CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002294
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Keratin, type II cytoskeletal 8 
Protein Synonyms/Alias
 Cytokeratin-8; CK-8; Keratin-8; K8; Type-II keratin Kb8 
Gene Name
 KRT8 
Gene Synonyms/Alias
 CYK8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MSIRVTQKSYKVSTSubiquitination[1]
11RVTQKSYKVSTSGPRacetylation[2]
11RVTQKSYKVSTSGPRubiquitination[1, 3, 4, 5, 6]
92QAVRTQEKEQIKTLNubiquitination[1]
96TQEKEQIKTLNNKFAubiquitination[1, 3, 5, 6]
101QIKTLNNKFASFIDKmalonylation[7]
101QIKTLNNKFASFIDKubiquitination[1, 3, 4, 5, 6]
108KFASFIDKVRFLEQQubiquitination[1, 3, 4, 5, 6]
117RFLEQQNKMLETKWSacetylation[8, 9]
117RFLEQQNKMLETKWSubiquitination[1, 3, 4, 5, 6]
122QNKMLETKWSLLQQQubiquitination[1, 3, 4, 5, 6]
130WSLLQQQKTARSNMDubiquitination[1, 3, 4, 5, 6]
158LETLGQEKLKLEAELubiquitination[1]
160TLGQEKLKLEAELGNubiquitination[1]
176QGLVEDFKNKYEDEIubiquitination[1, 3, 5, 6]
178LVEDFKNKYEDEINKubiquitination[1]
197ENEFVLIKKDVDEAYubiquitination[1, 5]
198NEFVLIKKDVDEAYMubiquitination[1, 5]
207VDEAYMNKVELESRLacetylation[8, 9, 10, 11]
207VDEAYMNKVELESRLubiquitination[1, 3, 4, 5, 6]
264DSIIAEVKAQYEDIAubiquitination[1, 4, 5]
285AESMYQIKYEELQSLacetylation[12]
285AESMYQIKYEELQSLsumoylation[13]
285AESMYQIKYEELQSLubiquitination[1, 4, 5, 14]
295ELQSLAGKHGDDLRRacetylation[8, 9]
295ELQSLAGKHGDDLRRubiquitination[1, 3, 4, 5, 6, 14]
304GDDLRRTKTEISEMNubiquitination[1, 4, 5]
325QAEIEGLKGQRASLEacetylation[8, 9]
325QAEIEGLKGQRASLEubiquitination[1, 3, 4, 5, 6, 14]
347QRGELAIKDANAKLSacetylation[8, 9, 15]
347QRGELAIKDANAKLSubiquitination[1, 4, 5, 14]
352AIKDANAKLSELEAAubiquitination[1, 3, 4, 5, 6, 14]
364EAALQRAKQDMARQLsumoylation[13]
393IEIATYRKLLEGEESacetylation[8]
393IEIATYRKLLEGEESubiquitination[1, 5]
414QNMSIHTKTTSGYAGubiquitination[5]
464SSRAVVVKKIETRDGacetylation[15]
465SRAVVVKKIETRDGKacetylation[15]
472KIETRDGKLVSESSDacetylation[2]
472KIETRDGKLVSESSDubiquitination[1, 4, 5, 14]
483ESSDVLPK*******acetylation[2, 16]
483ESSDVLPK*******ubiquitination[4]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Application of high-content analysis to the study of post-translational modifications of the cytoskeleton.
 Drake PJ, Griffiths GJ, Shaw L, Benson RP, Corfe BM.
 J Proteome Res. 2009 Jan;8(1):28-34. [PMID: 18983182]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation.
 Snider NT, Leonard JM, Kwan R, Griggs NW, Rui L, Omary MB.
 J Cell Biol. 2013 Feb 4;200(3):241-7. [PMID: 23358244]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [11] Generation of acetyllysine antibodies and affinity enrichment of acetylated peptides.
 Guan KL, Yu W, Lin Y, Xiong Y, Zhao S.
 Nat Protoc. 2010 Sep;5(9):1583-95. [PMID: 21085124]
 [12] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [13] Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation.
 Snider NT, Weerasinghe SV, Iñiguez-Lluhí JA, Herrmann H, Omary MB.
 J Biol Chem. 2011 Jan 21;286(3):2273-84. [PMID: 21062750]
 [14] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [15] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [16] The application of a hypothesis-driven strategy to the sensitive detection and location of acetylated lysine residues.
 Griffiths JR, Unwin RD, Evans CA, Leech SH, Corfe BM, Whetton AD.
 J Am Soc Mass Spectrom. 2007 Aug;18(8):1423-8. [PMID: 17543536
Functional Description
 Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. 
Sequence Annotation
 REGION 1 90 Head.
 REGION 91 398 Rod.
 REGION 91 126 Coil 1A.
 REGION 127 143 Linker 1.
 REGION 144 235 Coil 1B.
 REGION 236 259 Linker 12.
 REGION 260 398 Coil 2.
 REGION 261 382 Necessary for interaction with PNN.
 REGION 399 483 Tail.
 MOD_RES 9 9 Phosphoserine; by PKC/PRKCE.
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 24 24 Phosphoserine; by PKC/PRKCE.
 MOD_RES 27 27 Phosphoserine.
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 36 36 Phosphoserine.
 MOD_RES 37 37 Phosphoserine.
 MOD_RES 43 43 Phosphoserine.
 MOD_RES 74 74 Phosphoserine; by MAPK.
 MOD_RES 101 101 N6-malonyllysine.
 MOD_RES 117 117 N6-acetyllysine.
 MOD_RES 207 207 N6-acetyllysine.
 MOD_RES 253 253 Phosphoserine.
 MOD_RES 258 258 Phosphoserine.
 MOD_RES 295 295 N6-acetyllysine.
 MOD_RES 325 325 N6-acetyllysine.
 MOD_RES 330 330 Phosphoserine.
 MOD_RES 347 347 N6-acetyllysine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 410 410 Phosphoserine.
 MOD_RES 417 417 Phosphoserine (By similarity).
 MOD_RES 424 424 Phosphoserine (By similarity).
 MOD_RES 432 432 Phosphoserine; by CaMK2 and MAPK.
 MOD_RES 475 475 Phosphoserine.
 MOD_RES 478 478 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein; Host-virus interaction; Intermediate filament; Keratin; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 483 AA 
Protein Sequence
MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL GGGYGGASGM 60
GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN KFASFIDKVR FLEQQNKMLE 120
TKWSLLQQQK TARSNMDNMF ESYINNLRRQ LETLGQEKLK LEAELGNMQG LVEDFKNKYE 180
DEINKRTEME NEFVLIKKDV DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS 240
DTSVVLSMDN SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL 300
RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN AKLSELEAAL 360
QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES RLESGMQNMS IHTKTTSGYA 420
GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS SFSRTSSSRA VVVKKIETRD GKLVSESSDV 480
LPK 483 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005882; C:intermediate filament; NAS:UniProtKB.
 GO:0045095; C:keratin filament; IEA:InterPro.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0005198; F:structural molecule activity; NAS:UniProtKB.
 GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR003054; Keratin_II. 
Pfam
 PF00038; Filament 
SMART
  
PROSITE
 PS00226; IF 
PRINTS
 PR01276; TYPE2KERATIN.