CINP_MOUSE
ID CINP_MOUSE Reviewed; 212 AA.
AC Q9D0V8; Q8C063; Q9D8P9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cyclin-dependent kinase 2-interacting protein;
GN Name=Cinp;
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; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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=Mammary tumor;
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: Component of the DNA replication complex, which interacts
CC with two kinases, CDK2 and CDC7, thereby providing a functional and
CC physical link between CDK2 and CDC7 during firing of the origins of
CC replication. Regulates ATR-mediated checkpoint signaling in response to
CC DNA damage. Also involved in the cytoplasmic maturation steps of pre-
CC 60S ribosomal particles by promoting the release of shuttling protein
CC RSL24D1/RLP24 from the pre-ribosomal particles. Promotes maturation of
CC pre-60S ribosome together with SPATA5, SPATA5L1 and C1orf109.
CC {ECO:0000250|UniProtKB:Q9BW66}.
CC -!- SUBUNIT: Homodimer. Interacts with CDK2 and CDC7. Interacts with the
CC components of the replication complex, MCM2, MCM3, MCM4, MCM5, MCM6,
CC MCM7 and with ORC2-containing complexes. Interacts with ATRIP.
CC Interacts with CEP152. Associates with pre-60S ribosomal particles.
CC Interacts with C1orf109 ortholog. {ECO:0000250|UniProtKB:Q9BW66}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW66}.
CC Note=Binds to nuclear under G1 conditions, and dissociates from
CC chromatin with the start of DNA replication.
CC {ECO:0000250|UniProtKB:Q9BW66}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D0V8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0V8-2; Sequence=VSP_032525, VSP_032526;
CC Name=3;
CC IsoId=Q9D0V8-3; Sequence=VSP_032527, VSP_032528;
CC -!- PTM: Phosphorylated by CDC7 but not by CDK2.
CC {ECO:0000250|UniProtKB:Q9BW66}.
CC -!- SIMILARITY: Belongs to the CINP family. {ECO:0000305}.
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DR EMBL; AK004355; BAB23273.1; -; mRNA.
DR EMBL; AK007812; BAB25277.1; -; mRNA.
DR EMBL; AK076126; BAC36203.1; -; mRNA.
DR EMBL; AK032155; BAC27729.1; -; mRNA.
DR EMBL; BC011066; AAH11066.1; -; mRNA.
DR CCDS; CCDS36561.1; -. [Q9D0V8-1]
DR RefSeq; NP_080324.1; NM_026048.4. [Q9D0V8-1]
DR AlphaFoldDB; Q9D0V8; -.
DR SMR; Q9D0V8; -.
DR STRING; 10090.ENSMUSP00000035245; -.
DR PhosphoSitePlus; Q9D0V8; -.
DR EPD; Q9D0V8; -.
DR MaxQB; Q9D0V8; -.
DR PaxDb; Q9D0V8; -.
DR PRIDE; Q9D0V8; -.
DR ProteomicsDB; 283842; -. [Q9D0V8-1]
DR ProteomicsDB; 283843; -. [Q9D0V8-2]
DR ProteomicsDB; 283844; -. [Q9D0V8-3]
DR Antibodypedia; 27836; 130 antibodies from 21 providers.
DR DNASU; 67236; -.
DR Ensembl; ENSMUST00000043716; ENSMUSP00000035245; ENSMUSG00000021276. [Q9D0V8-1]
DR GeneID; 67236; -.
DR KEGG; mmu:67236; -.
DR UCSC; uc007pcb.2; mouse. [Q9D0V8-1]
DR UCSC; uc007pcd.2; mouse. [Q9D0V8-2]
DR UCSC; uc007pce.2; mouse. [Q9D0V8-3]
DR CTD; 51550; -.
DR MGI; MGI:1914486; Cinp.
DR VEuPathDB; HostDB:ENSMUSG00000021276; -.
DR eggNOG; ENOG502S092; Eukaryota.
DR GeneTree; ENSGT00390000015784; -.
DR HOGENOM; CLU_077982_0_0_1; -.
DR InParanoid; Q9D0V8; -.
DR OMA; DQDLMMV; -.
DR PhylomeDB; Q9D0V8; -.
DR TreeFam; TF329462; -.
DR BioGRID-ORCS; 67236; 29 hits in 108 CRISPR screens.
DR ChiTaRS; Cinp; mouse.
DR PRO; PR:Q9D0V8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D0V8; protein.
DR Bgee; ENSMUSG00000021276; Expressed in ectoplacental cone and 263 other tissues.
DR ExpressionAtlas; Q9D0V8; baseline and differential.
DR Genevisible; Q9D0V8; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990275; F:preribosome binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR InterPro; IPR023250; Cyclin-dep_Kinase_2_interact.
DR PRINTS; PR02040; CDK2IP.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW DNA damage; DNA repair; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis.
FT CHAIN 1..212
FT /note="Cyclin-dependent kinase 2-interacting protein"
FT /id="PRO_0000326056"
FT COILED 73..107
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW66"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW66"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW66"
FT VAR_SEQ 102..137
FT /note="LTKIQMKMEKLSSTTKGICELENYHYREESSRPPLF -> MVRPKDAGHRHH
FT CLGLLTVGAFRTVGGLSFHLPNKS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032527"
FT VAR_SEQ 103..117
FT /note="TKIQMKMEKLSSTTK -> GIQHPVLVCTAPTHK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032525"
FT VAR_SEQ 118..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032526"
FT VAR_SEQ 138..212
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032528"
SQ SEQUENCE 212 AA; 24104 MW; C9977FD22DBE8AF9 CRC64;
MEAKTLGIAT PRKPVLSVSA RKLKDNAADW HNLILKWDSL SDKGFTTASS IANLKVSLLS
KEKVELESSS PASMEEEEKT NLDYDKGLEA LCEELQAILD GLTKIQMKME KLSSTTKGIC
ELENYHYREE SSRPPLFHTW PTAFFYEVSR RLSEAYKKEL LLKHTIGAEL AHTADRNLSL
TYLSMWLHQP YIESNSKLQL ESMLLETGHR AL
