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Protein

Keratin, type II cytoskeletal 1

Gene

KRT1

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

Functioni

May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei433Stutter1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • receptor activity Source: UniProtKB
  • structural molecule activity Source: InterPro

GO - Biological processi

  • complement activation, lectin pathway Source: UniProtKB
  • establishment of skin barrier Source: Ensembl
  • fibrinolysis Source: UniProtKB
  • negative regulation of inflammatory response Source: Ensembl
  • regulation of angiogenesis Source: UniProtKB
  • response to oxidative stress Source: UniProtKB
  • retina homeostasis Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000167768-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 1
Alternative name(s):
67 kDa cytokeratin
Cytokeratin-1
Short name:
CK-1
Hair alpha protein
Keratin-1
Short name:
K1
Type-II keratin Kb1
Gene namesi
Name:KRT1
Synonyms:KRTA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6412. KRT1.

Subcellular locationi

  • Cell membrane 1 Publication

  • Note: Located on plasma membrane of neuroblastoma NMB7 cells.

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytoskeleton Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: UniProtKB
  • keratin filament Source: Ensembl
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Intermediate filament, Keratin, Membrane

Pathology & Biotechi

Involvement in diseasei

Epidermolytic hyperkeratosis (EHK)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop.
See also OMIM:113800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017820155V → D in EHK. 1 PublicationCorresponds to variant rs57959072dbSNPEnsembl.1
Natural variantiVAR_003853155V → G in EHK. 1 PublicationCorresponds to variant rs57959072dbSNPEnsembl.1
Natural variantiVAR_003854161L → P in EHK. 1 PublicationCorresponds to variant rs57695159dbSNPEnsembl.1
Natural variantiVAR_003855186S → P in EHK. 1 PublicationCorresponds to variant rs60022878dbSNPEnsembl.1
Natural variantiVAR_017821188N → K in EHK. 2 PublicationsCorresponds to variant rs59429455dbSNPEnsembl.1
Natural variantiVAR_003856188N → S in EHK. 3 PublicationsCorresponds to variant rs58928370dbSNPEnsembl.1
Natural variantiVAR_017822188N → T in EHK; severe. 1 PublicationCorresponds to variant rs58928370dbSNPEnsembl.1
Natural variantiVAR_003857193S → P in EHK. 1 PublicationCorresponds to variant rs60937700dbSNPEnsembl.1
Natural variantiVAR_017823214L → P in EHK. 1 PublicationCorresponds to variant rs61549035dbSNPEnsembl.1
Natural variantiVAR_017824340D → V in EHK. 1 PublicationCorresponds to variant rs58062863dbSNPEnsembl.1
Natural variantiVAR_071986478E → Q in EHK. 1 PublicationCorresponds to variant rs59089201dbSNPEnsembl.1
Natural variantiVAR_017826479I → T in AEI and EHK. 3 PublicationsCorresponds to variant rs57837128dbSNPEnsembl.1
Natural variantiVAR_017827482Y → C in EHK. 1 PublicationCorresponds to variant rs58420087dbSNPEnsembl.1
Natural variantiVAR_071987485L → P in EHK. 1 PublicationCorresponds to variant rs267607430dbSNPEnsembl.1
Natural variantiVAR_017828486L → P in EHK. 2 PublicationsCorresponds to variant rs56914602dbSNPEnsembl.1
Natural variantiVAR_071988490E → K in EHK. 1 PublicationCorresponds to variant rs60279707dbSNPEnsembl.1
Natural variantiVAR_003861490E → Q in EHK. 1 PublicationCorresponds to variant rs60279707dbSNPEnsembl.1
Ichthyosis hystrix, Curth-Macklin type (IHCM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA genodermatosis with severe verrucous hyperkeratosis. Affected individuals manifest congenital verrucous black scale on the scalp, neck, and limbs with truncal erythema, palmoplantar keratoderma and keratoses on the lips, ears, nipples and buttocks.
See also OMIM:146590
Keratoderma, palmoplantar, non-epidermolytic (NEPPK)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dermatological disorder characterized by well-demarcated hyperkeratosis is present over the palms and soles. A red band is frequently present at the periphery of the keratosis. It is usually non-transgredient, with a sharp demarcation of the lesions at the wrists.
See also OMIM:600962
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01781974K → I in NEPPK. 1 PublicationCorresponds to variant rs57977969dbSNPEnsembl.1
Ichthyosis annular epidermolytic (AEI)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months.
See also OMIM:607602
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017825479I → F in AEI. 2 PublicationsCorresponds to variant rs61218439dbSNPEnsembl.1
Natural variantiVAR_017826479I → T in AEI and EHK. 3 PublicationsCorresponds to variant rs57837128dbSNPEnsembl.1
Keratoderma, palmoplantar, striate 3 (SPPK3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dermatological disorder characterized by thickening of the stratum corneum and epidermal layers on palms and soles. There is no involvement of non-palmoplantar skin, and both hair and nails are normal.
See also OMIM:607654

Keywords - Diseasei

Disease mutation, Ichthyosis, Palmoplantar keratoderma

Organism-specific databases

DisGeNETi3848.
MalaCardsiKRT1.
MIMi113800. phenotype.
146590. phenotype.
600962. phenotype.
607602. phenotype.
607654. phenotype.
OpenTargetsiENSG00000167768.
Orphaneti281139. Annular epidermolytic ichthyosis.
312. Epidermolytic ichthyosis.
2199. Epidermolytic palmoplantar keratoderma.
79503. Ichthyosis hystrix of Curth-Macklin.
50942. Keratosis palmoplantaris striata.
PharmGKBiPA30199.

Polymorphism and mutation databases

BioMutaiKRT1.
DMDMi238054406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000637092 – 644Keratin, type II cytoskeletal 1Add BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineBy similarity1
Modified residuei18PhosphoserineBy similarity1
Modified residuei21PhosphoserineCombined sources1
Modified residuei45Omega-N-methylarginineBy similarity1
Modified residuei66PhosphoserineCombined sources1
Modified residuei82Omega-N-methylarginine1 Publication1
Modified residuei276N6,N6-dimethyllysine1 Publication1
Modified residuei344PhosphoserineCombined sources1
Modified residuei518Omega-N-methylarginineBy similarity1
Modified residuei588Omega-N-methylarginineBy similarity1

Post-translational modificationi

Undergoes deimination of some arginine residues (citrullination).2 Publications

Keywords - PTMi

Citrullination, Methylation, Phosphoprotein

Proteomic databases

EPDiP04264.
PaxDbiP04264.
PeptideAtlasiP04264.
PRIDEiP04264.

2D gel databases

REPRODUCTION-2DPAGEP04264.
SWISS-2DPAGEP04264.

PTM databases

iPTMnetiP04264.
PhosphoSitePlusiP04264.
SwissPalmiP04264.

Expressioni

Tissue specificityi

The source of this protein is neonatal foreskin. The 67-kDa type II keratins are expressed in terminally differentiating epidermis.

Gene expression databases

BgeeiENSG00000167768.
CleanExiHS_KRT1.
GenevisibleiP04264. HS.

Organism-specific databases

HPAiCAB002153.
HPA017917.
HPA062908.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Keratin-1 is generally associated with keratin-10. Interacts with ITGB1 in the presence of RACK1 and SRC, and with RACK1. Interacts with C1QBP; the association represents a cell surface kininogen receptor. Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (PubMed:16923132).3 Publications

Protein-protein interaction databases

BioGridi110046. 68 interactors.
IntActiP04264. 39 interactors.
MINTiMINT-4990403.
STRINGi9606.ENSP00000252244.

Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi387 – 476Combined sources90
Helixi478 – 488Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZRYX-ray3.30B370-489[»]
ProteinModelPortaliP04264.
SMRiP04264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 179HeadAdd BLAST178
Regioni180 – 489RodAdd BLAST310
Regioni180 – 215Coil 1AAdd BLAST36
Regioni216 – 234Linker 1Add BLAST19
Regioni235 – 326Coil 1BAdd BLAST92
Regioni327 – 350Linker 12Add BLAST24
Regioni351 – 489Coil 2Add BLAST139
Regioni490 – 644TailAdd BLAST155

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 151Gly/Phe/Ser-richAdd BLAST150
Compositional biasi502 – 641Gly/Ser-richAdd BLAST140

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP04264.
KOiK07605.
OMAiFLTTLYQ.
OrthoDBiEOG091G09KR.
PhylomeDBiP04264.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032449. Keratin_2_1_tail.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
PF16210. Keratin_2_tail. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
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.

P04264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG
60 70 80 90 100
GGGGSFGAGG GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG
110 120 130 140 150
GGGFGGGGFG GGGIGGGGFG GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG
160 170 180 190 200
GIQEVTINQS LLQPLNVEID PEIQKVKSRE REQIKSLNNQ FASFIDKVRF
210 220 230 240 250
LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR RVDQLKSDQS
260 270 280 290 300
RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD
310 320 330 340 350
LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI
360 370 380 390 400
IAEVKAQYED IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE
410 420 430 440 450
LNRVIQRLRS EIDNVKKQIS NLQQSISDAE QRGENALKDA KNKLNDLEDA
460 470 480 490 500
LQQAKEDLAR LLRDYQELMN TKLALDLEIA TYRTLLEGEE SRMSGECAPN
510 520 530 540 550
VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG SGGGGGGGRG
560 570 580 590 600
SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG
610 620 630 640
GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR
Length:644
Mass (Da):66,039
Last modified:May 26, 2009 - v6
Checksum:iCE5DDE97388F5017
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201L → M in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti206Q → K in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti238L → S in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti344 – 345SL → QF in AAA36153 (PubMed:2581964).Curated2
Sequence conflicti403R → H in BAG36698 (PubMed:14702039).Curated1
Sequence conflicti404V → M in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti447L → M in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti463R → C in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti466Q → H in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti504S → T in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti511 – 512TI → SM in AAA36153 (PubMed:2581964).Curated2
Sequence conflicti564G → S in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti613I → S in AAA36153 (PubMed:2581964).Curated1
Sequence conflicti638T → S in AAA36153 (PubMed:2581964).Curated1

Polymorphismi

There are two size variants of KRT1, termed allele 1A and allele 1B with allelic frequencies of 0.61 and 0.39. Allele 1B lacks 7 residues compared to allele 1A.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01781974K → I in NEPPK. 1 PublicationCorresponds to variant rs57977969dbSNPEnsembl.1
Natural variantiVAR_017820155V → D in EHK. 1 PublicationCorresponds to variant rs57959072dbSNPEnsembl.1
Natural variantiVAR_003853155V → G in EHK. 1 PublicationCorresponds to variant rs57959072dbSNPEnsembl.1
Natural variantiVAR_003854161L → P in EHK. 1 PublicationCorresponds to variant rs57695159dbSNPEnsembl.1
Natural variantiVAR_038627176 – 197Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas. Add BLAST22
Natural variantiVAR_003855186S → P in EHK. 1 PublicationCorresponds to variant rs60022878dbSNPEnsembl.1
Natural variantiVAR_017821188N → K in EHK. 2 PublicationsCorresponds to variant rs59429455dbSNPEnsembl.1
Natural variantiVAR_003856188N → S in EHK. 3 PublicationsCorresponds to variant rs58928370dbSNPEnsembl.1
Natural variantiVAR_017822188N → T in EHK; severe. 1 PublicationCorresponds to variant rs58928370dbSNPEnsembl.1
Natural variantiVAR_003857193S → P in EHK. 1 PublicationCorresponds to variant rs60937700dbSNPEnsembl.1
Natural variantiVAR_017823214L → P in EHK. 1 PublicationCorresponds to variant rs61549035dbSNPEnsembl.1
Natural variantiVAR_003858312I → V.1
Natural variantiVAR_003859330I → T.1
Natural variantiVAR_017824340D → V in EHK. 1 PublicationCorresponds to variant rs58062863dbSNPEnsembl.1
Natural variantiVAR_003860358Y → N.2 PublicationsCorresponds to variant rs1050872dbSNPEnsembl.1
Natural variantiVAR_038628454A → S.Corresponds to variant rs17678945dbSNPEnsembl.1
Natural variantiVAR_038629459 – 466Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas. 8
Natural variantiVAR_071986478E → Q in EHK. 1 PublicationCorresponds to variant rs59089201dbSNPEnsembl.1
Natural variantiVAR_017825479I → F in AEI. 2 PublicationsCorresponds to variant rs61218439dbSNPEnsembl.1
Natural variantiVAR_017826479I → T in AEI and EHK. 3 PublicationsCorresponds to variant rs57837128dbSNPEnsembl.1
Natural variantiVAR_017827482Y → C in EHK. 1 PublicationCorresponds to variant rs58420087dbSNPEnsembl.1
Natural variantiVAR_071987485L → P in EHK. 1 PublicationCorresponds to variant rs267607430dbSNPEnsembl.1
Natural variantiVAR_017828486L → P in EHK. 2 PublicationsCorresponds to variant rs56914602dbSNPEnsembl.1
Natural variantiVAR_071988490E → K in EHK. 1 PublicationCorresponds to variant rs60279707dbSNPEnsembl.1
Natural variantiVAR_003861490E → Q in EHK. 1 PublicationCorresponds to variant rs60279707dbSNPEnsembl.1
Natural variantiVAR_003862537G → C.1 Publication1
Natural variantiVAR_003864560 – 566Missing in allele 1B. 1 Publication7
Natural variantiVAR_003863633K → R.5 PublicationsCorresponds to variant rs14024dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98776 Genomic DNA. Translation: AAB47721.1.
AF237621 Genomic DNA. Translation: AAF60327.1.
AF304164 Genomic DNA. Translation: AAG41947.1.
AK313986 mRNA. Translation: BAG36698.1.
AC055716 Genomic DNA. No translation available.
BC063697 mRNA. Translation: AAH63697.1.
M10938 mRNA. Translation: AAA36153.1.
CCDSiCCDS8836.1.
PIRiA22940. KRHU2.
RefSeqiNP_006112.3. NM_006121.3.
UniGeneiHs.80828.

Genome annotation databases

EnsembliENST00000252244; ENSP00000252244; ENSG00000167768.
GeneIDi3848.
KEGGihsa:3848.
UCSCiuc001sau.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database
Wikipedia

Keratin-1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98776 Genomic DNA. Translation: AAB47721.1.
AF237621 Genomic DNA. Translation: AAF60327.1.
AF304164 Genomic DNA. Translation: AAG41947.1.
AK313986 mRNA. Translation: BAG36698.1.
AC055716 Genomic DNA. No translation available.
BC063697 mRNA. Translation: AAH63697.1.
M10938 mRNA. Translation: AAA36153.1.
CCDSiCCDS8836.1.
PIRiA22940. KRHU2.
RefSeqiNP_006112.3. NM_006121.3.
UniGeneiHs.80828.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZRYX-ray3.30B370-489[»]
ProteinModelPortaliP04264.
SMRiP04264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110046. 68 interactors.
IntActiP04264. 39 interactors.
MINTiMINT-4990403.
STRINGi9606.ENSP00000252244.

PTM databases

iPTMnetiP04264.
PhosphoSitePlusiP04264.
SwissPalmiP04264.

Polymorphism and mutation databases

BioMutaiKRT1.
DMDMi238054406.

2D gel databases

REPRODUCTION-2DPAGEP04264.
SWISS-2DPAGEP04264.

Proteomic databases

EPDiP04264.
PaxDbiP04264.
PeptideAtlasiP04264.
PRIDEiP04264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252244; ENSP00000252244; ENSG00000167768.
GeneIDi3848.
KEGGihsa:3848.
UCSCiuc001sau.1. human.

Organism-specific databases

CTDi3848.
DisGeNETi3848.
GeneCardsiKRT1.
H-InvDBHIX0036813.
HGNCiHGNC:6412. KRT1.
HPAiCAB002153.
HPA017917.
HPA062908.
MalaCardsiKRT1.
MIMi113800. phenotype.
139350. gene.
146590. phenotype.
600962. phenotype.
607602. phenotype.
607654. phenotype.
neXtProtiNX_P04264.
OpenTargetsiENSG00000167768.
Orphaneti281139. Annular epidermolytic ichthyosis.
312. Epidermolytic ichthyosis.
2199. Epidermolytic palmoplantar keratoderma.
79503. Ichthyosis hystrix of Curth-Macklin.
50942. Keratosis palmoplantaris striata.
PharmGKBiPA30199.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP04264.
KOiK07605.
OMAiFLTTLYQ.
OrthoDBiEOG091G09KR.
PhylomeDBiP04264.
TreeFamiTF317854.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000167768-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Miscellaneous databases

ChiTaRSiKRT1. human.
GeneWikiiKeratin_1.
GenomeRNAii3848.
PROiP04264.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167768.
CleanExiHS_KRT1.
GenevisibleiP04264. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032449. Keratin_2_1_tail.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
PF16210. Keratin_2_tail. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK2C1_HUMAN
AccessioniPrimary (citable) accession number: P04264
Secondary accession number(s): B2RA01
, P85925, P86104, Q14720, Q6GSJ0, Q9H298
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: May 26, 2009
Last modified: November 30, 2016
This is version 204 of the entry and version 6 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).

Caution

A peptide corresponding to residues 278 to 289 was isolated as part of plant proteomics studies and was originally thought to be of plant origin (PubMed:18602030, PubMed:19412582, PubMed:16529377). However, it was later shown that it is likely to be human type II keratin, a common contaminant in proteomic analyses (PubMed:23895828).1 Publication

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.