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P04264

- K2C1_HUMAN

UniProt

P04264 - K2C1_HUMAN

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Protein
Keratin, type II cytoskeletal 1
Gene
KRT1, KRTA
Organism
Homo sapiens (Human)
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). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei433 – 4331Stutter

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. receptor activity Source: UniProtKB
  4. structural molecule activity Source: InterPro

GO - Biological processi

  1. complement activation, lectin pathway Source: UniProtKB
  2. fibrinolysis Source: UniProtKB
  3. regulation of angiogenesis Source: UniProtKB
  4. response to oxidative stress Source: UniProtKB
  5. retina homeostasis Source: UniProt
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
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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6412. KRT1.

Subcellular locationi

Cell membrane
Note: Located on plasma membrane of neuroblastoma NMB7 cells.1 Publication

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cytoskeleton Source: ProtInc
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProt
  5. keratin filament Source: Ensembl
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProt
  8. 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) [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.11 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551V → D in EHK. 1 Publication
VAR_017820
Natural varianti155 – 1551V → G in EHK. 1 Publication
Corresponds to variant rs57959072 [ dbSNP | Ensembl ].
VAR_003853
Natural varianti161 – 1611L → P in EHK. 1 Publication
Corresponds to variant rs57695159 [ dbSNP | Ensembl ].
VAR_003854
Natural varianti186 – 1861S → P in EHK. 1 Publication
Corresponds to variant rs60022878 [ dbSNP | Ensembl ].
VAR_003855
Natural varianti188 – 1881N → K in EHK. 1 Publication
Corresponds to variant rs59429455 [ dbSNP | Ensembl ].
VAR_017821
Natural varianti188 – 1881N → S in EHK. 2 Publications
Corresponds to variant rs58928370 [ dbSNP | Ensembl ].
VAR_003856
Natural varianti188 – 1881N → T in EHK; severe. 1 Publication
VAR_017822
Natural varianti193 – 1931S → P in EHK. 1 Publication
Corresponds to variant rs60937700 [ dbSNP | Ensembl ].
VAR_003857
Natural varianti214 – 2141L → P in EHK. 1 Publication
Corresponds to variant rs61549035 [ dbSNP | Ensembl ].
VAR_017823
Natural varianti340 – 3401D → V in EHK. 1 Publication
Corresponds to variant rs58062863 [ dbSNP | Ensembl ].
VAR_017824
Natural varianti479 – 4791I → T in AEI and EHK. 2 Publications
Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
VAR_017826
Natural varianti482 – 4821Y → C in EHK. 1 Publication
Corresponds to variant rs58420087 [ dbSNP | Ensembl ].
VAR_017827
Natural varianti486 – 4861L → P in EHK. 1 Publication
Corresponds to variant rs56914602 [ dbSNP | Ensembl ].
VAR_017828
Natural varianti490 – 4901E → Q in EHK. 1 Publication
Corresponds to variant rs60279707 [ dbSNP | Ensembl ].
VAR_003861
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.1 Publication
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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741K → I in NEPPK. 1 Publication
Corresponds to variant rs57977969 [ dbSNP | Ensembl ].
VAR_017819
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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti479 – 4791I → F in AEI. 2 Publications
Corresponds to variant rs61218439 [ dbSNP | Ensembl ].
VAR_017825
Natural varianti479 – 4791I → T in AEI and EHK. 2 Publications
Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
VAR_017826
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.1 Publication

Keywords - Diseasei

Disease mutation, Ichthyosis, Palmoplantar keratoderma

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 644643Keratin, type II cytoskeletal 1
PRO_0000063709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine2 Publications
Modified residuei66 – 661Phosphoserine2 Publications
Modified residuei82 – 821Omega-N-methylarginine1 Publication
Modified residuei276 – 2761N6,N6-dimethyllysine1 Publication
Modified residuei344 – 3441Phosphoserine1 Publication

Post-translational modificationi

Undergoes deimination of some arginine residues (citrullination).

Keywords - PTMi

Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP04264.
PaxDbiP04264.
PRIDEiP04264.
ProMEXiP04264.

2D gel databases

REPRODUCTION-2DPAGEP04264.
SWISS-2DPAGEP04264.

PTM databases

PhosphoSiteiP04264.

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

ArrayExpressiP04264.
BgeeiP04264.
CleanExiHS_KRT1.
GenevestigatoriP04264.

Organism-specific databases

HPAiCAB002153.
HPA017917.

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 GNB2L1 and SRC, and with GNB2L1. Interacts with C1QBP; the association represents a cell surface kininogen receptor.2 Publications

Protein-protein interaction databases

BioGridi110046. 63 interactions.
IntActiP04264. 19 interactions.
MINTiMINT-4990403.
STRINGi9606.ENSP00000252244.

Structurei

3D structure databases

ProteinModelPortaliP04264.
SMRiP04264. Positions 180-319, 346-488.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 179178Head
Add
BLAST
Regioni180 – 489310Rod
Add
BLAST
Regioni180 – 21536Coil 1A
Add
BLAST
Regioni216 – 23419Linker 1
Add
BLAST
Regioni235 – 32692Coil 1B
Add
BLAST
Regioni327 – 35024Linker 12
Add
BLAST
Regioni351 – 489139Coil 2
Add
BLAST
Regioni490 – 644155Tail
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 151150Gly/Phe/Ser-rich
Add
BLAST
Compositional biasi502 – 641140Gly/Ser-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146769.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP04264.
KOiK07605.
OMAiTHISETN.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP04264.
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.

P04264-1 [UniParc]FASTAAdd to Basket

« Hide

MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG    50
GGGGSFGAGG GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG 100
GGGFGGGGFG GGGIGGGGFG GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG 150
GIQEVTINQS LLQPLNVEID PEIQKVKSRE REQIKSLNNQ FASFIDKVRF 200
LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR RVDQLKSDQS 250
RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD 300
LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI 350
IAEVKAQYED IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE 400
LNRVIQRLRS EIDNVKKQIS NLQQSISDAE QRGENALKDA KNKLNDLEDA 450
LQQAKEDLAR LLRDYQELMN TKLALDLEIA TYRTLLEGEE SRMSGECAPN 500
VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG SGGGGGGGRG 550
SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG 600
GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR 644
Length:644
Mass (Da):66,039
Last modified:May 26, 2009 - v6
Checksum:iCE5DDE97388F5017
GO

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741K → I in NEPPK. 1 Publication
Corresponds to variant rs57977969 [ dbSNP | Ensembl ].
VAR_017819
Natural varianti155 – 1551V → D in EHK. 1 Publication
VAR_017820
Natural varianti155 – 1551V → G in EHK. 1 Publication
Corresponds to variant rs57959072 [ dbSNP | Ensembl ].
VAR_003853
Natural varianti161 – 1611L → P in EHK. 1 Publication
Corresponds to variant rs57695159 [ dbSNP | Ensembl ].
VAR_003854
Natural varianti176 – 19722Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.
VAR_038627Add
BLAST
Natural varianti186 – 1861S → P in EHK. 1 Publication
Corresponds to variant rs60022878 [ dbSNP | Ensembl ].
VAR_003855
Natural varianti188 – 1881N → K in EHK. 1 Publication
Corresponds to variant rs59429455 [ dbSNP | Ensembl ].
VAR_017821
Natural varianti188 – 1881N → S in EHK. 2 Publications
Corresponds to variant rs58928370 [ dbSNP | Ensembl ].
VAR_003856
Natural varianti188 – 1881N → T in EHK; severe. 1 Publication
VAR_017822
Natural varianti193 – 1931S → P in EHK. 1 Publication
Corresponds to variant rs60937700 [ dbSNP | Ensembl ].
VAR_003857
Natural varianti214 – 2141L → P in EHK. 1 Publication
Corresponds to variant rs61549035 [ dbSNP | Ensembl ].
VAR_017823
Natural varianti312 – 3121I → V.
VAR_003858
Natural varianti330 – 3301I → T.
VAR_003859
Natural varianti340 – 3401D → V in EHK. 1 Publication
Corresponds to variant rs58062863 [ dbSNP | Ensembl ].
VAR_017824
Natural varianti358 – 3581Y → N.2 Publications
Corresponds to variant rs1050872 [ dbSNP | Ensembl ].
VAR_003860
Natural varianti454 – 4541A → S.
Corresponds to variant rs17678945 [ dbSNP | Ensembl ].
VAR_038628
Natural varianti459 – 4668Missing in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.
VAR_038629
Natural varianti479 – 4791I → F in AEI. 2 Publications
Corresponds to variant rs61218439 [ dbSNP | Ensembl ].
VAR_017825
Natural varianti479 – 4791I → T in AEI and EHK. 2 Publications
Corresponds to variant rs57837128 [ dbSNP | Ensembl ].
VAR_017826
Natural varianti482 – 4821Y → C in EHK. 1 Publication
Corresponds to variant rs58420087 [ dbSNP | Ensembl ].
VAR_017827
Natural varianti486 – 4861L → P in EHK. 1 Publication
Corresponds to variant rs56914602 [ dbSNP | Ensembl ].
VAR_017828
Natural varianti490 – 4901E → Q in EHK. 1 Publication
Corresponds to variant rs60279707 [ dbSNP | Ensembl ].
VAR_003861
Natural varianti537 – 5371G → C.1 Publication
VAR_003862
Natural varianti560 – 5667Missing in allele 1B.
VAR_003864
Natural varianti633 – 6331K → R.5 Publications
Corresponds to variant rs14024 [ dbSNP | Ensembl ].
VAR_003863

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011L → M in AAA36153. 1 Publication
Sequence conflicti206 – 2061Q → K in AAA36153. 1 Publication
Sequence conflicti238 – 2381L → S in AAA36153. 1 Publication
Sequence conflicti344 – 3452SL → QF in AAA36153. 1 Publication
Sequence conflicti403 – 4031R → H in BAG36698. 1 Publication
Sequence conflicti404 – 4041V → M in AAA36153. 1 Publication
Sequence conflicti447 – 4471L → M in AAA36153. 1 Publication
Sequence conflicti463 – 4631R → C in AAA36153. 1 Publication
Sequence conflicti466 – 4661Q → H in AAA36153. 1 Publication
Sequence conflicti504 – 5041S → T in AAA36153. 1 Publication
Sequence conflicti511 – 5122TI → SM in AAA36153. 1 Publication
Sequence conflicti564 – 5641G → S in AAA36153. 1 Publication
Sequence conflicti613 – 6131I → S in AAA36153. 1 Publication
Sequence conflicti638 – 6381T → S in AAA36153. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi238054406.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database
Wikipedia

Keratin-1 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8836.1.
PIRi A22940. KRHU2.
RefSeqi NP_006112.3. NM_006121.3.
UniGenei Hs.80828.

3D structure databases

ProteinModelPortali P04264.
SMRi P04264. Positions 180-319, 346-488.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110046. 63 interactions.
IntActi P04264. 19 interactions.
MINTi MINT-4990403.
STRINGi 9606.ENSP00000252244.

PTM databases

PhosphoSitei P04264.

Polymorphism databases

DMDMi 238054406.

2D gel databases

REPRODUCTION-2DPAGE P04264.
SWISS-2DPAGE P04264.

Proteomic databases

MaxQBi P04264.
PaxDbi P04264.
PRIDEi P04264.
ProMEXi P04264.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252244 ; ENSP00000252244 ; ENSG00000167768 .
GeneIDi 3848.
KEGGi hsa:3848.
UCSCi uc001sau.1. human.

Organism-specific databases

CTDi 3848.
GeneCardsi GC12M053069.
H-InvDB HIX0036813.
HGNCi HGNC:6412. KRT1.
HPAi CAB002153.
HPA017917.
MIMi 113800. phenotype.
139350. gene.
146590. phenotype.
600962. phenotype.
607602. phenotype.
607654. phenotype.
neXtProti NX_P04264.
Orphaneti 281139. Annular epidermolytic ichthyosis.
312. Epidermolytic ichthyosis.
2199. Epidermolytic palmoplantar keratoderma.
79503. Ichthyosis hystrix of Curth-Macklin.
50942. Keratosis palmoplantaris striata.
PharmGKBi PA30199.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG146769.
HOGENOMi HOG000230976.
HOVERGENi HBG013015.
InParanoidi P04264.
KOi K07605.
OMAi THISETN.
OrthoDBi EOG7FV3Q8.
PhylomeDBi P04264.
TreeFami TF317854.

Miscellaneous databases

GeneWikii Keratin_1.
GenomeRNAii 3848.
NextBioi 15141.
PROi P04264.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04264.
Bgeei P04264.
CleanExi HS_KRT1.
Genevestigatori P04264.

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. 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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiK2C1_HUMAN
AccessioniPrimary (citable) accession number: P04264
Secondary accession number(s): B2RA01
, Q14720, Q6GSJ0, Q9H298
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: May 26, 2009
Last modified: September 3, 2014
This is version 178 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).

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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