVVTTQ HHHHHHHCCEEEEEC	19.31	26657352
279	Phosphorylation	SQQIEESTTVVTTQS HHHHHHCCEEEEECC	27.22	24043423
280	Phosphorylation	QQIEESTTVVTTQSA HHHHHCCEEEEECCC	23.43	24043423
283	Phosphorylation	EESTTVVTTQSAEVG HHCCEEEEECCCCCC	18.12	24043423
284	Phosphorylation	ESTTVVTTQSAEVGA HCCEEEEECCCCCCC	14.66	26657352
286	Phosphorylation	TTVVTTQSAEVGAAE CEEEEECCCCCCCCH	25.06	24275569
294	Phosphorylation	AEVGAAETTLTELRR CCCCCCHHHHHHHHH	23.52	24043423
295	Phosphorylation	EVGAAETTLTELRRT CCCCCHHHHHHHHHH	24.16	24043423
297	Phosphorylation	GAAETTLTELRRTVQ CCCHHHHHHHHHHHH	30.77	24043423
302	Phosphorylation	TLTELRRTVQSLEID HHHHHHHHHHHHCCC	19.23	30278072
305	Phosphorylation	ELRRTVQSLEIDLDS HHHHHHHHHCCCHHH	24.51	28355574
312	Phosphorylation	SLEIDLDSMRNLKAS HHCCCHHHHHHHHHH	27.26	23403867
313	Sulfoxidation	LEIDLDSMRNLKASL HCCCHHHHHHHHHHH	3.08	28183972
317	2-Hydroxyisobutyrylation	LDSMRNLKASLENSL HHHHHHHHHHHHHHH	39.21	-
317	Acetylation	LDSMRNLKASLENSL HHHHHHHHHHHHHHH	39.21	23954790
317	Sumoylation	LDSMRNLKASLENSL HHHHHHHHHHHHHHH	39.21	-
317	Ubiquitination	LDSMRNLKASLENSL HHHHHHHHHHHHHHH	39.21	21906983
319	Phosphorylation	SMRNLKASLENSLRE HHHHHHHHHHHHHHH	34.33	26055452
323	Phosphorylation	LKASLENSLREVEAR HHHHHHHHHHHHHHH	21.30	30266825
331	Phosphorylation	LREVEARYALQMEQL HHHHHHHHHHHHHHH	20.79	22817900
335	Sulfoxidation	EARYALQMEQLNGIL HHHHHHHHHHHHCHH	3.54	28183972
347	Phosphorylation	GILLHLESELAQTRA CHHHHHHHHHHHHHH	44.25	25849741
363	Phosphorylation	GQRQAQEYEALLNIK HHHHHHHHHHHHCCC	8.40	28152594
370	2-Hydroxyisobutyrylation	YEALLNIKVKLEAEI HHHHHCCCHHHHHHH	32.04	-
370	Sumoylation	YEALLNIKVKLEAEI HHHHHCCCHHHHHHH	32.04	28112733
370	Ubiquitination	YEALLNIKVKLEAEI HHHHHCCCHHHHHHH	32.04	-
372	Sumoylation	ALLNIKVKLEAEIAT HHHCCCHHHHHHHHH	35.29	-
372	Sumoylation	ALLNIKVKLEAEIAT HHHCCCHHHHHHHHH	35.29	28112733
372	Ubiquitination	ALLNIKVKLEAEIAT HHHCCCHHHHHHHHH	35.29	-
379	Phosphorylation	KLEAEIATYRRLLED HHHHHHHHHHHHHHC	24.19	28152594
380	Phosphorylation	LEAEIATYRRLLEDG HHHHHHHHHHHHHCC	5.68	28152594
398	Phosphorylation	NLGDALDSSNSMQTI CHHHHCCCCCCCCHH	32.06	20201521
399	Phosphorylation	LGDALDSSNSMQTIQ HHHHCCCCCCCCHHH	32.37	25159151
401	Phosphorylation	DALDSSNSMQTIQKT HHCCCCCCCCHHHHC	17.76	25159151
402	Sulfoxidation	ALDSSNSMQTIQKTT HCCCCCCCCHHHHCC	4.82	28183972
404	Phosphorylation	DSSNSMQTIQKTTTR CCCCCCCHHHHCCCC	19.41	30278072
407	2-Hydroxyisobutyrylation	NSMQTIQKTTTRRIV CCCCHHHHCCCCEEE	43.94	-
407	Ubiquitination	NSMQTIQKTTTRRIV CCCCHHHHCCCCEEE	43.94	21890473
408	Phosphorylation	SMQTIQKTTTRRIVD CCCHHHHCCCCEEEC	19.61	22798277
409	Phosphorylation	MQTIQKTTTRRIVDG CCHHHHCCCCEEECC	25.91	24719451
417	Sumoylation	TRRIVDGKVVSETND CCEEECCEEEEECCC	34.69	-
417	2-Hydroxyisobutyrylation	TRRIVDGKVVSETND CCEEECCEEEEECCC	34.69	-
417	Acetylation	TRRIVDGKVVSETND CCEEECCEEEEECCC	34.69	27452117
417	Succinylation	TRRIVDGKVVSETND CCEEECCEEEEECCC	34.69	23954790
417	Sumoylation	TRRIVDGKVVSETND CCEEECCEEEEECCC	34.69	28112733
417	Ubiquitination	TRRIVDGKVVSETND CCEEECCEEEEECCC	34.69	-
420	O-linked_Glycosylation	IVDGKVVSETNDTKV EECCEEEEECCCCCC	41.51	32574038
420	Phosphorylation	IVDGKVVSETNDTKV EECCEEEEECCCCCC	41.51	28355574
422	Phosphorylation	DGKVVSETNDTKVLR CCEEEEECCCCCCCC	30.78	22617229
425	Phosphorylation	VVSETNDTKVLRH-- EEEECCCCCCCCC--	25.73	27794612
426	2-Hydroxyisobutyrylation	VSETNDTKVLRH--- EEECCCCCCCCC---	41.98	-
426	Acetylation	VSETNDTKVLRH--- EEECCCCCCCCC---	41.98	19608861
426	Methylation	VSETNDTKVLRH--- EEECCCCCCCCC---	41.98	22640181
426	Succinylation	VSETNDTKVLRH--- EEECCCCCCCCC---	41.98	23954790
426	Sumoylation	VSETNDTKVLRH--- EEECCCCCCCCC---	41.98	19608861
426	Ubiquitination	VSETNDTKVLRH--- EEECCCCCCCCC---	41.98	19608861

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
34	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
51	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
51	S	Phosphorylation	Kinase	MAPKAPK3	Q16644	Uniprot
53	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
53	S	Phosphorylation	Kinase	AURKA	O14965	Uniprot
53	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
53	S	Phosphorylation	Kinase	CAMK	-	Uniprot
53	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
53	S	Phosphorylation	Kinase	CAMK-FAMILY	-	GPS
53	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
53	S	Phosphorylation	Kinase	CAMK1-FAMILY	-	GPS
53	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
53	S	Phosphorylation	Kinase	RPS6KB2	Q9UBS0	GPS
53	S	Phosphorylation	Kinase	PKCE	P09216	PSP
53	S	Phosphorylation	Kinase	KPCE	Q02156	PhosphoELM
53	S	Phosphorylation	Kinase	CAMK1	Q63450	GPS
53	S	Phosphorylation	Kinase	KCC1A	Q14012	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
34	S	Phosphorylation	7523419
Phosphorylation at Ser-34 increases during mitosis.
53	S	Phosphorylation	7523419
Hyperphosphorylated at Ser-53 in diseased cirrhosis liver.

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 K1C18_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBL_HUMAN	CBL	physical	9367879
DNJB6_HUMAN	DNAJB6	physical	10954706
GCP4_HUMAN	TUBGCP4	physical	16189514
LDOC1_HUMAN	LDOC1	physical	16189514
EXOC8_HUMAN	EXOC8	physical	16189514
CC85B_HUMAN	CCDC85B	physical	16189514
HGS_HUMAN	HGS	physical	16189514
NDK7_HUMAN	NME7	physical	16189514
1433T_HUMAN	YWHAQ	physical	9524113
DEDD_HUMAN	DEDD	physical	12235123
KPCE_HUMAN	PRKCE	physical	1374067
TRADD_HUMAN	TRADD	physical	11684708
K2C72_HUMAN	KRT72	physical	9630597
K2C8_HUMAN	KRT8	physical	9630597
ZN363_HUMAN	RCHY1	physical	19282868
THIOM_HUMAN	TXN2	physical	21988832
MYOME_HUMAN	PDE4DIP	physical	21988832
K2C8_HUMAN	KRT8	physical	21988832
ORC5_HUMAN	ORC5	physical	21988832
SMRD1_HUMAN	SMARCD1	physical	21988832
POTE1_HUMAN	POT1	physical	21988832
TXD11_HUMAN	TXNDC11	physical	21988832
PIAS4_HUMAN	PIAS4	physical	21988832
YTDC1_HUMAN	YTHDC1	physical	21988832
CN166_HUMAN	C14orf166	physical	22863883
RTCB_HUMAN	RTCB	physical	22863883
CNOT1_HUMAN	CNOT1	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
RFC2_HUMAN	RFC2	physical	22863883
RL14_HUMAN	RPL14	physical	22863883
SC16A_HUMAN	SEC16A	physical	22863883
K1C18_HUMAN	KRT18	physical	25416956
CC146_HUMAN	CCDC146	physical	25416956
HAUS1_HUMAN	HAUS1	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
215600	Cirrhosis (CIRRH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of K1C18_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-111; LYS-131; LYS-167 ANDLYS-426, AND MASS SPECTROMETRY.	19608861 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Identification and mutational analysis of the glycosylation sites ofhuman keratin 18."; Ku N.-O., Omary M.B.; J. Biol. Chem. 270:11820-11827(1995). Cited for: GLYCOSYLATION AT SER-30; SER-31 AND SER-49, AND MUTAGENESIS OF SER-30;SER-31 AND SER-49.	7538124 [Abstract]
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-10; SER-34; SER-42;SER-53; SER-60; THR-302 AND SER-399, 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-42; SER-60 AND SER-399,AND MASS SPECTROMETRY.	18691976 [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-7; SER-10; SER-15;SER-18; SER-23; SER-31; SER-34; TYR-36; SER-42; SER-44; SER-47;SER-53; SER-100; THR-404 AND SER-420, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-18; SER-53 ANDSER-60, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Rescue of DeltaF508-CFTR (cystic fibrosis transmembrane conductanceregulator) by curcumin: involvement of the keratin 18 network."; Lipecka J., Norez C., Bensalem N., Baudouin-Legros M., Planelles G.,Becq F., Edelman A., Davezac N.; J. Pharmacol. Exp. Ther. 317:500-505(2006). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-53.	16424149 [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-7 AND SER-34, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Keratin 8 and 18 hyperphosphorylation is a marker of progression ofhuman liver disease."; Toivola D.M., Ku N.O., Resurreccion E.Z., Nelson D.R., Wright T.L.,Omary M.B.; Hepatology 40:459-466(2004). Cited for: PHOSPHORYLATION AT SER-34 AND SER-53.	15368451 [Abstract]
"Phosphorylation of human keratin 18 serine 33 regulates binding to14-3-3 proteins."; Ku N.O., Liao J., Omary M.B.; EMBO J. 17:1892-1906(1998). Cited for: FUNCTION, INTERACTION WITH YWHAE AND YWHAZ, PHOSPHORYLATION AT SER-34,AND MUTAGENESIS OF SER-34 AND SER-53.	9524113 [Abstract]
"Identification of the major physiologic phosphorylation site of humankeratin 18: potential kinases and a role in filament reorganization."; Ku N.O., Omary M.B.; J. Cell Biol. 127:161-171(1994). Cited for: FUNCTION, PHOSPHORYLATION AT SER-53, AND MUTAGENESIS OF SER-2; SER-7;SER-10; SER-15; SER-18; SER-23; SER-30; SER-31; SER-34; SER-42;SER-44; SER-47; SER-49; SER-51 AND SER-53.	7523419 [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-13, AND MASSSPECTROMETRY.	18083107 [Abstract]

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