CACL1_MOUSE
ID CACL1_MOUSE Reviewed; 377 AA.
AC Q8R0X2; Q3TE79; Q9CY95;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=CDK2-associated and cullin domain-containing protein 1;
GN Name=Cacul1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain, Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
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:0000250}.
CC -!- SUBUNIT: Interacts with CDK2. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0X2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0X2-2; Sequence=VSP_013938, VSP_013939;
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000305}.
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DR EMBL; AK019216; BAB31607.1; -; mRNA.
DR EMBL; AK147382; BAE27876.1; -; mRNA.
DR EMBL; AK169791; BAE41369.1; -; mRNA.
DR EMBL; BC026363; AAH26363.1; -; mRNA.
DR CCDS; CCDS38034.1; -. [Q8R0X2-1]
DR CCDS; CCDS50483.1; -. [Q8R0X2-2]
DR RefSeq; NP_001165567.1; NM_001172096.1.
DR RefSeq; NP_001165568.1; NM_001172097.1. [Q8R0X2-2]
DR RefSeq; NP_084473.1; NM_030197.2. [Q8R0X2-1]
DR AlphaFoldDB; Q8R0X2; -.
DR SMR; Q8R0X2; -.
DR STRING; 10090.ENSMUSP00000080480; -.
DR iPTMnet; Q8R0X2; -.
DR PhosphoSitePlus; Q8R0X2; -.
DR EPD; Q8R0X2; -.
DR MaxQB; Q8R0X2; -.
DR PaxDb; Q8R0X2; -.
DR PeptideAtlas; Q8R0X2; -.
DR PRIDE; Q8R0X2; -.
DR ProteomicsDB; 273826; -. [Q8R0X2-1]
DR ProteomicsDB; 273827; -. [Q8R0X2-2]
DR Antibodypedia; 32069; 139 antibodies from 22 providers.
DR DNASU; 78832; -.
DR Ensembl; ENSMUST00000081790; ENSMUSP00000080480; ENSMUSG00000033417. [Q8R0X2-1]
DR Ensembl; ENSMUST00000111460; ENSMUSP00000107086; ENSMUSG00000033417. [Q8R0X2-2]
DR GeneID; 78832; -.
DR KEGG; mmu:78832; -.
DR UCSC; uc008ibv.2; mouse. [Q8R0X2-1]
DR UCSC; uc012bof.1; mouse. [Q8R0X2-2]
DR CTD; 143384; -.
DR MGI; MGI:1926082; Cacul1.
DR VEuPathDB; HostDB:ENSMUSG00000033417; -.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00390000000403; -.
DR HOGENOM; CLU_062250_1_0_1; -.
DR InParanoid; Q8R0X2; -.
DR OMA; HNHNYRA; -.
DR OrthoDB; 991620at2759; -.
DR PhylomeDB; Q8R0X2; -.
DR TreeFam; TF329263; -.
DR BioGRID-ORCS; 78832; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Cacul1; mouse.
DR PRO; PR:Q8R0X2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R0X2; protein.
DR Bgee; ENSMUSG00000033417; Expressed in spermatid and 260 other tissues.
DR ExpressionAtlas; Q8R0X2; baseline and differential.
DR Genevisible; Q8R0X2; MM.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR042652; CACUL1.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR PANTHER; PTHR46636; PTHR46636; 1.
DR Pfam; PF00888; Cullin; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Reference proteome.
FT CHAIN 1..377
FT /note="CDK2-associated and cullin domain-containing protein
FT 1"
FT /id="PRO_0000119818"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 274..304
FT /note="PLLLEAQSTPFQVTPSTMANIVKGLYTLRPE -> QVISPGRELEMSWLITV
FT HLLVQVPGGIDSDG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013938"
FT VAR_SEQ 305..377
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013939"
SQ SEQUENCE 377 AA; 42106 MW; 1BBF30D5394FE381 CRC64;
MEESMEEEEM LTYEAMMDDQ NHNNWEAAAD SFRQPPPAPP LPPPPPPRPS SSIPDPGREL
PGGQLLAVHA GSMERKGPKE GLPMGPPPLP EPNGVIMMLK SCDAAAAVAK TAPAPTSSST
ININTSTSKF LMNVITIEDY KSTYWPKLDG AIDQLLTQSP GDYIPISYEQ IYSCVYKCVC
QQHSEQMYSD LIKKITSHLE RVSKELQASP PDLYIERFNI ALGQYMGALQ SIVPLFIYMN
KFYIETKLNR DLKDDLIKLF TEHVAEKHIY SLMPLLLEAQ STPFQVTPST MANIVKGLYT
LRPEWVQMAP TLFSKFIPNI LPPAVESELS EYAAQDQKLQ RELIQNGFTR GDQSRKRAGD
ELAYNSPSAC ASSRGYR
