Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Keratin, type I cytoskeletal 18

Gene

KRT18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei271Stutter1
Sitei331Stutter1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • scaffold protein binding Source: BHF-UCL
  • structural molecule activity Source: InterPro

GO - Biological processi

  • anatomical structure morphogenesis Source: ProtInc
  • cell cycle Source: UniProtKB-KW
  • extrinsic apoptotic signaling pathway Source: Ensembl
  • Golgi to plasma membrane CFTR protein transport Source: UniProtKB
  • hepatocyte apoptotic process Source: Ensembl
  • intermediate filament cytoskeleton organization Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • tumor necrosis factor-mediated signaling pathway Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111057-MONOMER.
ReactomeiR-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.
SignaLinkiP05783.
SIGNORiP05783.

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 18
Alternative name(s):
Cell proliferation-inducing gene 46 protein
Cytokeratin-18
Short name:
CK-18
Keratin-18
Short name:
K18
Gene namesi
Name:KRT18
Synonyms:CYK18
ORF Names:PIG46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6430. KRT18.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cell periphery Source: Ensembl
  • centriolar satellite Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • intermediate filament Source: BHF-UCL
  • keratin filament Source: UniProtKB
  • microtubule organizing center Source: BHF-UCL
  • nucleolus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cirrhosis (CIRRH)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension.
See also OMIM:215600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023054103T → A in CIRRH. 1 PublicationCorresponds to variant rs61136606dbSNPEnsembl.1
Natural variantiVAR_003852128H → L in CIRRH; interfers with the ability to form normal filaments. 2 PublicationsCorresponds to variant rs57758506dbSNPEnsembl.1
Natural variantiVAR_023056261R → Q in CIRRH. 1 PublicationCorresponds to variant rs57354642dbSNPEnsembl.1
Natural variantiVAR_023057340G → R in CIRRH. 1 PublicationCorresponds to variant rs57370769dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2S → A: No effect on phosphorylation; when associated with A-7 and A-10. 1 Publication1
Mutagenesisi7S → A: No effect on phosphorylation; when associated with A-2 and A-10. 1 Publication1
Mutagenesisi10S → A: No effect on phosphorylation; when associated with A-2 and A-7. 1 Publication1
Mutagenesisi15S → 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. 1 Publication1
Mutagenesisi18S → 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. 1 Publication1
Mutagenesisi23S → A: No effect on phosphorylation; when associated with A-15 and A-18. 1 Publication1
Mutagenesisi30S → 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. 2 Publications1
Mutagenesisi31S → 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. 2 Publications1
Mutagenesisi34S → 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. 2 Publications1
Mutagenesisi34S → D or E: Abolishes binding to YWHAE and YWHAZ. 2 Publications1
Mutagenesisi42S → A: No effect on phosphorylation; when associated with A-44. 1 Publication1
Mutagenesisi44S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. 1 Publication1
Mutagenesisi47S → 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. 1 Publication1
Mutagenesisi49S → 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. 2 Publications1
Mutagenesisi51S → 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. 1 Publication1
Mutagenesisi53S → 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. 3 Publications1
Mutagenesisi90R → C or H in transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation. 1 Publication1
Mutagenesisi238D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3875.
MalaCardsiKRT18.
MIMi215600. phenotype.
OpenTargetsiENSG00000111057.
PharmGKBiPA30217.

Polymorphism and mutation databases

BioMutaiKRT18.
DMDMi125083.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000636662 – 430Keratin, type I cytoskeletal 18Add BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei7PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei18PhosphoserineCombined sources1
Modified residuei30Phosphoserine; alternateBy similarity1
GlycosylationiCAR_00017530O-linked (GlcNAc); alternate2 Publications1
Modified residuei31Phosphoserine; alternateBy similarity1
GlycosylationiCAR_00019331O-linked (GlcNAc); alternate2 Publications1
Modified residuei34Phosphoserine; by CDK1Combined sources2 Publications1
Modified residuei36PhosphotyrosineBy similarity1
Modified residuei42PhosphoserineCombined sources1
Modified residuei45Omega-N-methylarginineCombined sources1
Modified residuei49Phosphoserine; alternateCombined sources1
GlycosylationiCAR_00019449O-linked (GlcNAc); alternate2 Publications1
Modified residuei51Phosphoserine; by MAPKAPK2 and MAPKAPK3Curated1
Modified residuei52PhosphothreonineCombined sources1
Modified residuei53Phosphoserine; by CAMK, PKC/PRKCE and AURKA3 Publications1
Modified residuei55Omega-N-methylarginineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei65PhosphothreonineCombined sources1
Modified residuei93PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Modified residuei302PhosphothreonineCombined sources1
Modified residuei305PhosphoserineCombined sources1
Modified residuei319PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei399PhosphoserineCombined sources1
Modified residuei401PhosphoserineCombined sources1
Modified residuei404PhosphothreonineCombined sources1
Modified residuei426N6-acetyllysine; alternateCombined sources1
Cross-linki426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources

Post-translational modificationi

Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6.6 Publications
Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7.1 Publication
O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei238 – 239Cleavage; by caspase-3, caspase-6 or caspase-72

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP05783.
MaxQBiP05783.
PaxDbiP05783.
PeptideAtlasiP05783.
PRIDEiP05783.
TopDownProteomicsiP05783.

2D gel databases

SWISS-2DPAGEP05783.

PTM databases

iPTMnetiP05783.
PhosphoSitePlusiP05783.
SwissPalmiP05783.
UniCarbKBiP05783.

Miscellaneous databases

PMAP-CutDBP05783.

Expressioni

Tissue specificityi

Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma.4 Publications

Inductioni

By IL6/interleukin-6.1 Publication

Gene expression databases

BgeeiENSG00000111057.
CleanExiHS_KRT18.
ExpressionAtlasiP05783. baseline and differential.
GenevisibleiP05783. HS.

Organism-specific databases

HPAiCAB000008.
CAB000030.
HPA001605.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. KRT18 associates with KRT8. 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. Interacts with FAM83H (PubMed:23902688). Interacts with EPPK1 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC146Q8IYE0-23EBI-297888,EBI-10247802
DNAJB6O751906EBI-297888,EBI-1053164
GOLGA2Q083793EBI-297888,EBI-618309
HAUS1Q96CS23EBI-297888,EBI-2514791
HGSO149643EBI-297888,EBI-740220
IKBKGQ9Y6K93EBI-297888,EBI-81279
KRT8P0578712EBI-297888,EBI-297852
NME7Q9Y5B83EBI-297888,EBI-744782
PKP1Q13835-24EBI-297888,EBI-9087684
TRADDQ1562811EBI-297888,EBI-359215

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110073. 90 interactors.
DIPiDIP-633N.
IntActiP05783. 64 interactors.
MINTiMINT-215967.
STRINGi9606.ENSP00000373487.

Structurei

3D structure databases

ProteinModelPortaliP05783.
SMRiP05783.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 79HeadAdd BLAST78
Regioni70 – 373Necessary for interaction with PNN1 PublicationAdd BLAST304
Regioni77 – 128Interaction with TRADD1 PublicationAdd BLAST52
Regioni80 – 387RodAdd BLAST308
Regioni80 – 115Coil 1AAdd BLAST36
Regioni116 – 132Linker 1Add BLAST17
Regioni133 – 224Coil 1BAdd BLAST92
Regioni225 – 248Linker 12Add BLAST24
Regioni243 – 391Interaction with DNAJB61 PublicationAdd BLAST149
Regioni249 – 387Coil 2Add BLAST139
Regioni388 – 430TailAdd BLAST43

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEYR. Eukaryota.
ENOG4111DJ8. LUCA.
GeneTreeiENSGT00760000119046.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP05783.
KOiK07604.
OMAiRAKYEKM.
OrthoDBiEOG091G0A3U.
PhylomeDBiP05783.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR
60 70 80 90 100
STSFRGGMGS GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS
110 120 130 140 150
LETENRRLES KIREHLEKKG PQVRDWSHYF KIIEDLRAQI FANTVDNARI
160 170 180 190 200
VLQIDNARLA ADDFRVKYET ELAMRQSVEN DIHGLRKVID DTNITRLQLE
210 220 230 240 250
TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP KSQDLAKIMA
260 270 280 290 300
DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR
310 320 330 340 350
RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA
360 370 380 390 400
QTRAEGQRQA QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN
410 420 430
SMQTIQKTTT RRIVDGKVVS ETNDTKVLRH
Length:430
Mass (Da):48,058
Last modified:January 23, 2007 - v2
Checksum:i1E5604C6BCC7A17A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti168Y → H in AAH00698 (PubMed:15489334).Curated1
Sequence conflicti202E → Q in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti208E → G in BAD96813 (Ref. 3) Curated1
Sequence conflicti246A → S in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti309D → R in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti312S → R in CAA31369 (PubMed:2422083).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023054103T → A in CIRRH. 1 PublicationCorresponds to variant rs61136606dbSNPEnsembl.1
Natural variantiVAR_003852128H → L in CIRRH; interfers with the ability to form normal filaments. 2 PublicationsCorresponds to variant rs57758506dbSNPEnsembl.1
Natural variantiVAR_023055230S → T.1 PublicationCorresponds to variant rs58472472dbSNPEnsembl.1
Natural variantiVAR_023056261R → Q in CIRRH. 1 PublicationCorresponds to variant rs57354642dbSNPEnsembl.1
Natural variantiVAR_023057340G → R in CIRRH. 1 PublicationCorresponds to variant rs57370769dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12881 mRNA. Translation: CAA31375.1.
AY762101 mRNA. Translation: AAX07828.1.
BT019412 mRNA. Translation: AAV38219.1.
AK223093 mRNA. Translation: BAD96813.1.
BC000180 mRNA. Translation: AAH00180.1.
BC000698 mRNA. Translation: AAH00698.1.
BC004253 mRNA. Translation: AAH04253.1.
BC008636 mRNA. Translation: AAH08636.1.
BC020982 mRNA. Translation: AAH20982.1.
BC072017 mRNA. Translation: AAH72017.1.
AF179904 Genomic DNA. Translation: AAA59461.1.
X12883 mRNA. Translation: CAA31377.1.
X12876 mRNA. Translation: CAA31369.1.
CCDSiCCDS31809.1.
PIRiS05481.
RefSeqiNP_000215.1. NM_000224.2.
NP_954657.1. NM_199187.1.
UniGeneiHs.406013.

Genome annotation databases

EnsembliENST00000388835; ENSP00000373487; ENSG00000111057.
ENST00000388837; ENSP00000373489; ENSG00000111057.
GeneIDi3875.
KEGGihsa:3875.
UCSCiuc001sbe.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12881 mRNA. Translation: CAA31375.1.
AY762101 mRNA. Translation: AAX07828.1.
BT019412 mRNA. Translation: AAV38219.1.
AK223093 mRNA. Translation: BAD96813.1.
BC000180 mRNA. Translation: AAH00180.1.
BC000698 mRNA. Translation: AAH00698.1.
BC004253 mRNA. Translation: AAH04253.1.
BC008636 mRNA. Translation: AAH08636.1.
BC020982 mRNA. Translation: AAH20982.1.
BC072017 mRNA. Translation: AAH72017.1.
AF179904 Genomic DNA. Translation: AAA59461.1.
X12883 mRNA. Translation: CAA31377.1.
X12876 mRNA. Translation: CAA31369.1.
CCDSiCCDS31809.1.
PIRiS05481.
RefSeqiNP_000215.1. NM_000224.2.
NP_954657.1. NM_199187.1.
UniGeneiHs.406013.

3D structure databases

ProteinModelPortaliP05783.
SMRiP05783.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110073. 90 interactors.
DIPiDIP-633N.
IntActiP05783. 64 interactors.
MINTiMINT-215967.
STRINGi9606.ENSP00000373487.

PTM databases

iPTMnetiP05783.
PhosphoSitePlusiP05783.
SwissPalmiP05783.
UniCarbKBiP05783.

Polymorphism and mutation databases

BioMutaiKRT18.
DMDMi125083.

2D gel databases

SWISS-2DPAGEP05783.

Proteomic databases

EPDiP05783.
MaxQBiP05783.
PaxDbiP05783.
PeptideAtlasiP05783.
PRIDEiP05783.
TopDownProteomicsiP05783.

Protocols and materials databases

DNASUi3875.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388835; ENSP00000373487; ENSG00000111057.
ENST00000388837; ENSP00000373489; ENSG00000111057.
GeneIDi3875.
KEGGihsa:3875.
UCSCiuc001sbe.4. human.

Organism-specific databases

CTDi3875.
DisGeNETi3875.
GeneCardsiKRT18.
H-InvDBHIX0040371.
HGNCiHGNC:6430. KRT18.
HPAiCAB000008.
CAB000030.
HPA001605.
MalaCardsiKRT18.
MIMi148070. gene.
215600. phenotype.
neXtProtiNX_P05783.
OpenTargetsiENSG00000111057.
PharmGKBiPA30217.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEYR. Eukaryota.
ENOG4111DJ8. LUCA.
GeneTreeiENSGT00760000119046.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP05783.
KOiK07604.
OMAiRAKYEKM.
OrthoDBiEOG091G0A3U.
PhylomeDBiP05783.
TreeFamiTF332742.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111057-MONOMER.
ReactomeiR-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.
SignaLinkiP05783.
SIGNORiP05783.

Miscellaneous databases

ChiTaRSiKRT18. human.
GeneWikiiKeratin_18.
GenomeRNAii3875.
PMAP-CutDBP05783.
PROiP05783.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111057.
CleanExiHS_KRT18.
ExpressionAtlasiP05783. baseline and differential.
GenevisibleiP05783. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK1C18_HUMAN
AccessioniPrimary (citable) accession number: P05783
Secondary accession number(s): Q53G38, Q5U0N8, Q9BW26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 193 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.