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Protein

Keratin, type I cytoskeletal 19

Gene

Krt19

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei270Stutter1
Sitei330Stutter1

GO - Molecular functioni

  • protein complex binding Source: RGD
  • structural constituent of muscle Source: Ensembl

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-6805567. Keratinization.
R-RNO-6809371. Formation of the cornified envelope.

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 19
Alternative name(s):
Cytokeratin-19
Short name:
CK-19
Keratin-19
Short name:
K19
Type I keratin Ka19
Gene namesi
Name:Krt19
Synonyms:Ka19, Krt1-19
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi619936. Krt19.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000636741 – 403Keratin, type I cytoskeletal 19Add BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Omega-N-methylarginineBy similarity1
Modified residuei14PhosphoserineBy similarity1
Modified residuei24Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei24Omega-N-methylarginine; alternateBy similarity1
Modified residuei27PhosphoserineCombined sources1
Modified residuei32Omega-N-methylarginineBy similarity1
Modified residuei35PhosphoserineCombined sources1
Modified residuei40PhosphoserineCombined sources1
Modified residuei43Omega-N-methylarginineBy similarity1
Modified residuei51Omega-N-methylarginineBy similarity1
Modified residuei57PhosphoserineCombined sources1
Modified residuei67PhosphoserineCombined sources1
Modified residuei326PhosphothreonineBy similarity1
Modified residuei394PhosphotyrosineBy similarity1
Modified residuei398PhosphoserineBy similarity1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ63279.
PRIDEiQ63279.

PTM databases

iPTMnetiQ63279.
PhosphoSitePlusiQ63279.

Expressioni

Tissue specificityi

Expressed in brain, heart, skin and in costameres of myoplasm at the sarcolemmal membrane in skeletal and cardiac muscle fibers. Undifferentiated gonads and somatic cells of ovarian cords throughout the fetal ovary development.2 Publications

Developmental stagei

Found in somatic cells of ovarian cords throughout the fetal ovary development.1 Publication

Gene expression databases

BgeeiENSRNOG00000014233.
GenevisibleiQ63279. RN.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Interacts with PNN (By similarity). Interacts with the actin-binding domain of DMD.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DmdP115303EBI-876985,EBI-706166

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

IntActiQ63279. 1 interactor.
STRINGi10116.ENSRNOP00000019133.

Structurei

3D structure databases

ProteinModelPortaliQ63279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 82HeadAdd BLAST82
Regioni83 – 390RodAdd BLAST308
Regioni83 – 118Coil 1AAdd BLAST36
Regioni119 – 136Linker 1Add BLAST18
Regioni137 – 228Coil 1BAdd BLAST92
Regioni229 – 251Linker 12Add BLAST23
Regioni247 – 393Necessary for interaction with PNNBy similarityAdd BLAST147
Regioni252 – 390Coil 2Add BLAST139
Regioni391 – 403Rod-like helical tailAdd BLAST13

Domaini

This keratin differs from all other IF proteins in lacking the C-terminal tail domain.

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ63279.
KOiK07604.
OMAiDAHYNNL.
OrthoDBiEOG091G087I.
PhylomeDBiQ63279.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSYSYRQSS AMSSYGGMGG GPVRFGSGGV FRAPSIHGGS GGRGVSVSST
60 70 80 90 100
RIVSSSSGGY VGGRGGSFSG ALTVTDGLLG GNEKITMQNL NDRLASYLDK
110 120 130 140 150
VRALEQANGE LEVKIRDWYQ KQGPGPFRDY SQYFKTIEDL RDKILGATIE
160 170 180 190 200
NSKIVLQIDN ARLAADDFRT KFETEQALRM SVEADINGLR RVLDELTLAR
210 220 230 240 250
TDLEMQIENL KEELAYLKKN HEEEISALRS QVGGQVSVEV DSTPGIDLAK
260 270 280 290 300
ILSEMRSQYE AMAEKNRKDA EAWYLTQIDE LNTQVAVHTT QIQINKTEVT
310 320 330 340 350
ELRRKVQDLE IELQSQLSMK AALEGTVAEI EARYGAQLSH IQGVISSIEV
360 370 380 390 400
QLSNVRADTE RQNQEYQQLM DIKSRLEQEI ATYRSLLEGQ EAHYNSLSIA

KAL
Length:403
Mass (Da):44,636
Last modified:August 30, 2005 - v2
Checksum:i8D8E4ED8109EE158
GO

Sequence cautioni

The sequence AAH88424 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti143K → N in CAA57205 (PubMed:8541209).Curated1
Sequence conflicti168F → L in CAA57205 (PubMed:8541209).Curated1
Sequence conflicti177A → G in CAA57205 (PubMed:8541209).Curated1
Sequence conflicti248L → H in CAA57205 (PubMed:8541209).Curated1
Sequence conflicti265 – 266KN → MD in CAA57205 (PubMed:8541209).Curated2
Sequence conflicti274 – 280YLTQIDE → LLKIDET in CAA57205 (PubMed:8541209).Curated7
Sequence conflicti303R → E in CAA57205 (PubMed:8541209).Curated1
Sequence conflicti364 – 365QE → HQ in CAA57205 (PubMed:8541209).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY464140 mRNA. Translation: AAR36876.1.
AABR03073341 Genomic DNA. No translation available.
BC088424 mRNA. Translation: AAH88424.1. Different initiation.
BC126075 mRNA. Translation: AAI26076.1.
AH006934 Genomic DNA. Translation: AAC64402.1.
X81449 mRNA. Translation: CAA57205.1.
BK004046 mRNA. Translation: DAA04480.1.
RefSeqiNP_955792.1. NM_199498.2.
UniGeneiRn.9359.

Genome annotation databases

EnsembliENSRNOT00000019133; ENSRNOP00000019133; ENSRNOG00000014233.
GeneIDi360626.
KEGGirno:360626.
UCSCiRGD:619936. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY464140 mRNA. Translation: AAR36876.1.
AABR03073341 Genomic DNA. No translation available.
BC088424 mRNA. Translation: AAH88424.1. Different initiation.
BC126075 mRNA. Translation: AAI26076.1.
AH006934 Genomic DNA. Translation: AAC64402.1.
X81449 mRNA. Translation: CAA57205.1.
BK004046 mRNA. Translation: DAA04480.1.
RefSeqiNP_955792.1. NM_199498.2.
UniGeneiRn.9359.

3D structure databases

ProteinModelPortaliQ63279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63279. 1 interactor.
STRINGi10116.ENSRNOP00000019133.

PTM databases

iPTMnetiQ63279.
PhosphoSitePlusiQ63279.

Proteomic databases

PaxDbiQ63279.
PRIDEiQ63279.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019133; ENSRNOP00000019133; ENSRNOG00000014233.
GeneIDi360626.
KEGGirno:360626.
UCSCiRGD:619936. rat.

Organism-specific databases

CTDi3880.
RGDi619936. Krt19.

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ63279.
KOiK07604.
OMAiDAHYNNL.
OrthoDBiEOG091G087I.
PhylomeDBiQ63279.
TreeFamiTF332742.

Enzyme and pathway databases

ReactomeiR-RNO-6805567. Keratinization.
R-RNO-6809371. Formation of the cornified envelope.

Miscellaneous databases

PROiQ63279.

Gene expression databases

BgeeiENSRNOG00000014233.
GenevisibleiQ63279. RN.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK1C19_RAT
AccessioniPrimary (citable) accession number: Q63279
Secondary accession number(s): A0JN08
, Q5M7V2, Q6S6J4, Q9Z253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 30, 2005
Last modified: November 30, 2016
This is version 128 of the entry and version 2 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).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.