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P04264 (K2C1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
Hair alpha protein
Keratin-1
Short name=K1
Type-II keratin Kb1
Gene names
Name:KRT1
Synonyms:KRTA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length644 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). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK. Ref.15 Ref.20

Subunit structure

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 GNB2L1 and SRC, and with GNB2L1. Interacts with C1QBP; the association represents a cell surface kininogen receptor. Ref.15 Ref.20

Subcellular location

Cell membrane. Note: Located on plasma membrane of neuroblastoma NMB7 cells. Ref.15

Tissue specificity

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

Post-translational modification

Undergoes deimination of some arginine residues (citrullination).

Polymorphism

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.

Involvement in disease

Epidermolytic hyperkeratosis (EHK) [MIM:113800]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.30 Ref.32 Ref.33 Ref.34 Ref.36

Ichthyosis hystrix, Curth-Macklin type (IHCM) [MIM:146590]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Keratoderma, palmoplantar, non-epidermolytic (NEPPK) [MIM:600962]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.27

Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29 Ref.31

Keratoderma, palmoplantar, striate 3 (SPPK3) [MIM:607654]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

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.

Ontologies

Keywords
   Cellular componentCell membrane
Intermediate filament
Keratin
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Ichthyosis
Palmoplantar keratoderma
   DomainCoiled coil
   PTMCitrullination
Methylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcomplement activation, lectin pathway

Inferred from physical interaction PubMed 11549596. Source: UniProtKB

fibrinolysis

Non-traceable author statement PubMed 11290596. Source: UniProtKB

regulation of angiogenesis

Non-traceable author statement PubMed 11290596. Source: UniProtKB

response to oxidative stress

Non-traceable author statement PubMed 11549596. Source: UniProtKB

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytoskeleton

Traceable author statement Ref.21. Source: ProtInc

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 11487543PubMed 19199708. Source: UniProt

keratin filament

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 11290596. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from physical interaction PubMed 11549596. Source: UniProtKB

receptor activity

Non-traceable author statement PubMed 11290596. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 644643Keratin, type II cytoskeletal 1
PRO_0000063709

Regions

Region2 – 179178Head
Region180 – 489310Rod
Region180 – 21536Coil 1A
Region216 – 23419Linker 1
Region235 – 32692Coil 1B
Region327 – 35024Linker 12
Region351 – 489139Coil 2
Region490 – 644155Tail
Compositional bias2 – 151150Gly/Phe/Ser-rich
Compositional bias502 – 641140Gly/Ser-rich

Sites

Site4331Stutter

Amino acid modifications

Modified residue211Phosphoserine Ref.17 Ref.18
Modified residue661Phosphoserine Ref.16 Ref.18
Modified residue821Omega-N-methylarginine Ref.8
Modified residue2761N6,N6-dimethyllysine Ref.8
Modified residue3441Phosphoserine Ref.18

Natural variations

Natural variant741K → I in NEPPK. Ref.27
Corresponds to variant rs57977969 [ dbSNP | Ensembl ].
VAR_017819
Natural variant1551V → D in EHK. Ref.34
VAR_017820
Natural variant1551V → G in EHK. Ref.25
Corresponds to variant rs57959072 [ dbSNP | Ensembl ].
VAR_003853
Natural variant1611L → P in EHK. Ref.21
Corresponds to variant rs57695159 [ dbSNP | Ensembl ].
VAR_003854
Natural variant176 – 19722Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.
VAR_038627
Natural variant1861S → P in EHK. Ref.26
Corresponds to variant rs60022878 [ dbSNP | Ensembl ].
VAR_003855
Natural variant1881N → K in EHK. Ref.36
Corresponds to variant rs59429455 [ dbSNP | Ensembl ].
VAR_017821
Natural variant1881N → S in EHK. Ref.25 Ref.26
Corresponds to variant rs58928370 [ dbSNP | Ensembl ].
VAR_003856
Natural variant1881N → T in EHK; severe. Ref.30
VAR_017822
Natural variant1931S → P in EHK. Ref.25
Corresponds to variant rs60937700 [ dbSNP | Ensembl ].
VAR_003857
Natural variant2141L → P in EHK. Ref.32
Corresponds to variant rs61549035 [ dbSNP | Ensembl ].
VAR_017823
Natural variant3121I → V.
VAR_003858
Natural variant3301I → T.
VAR_003859
Natural variant3401D → V in EHK. Ref.28
Corresponds to variant rs58062863 [ dbSNP | Ensembl ].
VAR_017824
Natural variant3581Y → N. Ref.1 Ref.2
Corresponds to variant rs1050872 [ dbSNP | Ensembl ].
VAR_003860
Natural variant4541A → S.
Corresponds to variant rs17678945 [ dbSNP | Ensembl ].
VAR_038628
Natural variant459 – 4668Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.
VAR_038629
Natural variant4791I → F in AEI. Ref.29 Ref.31
Corresponds to variant rs61218439 [ dbSNP | Ensembl ].
VAR_017825
Natural variant4791I → T in AEI and EHK. Ref.29 Ref.33
Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
VAR_017826
Natural variant4821Y → C in EHK. Ref.24
Corresponds to variant rs58420087 [ dbSNP | Ensembl ].
VAR_017827
Natural variant4861L → P in EHK. Ref.36
Corresponds to variant rs56914602 [ dbSNP | Ensembl ].
VAR_017828
Natural variant4901E → Q in EHK. Ref.23
Corresponds to variant rs60279707 [ dbSNP | Ensembl ].
VAR_003861
Natural variant5371G → C. Ref.9
VAR_003862
Natural variant560 – 5667Missing in allele 1B.
VAR_003864
Natural variant6331K → R. Ref.1 Ref.2 Ref.3 Ref.6 Ref.9
Corresponds to variant rs14024 [ dbSNP | Ensembl ].
VAR_003863

Experimental info

Sequence conflict2011L → M in AAA36153. Ref.9
Sequence conflict2061Q → K in AAA36153. Ref.9
Sequence conflict2381L → S in AAA36153. Ref.9
Sequence conflict344 – 3452SL → QF in AAA36153. Ref.9
Sequence conflict4031R → H in BAG36698. Ref.4
Sequence conflict4041V → M in AAA36153. Ref.9
Sequence conflict4471L → M in AAA36153. Ref.9
Sequence conflict4631R → C in AAA36153. Ref.9
Sequence conflict4661Q → H in AAA36153. Ref.9
Sequence conflict5041S → T in AAA36153. Ref.9
Sequence conflict511 – 5122TI → SM in AAA36153. Ref.9
Sequence conflict5641G → S in AAA36153. Ref.9
Sequence conflict6131I → S in AAA36153. Ref.9
Sequence conflict6381T → S in AAA36153. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P04264 [UniParc].

Last modified May 26, 2009. Version 6.
Checksum: CE5DDE97388F5017

FASTA64466,039
        10         20         30         40         50         60 
MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG GGGGSFGAGG 

        70         80         90        100        110        120 
GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG GGGFGGGGFG GGGIGGGGFG 

       130        140        150        160        170        180 
GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG GIQEVTINQS LLQPLNVEID PEIQKVKSRE 

       190        200        210        220        230        240 
REQIKSLNNQ FASFIDKVRF LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR 

       250        260        270        280        290        300 
RVDQLKSDQS RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD 

       310        320        330        340        350        360 
LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI IAEVKAQYED 

       370        380        390        400        410        420 
IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE LNRVIQRLRS EIDNVKKQIS 

       430        440        450        460        470        480 
NLQQSISDAE QRGENALKDA KNKLNDLEDA LQQAKEDLAR LLRDYQELMN TKLALDLEIA 

       490        500        510        520        530        540 
TYRTLLEGEE SRMSGECAPN VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG 

       550        560        570        580        590        600 
SGGGGGGGRG SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG 

       610        620        630        640 
GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR 

« Hide

References

« Hide 'large scale' references
[1]"Structure of a gene for the human epidermal 67-kDa keratin."
Johnson L.D., Idler W.W., Zhou X.-M., Roop D.R., Steinert P.M.
Proc. Natl. Acad. Sci. U.S.A. 82:1896-1900(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-358 AND ARG-633.
[2]"Genomic organization and amplification of the human epidermal type II keratin genes K1 and K5."
Whittock N.V., Eady R.A.J., McGrath J.A.
Biochem. Biophys. Res. Commun. 274:149-152(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-358 AND ARG-633.
[3]"Novel splice site mutation in keratin 1 underlies mild epidermolytic palmoplantar keratoderma in three kindreds."
Hatsell S.J., Eady R.A.J., Wennerstrand L., Dopping-Hepenstal P.J., Leigh I.M., Munro C., Kelsell D.P.
J. Invest. Dermatol. 116:606-609(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NEPPK, VARIANT ARG-633.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANT ARG-633.
Tissue: Skin.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8.
Tissue: Platelet.
[8]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 13-30; 66-82; 186-240; 258-276; 278-298; 344-355; 365-386; 396-403; 408-416; 418-432; 442-455 AND 461-588, METHYLATION AT ARG-82 AND LYS-276, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[9]"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: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 152-644, VARIANTS CYS-537 AND ARG-633.
[10]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 377-386, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[11]"Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis."
Senshu T., Kan S., Ogawa H., Manabe M., Asaga H.
Biochem. Biophys. Res. Commun. 225:712-719(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION.
[12]"Evidence for novel functions of the keratin tail emerging from a mutation causing ichthyosis hystrix."
Sprecher E., Ishida-Yamamoto A., Becker O.M., Marekov L.N., Miller C.J., Steinert P.M., Neldner K., Richard G.
J. Invest. Dermatol. 116:511-519(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IHCM.
[13]"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.
[14]"Frameshift mutation in the V2 domain of human keratin 1 results in striate palmoplantar keratoderma."
Whittock N.V., Smith F.J., Wan H., Mallipeddi R., Griffiths W.A.D., Dopping-Hepenstal P.J., Ashton G.H.S., Eady R.A.J., McLean W.H.I., McGrath J.A.
J. Invest. Dermatol. 118:838-844(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SPPK3.
[15]"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."
Chuang N.N., Huang C.C.
Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GNB2L1 AND ITGB1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-66 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore)."
Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A., Bdeir K., Cines D.B., Colman R.W.
Thromb. Haemost. 105:1053-1059(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH C1QBP.
[21]"A leucine-->proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis."
Chipev C.C., Korge B.P., Markova N., Bale S.J., Digiovanna J.J., Compton J.G., Steinert P.M.
Cell 70:821-828(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK PRO-161.
[22]"The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain."
Korge B.P., Compton J.G., Steinert P.M., Mischke D.
J. Invest. Dermatol. 99:697-702(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALLELE 1B 560-GLY--TYR-566 DEL.
[23]"Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis."
Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A., Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R.
Science 257:1128-1130(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK GLN-490.
[24]"Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity."
Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.
J. Clin. Invest. 93:1533-1542(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK CYS-482.
[25]"Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis."
Yang J.-M., Chipev C.C., Digiovanna J.J., Bale S.J., Marekov L.N., Steinert P.M., Compton J.G.
J. Invest. Dermatol. 102:17-23(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EHK GLY-155; SER-188 AND PRO-193.
[26]"Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE)."
McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R., Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G., Morley S.M.
J. Invest. Dermatol. 102:24-30(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EHK PRO-186 AND SER-188.
[27]"A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar-plantar keratoderma."
Kimonis V., DiGiovanna J.J., Yang J.-M., Doyle S.Z., Bale S.J., Compton J.G.
J. Invest. Dermatol. 103:764-769(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NEPPK ILE-74.
[28]"An atypical form of bullous congenital ichthyosiform erythroderma is caused by a mutation in the L12 linker region of keratin 1."
Kremer H., Lavrijsen A.P., McLean W.H.I., Lane E.B., Melchers D., Ruiter D.J., Mariman E.C., Steijlen P.M.
J. Invest. Dermatol. 111:1224-1226(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK VAL-340.
[29]"Cyclic ichthyosis with epidermolytic hyperkeratosis: a phenotype conferred by mutations in the 2B domain of keratin K1."
Sybert V.P., Francis J.S., Corden L.D., Smith L.T., Weaver M., Stephens K., McLean W.H.I.
Am. J. Hum. Genet. 64:732-738(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AEI PHE-479 AND THR-479.
[30]"An asparagine to threonine substitution in the 1A domain of keratin 1: a novel mutation that causes epidermolytic hyperkeratosis."
Arin M.J., Longley M.A., Kuster W., Huber M., Hohl D., Rothnagel J.A., Roop D.R.
Exp. Dermatol. 8:124-127(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK THR-188.
[31]"Epidermolytic hyperkeratosis with polycyclic psoriasiform plaques resulting from a mutation in the keratin 1 gene."
Michael E.J., Schneiderman P., Grossman M.E., Christiano A.M.
Exp. Dermatol. 8:501-503(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AEI PHE-479.
[32]"Epidermolytic hyperkeratosis in a Hispanic family resulting from a mutation in the keratin 1 gene."
Cserhalmi-Friedman P.B., Squeo R., Gordon D., Garzon M., Schneiderman P., Grossman M.E., Christiano A.M.
Clin. Exp. Dermatol. 25:241-243(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK PRO-214.
[33]"Identification of a novel mutation in keratin 1 in a family with epidermolytic hyperkeratosis."
Arin M.J., Longley M.A., Epstein E.H. Jr., Rothnagel J.A., Roop D.R.
Exp. Dermatol. 9:16-19(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK THR-479.
[34]"New mutations in keratin 1 that cause bullous congenital ichthyosiform erythroderma and keratin 2e that cause ichthyosis bullosa of Siemens."
Whittock N.V., Ashton G.H.S., Griffiths W.A.D., Eady R.A.J., McGrath J.A.
Br. J. Dermatol. 145:330-335(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EHK ASP-155.
[35]"Two cases of primarily palmoplantar keratoderma associated with novel mutations in keratin 1."
Terron-Kwiatkowski A., Paller A.S., Compton J., Atherton D.J., McLean W.H., Irvine A.D.
J. Invest. Dermatol. 119:966-971(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PALMOPLANTAR KERATODERMA VAL-176--LYS-197 DEL AND ALA-459--466-GLN DEL.
[36]"Two novel mutations in the keratin 1 gene in epidermolytic hyperkeratosis."
Lee D.-Y., Ahn K.-S., Lee C.-H., Rho N.-K., Lee J.-H., Lee E.-S., Steinert P.M., Yang J.-M.
J. Invest. Dermatol. 119:976-977(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EHK LYS-188 AND PRO-486.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKRHU2. A22940.
RefSeqNP_006112.3. NM_006121.3.
UniGeneHs.80828.

3D structure databases

ProteinModelPortalP04264.
SMRP04264. Positions 178-319, 346-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110046. 60 interactions.
IntActP04264. 19 interactions.
MINTMINT-4990403.
STRING9606.ENSP00000252244.

PTM databases

PhosphoSiteP04264.

Polymorphism databases

DMDM238054406.

2D gel databases

REPRODUCTION-2DPAGEP04264.
SWISS-2DPAGEP04264.

Proteomic databases

PaxDbP04264.
PRIDEP04264.
ProMEXP04264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252244; ENSP00000252244; ENSG00000167768.
GeneID3848.
KEGGhsa:3848.
UCSCuc001sau.1. human.

Organism-specific databases

CTD3848.
GeneCardsGC12M053069.
H-InvDBHIX0036813.
HGNCHGNC:6412. KRT1.
HPACAB002153.
HPA017917.
MIM113800. phenotype.
139350. gene.
146590. phenotype.
600962. phenotype.
607602. phenotype.
607654. phenotype.
neXtProtNX_P04264.
Orphanet281139. Annular epidermolytic ichthyosis.
312. Epidermolytic ichthyosis.
2199. Epidermolytic palmoplantar keratoderma.
79503. Ichthyosis hystrix of Curth-Macklin.
50942. Keratosis palmoplantaris striata.
PharmGKBPA30199.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146769.
HOGENOMHOG000230976.
HOVERGENHBG013015.
InParanoidP04264.
KOK07605.
OMATHISETN.
OrthoDBEOG7FV3Q8.
PhylomeDBP04264.
TreeFamTF317854.

Gene expression databases

ArrayExpressP04264.
BgeeP04264.
CleanExHS_KRT1.
GenevestigatorP04264.

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

GeneWikiKeratin_1.
GenomeRNAi3848.
NextBio15141.
PROP04264.
SOURCESearch...

Entry information

Entry nameK2C1_HUMAN
AccessionPrimary (citable) accession number: P04264
Secondary accession number(s): B2RA01 expand/collapse secondary AC list , Q14720, Q6GSJ0, Q9H298
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: May 26, 2009
Last modified: April 16, 2014
This is version 174 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM