CPLM-003957

Genbank Nucleotide ID

Keratin, type II cytoskeletal 8

Protein Synonyms/Alias

Cytokeratin endo A; Cytokeratin-8; CK-8; Keratin-8; K8; Type-II keratin Kb8

Mus musculus (Mouse)

Position	Peptide	Type	References
11	RVTQKSYKMSTSGPR	ubiquitination	[1]
107	QIKSLNNKFASFIDK	acetylation	[2, 3, 4]
107	QIKSLNNKFASFIDK	ubiquitination	[1]
114	KFASFIDKVRFLEQQ	acetylation	[5]
114	KFASFIDKVRFLEQQ	ubiquitination	[1]
123	RFLEQQNKMLETKWS	ubiquitination	[1]
128	QNKMLETKWSLLQQQ	acetylation	[2, 4]
128	QNKMLETKWSLLQQQ	ubiquitination	[1]
136	WSLLQQQKTSRSNMD	ubiquitination	[1]
164	LEALGQEKLKLEAEL	acetylation	[4]
164	LEALGQEKLKLEAEL	ubiquitination	[1]
184	LVEDFKNKYEDEINK	acetylation	[4, 5, 6]
191	KYEDEINKRTEMENE	acetylation	[4, 5, 6]
203	ENEFVLIKKDVDEAY	acetylation	[5]
203	ENEFVLIKKDVDEAY	ubiquitination	[1]
204	NEFVLIKKDVDEAYM	acetylation	[5]
204	NEFVLIKKDVDEAYM	ubiquitination	[1]
213	VDEAYMNKVELESRL	acetylation	[4, 5]
213	VDEAYMNKVELESRL	ubiquitination	[1]
301	ELQTLAGKHGDDLRR	ubiquitination	[1]
310	GDDLRRTKTEISEMN	ubiquitination	[1]
331	QAEIEALKGQRASLE	acetylation	[2, 5]
331	QAEIEALKGQRASLE	ubiquitination	[1]
353	QRGEMAIKDAQTKLA	ubiquitination	[1]
358	AIKDAQTKLAELEAA	acetylation	[4, 5]
479	KIETRDGKLVSESSD	acetylation	[2]
479	KIETRDGKLVSESSD	ubiquitination	[1]
490	ESSDVVSK*******	acetylation	[4]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[3] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
[4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[5] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[6] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]

Functional Description

Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle (By similarity).

REGION 1 96 Head.
REGION 97 403 Rod.
REGION 97 132 Coil 1A.
REGION 133 149 Linker 1.
REGION 150 241 Coil 1B.
REGION 242 265 Linker 12.
REGION 266 403 Coil 2.
REGION 267 387 Necessary for interaction with PNN (By
REGION 404 490 Tail.
MOD_RES 9 9 Phosphoserine; by PKC/PRKCE (By
MOD_RES 13 13 Phosphoserine (By similarity).
MOD_RES 21 21 Phosphoserine.
MOD_RES 24 24 Phosphoserine; by PKC/PRKCE (Probable).
MOD_RES 27 27 Phosphoserine (By similarity).
MOD_RES 34 34 Phosphoserine (By similarity).
MOD_RES 36 36 Phosphoserine (By similarity).
MOD_RES 37 37 Phosphoserine (By similarity).
MOD_RES 43 43 Phosphoserine.
MOD_RES 46 46 Phosphoserine.
MOD_RES 47 47 Phosphoserine.
MOD_RES 51 51 Phosphoserine (By similarity).
MOD_RES 80 80 Phosphoserine; by MAPK.
MOD_RES 107 107 N6-malonyllysine (By similarity).
MOD_RES 123 123 N6-acetyllysine (By similarity).
MOD_RES 213 213 N6-acetyllysine (By similarity).
MOD_RES 259 259 Phosphoserine (By similarity).
MOD_RES 301 301 N6-acetyllysine (By similarity).
MOD_RES 331 331 N6-acetyllysine (By similarity).
MOD_RES 336 336 Phosphoserine (By similarity).
MOD_RES 353 353 N6-acetyllysine (By similarity).
MOD_RES 406 406 Phosphoserine (By similarity).
MOD_RES 416 416 Phosphoserine (By similarity).
MOD_RES 423 423 Phosphoserine (By similarity).
MOD_RES 430 430 Phosphoserine (By similarity).
MOD_RES 432 432 Phosphoserine (By similarity).
MOD_RES 438 438 Phosphoserine (By similarity).
MOD_RES 482 482 Phosphoserine (By similarity).
MOD_RES 485 485 Phosphoserine (By similarity).

Acetylation; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Intermediate filament; Keratin; Nucleus; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0043034; C:costamere; IEA:Compara.
GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Compara.
GO:0005882; C:intermediate filament; IDA:MGI.
GO:0045095; C:keratin filament; IEA:Compara.
GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO:0042383; C:sarcolemma; IDA:MGI.
GO:0030018; C:Z disc; IDA:MGI.
GO:0005198; F:structural molecule activity; IEA:InterPro.
GO:0060706; P:cell differentiation involved in embryonic placenta development; IGI:MGI.
GO:0000904; P:cell morphogenesis involved in differentiation; TAS:UniProtKB.
GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO:0051599; P:response to hydrostatic pressure; IEA:Compara.
GO:0051707; P:response to other organism; IMP:MGI.
GO:0045214; P:sarcomere organization; IEA:Compara.
GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:MGI.

IPR016044; F.
IPR001664; IF.
IPR018039; Intermediate_filament_CS.
IPR003054; Keratin_II.
IPR009053; Prefoldin.

PR01276; TYPE2KERATIN.