ID   CACL1_HUMAN             Reviewed;         369 AA.
AC   Q86Y37; Q5XPL7; Q8IY11; Q8N7S4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=CDK2-associated and cullin domain-containing protein 1;
DE   AltName: Full=Cdk-associated cullin 1;
GN   Name=CACUL1; Synonyms=C10orf46, CAC1;
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] (ISOFORM 1).
RA   Huang C., Wu S., Liu S.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Rectum tumor;
RA   Kong Y., Chen Y., Xia Q.;
RT   "The expression of gene in human rectum carcinoma.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CDK2.
RX   PubMed=19829063; DOI=10.4161/cc.8.21.9955;
RA   Kong Y., Nan K., Yin Y.;
RT   "Identification and characterization of CAC1 as a novel CDK2-associated
RT   cullin.";
RL   Cell Cycle 8:3552-3561(2009).
CC   -!- FUNCTION: Cell cycle associated protein capable of promoting cell
CC       proliferation through the activation of CDK2 at the G1/S phase
CC       transition. {ECO:0000269|PubMed:19829063}.
CC   -!- SUBUNIT: Interacts with CDK2. {ECO:0000269|PubMed:19829063}.
CC   -!- INTERACTION:
CC       Q86Y37; P03372: ESR1; NbExp=5; IntAct=EBI-8168227, EBI-78473;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86Y37-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86Y37-2; Sequence=VSP_013936, VSP_013937;
CC       Name=4;
CC         IsoId=Q86Y37-4; Sequence=VSP_013933;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest expression in
CC       the mammary gland and large intestine. Highly expressed in cancer
CC       tissues and cancer cell lines. During cell cycle progression expression
CC       is high in G1/S, low in the middle of S phase, and increases again in
CC       S/G2 phase. {ECO:0000269|PubMed:19829063}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU89709.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ544771; CAD67614.1; -; mRNA.
DR   EMBL; AY743663; AAU89709.1; ALT_FRAME; mRNA.
DR   EMBL; AK097728; BAC05153.1; -; mRNA.
DR   EMBL; AL139407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038294; AAH38294.1; -; mRNA.
DR   CCDS; CCDS41570.1; -. [Q86Y37-1]
DR   RefSeq; NP_722517.3; NM_153810.4. [Q86Y37-1]
DR   AlphaFoldDB; Q86Y37; -.
DR   SMR; Q86Y37; -.
DR   BioGRID; 126801; 25.
DR   IntAct; Q86Y37; 3.
DR   MINT; Q86Y37; -.
DR   STRING; 9606.ENSP00000358147; -.
DR   GlyCosmos; Q86Y37; 1 site, 1 glycan.
DR   GlyGen; Q86Y37; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q86Y37; -.
DR   PhosphoSitePlus; Q86Y37; -.
DR   BioMuta; CACUL1; -.
DR   DMDM; 67460542; -.
DR   EPD; Q86Y37; -.
DR   jPOST; Q86Y37; -.
DR   MassIVE; Q86Y37; -.
DR   MaxQB; Q86Y37; -.
DR   PaxDb; 9606-ENSP00000358147; -.
DR   PeptideAtlas; Q86Y37; -.
DR   ProteomicsDB; 70367; -. [Q86Y37-1]
DR   ProteomicsDB; 70368; -. [Q86Y37-2]
DR   ProteomicsDB; 70369; -. [Q86Y37-4]
DR   Pumba; Q86Y37; -.
DR   Antibodypedia; 32069; 160 antibodies from 22 providers.
DR   DNASU; 143384; -.
DR   Ensembl; ENST00000369151.8; ENSP00000358147.2; ENSG00000151893.15. [Q86Y37-1]
DR   Ensembl; ENST00000493518.5; ENSP00000431329.1; ENSG00000151893.15. [Q86Y37-2]
DR   GeneID; 143384; -.
DR   KEGG; hsa:143384; -.
DR   MANE-Select; ENST00000369151.8; ENSP00000358147.2; NM_153810.5; NP_722517.3.
DR   UCSC; uc001lds.2; human. [Q86Y37-1]
DR   AGR; HGNC:23727; -.
DR   CTD; 143384; -.
DR   DisGeNET; 143384; -.
DR   GeneCards; CACUL1; -.
DR   HGNC; HGNC:23727; CACUL1.
DR   HPA; ENSG00000151893; Low tissue specificity.
DR   MIM; 618764; gene.
DR   neXtProt; NX_Q86Y37; -.
DR   OpenTargets; ENSG00000151893; -.
DR   PharmGKB; PA134869023; -.
DR   VEuPathDB; HostDB:ENSG00000151893; -.
DR   eggNOG; KOG2166; Eukaryota.
DR   GeneTree; ENSGT00390000000403; -.
DR   HOGENOM; CLU_062250_1_0_1; -.
DR   InParanoid; Q86Y37; -.
DR   OMA; PFWINPS; -.
DR   OrthoDB; 2938756at2759; -.
DR   PhylomeDB; Q86Y37; -.
DR   TreeFam; TF329263; -.
DR   PathwayCommons; Q86Y37; -.
DR   SignaLink; Q86Y37; -.
DR   BioGRID-ORCS; 143384; 13 hits in 1162 CRISPR screens.
DR   ChiTaRS; CACUL1; human.
DR   GenomeRNAi; 143384; -.
DR   Pharos; Q86Y37; Tbio.
DR   PRO; PR:Q86Y37; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q86Y37; Protein.
DR   Bgee; ENSG00000151893; Expressed in upper arm skin and 202 other cell types or tissues.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR   InterPro; IPR042652; CACUL1.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   PANTHER; PTHR46636; CDK2-ASSOCIATED AND CULLIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46636:SF1; CDK2-ASSOCIATED AND CULLIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SUPFAM; SSF74788; Cullin repeat-like; 1.
DR   Genevisible; Q86Y37; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Reference proteome.
FT   CHAIN           1..369
FT                   /note="CDK2-associated and cullin domain-containing protein
FT                   1"
FT                   /id="PRO_0000119817"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..123
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_013933"
FT   VAR_SEQ         296..303
FT                   /note="EWVQMAPT -> VSQNFTAV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013936"
FT   VAR_SEQ         304..369
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013937"
SQ   SEQUENCE   369 AA;  41064 MW;  7ABA2F6846C4F737 CRC64;
     MEESMEEEEG GSYEAMMDDQ NHNNWEAAVD GFRQPLPPPP PPSSIPAPAR EPPGGQLLAV
     PAVSVDRKGP KEGLPMGPQP PPEANGVIMM LKSCDAAAAV AKAAPAPTAS STININTSTS
     KFLMNVITIE DYKSTYWPKL DGAIDQLLTQ SPGDYIPISY EQIYSCVYKC VCQQHSEQMY
     SDLIKKITNH LERVSKELQA SPPDLYIERF NIALGQYMGA LQSIVPLFIY MNKFYIETKL
     NRDLKDDLIK LFTEHVAEKH IYSLMPLLLE AQSTPFQVTP STMANIVKGL YTLRPEWVQM
     APTLFSKFIP NILPPAVESE LSEYAAQDQK FQRELIQNGF TRGDQSRKRA GDELAYNSSS
     ACASSRGYR
//