KIN17_HUMAN
ID KIN17_HUMAN Reviewed; 393 AA.
AC O60870; B4DX32;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=DNA/RNA-binding protein KIN17;
DE AltName: Full=Binding to curved DNA;
DE AltName: Full=KIN, antigenic determinant of recA protein homolog;
GN Name=KIN {ECO:0000312|HGNC:HGNC:6327}; Synonyms=BTCD, KIN17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA06462.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION
RP BY UVC.
RC TISSUE=Testis {ECO:0000312|EMBL:CAA06462.1};
RX PubMed=10964102; DOI=10.1093/carcin/21.9.1701;
RA Kannouche P., Mauffrey P., Pinon-Lataillade G., Mattei M.-G., Sarasin A.,
RA Daya-Grosjean L., Angulo J.F.;
RT "Molecular cloning and characterization of the human KIN17 cDNA encoding a
RT component of the UVC response that is conserved among metazoans.";
RL Carcinogenesis 21:1701-1710(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000312|EMBL:AL158044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4] {ECO:0000312|EMBL:AAH17309.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic carcinoma {ECO:0000312|EMBL:AAH17309.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 130-150, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, METHYLATION AT LYS-135, AND MUTAGENESIS OF LYS-135.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=9266022; DOI=10.1007/s004030050220;
RA Biard D.S.F., Saintigny Y., Maratrat M., Vozenin M.-C., Martin M.,
RA Daburon F., Angulo J.F.;
RT "Differential expression of the HsKin17 protein during differentiation of
RT in vitro reconstructed human skin.";
RL Arch. Dermatol. Res. 289:448-456(1997).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=12359749;
RA Miccoli L., Biard D.S.F., Creminon C., Angulo J.F.;
RT "Human kin17 protein directly interacts with the simian virus 40 large T
RT antigen and inhibits DNA replication.";
RL Cancer Res. 62:5425-5435(2002).
RN [8] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11880372; DOI=10.1074/jbc.m200321200;
RA Biard D.S.F., Miccoli L., Despras E., Frobert Y., Creminon C., Angulo J.F.;
RT "Ionizing radiation triggers chromatin-bound kin17 complex formation in
RT human cells.";
RL J. Biol. Chem. 277:19156-19165(2002).
RN [9] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12754299;
RA Biard D.S.F., Miccoli L., Despras E., Harper F., Pichard E., Creminon C.,
RA Angulo J.F.;
RT "Participation of kin17 protein in replication factories and in other DNA
RT transactions mediated by high molecular weight nuclear complexes.";
RL Mol. Cancer Res. 1:519-531(2003).
RN [10] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12853634; DOI=10.1093/nar/gkg459;
RA Miccoli L., Biard D.S.F., Frouin I., Harper F., Maga G., Angulo J.F.;
RT "Selective interactions of human kin17 and RPA proteins with chromatin and
RT the nuclear matrix in a DNA damage- and cell cycle-regulated manner.";
RL Nucleic Acids Res. 31:4162-4175(2003).
RN [11] {ECO:0000305}
RP INDUCTION BY MITOMYCIN C.
RX PubMed=12525703; DOI=10.1073/pnas.0236176100;
RA Masson C., Menaa F., Pinon-Lataillade G., Frobert Y., Chevillard S.,
RA Radicella J.P., Sarasin A., Angulo J.F.;
RT "Global genome repair is required to activate KIN17, a UVC-responsive gene
RT involved in DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:616-621(2003).
RN [12] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15831485; DOI=10.1128/mcb.25.9.3814-3830.2005;
RA Miccoli L., Frouin I., Novac O., Di Paola D., Harper F.,
RA Zannis-Hadjopoulos M., Maga G., Biard D.S.F., Angulo J.F.;
RT "The human stress-activated protein kin17 belongs to the multiprotein DNA
RT replication complex and associates in vivo with mammalian replication
RT origins.";
RL Mol. Cell. Biol. 25:3814-3830(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 268-393, FUNCTION, DOMAIN
RP C-TERMINAL, AND MUTAGENESIS OF LYS-302 AND LYS-391.
RX PubMed=17045609; DOI=10.1016/j.jmb.2006.09.033;
RA le Maire A., Schiltz M., Stura E.A., Pinon-Lataillade G., Couprie J.,
RA Moutiez M., Gondry M., Angulo J.F., Zinn-Justin S.;
RT "A tandem of SH3-like domains participates in RNA binding in KIN17, a human
RT protein activated in response to genotoxics.";
RL J. Mol. Biol. 364:764-776(2006).
RN [17]
RP STRUCTURE BY NMR OF 51-160, AND WINGED HELIX REGION.
RX PubMed=18029424; DOI=10.1110/ps.073079107;
RA Carlier L., Couprie J., le Maire A., Guilhaudis L., Milazzo-Segalas I.,
RA Courcon M., Moutiez M., Gondry M., Davoust D., Gilquin B., Zinn-Justin S.;
RT "Solution structure of the region 51-160 of human KIN17 reveals an atypical
RT winged helix domain.";
RL Protein Sci. 16:2750-2755(2007).
CC -!- FUNCTION: Involved in DNA replication and the cellular response to DNA
CC damage. May participate in DNA replication factories and create a
CC bridge between DNA replication and repair mediated by high molecular
CC weight complexes. May play a role in illegitimate recombination and
CC regulation of gene expression. May participate in mRNA processing.
CC Binds, in vitro, to double-stranded DNA. Also shown to bind
CC preferentially to curved DNA in vitro and in vivo (By similarity).
CC Binds via its C-terminal domain to RNA in vitro.
CC {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372,
CC ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299,
CC ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485,
CC ECO:0000269|PubMed:17045609}.
CC -!- SUBUNIT: Associated with DNA polymerase alpha, RFC1 and cyclin A, in
CC multiprotein DNA replication complexes. Also associates with
CC replication origins at the G1/S phase boundary and throughout the S
CC phase in vivo. {ECO:0000269|PubMed:15831485}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 large T antigen.
CC {ECO:0000269|PubMed:12359749}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11880372,
CC ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299,
CC ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485}. Cytoplasm
CC {ECO:0000269|PubMed:11880372, ECO:0000269|PubMed:12359749,
CC ECO:0000269|PubMed:12754299, ECO:0000269|PubMed:12853634,
CC ECO:0000269|PubMed:15831485}. Note=During S phase, strongly associated
CC with the nuclear matrix, and to chromosomal DNA in the presence of DNA
CC damage. Also shows cytoplasmic localization in elongated spermatids.
CC {ECO:0000250|UniProtKB:Q8K339, ECO:0000269|PubMed:11880372,
CC ECO:0000269|PubMed:12359749, ECO:0000269|PubMed:12754299,
CC ECO:0000269|PubMed:12853634, ECO:0000269|PubMed:15831485}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60870-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60870-2; Sequence=VSP_056074;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined,
CC with highest levels in skeletal muscle, heart and testis.
CC Differentially expressed in non-tumorigenic and tumorigenic cell lines.
CC Highly expressed in proliferating epithelial keratinocyte cells in
CC vitro (at protein level). {ECO:0000269|PubMed:10964102,
CC ECO:0000269|PubMed:9266022}.
CC -!- INDUCTION: By UVC irradiation in quiescent primary fibroblasts. By
CC mitomycin C in human melanoma MeWO cells. {ECO:0000269|PubMed:10964102,
CC ECO:0000269|PubMed:12525703}.
CC -!- DOMAIN: The C-terminal domain (268-393) is organized into 2 subdomains
CC that bear structural similarities to SH3-like domains. Both subdomains
CC adopt a similar 5-stranded beta-barrel-like fold and are connected to
CC each other by a short linker of 5 residues. The 5 beta-sheets are
CC packed at approximately right angles against each other. A highly
CC conserved groove formed at the interface between the 2 subdomains,
CC comprised of Lys residues 302 and 391 and other positively charged
CC residues, may possibly be the site of RNA-binding.
CC {ECO:0000269|PubMed:17045609}.
CC -!- MISCELLANEOUS: Recognized by antibodies directed against the RecA
CC protein. {ECO:0000250|UniProtKB:Q8K339}.
CC -!- SIMILARITY: Belongs to the KIN17 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ005273; CAA06462.1; -; mRNA.
DR EMBL; AK301789; BAG63244.1; -; mRNA.
DR EMBL; AL158044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017309; AAH17309.1; -; mRNA.
DR CCDS; CCDS7080.1; -. [O60870-1]
DR RefSeq; NP_036443.1; NM_012311.3. [O60870-1]
DR RefSeq; XP_011517729.1; XM_011519427.1. [O60870-2]
DR PDB; 2CKK; X-ray; 1.45 A; A=268-393.
DR PDB; 2V1N; NMR; -; A=51-160.
DR PDB; 7ABH; EM; 4.50 A; 7=1-393.
DR PDB; 7ABI; EM; 8.00 A; 7=1-393.
DR PDBsum; 2CKK; -.
DR PDBsum; 2V1N; -.
DR PDBsum; 7ABH; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; O60870; -.
DR BMRB; O60870; -.
DR SMR; O60870; -.
DR BioGRID; 116600; 55.
DR CORUM; O60870; -.
DR IntAct; O60870; 6.
DR MINT; O60870; -.
DR STRING; 9606.ENSP00000368881; -.
DR iPTMnet; O60870; -.
DR MetOSite; O60870; -.
DR PhosphoSitePlus; O60870; -.
DR BioMuta; KIN; -.
DR EPD; O60870; -.
DR jPOST; O60870; -.
DR MassIVE; O60870; -.
DR MaxQB; O60870; -.
DR PaxDb; O60870; -.
DR PeptideAtlas; O60870; -.
DR PRIDE; O60870; -.
DR ProteomicsDB; 49638; -. [O60870-1]
DR ProteomicsDB; 5403; -.
DR Antibodypedia; 4279; 119 antibodies from 27 providers.
DR DNASU; 22944; -.
DR Ensembl; ENST00000379562.9; ENSP00000368881.3; ENSG00000151657.12. [O60870-1]
DR GeneID; 22944; -.
DR KEGG; hsa:22944; -.
DR MANE-Select; ENST00000379562.9; ENSP00000368881.3; NM_012311.4; NP_036443.1.
DR UCSC; uc001ijt.4; human. [O60870-1]
DR CTD; 22944; -.
DR DisGeNET; 22944; -.
DR GeneCards; KIN; -.
DR HGNC; HGNC:6327; KIN.
DR HPA; ENSG00000151657; Low tissue specificity.
DR MIM; 601720; gene.
DR neXtProt; NX_O60870; -.
DR OpenTargets; ENSG00000151657; -.
DR PharmGKB; PA30113; -.
DR VEuPathDB; HostDB:ENSG00000151657; -.
DR eggNOG; KOG2837; Eukaryota.
DR GeneTree; ENSGT00390000005903; -.
DR HOGENOM; CLU_030065_1_0_1; -.
DR InParanoid; O60870; -.
DR OMA; DKGHVHM; -.
DR OrthoDB; 1420569at2759; -.
DR PhylomeDB; O60870; -.
DR TreeFam; TF314393; -.
DR PathwayCommons; O60870; -.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SignaLink; O60870; -.
DR BioGRID-ORCS; 22944; 755 hits in 1080 CRISPR screens.
DR ChiTaRS; KIN; human.
DR EvolutionaryTrace; O60870; -.
DR GeneWiki; KIN_(gene); -.
DR GenomeRNAi; 22944; -.
DR Pharos; O60870; Tbio.
DR PRO; PR:O60870; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O60870; protein.
DR Bgee; ENSG00000151657; Expressed in monocyte and 188 other tissues.
DR ExpressionAtlas; O60870; baseline and differential.
DR Genevisible; O60870; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:UniProtKB.
DR CDD; cd13155; KOW_KIN17; 1.
DR Gene3D; 1.10.10.2030; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR019447; DNA/RNA-bd_Kin17_WH-like_dom.
DR InterPro; IPR037321; KIN17-like.
DR InterPro; IPR038254; KIN17_WH-like_sf.
DR InterPro; IPR041330; KN17_SH3.
DR InterPro; IPR041995; KOW_KIN17.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR12805; PTHR12805; 1.
DR Pfam; PF10357; Kin17_mid; 1.
DR Pfam; PF18131; KN17_SH3; 1.
DR SMART; SM01253; Kin17_mid; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW DNA replication; DNA-binding; Host-virus interaction; Metal-binding;
KW Methylation; mRNA processing; Nucleus; Reference proteome; RNA-binding;
KW Stress response; Zinc; Zinc-finger.
FT CHAIN 1..393
FT /note="DNA/RNA-binding protein KIN17"
FT /id="PRO_0000289134"
FT ZN_FING 28..50
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT REGION 51..160
FT /note="Winged helix-turn-helix (wHTH)"
FT REGION 209..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..334
FT /note="C-terminal subdomain A"
FT /evidence="ECO:0000269|PubMed:17045609"
FT REGION 340..391
FT /note="C-terminal subdomain B"
FT /evidence="ECO:0000269|PubMed:17045609"
FT COILED 147..180
FT /evidence="ECO:0000255"
FT COILED 250..277
FT /evidence="ECO:0000255"
FT COMPBIAS 209..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="N6,N6,N6-trimethyllysine; by METTL22; in vitro"
FT /evidence="ECO:0000269|PubMed:23349634,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 135
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 374..393
FT /note="GPLKGRRVEGIQYEDISKLA -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056074"
FT MUTAGEN 135
FT /note="K->R: Almost complete loss of in vitro methylation
FT by METTL22."
FT /evidence="ECO:0000269|PubMed:23349634"
FT MUTAGEN 302
FT /note="K->E: Significant reduction of RNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:17045609"
FT MUTAGEN 391
FT /note="K->E: Significant reduction of RNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:17045609"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2V1N"
FT HELIX 65..83
FT /evidence="ECO:0007829|PDB:2V1N"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2V1N"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:2V1N"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2V1N"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2V1N"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:2V1N"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2V1N"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2V1N"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:2V1N"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2V1N"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2CKK"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2CKK"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2CKK"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:2CKK"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:2CKK"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:2CKK"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2CKK"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:2CKK"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2CKK"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2CKK"
SQ SEQUENCE 393 AA; 45374 MW; 515A89B4C8A4C007 CRC64;
MGKSDFLTPK AIANRIKSKG LQKLRWYCQM CQKQCRDENG FKCHCMSESH QRQLLLASEN
PQQFMDYFSE EFRNDFLELL RRRFGTKRVH NNIVYNEYIS HREHIHMNAT QWETLTDFTK
WLGREGLCKV DETPKGWYIQ YIDRDPETIR RQLELEKKKK QDLDDEEKTA KFIEEQVRRG
LEGKEQEVPT FTELSRENDE EKVTFNLSKG ACSSSGATSS KSSTLGPSAL KTIGSSASVK
RKESSQSSTQ SKEKKKKKSA LDEIMEIEEE KKRTARTDYW LQPEIIVKII TKKLGEKYHK
KKAIVKEVID KYTAVVKMID SGDKLKLDQT HLETVIPAPG KRILVLNGGY RGNEGTLESI
NEKTFSATIV IETGPLKGRR VEGIQYEDIS KLA
