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P04104 (K2C1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Krt1
Synonyms:Krt2-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cell membrane By similarity.

Post-translational modification

Undergoes deimination of some arginine residues (citrullination).

Involvement in disease

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. Ref.7

Miscellaneous

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

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 637636Keratin, type II cytoskeletal 1
PRO_0000063710

Regions

Region2 – 187186Head
Region188 – 497310Rod
Region188 – 22336Coil 1A
Region224 – 24320Linker 1
Region244 – 33491Coil 1B
Region335 – 35824Linker 12
Region359 – 497139Coil 2
Region498 – 637140Tail
Coiled coil180 – 328149 Potential
Coiled coil397 – 48387 Potential
Compositional bias13 – 159147Gly-rich
Compositional bias522 – 621100Gly-rich

Sites

Site4521Stutter

Amino acid modifications

Modified residue241Phosphoserine By similarity
Modified residue671Phosphoserine By similarity
Modified residue2841N6,N6-dimethyllysine By similarity
Modified residue3521Phosphoserine By similarity

Natural variations

Natural variant1941S → P in EHK. Ref.7

Experimental info

Sequence conflict991G → R in AAD05191. Ref.1
Sequence conflict1311L → S in AAD05191. Ref.1
Sequence conflict1471R → T in BAB31776. Ref.3
Sequence conflict150 – 1512SM → GY in AAD05191. Ref.1
Sequence conflict156 – 1583PPG → SPS in AAD05191. Ref.1
Sequence conflict1651I → L in AAD05191. Ref.1
Sequence conflict1761E → K in AAD05191. Ref.1
Sequence conflict2141Q → K in AAD05191. Ref.1
Sequence conflict2611D → E in AAD05191. Ref.1
Sequence conflict3131A → R in AAD05191. Ref.1
Sequence conflict3211D → N in AAD05191. Ref.1
Sequence conflict3251A → T in AAD05191. Ref.1
Sequence conflict352 – 3532SL → QF in AAD05191. Ref.1
Sequence conflict4281S → Y in BAB31776. Ref.3
Sequence conflict572 – 5809Missing in AAD05191. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04104 [UniParc].

Last modified February 20, 2007. Version 4.
Checksum: D2016D15066FD0A5

FASTA63765,606
        10         20         30         40         50         60 
MSLQCSSRSL CRGGGGSRNF SSGSAGLVSF QRRSTSSSMR RSGGGGGGRF SGGGFCGSSG 

        70         80         90        100        110        120 
SGFGSKSLMN LGGGRSISKS VAGGGGSFCG GFGGGSYGGG GFGGGSYGGG GFGGGSFGGG 

       130        140        150        160        170        180 
GFGGSGFGGG LGGGGGFGSG GGFGGGRFGS MGPVCPPGGI QEVTINQSLL QPLNVEVDPQ 

       190        200        210        220        230        240 
IQKVKSQERE QIKSLNDKFA SFIDKVRFLE QQNQVLQTKW ELLQQVDTTT RTQNLDPFFE 

       250        260        270        280        290        300 
NYISILRRKV DSLKSDQSRM DSELKNMQDL VEEYRTKYED EINKRTNAEN EFVTIKKDVD 

       310        320        330        340        350        360 
SAYMTKVELQ AKADALQQDI DFFSALYQME MSQMQTQISE TNVVLSMDNN RSLDLDGIIS 

       370        380        390        400        410        420 
EVKAQYDSIC QRSKAEAETF YQSKYEELQI TAGKHGDSVR NTKMEISELN RMIQRLRSEI 

       430        440        450        460        470        480 
DGCKKQISQI QQNINDAEQR GEKALKDAQN KLNEIEDALS QCKEDLARLL RDFQELMNTK 

       490        500        510        520        530        540 
LALDMEIATY KKLLEGEEIR MSGECTPNVS VSVSTSHTSM SGSSSRGGGS GGGRYGGGGS 

       550        560        570        580        590        600 
YGGGSGGGSY GGSSGGGGSG GSYGGGSGGG SYGGGSGGGS SGSHRGGSGG GGGSSGGSYG 

       610        620        630 
GSSGGGRGGS SSGGGGVKSS GSSTVKFVST SYSRGTK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10937 mRNA. Translation: AAD05191.1.
AK019521 mRNA. Translation: BAB31776.1.
BC117842 mRNA. Translation: AAI17843.1.
BC117843 mRNA. Translation: AAI17844.1.
CCDSCCDS37221.1.
PIRKRMS2. A02951.
RefSeqNP_032499.2. NM_008473.2.
UniGeneMm.183137.

3D structure databases

ProteinModelPortalP04104.
SMRP04104. Positions 186-327, 354-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201030. 11 interactions.
IntActP04104. 2 interactions.
MINTMINT-1865848.

PTM databases

PhosphoSiteP04104.

2D gel databases

SWISS-2DPAGEP04104.

Proteomic databases

MaxQBP04104.
PaxDbP04104.
PRIDEP04104.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
GeneID16678.
KEGGmmu:16678.
UCSCuc007xuc.1. mouse.

Organism-specific databases

CTD3848.
MGIMGI:96698. Krt1.

Phylogenomic databases

eggNOGNOG146769.
GeneTreeENSGT00730000110687.
HOGENOMHOG000230976.
HOVERGENHBG013015.
InParanoidP04104.
KOK07605.
OMATHISETN.
OrthoDBEOG7FV3Q8.
PhylomeDBP04104.
TreeFamTF317854.

Gene expression databases

BgeeP04104.
CleanExMM_KRT1.
GenevestigatorP04104.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01276. TYPE2KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKRT1. mouse.
NextBio290417.
PROP04104.
SOURCESearch...

Entry information

Entry nameK2C1_MOUSE
AccessionPrimary (citable) accession number: P04104
Secondary accession number(s): Q149E0, Q9D2K8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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