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Protein

Keratin, type II cytoskeletal 3

Gene

KRT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. structural molecule activity Source: UniProtKB

GO - Biological processi

  1. epithelial cell differentiation Source: UniProtKB
  2. intermediate filament cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 3
Alternative name(s):
65 kDa cytokeratin
Cytokeratin-3
Short name:
CK-3
Keratin-3
Short name:
K3
Type-II keratin Kb3
Gene namesi
Name:KRT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6440. KRT3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. intermediate filament Source: UniProtKB
  3. keratin filament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy, Meesmann2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant corneal disease characterized by fragility of the anterior corneal epithelium. Patients are usually asymptomatic until adulthood when rupture of the corneal microcysts may cause erosions, producing clinical symptoms such as photophobia, contact lens intolerance and intermittent diminution of visual acuity. Rarely, subepithelial scarring causes irregular corneal astigmatism and permanent visual impairment. Histological examination shows a disorganized and thickened epithelium with widespread cytoplasmic vacuolation and numerous small, round, debris-laden intraepithelial cysts.

See also OMIM:122100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti503 – 5031R → P in MECD. 1 Publication
Corresponds to variant rs60410063 [ dbSNP | Ensembl ].
VAR_031327
Natural varianti509 – 5091E → K in MECD. 1 Publication
Corresponds to variant rs57872071 [ dbSNP | Ensembl ].
VAR_003868

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi122100. phenotype.
Orphaneti98954. Meesmann corneal dystrophy.
PharmGKBiPA30228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 628628Keratin, type II cytoskeletal 3PRO_0000063716Add
BLAST

Proteomic databases

MaxQBiP12035.
PaxDbiP12035.
PRIDEiP12035.

PTM databases

PhosphoSiteiP12035.

Expressioni

Tissue specificityi

Cornea specific.

Gene expression databases

BgeeiP12035.
CleanExiHS_KRT3.
ExpressionAtlasiP12035. baseline and differential.
GenevestigatoriP12035.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Keratin-3 associates with keratin-12.

Protein-protein interaction databases

BioGridi110048. 14 interactions.
IntActiP12035. 3 interactions.
STRINGi9606.ENSP00000413479.

Structurei

3D structure databases

ProteinModelPortaliP12035.
SMRiP12035. Positions 198-339, 366-508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 197197HeadAdd
BLAST
Regioni198 – 509312RodAdd
BLAST
Regioni198 – 23336Coil 1AAdd
BLAST
Regioni234 – 25421Linker 1Add
BLAST
Regioni255 – 34692Coil 1BAdd
BLAST
Regioni347 – 37024Linker 12Add
BLAST
Regioni371 – 509139Coil 2Add
BLAST
Regioni510 – 628119TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 169160Gly-richAdd
BLAST
Compositional biasi536 – 61277Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146968.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP12035.
KOiK07605.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP12035.
TreeFamiTF332742.

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.

P12035-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRQASKTSG GGSQGFSGRS AVVSGSSRMS CVAHSGGAGG GAYGFRSGAG
60 70 80 90 100
GFGSRSLYNL GGNKSISISV AAGGSRAGGF GGGRSSCAFA GGYGGGFGSG
110 120 130 140 150
YGGGFGGGFG GGRGMGGGFG GAGGFGGAGG FGGAGGFGGP GGFGGSGGFG
160 170 180 190 200
GPGSLGSPGG FGPGGFPGGI QEVTINQSLL QPLNVEIDPQ IGQVKAQERE
210 220 230 240 250
QIKTLNNKFA SFIDKVRFLE QQNKVLETKW NLLQQQGTSS ISGTNNLEPL
260 270 280 290 300
FENHINYLRS YLDNILGERG RLDSELKNME DLVEDFKKKY EDEINKRTAA
310 320 330 340 350
ENEFVTLKKD VDSAYMNKVE LQAKVDALID EIDFLRTLYD AELSQMQSHI
360 370 380 390 400
SDTSVVLSMD NNRSLDLDSI IAEVRAQYED IAQRSKAEAE ALYQTKLGEL
410 420 430 440 450
QTTAGRHGDD LRNTKSEIIE LNRMIQRLRA EIEGVKKQNA NLQTAIAEAE
460 470 480 490 500
QHGEMALKDA NAKLQELQAA LQQAKDDLAR LLRDYQELMN VKLALDVEIA
510 520 530 540 550
TYRKLLEGEE YRMSGECPSA VSISVVSSST TSASAGGYGG GYGGGMGGGL
560 570 580 590 600
GGGFSAGGGS GSGFGRGGGG GIGGGFGGGS SGFSGGSGFG SISGARYGVS
610 620
GGGFSSASNR GGSIKFSQSS QSSQRYSR
Length:628
Mass (Da):64,417
Last modified:November 30, 2010 - v3
Checksum:i65FDB8CAA7F3C960
GO

Sequence cautioni

The sequence CAF31522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621G → A in CAA28991. (PubMed:2439698)Curated
Sequence conflicti175 – 1751I → T in CAA28991. (PubMed:2439698)Curated
Sequence conflicti184 – 1841N → K in CAA28991. (PubMed:2439698)Curated
Sequence conflicti187 – 1871I → T in CAA28991. (PubMed:2439698)Curated
Sequence conflicti298 – 2981T → Y in CAA28993. (PubMed:2439698)Curated
Sequence conflicti397 – 3971L → M in CAA28996. (PubMed:2439698)Curated
Sequence conflicti409 – 4091D → G in CAF31522. (PubMed:15737194)Curated
Sequence conflicti448 – 4481E → Q in CAA28996. (PubMed:2439698)Curated
Sequence conflicti511 – 5111Y → YS in CAA28996. (PubMed:2439698)Curated
Sequence conflicti562 – 5621S → I in CAA28996. (PubMed:2439698)Curated
Sequence conflicti580 – 5801S → T in CAA28996. (PubMed:2439698)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441G → A.
Corresponds to variant rs28721426 [ dbSNP | Ensembl ].
VAR_061297
Natural varianti375 – 3751R → G.1 Publication
Corresponds to variant rs3887954 [ dbSNP | Ensembl ].
VAR_056023
Natural varianti503 – 5031R → P in MECD. 1 Publication
Corresponds to variant rs60410063 [ dbSNP | Ensembl ].
VAR_031327
Natural varianti509 – 5091E → K in MECD. 1 Publication
Corresponds to variant rs57872071 [ dbSNP | Ensembl ].
VAR_003868

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05418 Genomic DNA. Translation: CAA28991.1.
X05419 Genomic DNA. Translation: CAA28992.1.
X05420 Genomic DNA. Translation: CAA28993.1.
X05420 Genomic DNA. Translation: CAA28994.1.
X05420 Genomic DNA. Translation: CAA28995.1.
X05421 Genomic DNA. Translation: CAA28996.1.
AC107016 Genomic DNA. No translation available.
AJ628418 mRNA. Translation: CAF31522.1. Different initiation.
CCDSiCCDS44895.1.
PIRiA29666.
RefSeqiNP_476429.2. NM_057088.2.
UniGeneiHs.680652.

Genome annotation databases

EnsembliENST00000417996; ENSP00000413479; ENSG00000186442.
GeneIDi3850.
KEGGihsa:3850.
UCSCiuc001say.3. human.

Polymorphism databases

DMDMi313104225.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database
Wikipedia

Keratin-3 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05418 Genomic DNA. Translation: CAA28991.1.
X05419 Genomic DNA. Translation: CAA28992.1.
X05420 Genomic DNA. Translation: CAA28993.1.
X05420 Genomic DNA. Translation: CAA28994.1.
X05420 Genomic DNA. Translation: CAA28995.1.
X05421 Genomic DNA. Translation: CAA28996.1.
AC107016 Genomic DNA. No translation available.
AJ628418 mRNA. Translation: CAF31522.1. Different initiation.
CCDSiCCDS44895.1.
PIRiA29666.
RefSeqiNP_476429.2. NM_057088.2.
UniGeneiHs.680652.

3D structure databases

ProteinModelPortaliP12035.
SMRiP12035. Positions 198-339, 366-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110048. 14 interactions.
IntActiP12035. 3 interactions.
STRINGi9606.ENSP00000413479.

PTM databases

PhosphoSiteiP12035.

Polymorphism databases

DMDMi313104225.

Proteomic databases

MaxQBiP12035.
PaxDbiP12035.
PRIDEiP12035.

Protocols and materials databases

DNASUi3850.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000417996; ENSP00000413479; ENSG00000186442.
GeneIDi3850.
KEGGihsa:3850.
UCSCiuc001say.3. human.

Organism-specific databases

CTDi3850.
GeneCardsiGC12M053183.
H-InvDBHIX0036742.
HGNCiHGNC:6440. KRT3.
MIMi122100. phenotype.
148043. gene.
neXtProtiNX_P12035.
Orphaneti98954. Meesmann corneal dystrophy.
PharmGKBiPA30228.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG146968.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP12035.
KOiK07605.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP12035.
TreeFamiTF332742.

Miscellaneous databases

GeneWikiiKeratin_3.
GenomeRNAii3850.
NextBioi15149.
PROiP12035.
SOURCEiSearch...

Gene expression databases

BgeeiP12035.
CleanExiHS_KRT3.
ExpressionAtlasiP12035. baseline and differential.
GenevestigatoriP12035.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evolution of keratin genes: different protein domains evolve by different pathways."
    Klinge E.M., Sylvestre Y.R., Freedberg I.M., Blumenberg M.
    J. Mol. Evol. 24:319-329(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-375.
  2. "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].
  3. "Characterization of new members of the human type II keratin gene family and a general evaluation of the keratin gene domain on chromosome 12q13.13."
    Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I., Schweizer J.
    J. Invest. Dermatol. 124:536-544(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-628.
    Tissue: Eye.
  4. Cited for: VARIANT MECD LYS-509.
  5. "Novel mutations in the helix termination motif of keratin 3 and keratin 12 in 2 Taiwanese families with Meesmann corneal dystrophy."
    Chen Y.T., Tseng S.H., Chao S.C.
    Cornea 24:928-932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MECD PRO-503.

Entry informationi

Entry nameiK2C3_HUMAN
AccessioniPrimary (citable) accession number: P12035
Secondary accession number(s): A6NIS2, Q701L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 30, 2010
Last modified: January 7, 2015
This is version 144 of the entry and version 3 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.