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P04104

- K2C1_MOUSE

UniProt

P04104 - K2C1_MOUSE

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Protein

Keratin, type II cytoskeletal 1

Gene

Krt1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 kinase C (RACK1/GNB2L1). activated protein kinase C (RACK1/GNB2L1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei452 – 4521Stutter

GO - Molecular functioni

  1. carbohydrate binding Source: Ensembl
  2. structural molecule activity Source: InterPro

GO - Biological processi

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

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
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:96698. Krt1.

Subcellular locationi

Cell membrane By similarity

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. extracellular matrix Source: UniProtKB
  3. extracellular vesicular exosome Source: Ensembl
  4. keratin filament Source: MGI
  5. nucleus Source: Ensembl
  6. plasma membrane Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 637636Keratin, type II cytoskeletal 1PRO_0000063710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei284 – 2841N6,N6-dimethyllysineBy similarity
Modified residuei352 – 3521PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP04104.
PaxDbiP04104.
PRIDEiP04104.

2D gel databases

SWISS-2DPAGEP04104.

PTM databases

PhosphoSiteiP04104.

Expressioni

Gene expression databases

BgeeiP04104.
CleanExiMM_KRT1.
GenevestigatoriP04104.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Keratin-1 is generally associated with keratin-10. Interacts with ITB1 in the presence of GNB2L1 and SRC, and with GNB2L1 Interacts with C1QBP; the association represents a cell surface kininogen receptor (By similarity).By similarity

Protein-protein interaction databases

BioGridi201030. 11 interactions.
IntActiP04104. 2 interactions.
MINTiMINT-1865848.

Structurei

3D structure databases

ProteinModelPortaliP04104.
SMRiP04104. Positions 186-327, 354-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 187186HeadAdd
BLAST
Regioni188 – 497310RodAdd
BLAST
Regioni188 – 22336Coil 1AAdd
BLAST
Regioni224 – 24320Linker 1Add
BLAST
Regioni244 – 33491Coil 1BAdd
BLAST
Regioni335 – 35824Linker 12Add
BLAST
Regioni359 – 497139Coil 2Add
BLAST
Regioni498 – 637140TailAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili180 – 328149Sequence AnalysisAdd
BLAST
Coiled coili397 – 48387Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 159147Gly-richAdd
BLAST
Compositional biasi522 – 621100Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146769.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP04104.
KOiK07605.
OMAiTHISETN.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP04104.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991G → R in AAD05191. (PubMed:2581964)Curated
Sequence conflicti131 – 1311L → S in AAD05191. (PubMed:2581964)Curated
Sequence conflicti147 – 1471R → T in BAB31776. (PubMed:16141072)Curated
Sequence conflicti150 – 1512SM → GY in AAD05191. (PubMed:2581964)Curated
Sequence conflicti156 – 1583PPG → SPS in AAD05191. (PubMed:2581964)Curated
Sequence conflicti165 – 1651I → L in AAD05191. (PubMed:2581964)Curated
Sequence conflicti176 – 1761E → K in AAD05191. (PubMed:2581964)Curated
Sequence conflicti214 – 2141Q → K in AAD05191. (PubMed:2581964)Curated
Sequence conflicti261 – 2611D → E in AAD05191. (PubMed:2581964)Curated
Sequence conflicti313 – 3131A → R in AAD05191. (PubMed:2581964)Curated
Sequence conflicti321 – 3211D → N in AAD05191. (PubMed:2581964)Curated
Sequence conflicti325 – 3251A → T in AAD05191. (PubMed:2581964)Curated
Sequence conflicti352 – 3532SL → QF in AAD05191. (PubMed:2581964)Curated
Sequence conflicti428 – 4281S → Y in BAB31776. (PubMed:16141072)Curated
Sequence conflicti572 – 5809Missing in AAD05191. (PubMed:2581964)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti194 – 1941S → P in EHK. 1 Publication

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 .
CCDSi CCDS37221.1.
PIRi A02951. KRMS2.
RefSeqi NP_032499.2. NM_008473.2.
UniGenei Mm.183137.

3D structure databases

ProteinModelPortali P04104.
SMRi P04104. Positions 186-327, 354-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201030. 11 interactions.
IntActi P04104. 2 interactions.
MINTi MINT-1865848.

PTM databases

PhosphoSitei P04104.

2D gel databases

SWISS-2DPAGE P04104.

Proteomic databases

MaxQBi P04104.
PaxDbi P04104.
PRIDEi P04104.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023790 ; ENSMUSP00000023790 ; ENSMUSG00000046834 .
GeneIDi 16678.
KEGGi mmu:16678.
UCSCi uc007xuc.1. mouse.

Organism-specific databases

CTDi 3848.
MGIi MGI:96698. Krt1.

Phylogenomic databases

eggNOGi NOG146769.
GeneTreei ENSGT00760000118796.
HOGENOMi HOG000230976.
HOVERGENi HBG013015.
InParanoidi P04104.
KOi K07605.
OMAi THISETN.
OrthoDBi EOG7FV3Q8.
PhylomeDBi P04104.
TreeFami TF317854.

Miscellaneous databases

ChiTaRSi Krt1. mouse.
NextBioi 290417.
PROi P04104.
SOURCEi Search...

Gene expression databases

Bgeei P04104.
CleanExi MM_KRT1.
Genevestigatori P04104.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01276. TYPE2KERATIN.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits."
    Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C., Roop D.R.
    J. Biol. Chem. 260:7142-7149(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Roop D.R.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 199-205; 208-219 AND 286-296, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination."
    Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H., Akiyama M., Iizuka H.
    J. Invest. Dermatol. 118:282-287(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CITRULLINATION.
  7. "A mouse keratin 1 mutation causes dark skin and epidermolytic hyperkeratosis."
    McGowan K.A., Aradhya S., Fuchs H., de Angelis M.H., Barsh G.S.
    J. Invest. Dermatol. 126:1013-1016(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EHK PRO-194.

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 26, 2014
This is version 130 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

External Data

Dasty 3