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Protein

Keratin, type II cytoskeletal 1

Gene

Krt1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei452Stutter1

GO - Molecular functioni

GO - Biological processi

  • complement activation, lectin pathway Source: MGI
  • establishment of skin barrier Source: MGI
  • negative regulation of inflammatory response Source: MGI
  • retina homeostasis Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.
R-MMU-6805567. Keratinization.
R-MMU-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
Keratin-1
Short name:
K1
Type-II keratin Kb1
Gene namesi
Name:Krt1
Synonyms:Krt2-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:96698. Krt1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Intermediate filament, Keratin, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Krt1 are a cause of epidermolytic hyperkeratosis (EHK); also known as bullous congenital ichthyosiform erythroderma (BIE). EHK is a hereditary skin disorder characterized by intraepidermal blistering, a marked thickening of the stratum corneum, pigmentation of the skin and erosions at sites of trauma which are all present from birth.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000637102 – 637Keratin, type II cytoskeletal 1Add BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineCombined sources1
Modified residuei18Asymmetric dimethylarginineBy similarity1
Modified residuei21PhosphoserineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei49Omega-N-methylarginineCombined sources1
Modified residuei67PhosphoserineBy similarity1
Modified residuei284N6,N6-dimethyllysineBy similarity1
Modified residuei352PhosphoserineBy similarity1
Modified residuei526Omega-N-methylarginineCombined sources1
Modified residuei585Omega-N-methylarginineCombined sources1
Modified residuei607Omega-N-methylarginineCombined sources1

Post-translational modificationi

Undergoes deimination of some arginine residues (citrullination).1 Publication

Keywords - PTMi

Citrullination, Methylation, Phosphoprotein

Proteomic databases

EPDiP04104.
MaxQBiP04104.
PaxDbiP04104.
PeptideAtlasiP04104.
PRIDEiP04104.

2D gel databases

SWISS-2DPAGEP04104.

PTM databases

iPTMnetiP04104.
PhosphoSitePlusiP04104.

Expressioni

Gene expression databases

BgeeiENSMUSG00000046834.
CleanExiMM_KRT1.
GenevisibleiP04104. MM.

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.By similarity

Protein-protein interaction databases

BioGridi201030. 11 interactors.
IntActiP04104. 3 interactors.
MINTiMINT-1865848.
STRINGi10090.ENSMUSP00000023790.

Structurei

3D structure databases

ProteinModelPortaliP04104.
SMRiP04104.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 187HeadAdd BLAST186
Regioni188 – 497RodAdd BLAST310
Regioni188 – 223Coil 1AAdd BLAST36
Regioni224 – 243Linker 1Add BLAST20
Regioni244 – 334Coil 1BAdd BLAST91
Regioni335 – 358Linker 12Add BLAST24
Regioni359 – 497Coil 2Add BLAST139
Regioni498 – 637TailAdd BLAST140

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili180 – 328Sequence analysisAdd BLAST149
Coiled coili397 – 483Sequence analysisAdd BLAST87

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi13 – 159Gly-richAdd BLAST147
Compositional biasi522 – 621Gly-richAdd BLAST100

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP04104.
KOiK07605.
OMAiFLTTLYQ.
OrthoDBiEOG091G09KR.
PhylomeDBiP04104.
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. 3 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.

P04104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQCSSRSL CRGGGGSRNF SSGSAGLVSF QRRSTSSSMR RSGGGGGGRF
60 70 80 90 100
SGGGFCGSSG SGFGSKSLMN LGGGRSISKS VAGGGGSFCG GFGGGSYGGG
110 120 130 140 150
GFGGGSYGGG GFGGGSFGGG GFGGSGFGGG LGGGGGFGSG GGFGGGRFGS
160 170 180 190 200
MGPVCPPGGI QEVTINQSLL QPLNVEVDPQ IQKVKSQERE QIKSLNDKFA
210 220 230 240 250
SFIDKVRFLE QQNQVLQTKW ELLQQVDTTT RTQNLDPFFE NYISILRRKV
260 270 280 290 300
DSLKSDQSRM DSELKNMQDL VEEYRTKYED EINKRTNAEN EFVTIKKDVD
310 320 330 340 350
SAYMTKVELQ AKADALQQDI DFFSALYQME MSQMQTQISE TNVVLSMDNN
360 370 380 390 400
RSLDLDGIIS EVKAQYDSIC QRSKAEAETF YQSKYEELQI TAGKHGDSVR
410 420 430 440 450
NTKMEISELN RMIQRLRSEI DGCKKQISQI QQNINDAEQR GEKALKDAQN
460 470 480 490 500
KLNEIEDALS QCKEDLARLL RDFQELMNTK LALDMEIATY KKLLEGEEIR
510 520 530 540 550
MSGECTPNVS VSVSTSHTSM SGSSSRGGGS GGGRYGGGGS YGGGSGGGSY
560 570 580 590 600
GGSSGGGGSG GSYGGGSGGG SYGGGSGGGS SGSHRGGSGG GGGSSGGSYG
610 620 630
GSSGGGRGGS SSGGGGVKSS GSSTVKFVST SYSRGTK
Length:637
Mass (Da):65,606
Last modified:February 20, 2007 - v4
Checksum:iD2016D15066FD0A5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti99G → R in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti131L → S in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti147R → T in BAB31776 (PubMed:16141072).Curated1
Sequence conflicti150 – 151SM → GY in AAD05191 (PubMed:2581964).Curated2
Sequence conflicti156 – 158PPG → SPS in AAD05191 (PubMed:2581964).Curated3
Sequence conflicti165I → L in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti176E → K in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti214Q → K in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti261D → E in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti313A → R in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti321D → N in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti325A → T in AAD05191 (PubMed:2581964).Curated1
Sequence conflicti352 – 353SL → QF in AAD05191 (PubMed:2581964).Curated2
Sequence conflicti428S → Y in BAB31776 (PubMed:16141072).Curated1
Sequence conflicti572 – 580Missing in AAD05191 (PubMed:2581964).Curated9

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti194S → P in EHK. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10937 mRNA. Translation: AAD05191.1.
AK019521 mRNA. Translation: BAB31776.1.
BC117842 mRNA. Translation: AAI17843.1.
BC117843 mRNA. Translation: AAI17844.1.
CCDSiCCDS37221.1.
PIRiA02951. KRMS2.
RefSeqiNP_032499.2. NM_008473.2.
UniGeneiMm.183137.

Genome annotation databases

EnsembliENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
GeneIDi16678.
KEGGimmu:16678.
UCSCiuc007xuc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10937 mRNA. Translation: AAD05191.1.
AK019521 mRNA. Translation: BAB31776.1.
BC117842 mRNA. Translation: AAI17843.1.
BC117843 mRNA. Translation: AAI17844.1.
CCDSiCCDS37221.1.
PIRiA02951. KRMS2.
RefSeqiNP_032499.2. NM_008473.2.
UniGeneiMm.183137.

3D structure databases

ProteinModelPortaliP04104.
SMRiP04104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201030. 11 interactors.
IntActiP04104. 3 interactors.
MINTiMINT-1865848.
STRINGi10090.ENSMUSP00000023790.

PTM databases

iPTMnetiP04104.
PhosphoSitePlusiP04104.

2D gel databases

SWISS-2DPAGEP04104.

Proteomic databases

EPDiP04104.
MaxQBiP04104.
PaxDbiP04104.
PeptideAtlasiP04104.
PRIDEiP04104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
GeneIDi16678.
KEGGimmu:16678.
UCSCiuc007xuc.1. mouse.

Organism-specific databases

CTDi3848.
MGIiMGI:96698. Krt1.

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP04104.
KOiK07605.
OMAiFLTTLYQ.
OrthoDBiEOG091G09KR.
PhylomeDBiP04104.
TreeFamiTF317854.

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.
R-MMU-6805567. Keratinization.
R-MMU-6809371. Formation of the cornified envelope.

Miscellaneous databases

ChiTaRSiKrt1. mouse.
PROiP04104.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000046834.
CleanExiMM_KRT1.
GenevisibleiP04104. MM.

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. 3 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_MOUSE
AccessioniPrimary (citable) accession number: P04104
Secondary accession number(s): Q149E0, Q9D2K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: February 20, 2007
Last modified: November 30, 2016
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.