dbPTM

K2C8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K2C8_HUMAN
UniProt AC	P05787
Protein Name	Keratin, type II cytoskeletal 8
Gene Name	KRT8
Organism	Homo sapiens (Human).
Sequence Length	483
Subcellular Localization	Cytoplasm . Nucleus, nucleoplasm. Nucleus matrix.
Protein Description	Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle..
Protein Sequence	MSIRVTQKSYKVSTSGPRAFSSRSYTSGPGSRISSSSFSRVGSSNFRGGLGGGYGGASGMGGITAVTVNQSLLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAEIEGLKGQRASLEAAIADAEQRGELAIKDANAKLSELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLESGMQNMSIHTKTTSGYAGGLSSAYGGLTSPGLSYSLGSSFGSGAGSSSFSRTSSSRAVVVKKIETRDGKLVSESSDVLPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSIRVTQKS ------CCEEEEEEE	21.07	25394399
6	Phosphorylation	--MSIRVTQKSYKVS --CCEEEEEEEEEEE	22.04	24732914
8	Acetylation	MSIRVTQKSYKVSTS CCEEEEEEEEEEECC	46.52	70083
8	Methylation	MSIRVTQKSYKVSTS CCEEEEEEEEEEECC	46.52	70083
8	Ubiquitination	MSIRVTQKSYKVSTS CCEEEEEEEEEEECC	46.52	21906983
9	Phosphorylation	SIRVTQKSYKVSTSG CEEEEEEEEEEECCC	21.99	21955146
10	Phosphorylation	IRVTQKSYKVSTSGP EEEEEEEEEEECCCC	23.57	27273156
11	Ubiquitination	RVTQKSYKVSTSGPR EEEEEEEEEECCCCC	36.48	21890473
11	Sumoylation	RVTQKSYKVSTSGPR EEEEEEEEEECCCCC	36.48	-
11	Acetylation	RVTQKSYKVSTSGPR EEEEEEEEEECCCCC	36.48	18983182
11	Methylation	RVTQKSYKVSTSGPR EEEEEEEEEECCCCC	36.48	70071
11	Sumoylation	RVTQKSYKVSTSGPR EEEEEEEEEECCCCC	36.48	28112733
11	Ubiquitination	RVTQKSYKVSTSGPR EEEEEEEEEECCCCC	36.48	21890473
13	O-linked_Glycosylation	TQKSYKVSTSGPRAF EEEEEEEECCCCCCC	16.83	31373491
13	O-linked_Glycosylation	TQKSYKVSTSGPRAF EEEEEEEECCCCCCC	16.83	20068230
13	Phosphorylation	TQKSYKVSTSGPRAF EEEEEEEECCCCCCC	16.83	28355574
14	Phosphorylation	QKSYKVSTSGPRAFS EEEEEEECCCCCCCC	40.46	21955146
15	O-linked_Glycosylation	KSYKVSTSGPRAFSS EEEEEECCCCCCCCC	39.02	31373491
15	O-linked_Glycosylation	KSYKVSTSGPRAFSS EEEEEECCCCCCCCC	39.02	20068230
15	Phosphorylation	KSYKVSTSGPRAFSS EEEEEECCCCCCCCC	39.02	21955146
18	Dimethylation	KVSTSGPRAFSSRSY EEECCCCCCCCCCCC	52.36	-
18	Methylation	KVSTSGPRAFSSRSY EEECCCCCCCCCCCC	52.36	30762453
21	Phosphorylation	TSGPRAFSSRSYTSG CCCCCCCCCCCCCCC	24.69	27273156
22	Phosphorylation	SGPRAFSSRSYTSGP CCCCCCCCCCCCCCC	20.84	20201521
23	Methylation	GPRAFSSRSYTSGPG CCCCCCCCCCCCCCC	32.27	24129315
24	Phosphorylation	PRAFSSRSYTSGPGS CCCCCCCCCCCCCCC	34.41	20201521
25	Phosphorylation	RAFSSRSYTSGPGSR CCCCCCCCCCCCCCC	12.10	30278072
26	Phosphorylation	AFSSRSYTSGPGSRI CCCCCCCCCCCCCCC	28.58	28355574
27	Phosphorylation	FSSRSYTSGPGSRIS CCCCCCCCCCCCCCC	34.45	30278072
31	Phosphorylation	SYTSGPGSRISSSSF CCCCCCCCCCCCCCC	29.58	23927012
32	Methylation	YTSGPGSRISSSSFS CCCCCCCCCCCCCCC	38.43	24129315
34	O-linked_Glycosylation	SGPGSRISSSSFSRV CCCCCCCCCCCCCCC	24.06	30059200
34	Phosphorylation	SGPGSRISSSSFSRV CCCCCCCCCCCCCCC	24.06	28355574
35	Phosphorylation	GPGSRISSSSFSRVG CCCCCCCCCCCCCCC	27.85	23911959
36	O-linked_Glycosylation	PGSRISSSSFSRVGS CCCCCCCCCCCCCCC	28.72	30059200
36	Phosphorylation	PGSRISSSSFSRVGS CCCCCCCCCCCCCCC	28.72	30278072
37	O-linked_Glycosylation	GSRISSSSFSRVGSS CCCCCCCCCCCCCCC	29.23	30059200
37	Phosphorylation	GSRISSSSFSRVGSS CCCCCCCCCCCCCCC	29.23	28176443
39	O-linked_Glycosylation	RISSSSFSRVGSSNF CCCCCCCCCCCCCCC	28.18	30059200
39	Phosphorylation	RISSSSFSRVGSSNF CCCCCCCCCCCCCCC	28.18	28355574
40	Methylation	ISSSSFSRVGSSNFR CCCCCCCCCCCCCCC	34.50	24129315
43	Phosphorylation	SSFSRVGSSNFRGGL CCCCCCCCCCCCCCC	21.17	30183078
44	Phosphorylation	SFSRVGSSNFRGGLG CCCCCCCCCCCCCCC	33.78	30278072
47	Asymmetric dimethylarginine	RVGSSNFRGGLGGGY CCCCCCCCCCCCCCC	42.39	-
47	Methylation	RVGSSNFRGGLGGGY CCCCCCCCCCCCCCC	42.39	24129315
54	Phosphorylation	RGGLGGGYGGASGMG CCCCCCCCCCCCCCC	18.70	27251275
58	O-linked_Glycosylation	GGGYGGASGMGGITA CCCCCCCCCCCCEEE	32.36	30059200
58	Phosphorylation	GGGYGGASGMGGITA CCCCCCCCCCCCEEE	32.36	30183078
60	Sulfoxidation	GYGGASGMGGITAVT CCCCCCCCCCEEEEE	4.04	28183972
64	Phosphorylation	ASGMGGITAVTVNQS CCCCCCEEEEEECHH	20.53	30183078
67	Phosphorylation	MGGITAVTVNQSLLS CCCEEEEEECHHHHC	15.98	24732914
71	Phosphorylation	TAVTVNQSLLSPLVL EEEEECHHHHCCCEE	26.52	26657352
74	O-linked_Glycosylation	TVNQSLLSPLVLEVD EECHHHHCCCEEEEC	22.83	30059200
74	Phosphorylation	TVNQSLLSPLVLEVD EECHHHHCCCEEEEC	22.83	28355574
89	Phosphorylation	PNIQAVRTQEKEQIK CCCHHHCCCCHHHHH	34.19	-
92	Acetylation	QAVRTQEKEQIKTLN HHHCCCCHHHHHHHH	45.13	27178108
92	Ubiquitination	QAVRTQEKEQIKTLN HHHCCCCHHHHHHHH	45.13	21906983
96	Ubiquitination	TQEKEQIKTLNNKFA CCCHHHHHHHHHHHH	46.80	21890473
97	Phosphorylation	QEKEQIKTLNNKFAS CCHHHHHHHHHHHHH	36.03	28188228
101	Ubiquitination	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	21890473
101	N6-malonyllysine	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	-
101	Acetylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	70067
101	Malonylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	21908771
101	Methylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	70067
101	Sumoylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	-
101	Ubiquitination	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	21890473
104	Phosphorylation	TLNNKFASFIDKVRF HHHHHHHHHHHHHHH	26.35	28355574
108	Ubiquitination	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	21890473
108	Acetylation	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	7705633
108	Ubiquitination	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	21890473
117	Ubiquitination	RFLEQQNKMLETKWS HHHHHHHHHHHHHHH	40.29	21890473
117	Acetylation	RFLEQQNKMLETKWS HHHHHHHHHHHHHHH	40.29	23954790
117	Ubiquitination	RFLEQQNKMLETKWS HHHHHHHHHHHHHHH	40.29	21890473
122	Ubiquitination	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	21890473
122	Acetylation	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	27178108
122	Methylation	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	70075
122	Sumoylation	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	28112733
122	Ubiquitination	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	21890473
124	Phosphorylation	KMLETKWSLLQQQKT HHHHHHHHHHHHHHH	22.28	26657352
130	Ubiquitination	WSLLQQQKTARSNMD HHHHHHHHHHHHCHH	39.55	21890473
130	Sumoylation	WSLLQQQKTARSNMD HHHHHHHHHHHHCHH	39.55	-
130	Acetylation	WSLLQQQKTARSNMD HHHHHHHHHHHHCHH	39.55	22424773
130	Sumoylation	WSLLQQQKTARSNMD HHHHHHHHHHHHCHH	39.55	28112733
130	Ubiquitination	WSLLQQQKTARSNMD HHHHHHHHHHHHCHH	39.55	21890473
131	Phosphorylation	SLLQQQKTARSNMDN HHHHHHHHHHHCHHH	23.98	23909892
134	Phosphorylation	QQQKTARSNMDNMFE HHHHHHHHCHHHHHH	33.76	26657352
136	Sulfoxidation	QKTARSNMDNMFESY HHHHHHCHHHHHHHH	4.09	28183972
139	Sulfoxidation	ARSNMDNMFESYINN HHHCHHHHHHHHHHH	3.25	28183972
142	Phosphorylation	NMDNMFESYINNLRR CHHHHHHHHHHHHHH	21.76	26657352
143	Phosphorylation	MDNMFESYINNLRRQ HHHHHHHHHHHHHHH	10.64	22199227
158	Acetylation	LETLGQEKLKLEAEL HHHHCHHHHHHHHHH	42.93	27178108
158	Ubiquitination	LETLGQEKLKLEAEL HHHHCHHHHHHHHHH	42.93	21890473
160	Ubiquitination	TLGQEKLKLEAELGN HHCHHHHHHHHHHHH	56.18	21906983
176	Ubiquitination	QGLVEDFKNKYEDEI HHHHHHHHHHHHHHH	65.92	21890473
176	Ubiquitination	QGLVEDFKNKYEDEI HHHHHHHHHHHHHHH	65.92	21890473
178	Methylation	LVEDFKNKYEDEINK HHHHHHHHHHHHHHH	51.08	15606719
178	Ubiquitination	LVEDFKNKYEDEINK HHHHHHHHHHHHHHH	51.08	21890473
179	Phosphorylation	VEDFKNKYEDEINKR HHHHHHHHHHHHHHH	37.70	20736484
185	Methylation	KYEDEINKRTEMENE HHHHHHHHHHHCCCE	67.37	-
185	Ubiquitination	KYEDEINKRTEMENE HHHHHHHHHHHCCCE	67.37	-
187	Phosphorylation	EDEINKRTEMENEFV HHHHHHHHHCCCEEE	41.09	21406692
189	Sulfoxidation	EINKRTEMENEFVLI HHHHHHHCCCEEEEE	7.10	28183972
197	Acetylation	ENEFVLIKKDVDEAY CCEEEEEECCCCHHH	38.47	26051181
197	Sumoylation	ENEFVLIKKDVDEAY CCEEEEEECCCCHHH	38.47	25114211
197	Ubiquitination	ENEFVLIKKDVDEAY CCEEEEEECCCCHHH	38.47	21890473
198	Ubiquitination	NEFVLIKKDVDEAYM CEEEEEECCCCHHHH	56.86	21906983
204	Phosphorylation	KKDVDEAYMNKVELE ECCCCHHHHCHHHHH	10.12	26657352
207	Ubiquitination	VDEAYMNKVELESRL CCHHHHCHHHHHHHH	22.13	21890473
207	Acetylation	VDEAYMNKVELESRL CCHHHHCHHHHHHHH	22.13	19608861
207	Ubiquitination	VDEAYMNKVELESRL CCHHHHCHHHHHHHH	22.13	21890473
212	Phosphorylation	MNKVELESRLEGLTD HCHHHHHHHHHHHHH	55.58	22199227
218	Phosphorylation	ESRLEGLTDEINFLR HHHHHHHHHHHHHHH	42.30	28176443
228	Phosphorylation	INFLRQLYEEEIREL HHHHHHHHHHHHHHH	16.98	20068231
237	Phosphorylation	EEIRELQSQISDTSV HHHHHHHHHHCCCEE	41.95	21815630
240	Phosphorylation	RELQSQISDTSVVLS HHHHHHHCCCEEEEE	27.48	26657352
242	Phosphorylation	LQSQISDTSVVLSMD HHHHHCCCEEEEEEC	19.34	24732914
243	Phosphorylation	QSQISDTSVVLSMDN HHHHCCCEEEEEECC	18.41	21955146
247	Phosphorylation	SDTSVVLSMDNSRSL CCCEEEEEECCCCCC	16.69	26657352
248	Sulfoxidation	DTSVVLSMDNSRSLD CCEEEEEECCCCCCC	5.03	28183972
251	Phosphorylation	VVLSMDNSRSLDMDS EEEEECCCCCCCHHH	20.98	21955146
253	Phosphorylation	LSMDNSRSLDMDSII EEECCCCCCCHHHHH	28.65	30183078
256	Sulfoxidation	DNSRSLDMDSIIAEV CCCCCCCHHHHHHHH	5.44	28183972
258	Phosphorylation	SRSLDMDSIIAEVKA CCCCCHHHHHHHHHH	14.84	20201521
264	Sumoylation	DSIIAEVKAQYEDIA HHHHHHHHHHHHHHH	22.68	28112733
264	Ubiquitination	DSIIAEVKAQYEDIA HHHHHHHHHHHHHHH	22.68	21906983
267	Phosphorylation	IAEVKAQYEDIANRS HHHHHHHHHHHHHHH	22.04	27273156
274	Phosphorylation	YEDIANRSRAEAESM HHHHHHHHHHHHHHH	35.33	28355574
280	Phosphorylation	RSRAEAESMYQIKYE HHHHHHHHHHHHCHH	29.82	28355574
281	Sulfoxidation	SRAEAESMYQIKYEE HHHHHHHHHHHCHHH	1.83	28183972
282	Phosphorylation	RAEAESMYQIKYEEL HHHHHHHHHHCHHHH	19.16	27273156
285	Sumoylation	AESMYQIKYEELQSL HHHHHHHCHHHHHHH	30.96	-
285	Acetylation	AESMYQIKYEELQSL HHHHHHHCHHHHHHH	30.96	21466224
285	Methylation	AESMYQIKYEELQSL HHHHHHHCHHHHHHH	30.96	70079
285	Sumoylation	AESMYQIKYEELQSL HHHHHHHCHHHHHHH	30.96	28112733
285	Ubiquitination	AESMYQIKYEELQSL HHHHHHHCHHHHHHH	30.96	21890473
286	Phosphorylation	ESMYQIKYEELQSLA HHHHHHCHHHHHHHC	19.10	27273156
291	Phosphorylation	IKYEELQSLAGKHGD HCHHHHHHHCHHCCH	32.58	30576142
295	Ubiquitination	ELQSLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	21890473
295	Acetylation	ELQSLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	19608861
295	Sumoylation	ELQSLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	28112733
295	Ubiquitination	ELQSLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	21890473
303	Phosphorylation	HGDDLRRTKTEISEM CCHHHHHHHHHHHHH	35.56	22817900
304	Sumoylation	GDDLRRTKTEISEMN CHHHHHHHHHHHHHH	42.20	-
304	Acetylation	GDDLRRTKTEISEMN CHHHHHHHHHHHHHH	42.20	26051181
304	Sumoylation	GDDLRRTKTEISEMN CHHHHHHHHHHHHHH	42.20	28112733
304	Ubiquitination	GDDLRRTKTEISEMN CHHHHHHHHHHHHHH	42.20	21890473
305	Phosphorylation	DDLRRTKTEISEMNR HHHHHHHHHHHHHHH	37.63	22817900
308	Phosphorylation	RRTKTEISEMNRNIS HHHHHHHHHHHHHHH	25.26	21815630
315	Phosphorylation	SEMNRNISRLQAEIE HHHHHHHHHHHHHHC	30.41	28355574
325	Ubiquitination	QAEIEGLKGQRASLE HHHHCCHHHHHHHHH	64.95	21890473
325	Acetylation	QAEIEGLKGQRASLE HHHHCCHHHHHHHHH	64.95	19608861
325	Sumoylation	QAEIEGLKGQRASLE HHHHCCHHHHHHHHH	64.95	28112733
325	Ubiquitination	QAEIEGLKGQRASLE HHHHCCHHHHHHHHH	64.95	21890473
330	Phosphorylation	GLKGQRASLEAAIAD CHHHHHHHHHHHHHC	29.00	30278072
347	Acetylation	QRGELAIKDANAKLS HHCCHHHHHHHHHHH	45.22	23954790
347	Ubiquitination	QRGELAIKDANAKLS HHCCHHHHHHHHHHH	45.22	21906983
352	Ubiquitination	AIKDANAKLSELEAA HHHHHHHHHHHHHHH	52.97	21890473
352	Acetylation	AIKDANAKLSELEAA HHHHHHHHHHHHHHH	52.97	23954790
352	Ubiquitination	AIKDANAKLSELEAA HHHHHHHHHHHHHHH	52.97	21890473
354	Phosphorylation	KDANAKLSELEAALQ HHHHHHHHHHHHHHH	39.15	28857561
364	Sumoylation	EAALQRAKQDMARQL HHHHHHHHHHHHHHH	49.36	-
364	Sumoylation	EAALQRAKQDMARQL HHHHHHHHHHHHHHH	49.36	-
374	Phosphorylation	MARQLREYQELMNVK HHHHHHHHHHHHCHH	10.80	20068231
391	Phosphorylation	LDIEIATYRKLLEGE HHHHHHHHHHHHCCC	9.20	18083107
393	Sumoylation	IEIATYRKLLEGEES HHHHHHHHHHCCCHH	47.19	-
393	Acetylation	IEIATYRKLLEGEES HHHHHHHHHHCCCHH	47.19	23749302
393	Sumoylation	IEIATYRKLLEGEES HHHHHHHHHHCCCHH	47.19	28112733
393	Ubiquitination	IEIATYRKLLEGEES HHHHHHHHHHCCCHH	47.19	19608861
400	Phosphorylation	KLLEGEESRLESGMQ HHHCCCHHHHHHHCC	37.55	28355574
404	Phosphorylation	GEESRLESGMQNMSI CCHHHHHHHCCCCEE	44.12	21712546
406	Sulfoxidation	ESRLESGMQNMSIHT HHHHHHHCCCCEEEE	3.47	28183972
409	Sulfoxidation	LESGMQNMSIHTKTT HHHHCCCCEEEECCC	1.93	28183972
410	Phosphorylation	ESGMQNMSIHTKTTS HHHCCCCEEEECCCC	20.83	28355574
413	Phosphorylation	MQNMSIHTKTTSGYA CCCCEEEECCCCCCC	28.54	24732914
414	Ubiquitination	QNMSIHTKTTSGYAG CCCEEEECCCCCCCC	35.33	-
415	Phosphorylation	NMSIHTKTTSGYAGG CCEEEECCCCCCCCC	27.61	27966365
416	Phosphorylation	MSIHTKTTSGYAGGL CEEEECCCCCCCCCC	23.01	30175587
417	Phosphorylation	SIHTKTTSGYAGGLS EEEECCCCCCCCCCC	34.73	26657352
419	Phosphorylation	HTKTTSGYAGGLSSA EECCCCCCCCCCCHH	11.22	26657352
424	Phosphorylation	SGYAGGLSSAYGGLT CCCCCCCCHHCCCCC	19.05	20058876
425	Phosphorylation	GYAGGLSSAYGGLTS CCCCCCCHHCCCCCC	30.47	26657352
427	Phosphorylation	AGGLSSAYGGLTSPG CCCCCHHCCCCCCCC	17.42	21712546
431	Phosphorylation	SSAYGGLTSPGLSYS CHHCCCCCCCCCCEE	35.83	28355574
432	Phosphorylation	SAYGGLTSPGLSYSL HHCCCCCCCCCCEEC	23.24	28355574
436	Phosphorylation	GLTSPGLSYSLGSSF CCCCCCCCEECCCCC	20.70	30175587
437	Phosphorylation	LTSPGLSYSLGSSFG CCCCCCCEECCCCCC	16.98	21712546
438	Phosphorylation	TSPGLSYSLGSSFGS CCCCCCEECCCCCCC	23.91	21712546
441	Phosphorylation	GLSYSLGSSFGSGAG CCCEECCCCCCCCCC	27.99	30183078
442	Phosphorylation	LSYSLGSSFGSGAGS CCEECCCCCCCCCCC	31.65	30175587
445	Phosphorylation	SLGSSFGSGAGSSSF ECCCCCCCCCCCCCC	24.37	21712546
449	Phosphorylation	SFGSGAGSSSFSRTS CCCCCCCCCCCCCCC	23.44	22199227
450	Phosphorylation	FGSGAGSSSFSRTSS CCCCCCCCCCCCCCC	34.19	22199227
451	Phosphorylation	GSGAGSSSFSRTSSS CCCCCCCCCCCCCCC	29.01	21712546
453	Phosphorylation	GAGSSSFSRTSSSRA CCCCCCCCCCCCCCE	36.27	22199227
455	Phosphorylation	GSSSFSRTSSSRAVV CCCCCCCCCCCCEEE	31.59	24732914
456	Phosphorylation	SSSFSRTSSSRAVVV CCCCCCCCCCCEEEE	25.80	27273156
457	Phosphorylation	SSFSRTSSSRAVVVK CCCCCCCCCCEEEEE	24.19	28355574
458	Phosphorylation	SFSRTSSSRAVVVKK CCCCCCCCCEEEEEE	24.83	24732914
464	Acetylation	SSRAVVVKKIETRDG CCCEEEEEEEEECCC	36.10	22424773
465	Acetylation	SRAVVVKKIETRDGK CCEEEEEEEEECCCC	33.88	22424773
465	Ubiquitination	SRAVVVKKIETRDGK CCEEEEEEEEECCCC	33.88	-
468	Phosphorylation	VVVKKIETRDGKLVS EEEEEEEECCCCEEC	37.22	24719451
472	Sumoylation	KIETRDGKLVSESSD EEEECCCCEECCCCC	50.43	-
472	Acetylation	KIETRDGKLVSESSD EEEECCCCEECCCCC	50.43	18983182
472	Sumoylation	KIETRDGKLVSESSD EEEECCCCEECCCCC	50.43	25114211
472	Ubiquitination	KIETRDGKLVSESSD EEEECCCCEECCCCC	50.43	21890473
475	O-linked_Glycosylation	TRDGKLVSESSDVLP ECCCCEECCCCCCCC	42.04	19664994
475	O-linked_Glycosylation	TRDGKLVSESSDVLP ECCCCEECCCCCCCC	42.04	19664994
475	Phosphorylation	TRDGKLVSESSDVLP ECCCCEECCCCCCCC	42.04	19664994
477	Phosphorylation	DGKLVSESSDVLPK- CCCEECCCCCCCCC-	25.08	28355574
478	Phosphorylation	GKLVSESSDVLPK-- CCEECCCCCCCCC--	27.90	28355574
483	Acetylation	ESSDVLPK------- CCCCCCCC-------	69.66	18983182
483	Ubiquitination	ESSDVLPK------- CCCCCCCC-------	69.66	-

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
6	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
9	S	Phosphorylation	Kinase	PRKCE	Q02156	Uniprot
24	S	Phosphorylation	Kinase	PRKCE	Q02156	Uniprot
74	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
74	S	Phosphorylation	Kinase	MAPK	-	Uniprot
74	S	Phosphorylation	Kinase	MAP2K2	P36507	GPS
74	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
74	S	Phosphorylation	Kinase	MAP2K1	Q02750	GPS
74	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
432	S	Phosphorylation	Kinase	MAPK	-	Uniprot
432	S	Phosphorylation	Kinase	AKT1	P31749	PSP
432	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
432	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
432	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
432	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
432	S	Phosphorylation	Kinase	ERK2	P28482	PSP
432	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
74	S	Phosphorylation		11781324
Ser-74 phosphorylation plays an important role in keratin filament reorganization.

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 K2C8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS74L_HUMAN	HSPA4L	physical	17353931
CLN5_HUMAN	CLN5	physical	17353931
TPA_HUMAN	PLAT	physical	9988531
KPCE_HUMAN	PRKCE	physical	1374067
ZN363_HUMAN	RCHY1	physical	19282868
STAM2_HUMAN	STAM2	physical	22939629
K1C13_HUMAN	KRT13	physical	25416956
K1C15_HUMAN	KRT15	physical	25416956
K1H1_HUMAN	KRT31	physical	25416956
KRT38_HUMAN	KRT38	physical	25416956
TFP11_HUMAN	TFIP11	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
CAV1_HUMAN	CAV1	physical	20808760

Drug and Disease Associations

Kegg Disease
OMIM Disease
215600	Cirrhosis (CIRRH)
Kegg Drug
DrugBank
DB00031	Tenecteplase

Regulatory Network of K2C8_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-117; LYS-207; LYS-295;LYS-325 AND LYS-347, AND MASS SPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-101.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-101.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-43; SER-253;SER-432 AND SER-475, AND MASS SPECTROMETRY.	19369195 [Abstract]
"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-21; SER-24; SER-27;SER-34; SER-36; SER-37; SER-43; SER-251; SER-253; SER-258; SER-274;SER-330; SER-400; SER-410; SER-432; SER-475 AND SER-478, AND MASSSPECTROMETRY.	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-37; SER-43; SER-74;SER-253; SER-258 AND SER-274, 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-13; THR-14; SER-21;SER-22; SER-24; THR-26; SER-34; SER-36; SER-37; SER-39; SER-43;SER-74; SER-243; SER-258; SER-330; SER-400; SER-410; SER-438; SER-441;SER-442; SER-456; SER-475 AND SER-478, 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-24 AND THR-26, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND MASSSPECTROMETRY.	16565220 [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-27, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-330, ANDMASS SPECTROMETRY.	17081983 [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-21; SER-22; SER-24;SER-37 AND SER-43, AND MASS SPECTROMETRY.	16083285 [Abstract]
"Keratin 8 phosphorylation by p38 kinase regulates cellular keratinfilament reorganization: modulation by a keratin 1-like diseasecausing mutation."; Ku N.O., Azhar S., Omary M.B.; J. Biol. Chem. 277:10775-10782(2002). Cited for: PHOSPHORYLATION AT SER-74, AND MUTAGENESIS OF LEU-72 AND SER-74.	11788583 [Abstract]
"The intermediate filament protein keratin 8 is a novel cytoplasmicsubstrate for c-Jun N-terminal kinase."; He T., Stepulak A., Holmstrom T.H., Omary M.B., Eriksson J.E.; J. Biol. Chem. 277:10767-10774(2002). Cited for: PHOSPHORYLATION AT SER-74.	11781324 [Abstract]
"PKC epsilon-related kinase associates with and phosphorylatescytokeratin 8 and 18."; Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y.,Strulovici B.; J. Cell Biol. 117:583-593(1992). Cited for: PHOSPHORYLATION AT SER-9 AND SER-24.	1374067 [Abstract]
"Phosphorylation of human keratin 8 in vivo at conserved head domainserine 23 and at epidermal growth factor-stimulated tail domain serine431."; Ku N.-O., Omary M.B.; J. Biol. Chem. 272:7556-7564(1997). Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-24 AND SER-432.	9054461 [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-204 AND TYR-267, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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