Reviewed, UniProtKB/Swiss-Prot O60870 (KIN17_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA/RNA-binding protein KIN17
Alternative name(s):
    KIN, antigenic determinant of recA protein homolog
    Binding to curved DNA

Gene names

Name:	KIN
Synonyms:	BTCD, KIN17

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 By similarity. Binds via its C-terminal domain to RNA in vitro.
Subunit structure	Interacts with SV40 large T antigen. 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.
Subcellular location	Nucleus. Cytoplasm. Note= During S phase, strongly associated with the nuclear matrix, and to chromosomal DNA in the presence of DNA damage. Also shows cytoplasmic localization in elongated spermatids.
Tissue specificity	Ubiquitously expressed in all tissues examined, with highest levels in skeletal muscle, heart and testis. Differentially expressed in non-tumorigenic and tumorigenic cell lines. Highly expressed in proliferating epithelial keratinocyte cells in vitro (at protein level).
Induction	By UVC irradiation in quiescent primary fibroblasts. By mitomycin C in human melanoma MeWO cells.
Domain	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.
Miscellaneous	Recognized by antibodies directed against the RecA protein By similarity.
Sequence similarities	Belongs to the KIN17 family. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair DNA replication Host-virus interaction Stress response mRNA processing
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil Zinc-finger
Ligand	DNA-binding Metal-binding RNA-binding Zinc
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Ref.5 Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Ref.11 Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nuclear matrix Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Ref.11 Inferred from direct assay. Source: UniProtKB double-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 393

393

DNA/RNA-binding protein KIN17

PRO_0000289134

Regions

Zinc finger

28 – 50

23

C2H2-type

Region

284 – 334

51

C-terminal subdomain A

Region

340 – 391

52

C-terminal subdomain B

Coiled coil

147 – 180

34

Potential

Coiled coil

250 – 277

28

Potential

Experimental info

Mutagenesis

302

1

K → E: Significant reduction of RNA-binding activity

Mutagenesis

391

1

K → E: Significant reduction of RNA-binding activity

Secondary structure

1

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393

Helix Strand Turn

Details...

Helix

61 – 63

3

Helix

65 – 83

19

Beta strand

88 – 90

3

Helix

91 – 98

8

Helix

107 – 109

3

Helix

115 – 122

8

Turn

123 – 126

4

Beta strand

127 – 133

7

Beta strand

136 – 141

6

Helix

146 – 154

9

Helix

156 – 158

3

Beta strand

285 – 289

5

Helix

296 – 298

3

Beta strand

302 – 309

8

Turn

310 – 312

3

Beta strand

313 – 318

6

Turn

319 – 321

3

Beta strand

324 – 328

5

Helix

329 – 331

3

Beta strand

332 – 334

3

Beta strand

342 – 345

4

Turn

349 – 352

4

Beta strand

354 – 361

8

Helix

362 – 364

3

Beta strand

366 – 371

6

Turn

375 – 378

4

Beta strand

380 – 385

6

Helix

386 – 388

3

Beta strand

389 – 392

4

Sequences

	Sequence		Length	Mass (Da)
	O60870-1 [UniParc]. Last modified January 1, 1999. Version 2. Checksum: 515A89B4C8A4C007	FASTA	393	45,374
	10 20 30 40 50 60 MGKSDFLTPK AIANRIKSKG LQKLRWYCQM CQKQCRDENG FKCHCMSESH QRQLLLASEN 70 80 90 100 110 120 PQQFMDYFSE EFRNDFLELL RRRFGTKRVH NNIVYNEYIS HREHIHMNAT QWETLTDFTK 130 140 150 160 170 180 WLGREGLCKV DETPKGWYIQ YIDRDPETIR RQLELEKKKK QDLDDEEKTA KFIEEQVRRG 190 200 210 220 230 240 LEGKEQEVPT FTELSRENDE EKVTFNLSKG ACSSSGATSS KSSTLGPSAL KTIGSSASVK 250 260 270 280 290 300 RKESSQSSTQ SKEKKKKKSA LDEIMEIEEE KKRTARTDYW LQPEIIVKII TKKLGEKYHK 310 320 330 340 350 360 KKAIVKEVID KYTAVVKMID SGDKLKLDQT HLETVIPAPG KRILVLNGGY RGNEGTLESI 370 380 390 NEKTFSATIV IETGPLKGRR VEGIQYEDIS KLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans." Kannouche P., Mauffrey P., Pinon-Lataillade G., Mattei M.-G., Sarasin A., Daya-Grosjean L., Angulo J.F. Carcinogenesis 21:1701-1710(2000) [PubMed: 10964102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY UVC. Tissue: Testis.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreatic carcinoma.
[4]	"Differential expression of the HsKin17 protein during differentiation of in vitro reconstructed human skin." Biard D.S.F., Saintigny Y., Maratrat M., Vozenin M.-C., Martin M., Daburon F., Angulo J.F. Arch. Dermatol. Res. 289:448-456(1997) [PubMed: 9266022] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Human kin17 protein directly interacts with the simian virus 40 large T antigen and inhibits DNA replication." Miccoli L., Biard D.S.F., Creminon C., Angulo J.F. Cancer Res. 62:5425-5435(2002) [PubMed: 12359749] [Abstract] Cited for: FUNCTION, INTERACTION WITH SV40 LARGE T ANTIGEN, SUBCELLULAR LOCATION.
[6]	"Ionizing radiation triggers chromatin-bound kin17 complex formation in human cells." Biard D.S.F., Miccoli L., Despras E., Frobert Y., Creminon C., Angulo J.F. J. Biol. Chem. 277:19156-19165(2002) [PubMed: 11880372] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Participation of kin17 protein in replication factories and in other DNA transactions mediated by high molecular weight nuclear complexes." Biard D.S.F., Miccoli L., Despras E., Harper F., Pichard E., Creminon C., Angulo J.F. Mol. Cancer Res. 1:519-531(2003) [PubMed: 12754299] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Selective interactions of human kin17 and RPA proteins with chromatin and the nuclear matrix in a DNA damage- and cell cycle-regulated manner." Miccoli L., Biard D.S.F., Frouin I., Harper F., Maga G., Angulo J.F. Nucleic Acids Res. 31:4162-4175(2003) [PubMed: 12853634] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Global genome repair is required to activate KIN17, a UVC-responsive gene involved in DNA replication." Masson C., Menaa F., Pinon-Lataillade G., Frobert Y., Chevillard S., Radicella J.P., Sarasin A., Angulo J.F. Proc. Natl. Acad. Sci. U.S.A. 100:616-621(2003) [PubMed: 12525703] [Abstract] Cited for: INDUCTION BY MITOMYCIN C.
[10]	"The human stress-activated protein kin17 belongs to the multiprotein DNA replication complex and associates in vivo with mammalian replication origins." Miccoli L., Frouin I., Novac O., Di Paola D., Harper F., Zannis-Hadjopoulos M., Maga G., Biard D.S.F., Angulo J.F. Mol. Cell. Biol. 25:3814-3830(2005) [PubMed: 15831485] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[11]	"A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics." le Maire A., Schiltz M., Stura E.A., Pinon-Lataillade G., Couprie J., Moutiez M., Gondry M., Angulo J.F., Zinn-Justin S. J. Mol. Biol. 364:764-776(2006) [PubMed: 17045609] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 268-393, FUNCTION, DOMAIN C-TERMINAL, MUTAGENESIS OF LYS-302 AND LYS-391.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ005273 mRNA. Translation: CAA06462.1.
AL158044 Genomic DNA. Translation: CAI12959.1.
BC017309 mRNA. Translation: AAH17309.1.

RefSeq

NP_036443.1.

UniGene

Hs.397918

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CKK	X-ray	1.45	A	268-393	[»]
2V1N	NMR	-	A	51-160	[»]

ModBase

Search...

PTM databases

PhosphoSite

O60870.

Genome annotation databases

Ensembl

ENSG00000151657. Homo sapiens. [Contig view]

GeneID

22944.

KEGG

hsa:22944.

Organism-specific databases

HGNC

HGNC:6327. KIN.

HPA

CAB016339.

MIM

601720. gene.

PharmGKB

PA30113.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

O60870.

HOVERGEN

O60870.

Gene expression databases

ArrayExpress

O60870.

CleanEx

HS_KIN.

Family and domain databases

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

43701.

SOURCE

Search...

Entry information

Entry name

KIN17_HUMAN

Accession

Primary (citable) accession number: O60870

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	January 1, 1999
Last modified:	November 25, 2008
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)