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Protein

Keratin, type II cytoskeletal 7

Gene

Krt7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Blocks interferon-dependent interphase and stimulates DNA synthesis in cells.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei337 – 3371StutterSequence analysis

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 7
Alternative name(s):
Cytokeratin-7
Short name:
CK-7
Keratin-7
Short name:
K7
Type-II keratin Kb7
Gene namesi
Name:Krt7By similarity
Synonyms:Kb71 Publication, Krt2-7Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310865. Krt7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 457456Keratin, type II cytoskeletal 7PRO_0000307638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei15 – 151Dimethylated arginine; alternateBy similarity
Modified residuei15 – 151Omega-N-methylarginine; alternateBy similarity
Modified residuei47 – 471PhosphoserineBy similarity
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei91 – 911PhosphothreonineBy similarity
Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei173 – 1731N6-acetyllysineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei248 – 2481PhosphoserineCombined sources
Modified residuei283 – 2831PhosphothreonineBy similarity

Post-translational modificationi

Arg-15 is dimethylated, probably to asymmetric dimethylarginine.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ6IG12.

PTM databases

iPTMnetiQ6IG12.
PhosphoSiteiQ6IG12.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10. Interacts with GPER1 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6IG12.
SMRiQ6IG12. Positions 82-234, 250-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 8483HeadSequence analysisAdd
BLAST
Regioni84 – 12037Coil 1ASequence analysisAdd
BLAST
Regioni85 – 393309RodSequence analysisAdd
BLAST
Regioni121 – 13818Linker 1Sequence analysisAdd
BLAST
Regioni139 – 23092Coil 1BSequence analysisAdd
BLAST
Regioni231 – 25424Linker 12Sequence analysisAdd
BLAST
Regioni255 – 393139Coil 2Sequence analysisAdd
BLAST
Regioni394 – 45764TailSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ6IG12.
KOiK07605.
PhylomeDBiQ6IG12.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6IG12-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIHFSSRST AYPGRGAQVR LSSGRASFGS RSLYGLGSSR PRVAVRSAYG
60 70 80 90 100
GPVGAGIREI TINQSLLAPL SVDIDPTIQQ VRQEEREQIK TLNNKFASFI
110 120 130 140 150
DKVRFLEQQN KMLETKWALL QEQKSAKSSQ LPRIFEAQIA GLRQQLETLQ
160 170 180 190 200
LDGGRLEVEL RNMQDVVEDF KNKYEEEINR RTAAENEFVL LKKDVDAAYT
210 220 230 240 250
NKVELEAKAD SLQDEINFLK TLHETELAEL QSQISDTSVV LSMDNSRSLD
260 270 280 290 300
LDGIIADVKA QYEEMANHSR AEAEAWYQTK FETLQAQAGK HGDDLRNTRN
310 320 330 340 350
EIAEMNRSIQ RLQAEIDTLK NQRAKLESSI AEAEEQGELA IKDAHAKQGE
360 370 380 390 400
LEAALQKAKQ DVARQLREYQ ELLNTKLALD IEIATYRKLL EGEESRLSGD
410 420 430 440 450
GMGPVNISVV NSTGGNGGKL IFGGTMGSNA LSFSGGPGAL RAYSIKTTST

TRRGTHN
Length:457
Mass (Da):50,709
Last modified:July 5, 2004 - v1
Checksum:iD6AD866E4949DEF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03058117 Genomic DNA. No translation available.
AABR03059386 Genomic DNA. No translation available.
BK003973 mRNA. Translation: DAA02218.1.
RefSeqiNP_001041335.1. NM_001047870.1.
UniGeneiRn.7913.

Genome annotation databases

GeneIDi300242.
KEGGirno:300242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03058117 Genomic DNA. No translation available.
AABR03059386 Genomic DNA. No translation available.
BK003973 mRNA. Translation: DAA02218.1.
RefSeqiNP_001041335.1. NM_001047870.1.
UniGeneiRn.7913.

3D structure databases

ProteinModelPortaliQ6IG12.
SMRiQ6IG12. Positions 82-234, 250-392.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ6IG12.
PhosphoSiteiQ6IG12.

Proteomic databases

PRIDEiQ6IG12.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi300242.
KEGGirno:300242.

Organism-specific databases

CTDi3855.
RGDi1310865. Krt7.

Phylogenomic databases

HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ6IG12.
KOiK07605.
PhylomeDBiQ6IG12.

Miscellaneous databases

PROiQ6IG12.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
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 Norway1 Publication.
  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.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiK2C7_RAT
AccessioniPrimary (citable) accession number: Q6IG12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 85 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; 40-55 kDa) and II (neutral to basic; 56-70 kDa).Curated

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.