ID   CKS2_HUMAN              Reviewed;          79 AA.
AC   P33552; Q6FGI9; Q6LET5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Cyclin-dependent kinases regulatory subunit 2;
DE            Short=CKS-2;
GN   Name=CKS2;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2227411; DOI=10.1101/gad.4.8.1332;
RA   Richardson H.E., Stueland C.S., Thomas J., Russell P., Reed S.I.;
RT   "Human cDNAs encoding homologs of the small p34Cdc28/Cdc2-associated
RT   protein of Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL   Genes Dev. 4:1332-1344(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=8211159; DOI=10.1126/science.8211159;
RA   Parge H.E., Arvai A.S., Murtari D.J., Reed S.I., Tainer J.A.;
RT   "Human CksHs2 atomic structure: a role for its hexameric assembly in cell
RT   cycle control.";
RL   Science 262:387-395(1993).
CC   -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC       kinases and is essential for their biological function.
CC   -!- SUBUNIT: Forms a homohexamer that can probably bind six kinase
CC       subunits.
CC   -!- INTERACTION:
CC       P33552; Q00526: CDK3; NbExp=4; IntAct=EBI-711840, EBI-1245761;
CC   -!- SIMILARITY: Belongs to the CKS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cks2/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CKS2ID40093ch9q22.html";
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DR   EMBL; X54942; CAA38703.1; -; mRNA.
DR   EMBL; AF506708; AAM22232.1; -; Genomic_DNA.
DR   EMBL; BT006630; AAP35276.1; -; mRNA.
DR   EMBL; CR407630; CAG28558.1; -; mRNA.
DR   EMBL; CR542118; CAG46915.1; -; mRNA.
DR   EMBL; AL160054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62762.1; -; Genomic_DNA.
DR   EMBL; BC006458; AAH06458.1; -; mRNA.
DR   CCDS; CCDS6682.1; -.
DR   PIR; B36670; B36670.
DR   RefSeq; NP_001818.1; NM_001827.2.
DR   PDB; 1CKS; X-ray; 2.10 A; A/B/C=1-79.
DR   PDB; 4Y72; X-ray; 2.30 A; C=1-79.
DR   PDB; 4YC3; X-ray; 2.70 A; C=1-79.
DR   PDB; 5HQ0; X-ray; 2.30 A; C=1-79.
DR   PDB; 5LQF; X-ray; 2.06 A; C/F=1-79.
DR   PDB; 6GU2; X-ray; 2.00 A; C=1-79.
DR   PDB; 6GU3; X-ray; 2.65 A; C=1-79.
DR   PDB; 6GU4; X-ray; 2.73 A; C=1-79.
DR   PDB; 6GU6; X-ray; 2.33 A; B=1-79.
DR   PDB; 6GU7; X-ray; 2.75 A; B/D/F/H=1-79.
DR   PDBsum; 1CKS; -.
DR   PDBsum; 4Y72; -.
DR   PDBsum; 4YC3; -.
DR   PDBsum; 5HQ0; -.
DR   PDBsum; 5LQF; -.
DR   PDBsum; 6GU2; -.
DR   PDBsum; 6GU3; -.
DR   PDBsum; 6GU4; -.
DR   PDBsum; 6GU6; -.
DR   PDBsum; 6GU7; -.
DR   AlphaFoldDB; P33552; -.
DR   SMR; P33552; -.
DR   BioGRID; 107583; 45.
DR   IntAct; P33552; 28.
DR   MINT; P33552; -.
DR   STRING; 9606.ENSP00000364976; -.
DR   iPTMnet; P33552; -.
DR   PhosphoSitePlus; P33552; -.
DR   BioMuta; CKS2; -.
DR   EPD; P33552; -.
DR   jPOST; P33552; -.
DR   MassIVE; P33552; -.
DR   PaxDb; P33552; -.
DR   PeptideAtlas; P33552; -.
DR   PRIDE; P33552; -.
DR   ProteomicsDB; 54921; -.
DR   TopDownProteomics; P33552; -.
DR   Antibodypedia; 27992; 256 antibodies from 33 providers.
DR   DNASU; 1164; -.
DR   Ensembl; ENST00000314355.7; ENSP00000364976.3; ENSG00000123975.5.
DR   GeneID; 1164; -.
DR   KEGG; hsa:1164; -.
DR   MANE-Select; ENST00000314355.7; ENSP00000364976.3; NM_001827.3; NP_001818.1.
DR   UCSC; uc004aqh.3; human.
DR   CTD; 1164; -.
DR   DisGeNET; 1164; -.
DR   GeneCards; CKS2; -.
DR   HGNC; HGNC:2000; CKS2.
DR   HPA; ENSG00000123975; Tissue enhanced (bone marrow, testis).
DR   MIM; 116901; gene.
DR   neXtProt; NX_P33552; -.
DR   OpenTargets; ENSG00000123975; -.
DR   PharmGKB; PA26536; -.
DR   VEuPathDB; HostDB:ENSG00000123975; -.
DR   eggNOG; KOG3484; Eukaryota.
DR   GeneTree; ENSGT00950000182971; -.
DR   HOGENOM; CLU_140546_2_0_1; -.
DR   InParanoid; P33552; -.
DR   OMA; CIQNCER; -.
DR   OrthoDB; 1377855at2759; -.
DR   PhylomeDB; P33552; -.
DR   TreeFam; TF101142; -.
DR   PathwayCommons; P33552; -.
DR   SignaLink; P33552; -.
DR   BioGRID-ORCS; 1164; 123 hits in 1083 CRISPR screens.
DR   ChiTaRS; CKS2; human.
DR   EvolutionaryTrace; P33552; -.
DR   GeneWiki; CKS2; -.
DR   GenomeRNAi; 1164; -.
DR   Pharos; P33552; Tbio.
DR   PRO; PR:P33552; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P33552; protein.
DR   Bgee; ENSG00000123975; Expressed in ventricular zone and 171 other tissues.
DR   Genevisible; P33552; HS.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0007127; P:meiosis I; IEA:Ensembl.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:Ensembl.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   Gene3D; 3.30.170.10; -; 1.
DR   InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR   InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR   Pfam; PF01111; CKS; 1.
DR   PRINTS; PR00296; CYCLINKINASE.
DR   SMART; SM01084; CKS; 1.
DR   SUPFAM; SSF55637; SSF55637; 1.
DR   PROSITE; PS00944; CKS_1; 1.
DR   PROSITE; PS00945; CKS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division; Reference proteome.
FT   CHAIN           1..79
FT                   /note="Cyclin-dependent kinases regulatory subunit 2"
FT                   /id="PRO_0000206237"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CONFLICT        20
FT                   /note="R -> L (in Ref. 4; CAG28558)"
FT                   /evidence="ECO:0000305"
FT   STRAND          15..23
FT                   /evidence="ECO:0007829|PDB:5LQF"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:5LQF"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:5LQF"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:5LQF"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:5LQF"
FT   STRAND          66..72
FT                   /evidence="ECO:0007829|PDB:5LQF"
SQ   SEQUENCE   79 AA;  9860 MW;  811B5927691EEC5C CRC64;
     MAHKQIYYSD KYFDEHYEYR HVMLPRELSK QVPKTHLMSE EEWRRLGVQQ SLGWVHYMIH
     EPEPHILLFR RPLPKDQQK