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UniProtKB/Swiss-Prot entry P05783

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name K1C18_HUMAN
Primary accession number P05783
Secondary accession numbers Q53G38 Q5U0N8 Q9BW26
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 104)
Name and origin of the protein
Protein name Keratin, type I cytoskeletal 18
Synonyms Cytokeratin-18
CK-18
Keratin-18
K18
Cell proliferation-inducing gene 46 protein
Gene name
Name: KRT18
Synonyms: CYK18
ORFNames: PIG46
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=2434380 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima R.G., Millan J.L., Cecena G.;
"Comparison of mouse and human keratin 18: a component of intermediate filaments expressed prior to implantation.";
Differentiation 33:61-68(1986).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a cell proliferation-inducing gene.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, Colon, Pancreas, Placenta, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167.
PubMed=2454392 [NCBI, ExPASy, EBI, Israel, Japan]
Kulesh D.A., Oshima R.G.;
"Cloning of the human keratin 18 gene and its expression in nonepithelial mouse cells.";
Mol. Cell. Biol. 8:1540-1550(1988).
[7]
 NUCLEOTIDE SEQUENCE [MRNA] OF 7-430, AND TISSUE SPECIFICITY.
TISSUE=Vulva;
PubMed=2434381 [NCBI, ExPASy, EBI, Israel, Japan]
Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H., Franke W.W.;
"Cytokeratin expression in simple epithelia. III. Detection of mRNAs encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by hybridization with cDNA sequences in vitro and in situ.";
Differentiation 33:69-85(1986).
[8]
 NUCLEOTIDE SEQUENCE [MRNA] OF 199-430, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=2422083 [NCBI, ExPASy, EBI, Israel, Japan]
Romano V., Hatzfeld M., Magin T.M., Zimbelmann R., Franke W.W., Maier G., Ponstingl H.;
"Cytokeratin expression in simple epithelia. I. Identification of mRNA coding for human cytokeratin no. 18 by a cDNA clone.";
Differentiation 30:244-253(1986).
[9]
 PARTIAL PROTEIN SEQUENCE.
TISSUE=Colon carcinoma;
DOI=10.1002/elps.1150180344; PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan]
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[10]
 GLYCOSYLATION.
PubMed=1371281 [NCBI, ExPASy, EBI, Israel, Japan]
Chou C.F., Smith A.J., Omary M.B.;
"Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.";
J. Biol. Chem. 267:3901-3906(1992).
[11]
 FUNCTION, PHOSPHORYLATION AT SER-53, AND MUTAGENESIS OF SER-2; SER-7; SER-10; SER-15; SER-18; SER-23; SER-30; SER-31; SER-34; SER-42; SER-44; SER-47; SER-49; SER-51 AND SER-53.
DOI=10.1083/jcb.127.1.161; PubMed=7523419 [NCBI, ExPASy, EBI, Israel, Japan]
Ku N.O., Omary M.B.;
"Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.";
J. Cell Biol. 127:161-171(1994).
[12]
 GLYCOSYLATION AT SER-30; SER-31 AND SER-49, AND MUTAGENESIS OF SER-30; SER-31 AND SER-49.
DOI=10.1074/jbc.270.20.11820; PubMed=7538124 [NCBI, ExPASy, EBI, Israel, Japan]
Ku N.-O., Omary M.B.;
"Identification and mutational analysis of the glycosylation sites of human keratin 18.";
J. Biol. Chem. 270:11820-11827(1995).
[13]
 FUNCTION, AND MUTAGENESIS OF ARG-90.
DOI=10.1083/jcb.131.5.1303; PubMed=8522591 [NCBI, ExPASy, EBI, Israel, Japan]
Ku N.O., Michie S., Oshima R.G., Omary M.B.;
"Chronic hepatitis, hepatocyte fragility, and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginine mutant.";
J. Cell Biol. 131:1303-1314(1995).
[14]
 PHOSPHORYLATION, AND INTERACTION WITH YWHAE, YWHAH AND YWHAZ.
DOI=10.1083/jcb.133.2.345; PubMed=8609167 [NCBI, ExPASy, EBI, Israel, Japan]
Liao J., Omary M.B.;
"14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor.";
J. Cell Biol. 133:345-357(1996).
[15]
 FUNCTION, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF SER-53 AND ASP-238.
DOI=10.1083/jcb.138.6.1379; PubMed=9298992 [NCBI, ExPASy, EBI, Israel, Japan]
Caulin C., Salvesen G.S., Oshima R.G.;
"Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis.";
J. Cell Biol. 138:1379-1394(1997).
[16]
 FUNCTION, INTERACTION WITH YWHAE AND YWHAZ, PHOSPHORYLATION AT SER-34, AND MUTAGENESIS OF SER-34 AND SER-53.
DOI=10.1093/emboj/17.7.1892; PubMed=9524113 [NCBI, ExPASy, EBI, Israel, Japan]
Ku N.O., Liao J., Omary M.B.;
"Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins.";
EMBO J. 17:1892-1906(1998).
[17]
 INTERACTION WITH PNN.
DOI=10.1074/jbc.275.20.14910; PubMed=10809736 [NCBI, ExPASy, EBI, Israel, Japan]
Shi J., Sugrue S.P.;
"Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus.";
J. Biol. Chem. 275:14910-14915(2000).
[18]
 INTERACTION WITH DNAJB6.
DOI=10.1074/jbc.M003492200; PubMed=10954706 [NCBI, ExPASy, EBI, Israel, Japan]
Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M.;
"Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein.";
J. Biol. Chem. 275:34521-34527(2000).
[19]
 INTERACTION WITH TRADD.
DOI=10.1083/jcb.200103078; PubMed=11684708 [NCBI, ExPASy, EBI, Israel, Japan]
Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T., Momoi T., Inagaki M.;
"Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD.";
J. Cell Biol. 155:415-426(2001).
[20]
 ASSOCIATION WITH KRT8.
DOI=10.1021/bi035072s; PubMed=14756564 [NCBI, ExPASy, EBI, Israel, Japan]
Waseem A., Karsten U., Leigh I.M., Purkis P., Waseem N.H., Lane E.B.;
"Conformational changes in the rod domain of human keratin 8 following heterotypic association with keratin 18 and its implication for filament stability.";
Biochemistry 43:1283-1295(2004).
[21]
 PHOSPHORYLATION AT SER-34 AND SER-53.
DOI=10.1002/hep.20277; PubMed=15368451 [NCBI, ExPASy, EBI, Israel, Japan]
Toivola D.M., Ku N.O., Resurreccion E.Z., Nelson D.R., Wright T.L., Omary M.B.;
"Keratin 8 and 18 hyperphosphorylation is a marker of progression of human liver disease.";
Hepatology 40:459-466(2004).
[22]
 FUNCTION, INTERACTION WITH MUTATED CFTR, AND SUBCELLULAR LOCATION.
DOI=10.1002/pmic.200400850; PubMed=15529338 [NCBI, ExPASy, EBI, Israel, Japan]
Davezac N., Tondelier D., Lipecka J., Fanen P., Demaugre F., Debski J., Dadlez M., Schrattenholz A., Cahill M.A., Edelman A.;
"Global proteomic approach unmasks involvement of keratins 8 and 18 in the delivery of cystic fibrosis transmembrane conductance regulator (CFTR)/deltaF508-CFTR to the plasma membrane.";
Proteomics 4:3833-3844(2004).
[23]
 INTERACTION WITH TCHP.
DOI=10.1242/jcs.01667; PubMed=15731013 [NCBI, ExPASy, EBI, Israel, Japan]
Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., Usukura J., Inagaki M.;
"Identification of trichoplein, a novel keratin filament-binding protein.";
J. Cell Sci. 118:1081-1090(2005).
[24]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-34, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[25]
 FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-53.
DOI=10.1124/jpet.105.097667; PubMed=16424149 [NCBI, ExPASy, EBI, Israel, Japan]
Lipecka J., Norez C., Bensalem N., Baudouin-Legros M., Planelles G., Becq F., Edelman A., Davezac N.;
"Rescue of DeltaF508-CFTR (cystic fibrosis transmembrane conductance regulator) by curcumin: involvement of the keratin 18 network.";
J. Pharmacol. Exp. Ther. 317:500-505(2006).
[26]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[27]
 FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INDUCTION.
DOI=10.1074/jbc.M604068200; PubMed=17213200 [NCBI, ExPASy, EBI, Israel, Japan]
Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.;
"Interleukin-6 induces keratin expression in intestinal epithelial cells: potential role of keratin-8 in interleukin-6-induced barrier function alterations.";
J. Biol. Chem. 282:8219-8227(2007).
[28]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-18; SER-53 AND SER-60, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[29]
 VARIANT CRYPTOGENIC CIRRHOSIS LEU-128.
PubMed=9011570 [NCBI, ExPASy, EBI, Israel, Japan]
Ku N.-O., Wright T.L., Terrault N.A., Gish R., Omary M.B.;
"Mutation of human keratin 18 in association with cryptogenic cirrhosis.";
J. Clin. Invest. 99:19-23(1997).
[30]
 VARIANTS CRYPTOGENIC CIRRHOSIS ALA-103; LEU-128; GLN-261 AND ARG-340, AND VARIANT THR-230.
DOI=10.1073/pnas.0936165100; PubMed=12724528 [NCBI, ExPASy, EBI, Israel, Japan]
Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.;
"Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies.";
Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003).
Comments
  • FUNCTION: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.
  • SUBUNIT: Heterotetramer of two type I and two type II keratins. Keratin-18 associates with keratin-8. Interacts with the thrombin-antithrombin complex (By similarity). Interacts with PNN, HCV core protein and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with DNAJB6, TCHP and TRADD.
  • INTERACTION:
    Q6FGX6:CLEC3B; NbExp=1; IntAct=EBI-297888, EBI-1047626;
    O75190:DNAJB6; NbExp=3; IntAct=EBI-297888, EBI-1053164;
    P05787:KRT8; NbExp=2; IntAct=EBI-297888, EBI-297852;
    P23508:MCC; NbExp=1; IntAct=EBI-297888, EBI-307531;
    O75688:PPM1B; NbExp=1; IntAct=EBI-297888, EBI-1047039;
    Q15628:TRADD; NbExp=3; IntAct=EBI-297888, EBI-359215;
  • SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
  • TISSUE SPECIFICITY: Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma.
  • INDUCTION: By IL-6.
  • PTM: Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6.
  • PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7.
  • PTM: O-glycosylated at multiple sites; glycans consist of single N-acetylglucosamine residues.
  • DISEASE: Defects in KRT18 are a cause of cryptogenic cirrhosis [MIM:215600].
  • MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
  • SIMILARITY: Belongs to the intermediate filament family.
  • WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; URL="http://www.interfil.org";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X12881; CAA31375.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY762101; AAX07828.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019412; AAV38219.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223093; BAD96813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000180; AAH00180.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000698; AAH00698.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004253; AAH04253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008636; AAH08636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020982; AAH20982.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC072017; AAH72017.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF179904; AAA59461.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12883; CAA31377.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12876; CAA31369.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S05481; S05481.
RefSeq NP_000215.1; -.
NP_954657.1; -.
UniGene Hs.406013
3D structure databases
HSSP P08670; 1GK7. [HSSP ENTRY / PDB]
ModBase P05783.
Protein-protein interaction databases
DIP DIP:633N; -.
IntAct P05783; -.
PTM databases
GlycoSuiteDB P05783; -.
PhosphoSite P05783; -.
2D gel databases
SWISS-2DPAGE P05783; -.
PMMA-2DPAGE P05783; -.
Siena-2DPAGE P05783; -.
Organism-specific databases
H-InvDB HIX0010657; -.
HIX0029655; -.
HIX0030618; -.
HIX0040371; -.
HIX0056530; -.
HIX0056886; -.
HIX0058984; -.
HGNC HGNC:6430; KRT18.
GenAtlas KRT18.
HPA CAB000008; -.
CAB000030; -.
CAB000092; -.
HPA001605; -.
MIM 148070; gene. [NCBI / EBI]
215600; phenotype. [NCBI / EBI]
PharmGKB PA30217; -.
GeneCards P05783.
Gene expression databases
CleanEx HS_KRT18; -.
GermOnline ENSG00000111057; Homo sapiens.
Ontologies
GO
GO:0034451; Cellular component: centriolar satellite (inferred from direct assay from UniProtKB).
GO:0045095; Cellular component: keratin filament (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0009653; Biological process: anatomical structure morphogenesis (traceable author statement from ProtInc).
GO:0043000; Biological process: Golgi to plasma membrane CFTR protein transport (inferred from direct assay from UniProtKB).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016044; F.
IPR001664; IF.
IPR002957; Keratin_I.
Graphical view of domain structure.
PANTHER PTHR23239; IF; 1.
Pfam PF00038; Filament; 1.
Pfam graphical view of domain structure.
PRINTS PR01248; TYPE1KERATIN.
PROSITE PS00226; IF; 1.
BLOCKS P05783.
ProtoNet P05783.
Genome annotation databases
Ensembl ENSG00000111057; Homo sapiens. [Contig view]
GeneID 3875; -.
KEGG hsa:3875; -.
Phylogenomic databases
HOVERGEN P05783; -.
Other
LinkHub P05783; -.
NextBio 15217; -.
SOURCE KRT18; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cell cycle; Coiled coil; Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein; Host-virus interaction; Intermediate filament; Keratin; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   430  429     Keratin, type I cytoskeletal 18. PRO_0000063666
REGION   2    79  78     Head. 
REGION   70   373  304     Necessary for interaction with PNN. 
REGION   77   128  52     Interaction with TRADD. 
REGION   80   387  308     Rod. 
REGION   80   115  36     Coil 1A. 
REGION   116   132  17     Linker 1. 
REGION   133   224  92     Coil 1B. 
REGION   225   248  24     Linker 12. 
REGION   243   391  149     Interaction with DNAJB6. 
REGION   249   387  139     Coil 2. 
REGION   388   430  43     Tail. 
SITE   238   239  2     Cleavage; by caspase-3, caspase-6 or caspase-7. 
SITE   271   271  1     Stutter. 
SITE   331   331  1     Stutter. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   7     7        Phosphoserine. 
MOD_RES   8     8        Phosphothreonine (By similarity). 
MOD_RES   11    11        Phosphothreonine (By similarity). 
MOD_RES   13    13        Phosphotyrosine. 
MOD_RES   15    15        Phosphoserine. 
MOD_RES   18    18        Phosphoserine. 
MOD_RES   30    30        Phosphoserine (By similarity). 
MOD_RES   31    31        Phosphoserine (By similarity). 
MOD_RES   34    34        Phosphoserine; by CDC2. 
MOD_RES   36    36        Phosphotyrosine (By similarity). 
MOD_RES   42    42        Phosphoserine (By similarity). 
MOD_RES   53    53        Phosphoserine; by CAMK, PKC/PRKCE and STK6. 
MOD_RES   60    60        Phosphoserine. 
MOD_RES   401   401        Phosphoserine (By similarity). 
MOD_RES   404   404        Phosphothreonine (By similarity). 
CARBOHYD   30    30        O-linked (GlcNAc) [GlycoSuiteDB]. CAR_000175
CARBOHYD   31    31        O-linked (GlcNAc) [GlycoSuiteDB]. CAR_000193
CARBOHYD   49    49        O-linked (GlcNAc) [GlycoSuiteDB]. CAR_000194
VARIANT   103   103  1     T -> A (in cryptogenic cirrhosis). VAR_023054 
VARIANT   128   128  1     H -> L (in cryptogenic cirrhosis; interfers with the ability to form normal filaments). VAR_003852 
VARIANT   230   230  1     S -> T. VAR_023055 
VARIANT   261   261  1     R -> Q (in cryptogenic cirrhosis). VAR_023056 
VARIANT   340   340  1     G -> R (in cryptogenic cirrhosis). VAR_023057 
MUTAGEN   2     2        S->A: No effect on phosphorylation; when associated with A-7 and A-10. 
MUTAGEN   7     7        S->A: No effect on phosphorylation; when associated with A-2 and A-10. 
MUTAGEN   10    10        S->A: No effect on phosphorylation; when associated with A-2 and A-7. 
MUTAGEN   15    15        S->A: No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53. 
MUTAGEN   18    18        S->A: No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53. 
MUTAGEN   23    23        S->A: No effect on phosphorylation; when associated with A-15 and A-18. 
MUTAGEN   30    30        S->A: No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49. 
MUTAGEN   31    31        S->A: No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49. 
MUTAGEN   34    34        S->A: No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53. 
MUTAGEN   34    34        S->D,E: Abolishes binding to YWHAE and YWHAZ. 
MUTAGEN   42    42        S->A: No effect on phosphorylation; when associated with A-44. 
MUTAGEN   44    44        S->A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. 
MUTAGEN   47    47        S->A: No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53. 
MUTAGEN   49    49        S->A: No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31. 
MUTAGEN   51    51        S->A: No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53. 
MUTAGEN   53    53        S->A: Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis. 
MUTAGEN