CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001014
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA/RNA-binding protein KIN17 
Protein Synonyms/Alias
 Binding to curved DNA; KIN, antigenic determinant of recA protein homolog 
Gene Name
 KIN 
Gene Synonyms/Alias
 BTCD; KIN17 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
292IIVKIITKKLGEKYHubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. 
Sequence Annotation
 ZN_FING 28 50 C2H2-type.
 REGION 284 334 C-terminal subdomain A.
 REGION 340 391 C-terminal subdomain B.
 MOD_RES 135 135 N6,N6,N6-trimethyllysine; by METTL22; in  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding; Host-virus interaction; Metal-binding; Methylation; mRNA processing; Nucleus; Reference proteome; RNA-binding; Stress response; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 393 AA 
Protein Sequence
MGKSDFLTPK AIANRIKSKG LQKLRWYCQM CQKQCRDENG FKCHCMSESH QRQLLLASEN 60
PQQFMDYFSE EFRNDFLELL RRRFGTKRVH NNIVYNEYIS HREHIHMNAT QWETLTDFTK 120
WLGREGLCKV DETPKGWYIQ YIDRDPETIR RQLELEKKKK QDLDDEEKTA KFIEEQVRRG 180
LEGKEQEVPT FTELSRENDE EKVTFNLSKG ACSSSGATSS KSSTLGPSAL KTIGSSASVK 240
RKESSQSSTQ SKEKKKKKSA LDEIMEIEEE KKRTARTDYW LQPEIIVKII TKKLGEKYHK 300
KKAIVKEVID KYTAVVKMID SGDKLKLDQT HLETVIPAPG KRILVLNGGY RGNEGTLESI 360
NEKTFSATIV IETGPLKGRR VEGIQYEDIS KLA 393 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IDA:UniProtKB.
 GO:0006397; P:mRNA processing; TAS:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; IEP:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR019447; DNA/RNA-bd_Kin17_cons_domain.
 IPR015880; Znf_C2H2-like. 
Pfam
 PF10357; Kin17_mid 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS