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Protein

Keratin, type I cytoskeletal 39

Gene

Krt39

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

May play a role in late hair differentiation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei339 – 3391Stutter

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: RGD

GO - Biological processi

  • intermediate filament-based process Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 39
Alternative name(s):
Cytokeratin-39
Short name:
CK-39
Keratin-39
Short name:
K39
Type I hair keratin Ka35
Gene namesi
Name:Krt39
Synonyms:Ka35
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303032. Krt39.

Subcellular locationi

GO - Cellular componenti

  • intermediate filament Source: RGD
  • keratin filament Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481Keratin, type I cytoskeletal 39PRO_0000314855Add
BLAST

Proteomic databases

PaxDbiQ6IFW3.
PRIDEiQ6IFW3.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039322.

Structurei

3D structure databases

ProteinModelPortaliQ6IFW3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9090HeadAdd
BLAST
Regioni91 – 397307RodAdd
BLAST
Regioni91 – 12535Coil 1AAdd
BLAST
Regioni126 – 13611Linker 1Add
BLAST
Regioni137 – 237101Coil 1BAdd
BLAST
Regioni238 – 25316Linker 12Add
BLAST
Regioni254 – 397144Coil 2Add
BLAST
Regioni398 – 48184TailAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIZN. Eukaryota.
ENOG4111DA1. LUCA.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ6IFW3.
KOiK07604.
PhylomeDBiQ6IFW3.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6IFW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTKGSTVTI SSSTPPQNCS GNTNVRTNSS NKSCYHDVQS TGHALQTPQG
60 70 80 90 100
QGCRPSPCLY RCPNYLIRTY SFHPCPDDCS RCSDGINSHE KETMQILNER
110 120 130 140 150
LASYLEKVRM LEGENADLED KIQEECSKTL PILCPDYLSY YTTIEQLQQK
160 170 180 190 200
ILCTKAENSR LVSQIDNTKL AADDLRAKYE AELSLRQLVE ADANGLKQIL
210 220 230 240 250
DALTLSKADL EARVQSLTEE LLCLKTNHEE EINSLQCQLG DRINIEVTAA
260 270 280 290 300
PSVDLNQILQ KMRCQYESIV ETNRKDVEEW FNTQMEELNQ QVVSSSQQQQ
310 320 330 340 350
CCQKDIIELR RTISALEVEL QAQHRMRDSQ ECILAETEAR YTALLAQIQS
360 370 380 390 400
LIHNLEAQVA EIRSALQRQN QEYEVLLDIK SRLECEIATY RSLLESLDGR
410 420 430 440 450
LPCNPCTTTW EPSCQARAME CLTPVYTSIS LPGIHKPCRA SGPPSRILVK
460 470 480
ICTITKEIKD GKVISSHEHV QPCYITRPAK V
Length:481
Mass (Da):54,338
Last modified:July 5, 2004 - v1
Checksum:i5606D6E04F5CBB31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073663 Genomic DNA. No translation available.
BK004035 mRNA. Translation: DAA04469.1.
RefSeqiNP_001004130.1. NM_001004130.1.
UniGeneiRn.162196.

Genome annotation databases

GeneIDi303523.
KEGGirno:303523.
UCSCiRGD:1303032. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073663 Genomic DNA. No translation available.
BK004035 mRNA. Translation: DAA04469.1.
RefSeqiNP_001004130.1. NM_001004130.1.
UniGeneiRn.162196.

3D structure databases

ProteinModelPortaliQ6IFW3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039322.

Proteomic databases

PaxDbiQ6IFW3.
PRIDEiQ6IFW3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi303523.
KEGGirno:303523.
UCSCiRGD:1303032. rat.

Organism-specific databases

CTDi390792.
RGDi1303032. Krt39.

Phylogenomic databases

eggNOGiENOG410IIZN. Eukaryota.
ENOG4111DA1. LUCA.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ6IFW3.
KOiK07604.
PhylomeDBiQ6IFW3.

Miscellaneous databases

PROiQ6IFW3.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Comprehensive analysis of keratin gene clusters in humans and rodents."
    Hesse M., Zimek A., Weber K., Magin T.M.
    Eur. J. Cell Biol. 83:19-26(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiK1C39_RAT
AccessioniPrimary (citable) accession number: Q6IFW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.