CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002293
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Keratin, type I cytoskeletal 18 
Protein Synonyms/Alias
 Cytokeratin endo B; Keratin D; Cytokeratin-18; CK-18; Keratin-18; K18 
Gene Name
 Krt18 
Gene Synonyms/Alias
 Kerd; Krt1-18 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
89RLASYLDKVKSLETEubiquitination[1]
103ENRRLESKIREHLEKacetylation[2]
124RDWGHYFKIIEDLRAacetylation[2, 3]
124RDWGHYFKIIEDLRAubiquitination[1]
160AADDFRVKYETELAMacetylation[2]
160AADDFRVKYETELAMubiquitination[1]
180SDIHGLRKVVDDTNIacetylation[4]
180SDIHGLRKVVDDTNIubiquitination[1]
200ETEIEALKEELLFMKacetylation[4]
234TVEVDAPKSQDLSKIubiquitination[1]
240PKSQDLSKIMADIRAacetylation[2, 4]
240PKSQDLSKIMADIRAubiquitination[1]
255QYEALAQKNREELDKubiquitination[1]
262KNREELDKYWSQQIEubiquitination[1]
278STTVVTTKSAEIRDAubiquitination[1]
363YEALLNIKVKLEAEIubiquitination[1]
400NSMQTVQKTTTRKIVubiquitination[1]
Reference
 [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] 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]
 [3] 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]
 [4] 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] 
Functional Description
 When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. 
Sequence Annotation
 REGION 2 71 Head.
 REGION 62 366 Necessary for interaction with PNN (By
 REGION 69 121 Interaction with TRADD (By similarity).
 REGION 72 380 Rod.
 REGION 72 107 Coil 1A.
 REGION 108 125 Linker 1.
 REGION 126 217 Coil 1B.
 REGION 218 241 Linker 12.
 REGION 236 384 Interaction with DNAJB6 (By similarity).
 REGION 242 380 Coil 2.
 REGION 381 423 Tail.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 8 8 Phosphothreonine.
 MOD_RES 11 11 Phosphoserine (By similarity).
 MOD_RES 12 12 Phosphothreonine.
 MOD_RES 16 16 Phosphoserine (By similarity).
 MOD_RES 19 19 Phosphoserine (By similarity).
 MOD_RES 31 31 Phosphoserine; alternate.
 MOD_RES 32 32 Phosphoserine; alternate.
 MOD_RES 35 35 Phosphoserine.
 MOD_RES 37 37 Phosphotyrosine (By similarity).
 MOD_RES 43 43 Phosphoserine (By similarity).
 MOD_RES 52 52 Phosphoserine; by MAPKAPK2 and MAPKAPK3.
 MOD_RES 60 60 Phosphoserine (By similarity).
 MOD_RES 92 92 Phosphoserine (By similarity).
 MOD_RES 124 124 N6-acetyllysine (By similarity).
 MOD_RES 170 170 Phosphoserine (By similarity).
 MOD_RES 295 295 Phosphothreonine (By similarity).
 MOD_RES 392 392 Phosphoserine (By similarity).
 MOD_RES 394 394 Phosphoserine.
 MOD_RES 397 397 Phosphothreonine.
 CARBOHYD 31 31 O-linked (GlcNAc); alternate (By
 CARBOHYD 32 32 O-linked (GlcNAc); alternate (By
 CARBOHYD 50 50 O-linked (GlcNAc) (By similarity).  
Keyword
 Acetylation; Coiled coil; Complete proteome; Cytoplasm; Glycoprotein; Intermediate filament; Keratin; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 423 AA 
Protein Sequence
MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS RSVWGGSVGS 60
AGLAGMGGIQ TEKETMQDLN DRLASYLDKV KSLETENRRL ESKIREHLEK KGPQGVRDWG 120
HYFKIIEDLR AQIFANSVDN ARIVLQIDNA RLAADDFRVK YETELAMRQS VESDIHGLRK 180
VVDDTNITRL QLETEIEALK EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK 240
IMADIRAQYE ALAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLT ELRRTLQTLE 300
IDLDSMKNQN INLENSLGDV EARYKAQMEQ LNGVLLHLES ELAQTRAEGQ RQAQEYEALL 360
NIKVKLEAEI ATYRRLLEDG EDFSLNDALD SSNSMQTVQK TTTRKIVDGR VVSETNDTRV 420
LRH 423 
Gene Ontology
 GO:0034451; C:centriolar satellite; IEA:Compara.
 GO:0045095; C:keratin filament; IDA:MGI.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
 GO:0043000; P:Golgi to plasma membrane CFTR protein transport; IEA:Compara.
 GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IGI:MGI. 
Interpro
 IPR016044; F.
 IPR001664; IF.
 IPR018039; Intermediate_filament_CS.
 IPR002957; Keratin_I. 
Pfam
 PF00038; Filament 
SMART
  
PROSITE
 PS00226; IF 
PRINTS
 PR01248; TYPE1KERATIN.