Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Keratin, type II cytoskeletal 1

Gene

Krt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei432StutterSequence analysis1

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 1
Alternative name(s):
Cytokeratin-1
Short name:
CK-1
Keratin-1
Short name:
K1
Type-II keratin Kb1
Gene namesi
Name:Krt1By similarity
Synonyms:Kb1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359664. Krt1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Intermediate filament, Keratin, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002780982 – 625Keratin, type II cytoskeletal 1Add BLAST624

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineBy similarity1
Modified residuei20Asymmetric dimethylarginineBy similarity1
Modified residuei23PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei51Omega-N-methylarginineBy similarity1
Modified residuei69PhosphoserineBy similarity1
Modified residuei275N6,N6-dimethyllysineBy similarity1
Modified residuei517Omega-N-methylarginineBy similarity1
Modified residuei574Omega-N-methylarginineBy similarity1
Modified residuei596Omega-N-methylarginineBy similarity1

Post-translational modificationi

Undergoes deimination of some arginine residues (citrullination).

Keywords - PTMi

Citrullination, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ6IMF3.
PRIDEiQ6IMF3.

PTM databases

iPTMnetiQ6IMF3.
PhosphoSitePlusiQ6IMF3.

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 RACK1 and SRC, and with RACK1. Interacts with C1QBP; the association represents a cell surface kininogen receptor. Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament.By similarity

Protein-protein interaction databases

BioGridi256511. 3 interactors.
STRINGi10116.ENSRNOP00000029276.

Structurei

3D structure databases

ProteinModelPortaliQ6IMF3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 178HeadSequence analysisAdd BLAST177
Regioni179 – 488RodSequence analysisAdd BLAST310
Regioni179 – 214Coil 1ASequence analysisAdd BLAST36
Regioni215 – 233Linker 1Sequence analysisAdd BLAST19
Regioni234 – 325Coil 1BSequence analysisAdd BLAST92
Regioni326 – 349Linker 12Sequence analysisAdd BLAST24
Regioni350 – 488Coil 2Sequence analysisAdd BLAST139
Regioni489 – 625TailSequence analysisAdd BLAST137

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili171 – 319Sequence analysisAdd BLAST149
Coiled coili388 – 475Sequence analysisAdd BLAST88

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi14 – 150Gly-richSequence analysisAdd BLAST137
Compositional biasi513 – 609Gly-richSequence analysisAdd BLAST97

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ6IMF3.
KOiK07605.
PhylomeDBiQ6IMF3.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032449. Keratin_2_1_tail.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
PF16210. Keratin_2_tail. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6IMF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFQCSSRSL CRSGGGGGGR NFSSGSAGLV SFQRRSTSSS MRRSGGGGGG
60 70 80 90 100
RFSGGGFCGS SGGGFGSKSL VNLGGGRSIS ISVAGGGSSY GGGFGGGSYG
110 120 130 140 150
GGSFGGGSFG GGVGGGFGGG GFGGGGFGSG GGFGGGRFGG GFGPVCPPGG
160 170 180 190 200
IQEVTINQSL LQPLNVEVDP QIQKVKSQER EQIKSLNDKF ASFIDKVRFL
210 220 230 240 250
EQQNQVLQTK WELLQQVDTS TRTQNLDPFF ESYISNLRRQ VDSLKNDQSR
260 270 280 290 300
MDSELKNMQD LVEEYRTKYE DEINKRTNAE NEFVTIKKDV DSAYMNKAEL
310 320 330 340 350
QARVDNLQQD IDFFSTLYQM ELSQMQTQIS ETNVVLSMDN NRTLDLDGII
360 370 380 390 400
AEVKAQYDSI CQRSKAEAET FYQSKYEELQ ITAGKHGDSV KNTKMEISEL
410 420 430 440 450
NRVIQRLRSE IDSVKKQISQ MQQNISDAEQ RGEKALKDAQ NKLNEIEDAL
460 470 480 490 500
TQAKEELTRL LRDYQELMNT KLALDMEIAT YRKLLEGEEI RMSGECTPNV
510 520 530 540 550
SVSVSTSHTS MSGTSSRGGG RYGSGGGGGG GTYGGGSRGG SYGGGSGGGS
560 570 580 590 600
YGGCSSGGGS GGGSYGGGSS GGHRGGSGGG GGSSGGSYGG SSGGGRGGSS
610 620
SGGGVKSSGS SSVKFVSTTY SRGTN
Length:625
Mass (Da):64,831
Last modified:July 5, 2004 - v1
Checksum:i790AAC59E2A2707B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti514T → S in AAI27465 (PubMed:15489334).Curated1
Sequence conflicti532T → S in AAI27465 (PubMed:15489334).Curated1
Sequence conflicti554C → G in AAI27465 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03057642 Genomic DNA. No translation available.
BC127464 mRNA. Translation: AAI27465.1.
X54806 mRNA. Translation: CAA38577.1.
BK001580 mRNA. Translation: DAA02055.1.
PIRiS21359.
RefSeqiNP_001008802.2. NM_001008802.2.
UniGeneiRn.31789.

Genome annotation databases

GeneIDi300250.
KEGGirno:300250.
UCSCiRGD:1359664. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03057642 Genomic DNA. No translation available.
BC127464 mRNA. Translation: AAI27465.1.
X54806 mRNA. Translation: CAA38577.1.
BK001580 mRNA. Translation: DAA02055.1.
PIRiS21359.
RefSeqiNP_001008802.2. NM_001008802.2.
UniGeneiRn.31789.

3D structure databases

ProteinModelPortaliQ6IMF3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi256511. 3 interactors.
STRINGi10116.ENSRNOP00000029276.

PTM databases

iPTMnetiQ6IMF3.
PhosphoSitePlusiQ6IMF3.

Proteomic databases

PaxDbiQ6IMF3.
PRIDEiQ6IMF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi300250.
KEGGirno:300250.
UCSCiRGD:1359664. rat.

Organism-specific databases

CTDi3848.
RGDi1359664. Krt1.

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ6IMF3.
KOiK07605.
PhylomeDBiQ6IMF3.
TreeFamiTF317854.

Miscellaneous databases

PROiQ6IMF3.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032449. Keratin_2_1_tail.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
PF16210. Keratin_2_tail. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK2C1_RAT
AccessioniPrimary (citable) accession number: Q6IMF3
Secondary accession number(s): A1L113, Q63115
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 88 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).

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.