dbPTM

K2C8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	K2C8_MOUSE
UniProt AC	P11679
Protein Name	Keratin, type II cytoskeletal 8
Gene Name	Krt8
Organism	Mus musculus (Mouse).
Sequence Length	490
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	MSIRVTQKSYKMSTSGPRAFSSRSFTSGPGARISSSSFSRVGSSSSSFRGSMGTGVGLGGFGGAGVGGITAVTVNQSLLSPLKLEVDPNIQAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLREYQELMNVKLALDIEITTYRKLLEGEESRLESGMQNMSIHTKTTSGYSGGLSSSYGGLTSPGFSYGMSSFQPGFGSAGGSNTFSRTTKAVVVKKIETRDGKLVSESSDVVSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSIRVTQKS ------CCCEEEECE	21.07	23375375
8	Malonylation	MSIRVTQKSYKMSTS CCCEEEECEEECCCC	46.52	26320211
9	Phosphorylation	SIRVTQKSYKMSTSG CCEEEECEEECCCCC	21.84	22817900
11	Malonylation	RVTQKSYKMSTSGPR EEEECEEECCCCCCC	33.20	26320211
11	Ubiquitination	RVTQKSYKMSTSGPR EEEECEEECCCCCCC	33.20	27667366
13	Phosphorylation	TQKSYKMSTSGPRAF EECEEECCCCCCCCC	18.44	22817900
14	Phosphorylation	QKSYKMSTSGPRAFS ECEEECCCCCCCCCC	33.92	22817900
15	Phosphorylation	KSYKMSTSGPRAFSS CEEECCCCCCCCCCC	39.22	22817900
18	Methylation	KMSTSGPRAFSSRSF ECCCCCCCCCCCCCC	52.36	30762455
21	Phosphorylation	TSGPRAFSSRSFTSG CCCCCCCCCCCCCCC	24.69	25521595
22	Phosphorylation	SGPRAFSSRSFTSGP CCCCCCCCCCCCCCC	26.03	27087446
23	Methylation	GPRAFSSRSFTSGPG CCCCCCCCCCCCCCC	34.29	-
24	Phosphorylation	PRAFSSRSFTSGPGA CCCCCCCCCCCCCCC	34.52	25521595
26	Phosphorylation	AFSSRSFTSGPGARI CCCCCCCCCCCCCEE	33.74	25521595
27	Phosphorylation	FSSRSFTSGPGARIS CCCCCCCCCCCCEEC	40.77	26239621
32	Methylation	FTSGPGARISSSSFS CCCCCCCEECCCCCC	34.93	-
34	Phosphorylation	SGPGARISSSSFSRV CCCCCEECCCCCCCC	20.72	26239621
35	Phosphorylation	GPGARISSSSFSRVG CCCCEECCCCCCCCC	27.85	26239621
36	Phosphorylation	PGARISSSSFSRVGS CCCEECCCCCCCCCC	28.72	26239621
37	Phosphorylation	GARISSSSFSRVGSS CCEECCCCCCCCCCC	29.23	27087446
39	Phosphorylation	RISSSSFSRVGSSSS EECCCCCCCCCCCCC	28.18	26239621
40	Methylation	ISSSSFSRVGSSSSS ECCCCCCCCCCCCCC	34.50	-
43	Phosphorylation	SSFSRVGSSSSSFRG CCCCCCCCCCCCCCC	24.96	27087446
44	Phosphorylation	SFSRVGSSSSSFRGS CCCCCCCCCCCCCCC	28.45	27087446
45	Phosphorylation	FSRVGSSSSSFRGSM CCCCCCCCCCCCCCC	31.53	26239621
46	Phosphorylation	SRVGSSSSSFRGSMG CCCCCCCCCCCCCCC	35.13	27087446
47	Phosphorylation	RVGSSSSSFRGSMGT CCCCCCCCCCCCCCC	22.40	27087446
49	Asymmetric dimethylarginine	GSSSSSFRGSMGTGV CCCCCCCCCCCCCCC	37.92	-
49	Methylation	GSSSSSFRGSMGTGV CCCCCCCCCCCCCCC	37.92	-
51	Phosphorylation	SSSSFRGSMGTGVGL CCCCCCCCCCCCCCC	15.13	23984901
54	Phosphorylation	SFRGSMGTGVGLGGF CCCCCCCCCCCCCCC	21.76	26239621
70	Phosphorylation	GAGVGGITAVTVNQS CCCCCCEEEEEECHH	20.53	23984901
73	Phosphorylation	VGGITAVTVNQSLLS CCCEEEEEECHHHHC	15.98	23984901
77	Phosphorylation	TAVTVNQSLLSPLKL EEEEECHHHHCCCCC	26.52	26239621
80	Phosphorylation	TVNQSLLSPLKLEVD EECHHHHCCCCCEEC	33.22	16563375
83	Ubiquitination	QSLLSPLKLEVDPNI HHHHCCCCCEECCCH	46.08	-
98	Acetylation	QAVRTQEKEQIKSLN HHHHHHCHHHHHHHH	45.13	7718903
102	Malonylation	TQEKEQIKSLNNKFA HHCHHHHHHHHHHHH	48.89	26320211
102	Ubiquitination	TQEKEQIKSLNNKFA HHCHHHHHHHHHHHH	48.89	27667366
107	N6-malonyllysine	QIKSLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	-
107	Acetylation	QIKSLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	23864654
107	Malonylation	QIKSLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	26320211
107	Ubiquitination	QIKSLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	-
110	Phosphorylation	SLNNKFASFIDKVRF HHHHHHHHHHHHHHH	26.35	29472430
114	Acetylation	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	-
114	Ubiquitination	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	22790023
123	Glutarylation	RFLEQQNKMLETKWS HHHHHHHHHHHHHHH	40.29	24703693
123	Malonylation	RFLEQQNKMLETKWS HHHHHHHHHHHHHHH	40.29	26320211
123	Ubiquitination	RFLEQQNKMLETKWS HHHHHHHHHHHHHHH	40.29	-
128	Acetylation	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	23864654
128	Malonylation	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	26320211
128	Ubiquitination	QNKMLETKWSLLQQQ HHHHHHHHHHHHHHH	25.96	27667366
130	Phosphorylation	KMLETKWSLLQQQKT HHHHHHHHHHHHHHH	22.28	-
136	Glutarylation	WSLLQQQKTSRSNMD HHHHHHHHHCCCCHH	44.10	24703693
136	Malonylation	WSLLQQQKTSRSNMD HHHHHHHHHCCCCHH	44.10	26320211
136	Ubiquitination	WSLLQQQKTSRSNMD HHHHHHHHHCCCCHH	44.10	27667366
140	Phosphorylation	QQQKTSRSNMDNMFE HHHHHCCCCHHHHHH	35.95	23984901
148	Phosphorylation	NMDNMFESYINNLRR CHHHHHHHHHHHHHH	21.76	19060867
149	Phosphorylation	MDNMFESYINNLRRQ HHHHHHHHHHHHHHH	10.64	23984901
164	Acetylation	LEALGQEKLKLEAEL HHHHCHHHHHHHHHH	42.93	23864654
164	Ubiquitination	LEALGQEKLKLEAEL HHHHCHHHHHHHHHH	42.93	22790023
184	Acetylation	LVEDFKNKYEDEINK HHHHHHHHHHHHHHH	51.08	21728379
191	Acetylation	KYEDEINKRTEMENE HHHHHHHHHHHCCCE	67.37	21728379
203	Acetylation	ENEFVLIKKDVDEAY CCEEEEEECCCCHHH	38.47	23201123
203	Ubiquitination	ENEFVLIKKDVDEAY CCEEEEEECCCCHHH	38.47	22790023
204	Acetylation	NEFVLIKKDVDEAYM CEEEEEECCCCHHHH	56.86	23201123
204	Glutarylation	NEFVLIKKDVDEAYM CEEEEEECCCCHHHH	56.86	24703693
204	Malonylation	NEFVLIKKDVDEAYM CEEEEEECCCCHHHH	56.86	26320211
204	Ubiquitination	NEFVLIKKDVDEAYM CEEEEEECCCCHHHH	56.86	27667366
210	Phosphorylation	KKDVDEAYMNKVELE ECCCCHHHHCHHHHH	10.12	-
213	Acetylation	VDEAYMNKVELESRL CCHHHHCHHHHHHHH	22.13	23864654
213	Ubiquitination	VDEAYMNKVELESRL CCHHHHCHHHHHHHH	22.13	22790023
218	Phosphorylation	MNKVELESRLEGLTD HCHHHHHHHHHHHHH	55.58	-
248	Phosphorylation	LQSQISDTSVVLSMD HHHHHCCCEEEEEEC	19.34	23140645
249	Phosphorylation	QSQISDTSVVLSMDN HHHHCCCEEEEEECC	18.41	23140645
253	Phosphorylation	SDTSVVLSMDNSRSL CCCEEEEEECCCCCC	16.69	29472430
257	Phosphorylation	VVLSMDNSRSLDMDG EEEEECCCCCCCCCC	20.98	28973931
259	Phosphorylation	LSMDNSRSLDMDGII EEECCCCCCCCCCHH	28.65	21082442
273	Phosphorylation	IAEVRAQYEDIANRS HHHHHHHHHHHHHHH	18.00	-
280	Phosphorylation	YEDIANRSRAEAETM HHHHHHHHHHHHHHH	35.33	25521595
301	Acetylation	ELQTLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	-
301	Glutarylation	ELQTLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	24703693
301	Malonylation	ELQTLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	26320211
301	Ubiquitination	ELQTLAGKHGDDLRR HHHHHCHHCCHHHHH	38.52	-
310	Malonylation	GDDLRRTKTEISEMN CHHHHHHHHHHHHHH	42.20	26320211
310	Ubiquitination	GDDLRRTKTEISEMN CHHHHHHHHHHHHHH	42.20	27667366
311	Phosphorylation	DDLRRTKTEISEMNR HHHHHHHHHHHHHHH	37.63	-
314	Phosphorylation	RRTKTEISEMNRNIN HHHHHHHHHHHHHHH	25.26	-
331	Acetylation	QAEIEALKGQRASLE HHHHHHHHHCHHHHH	61.11	22733758
331	Malonylation	QAEIEALKGQRASLE HHHHHHHHHCHHHHH	61.11	26320211
331	Ubiquitination	QAEIEALKGQRASLE HHHHHHHHHCHHHHH	61.11	27667366
336	Phosphorylation	ALKGQRASLEAAIAD HHHHCHHHHHHHHHC	29.00	25521595
353	Glutarylation	QRGEMAIKDAQTKLA HHHHHHHHHHHHHHH	37.16	24703693
353	Malonylation	QRGEMAIKDAQTKLA HHHHHHHHHHHHHHH	37.16	26320211
353	Ubiquitination	QRGEMAIKDAQTKLA HHHHHHHHHHHHHHH	37.16	27667366
358	Acetylation	AIKDAQTKLAELEAA HHHHHHHHHHHHHHH	33.35	23864654
380	Phosphorylation	MARQLREYQELMNVK HHHHHHHHHHHHCHH	10.80	-
399	Glutarylation	IEITTYRKLLEGEES EEEHHHHHHHCCHHH	47.19	24703693
399	Ubiquitination	IEITTYRKLLEGEES EEEHHHHHHHCCHHH	47.19	27667366
406	Phosphorylation	KLLEGEESRLESGMQ HHHCCHHHHHHHHCC	37.55	28066266
410	Phosphorylation	GEESRLESGMQNMSI CHHHHHHHHCCCCEE	44.12	29472430
416	Phosphorylation	ESGMQNMSIHTKTTS HHHCCCCEEEECCCC	20.83	25521595
419	Phosphorylation	MQNMSIHTKTTSGYS CCCCEEEECCCCCCC	28.54	29472430
421	Phosphorylation	NMSIHTKTTSGYSGG CCEEEECCCCCCCCC	27.61	23984901
422	Phosphorylation	MSIHTKTTSGYSGGL CEEEECCCCCCCCCC	23.01	23984901
423	Phosphorylation	SIHTKTTSGYSGGLS EEEECCCCCCCCCCC	40.75	23984901
425	Phosphorylation	HTKTTSGYSGGLSSS EECCCCCCCCCCCCC	12.15	23984901
426	Phosphorylation	TKTTSGYSGGLSSSY ECCCCCCCCCCCCCC	29.88	23984901
430	Phosphorylation	SGYSGGLSSSYGGLT CCCCCCCCCCCCCCC	22.10	23984901
431	Phosphorylation	GYSGGLSSSYGGLTS CCCCCCCCCCCCCCC	32.40	23984901
432	Phosphorylation	YSGGLSSSYGGLTSP CCCCCCCCCCCCCCC	25.15	26239621
433	Phosphorylation	SGGLSSSYGGLTSPG CCCCCCCCCCCCCCC	19.70	26239621
437	Phosphorylation	SSSYGGLTSPGFSYG CCCCCCCCCCCCCCC	35.83	26239621
438	Phosphorylation	SSYGGLTSPGFSYGM CCCCCCCCCCCCCCC	28.24	16563375
442	Phosphorylation	GLTSPGFSYGMSSFQ CCCCCCCCCCCCCCC	27.05	26239621
443	Phosphorylation	LTSPGFSYGMSSFQP CCCCCCCCCCCCCCC	18.00	26239621
446	Phosphorylation	PGFSYGMSSFQPGFG CCCCCCCCCCCCCCC	24.52	23984901
447	Phosphorylation	GFSYGMSSFQPGFGS CCCCCCCCCCCCCCC	21.00	26239621
454	Phosphorylation	SFQPGFGSAGGSNTF CCCCCCCCCCCCCCC	22.83	23140645
458	Phosphorylation	GFGSAGGSNTFSRTT CCCCCCCCCCCCCCE	31.60	23140645
460	Phosphorylation	GSAGGSNTFSRTTKA CCCCCCCCCCCCEEE	25.37	23140645
462	Phosphorylation	AGGSNTFSRTTKAVV CCCCCCCCCCEEEEE	27.03	23140645
466	Malonylation	NTFSRTTKAVVVKKI CCCCCCEEEEEEEEE	38.27	26320211
475	Phosphorylation	VVVKKIETRDGKLVS EEEEEEECCCCCEEC	37.22	-
479	Acetylation	KIETRDGKLVSESSD EEECCCCCEECCCCC	50.43	22733758
479	Malonylation	KIETRDGKLVSESSD EEECCCCCEECCCCC	50.43	26320211
479	Ubiquitination	KIETRDGKLVSESSD EEECCCCCEECCCCC	50.43	27667366
482	O-linked_Glycosylation	TRDGKLVSESSDVVS CCCCCEECCCCCCCC	42.04	30042374
482	Phosphorylation	TRDGKLVSESSDVVS CCCCCEECCCCCCCC	42.04	25521595
484	Phosphorylation	DGKLVSESSDVVSK- CCCEECCCCCCCCC-	25.08	26239621
485	Phosphorylation	GKLVSESSDVVSK-- CCEECCCCCCCCC--	30.30	25521595
489	Phosphorylation	SESSDVVSK------ CCCCCCCCC------	32.28	25521595
490	Acetylation	ESSDVVSK------- CCCCCCCC-------	53.39	23864654
490	Ubiquitination	ESSDVVSK------- CCCCCCCC-------	53.39	-

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
9	S	Phosphorylation	Kinase	PKCE	Q02156	PSP
9	S	Phosphorylation	Kinase	PRKCE	P16054	Uniprot
9	S	Phosphorylation	Kinase	PKCE	P09216	PSP
24	S	Phosphorylation	Kinase	PKCE	Q02156	PSP
24	S	Phosphorylation	Kinase	PRKCE	P16054	Uniprot
24	S	Phosphorylation	Kinase	PKCE	P09216	PSP
47	S	Phosphorylation	Kinase	PKCE	Q02156	PSP
80	S	Phosphorylation	Kinase	MAPK14	P47811	GPS
80	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
80	S	Phosphorylation	Kinase	MAPK	-	Uniprot
438	S	Phosphorylation	Kinase	MAPK14	P47811	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
80	S	Phosphorylation		20724476
Ser-80 phosphorylation plays an important role in keratin filament reorganization (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 K2C8_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSB5_MOUSE	Psmb5	physical	12231209
PRS6B_MOUSE	Psmc4	physical	12231209
TGM2_MOUSE	Tgm2	physical	12231209
HS71B_MOUSE	Hspa1b	physical	12231209
HS90A_MOUSE	Hsp90aa1	physical	12231209

Drug and Disease Associations

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

Regulatory Network of K2C8_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylateepithelial keratins."; Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,Seidler U., Omary M.B., Kotlyarov A., Gaestel M.; J. Biol. Chem. 285:33242-33251(2010). Cited for: PHOSPHORYLATION AT SER-80 BY MAPK.	20724476 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-43, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-46 AND SER-47,AND MASS SPECTROMETRY.	17242355 [Abstract]

show