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Protein

DNA/RNA-binding protein KIN17

Gene

Kin

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo. Binds via its C-terminal domain to RNA in vitro.By similarity4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri28 – 50C2H2-typeSequence analysisAdd BLAST23

GO - Molecular functioni

  • double-stranded DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • DNA replication Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication, mRNA processing, Stress response

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA/RNA-binding protein KIN17
Alternative name(s):
Binding to curved DNA
KIN, antigenic determinant of recA protein
Gene namesi
Name:KinImported
Synonyms:Btcd, Kin17
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:96676. Kin.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: MGI
  • nuclear matrix Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002891351 – 391DNA/RNA-binding protein KIN17Add BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei135N6,N6,N6-trimethyllysine; by METTL22; alternateBy similarity1
Modified residuei135N6-methyllysine; alternateBy similarity1

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ8K339.
MaxQBiQ8K339.
PaxDbiQ8K339.
PeptideAtlasiQ8K339.
PRIDEiQ8K339.

PTM databases

iPTMnetiQ8K339.
PhosphoSitePlusiQ8K339.

Expressioni

Tissue specificityi

Highly expressed in transformed mouse AtT20 neuroendocrine cells. Expressed at a lower level in testis, kidney, skeletal muscle, liver, lung, spleen, brain and heart and kidney. In testis, expressed at much higher levels in proliferating cells than in differentiating cells. Not detected in embryo.3 Publications

Developmental stagei

In testis, expression almost doubled from day 5 to days 17-22 postpartum (dpp) and then decreased by 28 dpp to reach a stable level in adult testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000037262.
CleanExiMM_KIN.
GenevisibleiQ8K339. MM.

Interactioni

Subunit structurei

Associated with DNA polymerase alpha, RFC1 and cyclin A, in multiprotein DNA replication complexes. Also associates with replication origins at the G1/S phase boundary and throughout the S phase in vivo (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8K339. 2 interactors.
MINTiMINT-4117607.
STRINGi10090.ENSMUSP00000043614.

Structurei

3D structure databases

ProteinModelPortaliQ8K339.
SMRiQ8K339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 160Winged helix-turn-helix (wHTH)By similarityAdd BLAST110
Regioni282 – 332C-terminal subdomain ABy similarityAdd BLAST51
Regioni338 – 389C-terminal subdomain BBy similarityAdd BLAST52

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili147 – 180Sequence analysisAdd BLAST34
Coiled coili252 – 275Sequence analysisAdd BLAST24

Domaini

The C-terminal domain (268-393) is organized into 2 subdomains that bear structural similarities to SH3-like domains. Both subdomains adopt a similar 5-stranded beta-barrel-like fold and are connected to each other by a short linker of 5 residues. The 5 beta-sheets are packed at approximately right angles against each other. A highly conserved groove formed at the interface between the 2 subdomains, comprised of Lys residues 302 and 391 and other positively charged residues, may possibly be the site of RNA-binding (By similarity).By similarity

Sequence similaritiesi

Belongs to the KIN17 family.Curated
Contains 1 C2H2-type zinc finger.Sequence analysis

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri28 – 50C2H2-typeSequence analysisAdd BLAST23

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2837. Eukaryota.
ENOG410XRJ7. LUCA.
GeneTreeiENSGT00390000005903.
HOGENOMiHOG000178663.
HOVERGENiHBG053068.
InParanoidiQ8K339.
KOiK13102.
OMAiESINEKA.
OrthoDBiEOG091G0AQX.
PhylomeDBiQ8K339.
TreeFamiTF314393.

Family and domain databases

InterProiIPR019447. DNA/RNA-bd_Kin17_cons_domain.
[Graphical view]
PfamiPF10357. Kin17_mid. 1 hit.
[Graphical view]
SMARTiSM01253. Kin17_mid. 1 hit.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKSDFLSPK AIANRIKSKG LQKLRWYCQM CQKQCRDENG FKCHCMSESH
60 70 80 90 100
QRQLLLASEN PQQFMDYFSE EFRNDFLELL RRRFGTKRVH NNIVYNEYIS
110 120 130 140 150
HREHIHMNAT QWETLTDFTK WLGREGLCKV DETPKGWYIQ YIDRDPETIR
160 170 180 190 200
RQLELEKKKK QDLDDEEKTA KFIEEQVRRG LEGKEQETPV FTELSRENEE
210 220 230 240 250
EKVTFNLNKG AGGSAGATTS KSSSLGPSAL KLLGSAASGK RKESSQSSAQ
260 270 280 290 300
PAKKKKSALD EIMELEEEKK RTARTDAWLQ PGIVVKIITK KLGEKYHKKK
310 320 330 340 350
GVVKEVIDRY TAVVKMTDSG DRLKLDQTHL ETVIPAPGKR VLVLNGGYRG
360 370 380 390
NEGTLESINE KAFSATIVIE TGPLKGRRVE GIQYEDISKL A
Length:391
Mass (Da):44,722
Last modified:October 1, 2002 - v1
Checksum:i955BC6A4FF4D3B6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58472 mRNA. No translation available.
AK009429 mRNA. Translation: BAB26281.3.
AK167740 mRNA. Translation: BAE39778.1.
AL772367 Genomic DNA. Translation: CAM13915.1.
BC028860 mRNA. Translation: AAH28860.1.
CCDSiCCDS15676.1.
PIRiS18666.
RefSeqiNP_079556.1. NM_025280.2.
UniGeneiMm.35498.

Genome annotation databases

EnsembliENSMUST00000042512; ENSMUSP00000043614; ENSMUSG00000037262.
GeneIDi16588.
KEGGimmu:16588.
UCSCiuc008ihp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58472 mRNA. No translation available.
AK009429 mRNA. Translation: BAB26281.3.
AK167740 mRNA. Translation: BAE39778.1.
AL772367 Genomic DNA. Translation: CAM13915.1.
BC028860 mRNA. Translation: AAH28860.1.
CCDSiCCDS15676.1.
PIRiS18666.
RefSeqiNP_079556.1. NM_025280.2.
UniGeneiMm.35498.

3D structure databases

ProteinModelPortaliQ8K339.
SMRiQ8K339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K339. 2 interactors.
MINTiMINT-4117607.
STRINGi10090.ENSMUSP00000043614.

PTM databases

iPTMnetiQ8K339.
PhosphoSitePlusiQ8K339.

Proteomic databases

EPDiQ8K339.
MaxQBiQ8K339.
PaxDbiQ8K339.
PeptideAtlasiQ8K339.
PRIDEiQ8K339.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042512; ENSMUSP00000043614; ENSMUSG00000037262.
GeneIDi16588.
KEGGimmu:16588.
UCSCiuc008ihp.1. mouse.

Organism-specific databases

CTDi22944.
MGIiMGI:96676. Kin.

Phylogenomic databases

eggNOGiKOG2837. Eukaryota.
ENOG410XRJ7. LUCA.
GeneTreeiENSGT00390000005903.
HOGENOMiHOG000178663.
HOVERGENiHBG053068.
InParanoidiQ8K339.
KOiK13102.
OMAiESINEKA.
OrthoDBiEOG091G0AQX.
PhylomeDBiQ8K339.
TreeFamiTF314393.

Miscellaneous databases

PROiQ8K339.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037262.
CleanExiMM_KIN.
GenevisibleiQ8K339. MM.

Family and domain databases

InterProiIPR019447. DNA/RNA-bd_Kin17_cons_domain.
[Graphical view]
PfamiPF10357. Kin17_mid. 1 hit.
[Graphical view]
SMARTiSM01253. Kin17_mid. 1 hit.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKIN17_MOUSE
AccessioniPrimary (citable) accession number: Q8K339
Secondary accession number(s): Q9CV58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Recognized by antibodies directed against the RecA protein.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.