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Protein

Keratin, type II cytoskeletal 8

Gene

KRT8

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

Functioni

Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei342Stutter1

GO - Molecular functioni

  • scaffold protein binding Source: BHF-UCL
  • structural molecule activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170421-MONOMER.
ReactomeiR-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.
SignaLinkiP05787.
SIGNORiP05787.

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 8
Alternative name(s):
Cytokeratin-8
Short name:
CK-8
Keratin-8
Short name:
K8
Type-II keratin Kb8
Gene namesi
Name:KRT8
Synonyms:CYK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6446. KRT8.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • costamere Source: Ensembl
  • cytoplasm Source: UniProtKB
  • dystrophin-associated glycoprotein complex Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • intermediate filament Source: BHF-UCL
  • keratin filament Source: Ensembl
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • sarcolemma Source: Ensembl
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cirrhosis (CIRRH)1 Publication
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_02305853G → V in CIRRH. 1 PublicationCorresponds to variant rs61710484dbSNPEnsembl.1
Natural variantiVAR_02305954Y → C in CIRRH. 1 Publication1
Natural variantiVAR_02306062G → C in CIRRH. 2 PublicationsCorresponds to variant rs11554495dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72L → P: Increases phosphorylation. 1 Publication1
Mutagenesisi74S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. 1 Publication1
Mutagenesisi74S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3856.
MalaCardsiKRT8.
MIMi215600. phenotype.
OpenTargetsiENSG00000170421.
PharmGKBiPA30234.

Chemistry databases

DrugBankiDB00031. Tenecteplase.

Polymorphism and mutation databases

BioMutaiKRT8.
DMDMi90110027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000637401 – 483Keratin, type II cytoskeletal 8Add BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Phosphoserine; by PKC/PRKCE1 Publication1
Modified residuei13PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei22PhosphoserineCombined sources1
Modified residuei23Omega-N-methylarginineCombined sources1
Modified residuei24Phosphoserine; by PKC/PRKCECombined sources2 Publications1
Modified residuei26PhosphothreonineBy similarity1
Modified residuei27PhosphoserineCombined sources1
Modified residuei31PhosphoserineCombined sources1
Modified residuei32Omega-N-methylarginineCombined sources1
Modified residuei34PhosphoserineCombined sources1
Modified residuei37PhosphoserineBy similarity1
Modified residuei39PhosphoserineCombined sources1
Modified residuei40Omega-N-methylarginineCombined sources1
Modified residuei43PhosphoserineCombined sources1
Modified residuei44PhosphoserineBy similarity1
Modified residuei47Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei47Omega-N-methylarginine; alternateCombined sources1
Modified residuei74Phosphoserine; by MAPK2 Publications1
Modified residuei101N6-malonyllysine1 Publication1
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei207N6-acetyllysineCombined sources1
Modified residuei228PhosphotyrosineCombined sources1
Modified residuei253PhosphoserineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei274PhosphoserineCombined sources1
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei291PhosphoserineCombined sources1
Modified residuei295N6-acetyllysineCombined sources1
Cross-linki304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei325N6-acetyllysineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei404PhosphoserineCombined sources1
Modified residuei410PhosphoserineCombined sources1
Modified residuei417PhosphoserineBy similarity1
Modified residuei424PhosphoserineBy similarity1
Modified residuei432Phosphoserine; by CaMK2 and MAPKCombined sources1 Publication1
Cross-linki472Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki472Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei475PhosphoserineCombined sources1
Modified residuei477PhosphoserineCombined sources1
Modified residuei478PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization.4 Publications
O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation.
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.

Keywords - PTMi

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

Proteomic databases

EPDiP05787.
PaxDbiP05787.
PeptideAtlasiP05787.
PRIDEiP05787.
TopDownProteomicsiP05787-1. [P05787-1]
P05787-2. [P05787-2]

2D gel databases

SWISS-2DPAGEP05787.

PTM databases

iPTMnetiP05787.
PhosphoSitePlusiP05787.
SwissPalmiP05787.
UniCarbKBiP05787.

Miscellaneous databases

PMAP-CutDBP05787.

Expressioni

Tissue specificityi

Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma membrane in structures that contain dystrophin and spectrin. Expressed in gingival mucosa and hard palate of the oral cavity.2 Publications

Gene expression databases

BgeeiENSG00000170421.
ExpressionAtlasiP05787. baseline and differential.
GenevisibleiP05787. HS.

Organism-specific databases

HPAiCAB000131.
CAB001696.
HPA049866.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with HCV core protein and PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1. Interacts with GPER1. Interacts with EPPK1 (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CFTRP135697EBI-297852,EBI-349854
GRB2P629933EBI-297852,EBI-401755
IKBKGQ9Y6K92EBI-297852,EBI-81279
KRT13A1A4E93EBI-10194642,EBI-10171552
KRT15P190123EBI-297852,EBI-739566
KRT18P0578312EBI-297852,EBI-297888
KRT31Q153235EBI-297852,EBI-948001
KRT38O760155EBI-297852,EBI-1047263
KRT40Q6A1625EBI-297852,EBI-10171697
PKP1Q13835-23EBI-297852,EBI-9087684
taxP140793EBI-297852,EBI-9675698From a different organism.
TFIP11Q9UBB93EBI-297852,EBI-1105213

GO - Molecular functioni

  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110054. 53 interactors.
DIPiDIP-424N.
IntActiP05787. 44 interactors.
MINTiMINT-256526.
STRINGi9606.ENSP00000293308.

Structurei

3D structure databases

ProteinModelPortaliP05787.
SMRiP05787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 90HeadAdd BLAST90
Regioni91 – 398RodAdd BLAST308
Regioni91 – 126Coil 1AAdd BLAST36
Regioni127 – 143Linker 1Add BLAST17
Regioni144 – 235Coil 1BAdd BLAST92
Regioni236 – 259Linker 12Add BLAST24
Regioni260 – 398Coil 2Add BLAST139
Regioni261 – 382Necessary for interaction with PNN1 PublicationAdd BLAST122
Regioni399 – 483TailAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 49Ser-richAdd BLAST41

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOVERGENiHBG013015.
InParanoidiP05787.
KOiK07605.
OMAiIKGQRAN.
OrthoDBiEOG091G09KR.
PhylomeDBiP05787.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05787-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL
60 70 80 90 100
GGGYGGASGM GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN
110 120 130 140 150
KFASFIDKVR FLEQQNKMLE TKWSLLQQQK TARSNMDNMF ESYINNLRRQ
160 170 180 190 200
LETLGQEKLK LEAELGNMQG LVEDFKNKYE DEINKRTEME NEFVLIKKDV
210 220 230 240 250
DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS DTSVVLSMDN
260 270 280 290 300
SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL
310 320 330 340 350
RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN
360 370 380 390 400
AKLSELEAAL QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES
410 420 430 440 450
RLESGMQNMS IHTKTTSGYA GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS
460 470 480
SFSRTSSSRA VVVKKIETRD GKLVSESSDV LPK
Length:483
Mass (Da):53,704
Last modified:January 23, 2007 - v7
Checksum:iB0BC730B65929D37
GO
Isoform 2 (identifier: P05787-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MNGVSWSQDLQEGISAWFGPPASTPASTM

Note: No experimental confirmation available.
Show »
Length:511
Mass (Da):56,608
Checksum:iDB55C0367CD6C37C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56G → V in BAF83627 (PubMed:14702039).Curated1
Sequence conflicti77V → S in AAA35748 (PubMed:1692965).Curated1
Sequence conflicti201D → DVD in CAA52882 (PubMed:1705144).Curated1
Sequence conflicti232I → L in CAA67203 (PubMed:2434381).Curated1
Sequence conflicti257D → E in AAA35748 (PubMed:1692965).Curated1
Sequence conflicti310M → I in CAA31376 (PubMed:2434381).Curated1
Sequence conflicti324L → F in BAD96661 (Ref. 6) Curated1
Sequence conflicti384L → M in CAA67203 (PubMed:2434381).Curated1
Sequence conflicti387E → D in AAA35748 (PubMed:1692965).Curated1
Sequence conflicti401R → P in AAA35748 (PubMed:1692965).Curated1
Sequence conflicti430 – 433LTSP → SQA in AAA35763 (PubMed:1691124).Curated4
Sequence conflicti431T → A in CAA67203 (PubMed:2434381).Curated1
Sequence conflicti432S → D in AAA35748 (PubMed:1692965).Curated1
Sequence conflicti432S → D in CAA67203 (PubMed:2434381).Curated1
Sequence conflicti432S → D in CAA31376 (PubMed:2434381).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02305853G → V in CIRRH. 1 PublicationCorresponds to variant rs61710484dbSNPEnsembl.1
Natural variantiVAR_02305954Y → C in CIRRH. 1 Publication1
Natural variantiVAR_02306062G → C in CIRRH. 2 PublicationsCorresponds to variant rs11554495dbSNPEnsembl.1
Natural variantiVAR_02306163I → V.1 PublicationCorresponds to variant rs59536457dbSNPEnsembl.1
Natural variantiVAR_049805401R → W.Corresponds to variant rs2277330dbSNPEnsembl.1
Natural variantiVAR_069106417S → G.2 PublicationsCorresponds to variant rs1065591dbSNPEnsembl.1
Natural variantiVAR_069107429G → D.1 PublicationCorresponds to variant rs1065648dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0460001M → MNGVSWSQDLQEGISAWFGP PASTPASTM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34482 Genomic DNA. Translation: AAA35763.1.
M34225 mRNA. Translation: AAA35748.1.
X74929 mRNA. Translation: CAA52882.1.
X74981 Genomic DNA. Translation: CAA52916.1.
U76549 mRNA. Translation: AAB18966.1.
AK290938 mRNA. Translation: BAF83627.1.
AK310257 mRNA. No translation available.
AK315826 mRNA. Translation: BAF98717.1.
AK222941 mRNA. Translation: BAD96661.1.
AC107016 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96653.1.
BC000654 mRNA. Translation: AAH00654.3.
BC063513 mRNA. Translation: AAH63513.2.
BC073760 mRNA. Translation: AAH73760.1.
BC075839 mRNA. Translation: AAH75839.1.
M26512 mRNA. Translation: AAA51542.1.
X12882 mRNA. Translation: CAA31376.1.
X98614 mRNA. Translation: CAA67203.1.
CCDSiCCDS58234.1. [P05787-2]
CCDS8841.1. [P05787-1]
PIRiA34720.
RefSeqiNP_001243222.1. NM_001256293.1. [P05787-1]
NP_002264.1. NM_002273.3. [P05787-1]
UniGeneiHs.533782.
Hs.708445.

Genome annotation databases

EnsembliENST00000293308; ENSP00000293308; ENSG00000170421. [P05787-1]
ENST00000546897; ENSP00000447402; ENSG00000170421. [P05787-1]
ENST00000552150; ENSP00000449404; ENSG00000170421. [P05787-2]
ENST00000552551; ENSP00000447566; ENSG00000170421. [P05787-1]
GeneIDi3856.
KEGGihsa:3856.
UCSCiuc001sbd.3. human. [P05787-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34482 Genomic DNA. Translation: AAA35763.1.
M34225 mRNA. Translation: AAA35748.1.
X74929 mRNA. Translation: CAA52882.1.
X74981 Genomic DNA. Translation: CAA52916.1.
U76549 mRNA. Translation: AAB18966.1.
AK290938 mRNA. Translation: BAF83627.1.
AK310257 mRNA. No translation available.
AK315826 mRNA. Translation: BAF98717.1.
AK222941 mRNA. Translation: BAD96661.1.
AC107016 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96653.1.
BC000654 mRNA. Translation: AAH00654.3.
BC063513 mRNA. Translation: AAH63513.2.
BC073760 mRNA. Translation: AAH73760.1.
BC075839 mRNA. Translation: AAH75839.1.
M26512 mRNA. Translation: AAA51542.1.
X12882 mRNA. Translation: CAA31376.1.
X98614 mRNA. Translation: CAA67203.1.
CCDSiCCDS58234.1. [P05787-2]
CCDS8841.1. [P05787-1]
PIRiA34720.
RefSeqiNP_001243222.1. NM_001256293.1. [P05787-1]
NP_002264.1. NM_002273.3. [P05787-1]
UniGeneiHs.533782.
Hs.708445.

3D structure databases

ProteinModelPortaliP05787.
SMRiP05787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110054. 53 interactors.
DIPiDIP-424N.
IntActiP05787. 44 interactors.
MINTiMINT-256526.
STRINGi9606.ENSP00000293308.

Chemistry databases

DrugBankiDB00031. Tenecteplase.

PTM databases

iPTMnetiP05787.
PhosphoSitePlusiP05787.
SwissPalmiP05787.
UniCarbKBiP05787.

Polymorphism and mutation databases

BioMutaiKRT8.
DMDMi90110027.

2D gel databases

SWISS-2DPAGEP05787.

Proteomic databases

EPDiP05787.
PaxDbiP05787.
PeptideAtlasiP05787.
PRIDEiP05787.
TopDownProteomicsiP05787-1. [P05787-1]
P05787-2. [P05787-2]

Protocols and materials databases

DNASUi3856.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293308; ENSP00000293308; ENSG00000170421. [P05787-1]
ENST00000546897; ENSP00000447402; ENSG00000170421. [P05787-1]
ENST00000552150; ENSP00000449404; ENSG00000170421. [P05787-2]
ENST00000552551; ENSP00000447566; ENSG00000170421. [P05787-1]
GeneIDi3856.
KEGGihsa:3856.
UCSCiuc001sbd.3. human. [P05787-1]

Organism-specific databases

CTDi3856.
DisGeNETi3856.
GeneCardsiKRT8.
H-InvDBHIX0026255.
HIX0034365.
HIX0168895.
HGNCiHGNC:6446. KRT8.
HPAiCAB000131.
CAB001696.
HPA049866.
MalaCardsiKRT8.
MIMi148060. gene.
215600. phenotype.
neXtProtiNX_P05787.
OpenTargetsiENSG00000170421.
PharmGKBiPA30234.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOVERGENiHBG013015.
InParanoidiP05787.
KOiK07605.
OMAiIKGQRAN.
OrthoDBiEOG091G09KR.
PhylomeDBiP05787.
TreeFamiTF317854.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170421-MONOMER.
ReactomeiR-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.
SignaLinkiP05787.
SIGNORiP05787.

Miscellaneous databases

ChiTaRSiKRT8. human.
GeneWikiiKeratin_8.
GenomeRNAii3856.
PMAP-CutDBP05787.
PROiP05787.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170421.
ExpressionAtlasiP05787. baseline and differential.
GenevisibleiP05787. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK2C8_HUMAN
AccessioniPrimary (citable) accession number: P05787
Secondary accession number(s): A8K4H3
, B0AZN5, F8VXB4, Q14099, Q14716, Q14717, Q53GJ0, Q6DHW5, Q6GMY0, Q6P4C7, Q96J60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 203 of the entry and version 7 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.