CKS1_HUMAN
ID CKS1_HUMAN Reviewed; 79 AA.
AC P61024; P33551;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cyclin-dependent kinases regulatory subunit 1;
DE Short=CKS-1;
GN Name=CKS1B; Synonyms=CKS1; ORFNames=PNAS-143, PNAS-16;
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 [LARGE SCALE MRNA].
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) 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].
RC TISSUE=Brain, Muscle, and Prostate;
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 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=7791211; DOI=10.1006/jmbi.1995.0341;
RA Arvai A.S., Bourne Y., Hickey M.J., Tainer J.A.;
RT "Crystal structure of the human cell cycle protein CksHs1: single domain
RT fold with similarity to kinase N-lobe domain.";
RL J. Mol. Biol. 249:835-842(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH CDK2.
RX PubMed=8601310; DOI=10.1016/s0092-8674(00)81065-x;
RA Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I.,
RA Tainer J.A.;
RT "Crystal structure and mutational analysis of the human CDK2 kinase complex
RT with cell cycle-regulatory protein CksHs1.";
RL Cell 84:863-874(1996).
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 P61024; Q03989: ARID5A; NbExp=5; IntAct=EBI-456371, EBI-948603;
CC P61024; Q8NA61: CBY2; NbExp=3; IntAct=EBI-456371, EBI-741724;
CC P61024; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-456371, EBI-11524851;
CC P61024; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-456371, EBI-744556;
CC P61024; P24863: CCNC; NbExp=3; IntAct=EBI-456371, EBI-395261;
CC P61024; P06493: CDK1; NbExp=10; IntAct=EBI-456371, EBI-444308;
CC P61024; P24941: CDK2; NbExp=20; IntAct=EBI-456371, EBI-375096;
CC P61024; Q00526: CDK3; NbExp=5; IntAct=EBI-456371, EBI-1245761;
CC P61024; O14627: CDX4; NbExp=3; IntAct=EBI-456371, EBI-10181162;
CC P61024; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-456371, EBI-12051833;
CC P61024; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-456371, EBI-10303987;
CC P61024; O95995: GAS8; NbExp=3; IntAct=EBI-456371, EBI-1052570;
CC P61024; O75031: HSF2BP; NbExp=3; IntAct=EBI-456371, EBI-7116203;
CC P61024; Q13422: IKZF1; NbExp=3; IntAct=EBI-456371, EBI-745305;
CC P61024; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-456371, EBI-11522367;
CC P61024; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-456371, EBI-747204;
CC P61024; Q0VD86: INCA1; NbExp=3; IntAct=EBI-456371, EBI-6509505;
CC P61024; Q5T749: KPRP; NbExp=3; IntAct=EBI-456371, EBI-10981970;
CC P61024; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-456371, EBI-10172052;
CC P61024; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-456371, EBI-3958099;
CC P61024; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-456371, EBI-12039345;
CC P61024; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-456371, EBI-1216080;
CC P61024; Q86YW9: MED12L; NbExp=3; IntAct=EBI-456371, EBI-3957138;
CC P61024; P50221: MEOX1; NbExp=6; IntAct=EBI-456371, EBI-2864512;
CC P61024; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-456371, EBI-16439278;
CC P61024; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-456371, EBI-2548751;
CC P61024; Q13285: NR5A1; NbExp=3; IntAct=EBI-456371, EBI-874629;
CC P61024; Q02548: PAX5; NbExp=3; IntAct=EBI-456371, EBI-296331;
CC P61024; P26367: PAX6; NbExp=3; IntAct=EBI-456371, EBI-747278;
CC P61024; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-456371, EBI-1105153;
CC P61024; Q04864: REL; NbExp=3; IntAct=EBI-456371, EBI-307352;
CC P61024; Q9HAT0: ROPN1; NbExp=6; IntAct=EBI-456371, EBI-1378139;
CC P61024; Q9UH03: SEPTIN3; NbExp=6; IntAct=EBI-456371, EBI-727037;
CC P61024; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-456371, EBI-748601;
CC P61024; Q14140: SERTAD2; NbExp=3; IntAct=EBI-456371, EBI-2822051;
CC P61024; Q13309: SKP2; NbExp=7; IntAct=EBI-456371, EBI-456291;
CC P61024; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-456371, EBI-12938570;
CC P61024; A6NLX3: SPDYE4; NbExp=6; IntAct=EBI-456371, EBI-12047907;
CC P61024; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-456371, EBI-10175576;
CC P61024; Q99081-3: TCF12; NbExp=3; IntAct=EBI-456371, EBI-11952764;
CC P61024; P15884: TCF4; NbExp=3; IntAct=EBI-456371, EBI-533224;
CC P61024; P15884-3: TCF4; NbExp=3; IntAct=EBI-456371, EBI-13636688;
CC P61024; Q14142: TRIM14; NbExp=3; IntAct=EBI-456371, EBI-2820256;
CC P61024; P14373: TRIM27; NbExp=3; IntAct=EBI-456371, EBI-719493;
CC P61024; P0CI25: TRIM49; NbExp=4; IntAct=EBI-456371, EBI-6427421;
CC P61024; P0CI26: TRIM49C; NbExp=3; IntAct=EBI-456371, EBI-12889036;
CC P61024; Q9UPY6-2: WASF3; NbExp=3; IntAct=EBI-456371, EBI-12026286;
CC P61024; P98170: XIAP; NbExp=7; IntAct=EBI-456371, EBI-517127;
CC P61024; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-456371, EBI-395708;
CC -!- SIMILARITY: Belongs to the CKS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CKS1BID40092ch1q21.html";
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DR EMBL; X54941; CAA38702.1; -; mRNA.
DR EMBL; AF274941; AAK07518.1; -; mRNA.
DR EMBL; AF279897; AAK07553.1; -; mRNA.
DR EMBL; BT007196; AAP35860.1; -; mRNA.
DR EMBL; BC007751; AAH07751.1; -; mRNA.
DR EMBL; BC015629; AAH15629.1; -; mRNA.
DR EMBL; BC070319; AAH70319.1; -; mRNA.
DR EMBL; BC070320; AAH70320.1; -; mRNA.
DR CCDS; CCDS1077.1; -.
DR PIR; A36670; A36670.
DR RefSeq; NP_001817.1; NM_001826.2.
DR PDB; 1BUH; X-ray; 2.60 A; B=1-79.
DR PDB; 1DKS; X-ray; 3.20 A; A/B=1-79.
DR PDB; 1DKT; X-ray; 2.90 A; A/B=1-79.
DR PDB; 2ASS; X-ray; 3.00 A; C=5-73.
DR PDB; 2AST; X-ray; 2.30 A; C=5-73.
DR PDB; 4YC6; X-ray; 2.60 A; B/D/F/H=1-79.
DR PDB; 7B5L; EM; 3.80 A; K=1-73.
DR PDB; 7B5M; EM; 3.91 A; K=1-79.
DR PDB; 7B5R; EM; 3.80 A; K=1-79.
DR PDB; 7NJ0; EM; 3.60 A; D=1-79.
DR PDBsum; 1BUH; -.
DR PDBsum; 1DKS; -.
DR PDBsum; 1DKT; -.
DR PDBsum; 2ASS; -.
DR PDBsum; 2AST; -.
DR PDBsum; 4YC6; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5M; -.
DR PDBsum; 7B5R; -.
DR PDBsum; 7NJ0; -.
DR AlphaFoldDB; P61024; -.
DR SMR; P61024; -.
DR BioGRID; 107582; 95.
DR CORUM; P61024; -.
DR DIP; DIP-102N; -.
DR IntAct; P61024; 72.
DR MINT; P61024; -.
DR STRING; 9606.ENSP00000311083; -.
DR DrugBank; DB02681; 2,8-bis[oxido(oxo)vanadio]-1,1,1,3,5,5,7,7,9,9,9-undecaoxopentavanadoxane-2,8-diium.
DR DrugBank; DB00472; Fluoxetine.
DR iPTMnet; P61024; -.
DR MetOSite; P61024; -.
DR PhosphoSitePlus; P61024; -.
DR BioMuta; CKS1B; -.
DR EPD; P61024; -.
DR jPOST; P61024; -.
DR MassIVE; P61024; -.
DR PaxDb; P61024; -.
DR PeptideAtlas; P61024; -.
DR PRIDE; P61024; -.
DR ProteomicsDB; 57254; -.
DR TopDownProteomics; P61024; -.
DR Antibodypedia; 47036; 251 antibodies from 26 providers.
DR DNASU; 1163; -.
DR Ensembl; ENST00000308987.6; ENSP00000311083.5; ENSG00000173207.13.
DR GeneID; 1163; -.
DR KEGG; hsa:1163; -.
DR MANE-Select; ENST00000308987.6; ENSP00000311083.5; NM_001826.3; NP_001817.1.
DR CTD; 1163; -.
DR DisGeNET; 1163; -.
DR GeneCards; CKS1B; -.
DR HGNC; HGNC:19083; CKS1B.
DR HPA; ENSG00000173207; Low tissue specificity.
DR MIM; 116900; gene.
DR neXtProt; NX_P61024; -.
DR OpenTargets; ENSG00000173207; -.
DR PharmGKB; PA38791; -.
DR VEuPathDB; HostDB:ENSG00000173207; -.
DR eggNOG; KOG3484; Eukaryota.
DR GeneTree; ENSGT00950000182971; -.
DR HOGENOM; CLU_140546_2_0_1; -.
DR InParanoid; P61024; -.
DR OMA; NPEPHVL; -.
DR OrthoDB; 1377855at2759; -.
DR PhylomeDB; P61024; -.
DR TreeFam; TF101142; -.
DR PathwayCommons; P61024; -.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR SignaLink; P61024; -.
DR BioGRID-ORCS; 1163; 72 hits in 653 CRISPR screens.
DR ChiTaRS; CKS1B; human.
DR EvolutionaryTrace; P61024; -.
DR GeneWiki; CKS1B; -.
DR GenomeRNAi; 1163; -.
DR Pharos; P61024; Tbio.
DR PRO; PR:P61024; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P61024; protein.
DR Bgee; ENSG00000173207; Expressed in ventricular zone and 100 other tissues.
DR ExpressionAtlas; P61024; baseline and differential.
DR Genevisible; P61024; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
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: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:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
DR Gene3D; 3.30.170.10; -; 1.
DR IDEAL; IID00309; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..79
FT /note="Cyclin-dependent kinases regulatory subunit 1"
FT /id="PRO_0000206235"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1DKT"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1DKS"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2AST"
SQ SEQUENCE 79 AA; 9660 MW; E64207B140FA38D5 CRC64;
MSHKQIYYSD KYDDEEFEYR HVMLPKDIAK LVPKTHLMSE SEWRNLGVQQ SQGWVHYMIH
EPEPHILLFR RPLPKKPKK
