CINP_HUMAN
ID CINP_HUMAN Reviewed; 212 AA.
AC Q9BW66; F5H7P3; F5H8A7; Q9NPF9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cyclin-dependent kinase 2-interacting protein {ECO:0000303|PubMed:16082200};
DE Short=CDK2-interacting protein {ECO:0000303|PubMed:16082200};
GN Name=CINP {ECO:0000303|PubMed:19889979, ECO:0000312|HGNC:HGNC:23789};
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), SUBUNIT, FUNCTION, INTERACTION WITH
RP CDK2; CDC7; MCM2; MCM3; MCM4; MCM5; MCM6; MCM7 AND ORC2, AND
RP PHOSPHORYLATION.
RX PubMed=16082200;
RA Grishina I., Lattes B.;
RT "A novel Cdk2 interactor is phosphorylated by Cdc7 and associates with
RT components of the replication complexes.";
RL Cell Cycle 4:1120-1126(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Pancreatic carcinoma, and Skin;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, INTERACTION WITH ATRIP, AND SUBCELLULAR LOCATION.
RX PubMed=19889979; DOI=10.1073/pnas.0909345106;
RA Lovejoy C.A., Xu X., Bansbach C.E., Glick G.G., Zhao R., Ye F., Sirbu B.M.,
RA Titus L.C., Shyr Y., Cortez D.;
RT "Functional genomic screens identify CINP as a genome maintenance
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19304-19309(2009).
RN [10]
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 [11]
RP INTERACTION WITH CEP152.
RX PubMed=21131973; DOI=10.1038/ng.725;
RA Kalay E., Yigit G., Aslan Y., Brown K.E., Pohl E., Bicknell L.S.,
RA Kayserili H., Li Y., Tuysuz B., Nurnberg G., Kiess W., Koegl M.,
RA Baessmann I., Buruk K., Toraman B., Kayipmaz S., Kul S., Ikbal M.,
RA Turner D.J., Taylor M.S., Aerts J., Scott C., Milstein K., Dollfus H.,
RA Wieczorek D., Brunner H.G., Hurles M., Jackson A.P., Rauch A., Nurnberg P.,
RA Karaguzel A., Wollnik B.;
RT "CEP152 is a genome maintenance protein disrupted in Seckel syndrome.";
RL Nat. Genet. 43:23-26(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-73, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP FUNCTION, INTERACTION WITH C1ORF109, AND INTERACTION WITH PRE-60S RIBOSOMAL
RP PARTICLES.
RX PubMed=35354024; DOI=10.1016/j.celrep.2022.110597;
RA Ni C., Schmitz D.A., Lee J., Pawlowski K., Wu J., Buszczak M.;
RT "Labeling of heterochronic ribosomes reveals C1ORF109 and SPATA5 control a
RT late step in human ribosome assembly.";
RL Cell Rep. 38:110597-110597(2022).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-177.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:16082200, PubMed:19889979). Regulates ATR-mediated
CC checkpoint signaling in response to DNA damage (PubMed:19889979). Also
CC involved in the cytoplasmic maturation steps of pre-60S ribosomal
CC particles by promoting the release of shuttling protein RSL24D1/RLP24
CC from the pre-ribosomal particles (PubMed:35354024). Promotes maturation
CC of pre-60S ribosome together with SPATA5, SPATA5L1 and C1orf109
CC (PubMed:35354024). {ECO:0000269|PubMed:16082200,
CC ECO:0000269|PubMed:19889979, ECO:0000269|PubMed:35354024}.
CC -!- SUBUNIT: Homodimer (PubMed:16082200). Interacts with CDK2 and CDC7
CC (PubMed:16082200). Interacts with the components of the replication
CC complex, MCM2, MCM3, MCM4, MCM5, MCM6, MCM7 and with ORC2-containing
CC complexes (PubMed:16082200). Interacts with ATRIP (PubMed:19889979).
CC Interacts with CEP152 (PubMed:21131973). Associates with pre-60S
CC ribosomal particles (PubMed:35354024). Interacts with C1orf109
CC (PubMed:35354024). {ECO:0000269|PubMed:16082200,
CC ECO:0000269|PubMed:19889979, ECO:0000269|PubMed:21131973,
CC ECO:0000269|PubMed:35354024}.
CC -!- INTERACTION:
CC Q9BW66; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-739784, EBI-746752;
CC Q9BW66; Q13535: ATR; NbExp=5; IntAct=EBI-739784, EBI-968983;
CC Q9BW66; Q8WXE1: ATRIP; NbExp=9; IntAct=EBI-739784, EBI-747353;
CC Q9BW66; Q9H2G9: BLZF1; NbExp=7; IntAct=EBI-739784, EBI-2548012;
CC Q9BW66; Q9BX70: BTBD2; NbExp=3; IntAct=EBI-739784, EBI-710091;
CC Q9BW66; Q9NX04: C1orf109; NbExp=9; IntAct=EBI-739784, EBI-8643161;
CC Q9BW66; Q8NEF3-2: CCDC112; NbExp=3; IntAct=EBI-739784, EBI-12095166;
CC Q9BW66; Q6P656: CFAP161; NbExp=3; IntAct=EBI-739784, EBI-11901329;
CC Q9BW66; Q96AJ1: CLUAP1; NbExp=5; IntAct=EBI-739784, EBI-739780;
CC Q9BW66; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-739784, EBI-9091495;
CC Q9BW66; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-739784, EBI-7225287;
CC Q9BW66; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-739784, EBI-10244131;
CC Q9BW66; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-739784, EBI-744935;
CC Q9BW66; O95995: GAS8; NbExp=3; IntAct=EBI-739784, EBI-1052570;
CC Q9BW66; Q08379: GOLGA2; NbExp=6; IntAct=EBI-739784, EBI-618309;
CC Q9BW66; A5PKX9: INADL; NbExp=3; IntAct=EBI-739784, EBI-12035052;
CC Q9BW66; Q0VD86: INCA1; NbExp=3; IntAct=EBI-739784, EBI-6509505;
CC Q9BW66; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-739784, EBI-2556193;
CC Q9BW66; P43357: MAGEA3; NbExp=3; IntAct=EBI-739784, EBI-5651459;
CC Q9BW66; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-739784, EBI-16439278;
CC Q9BW66; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-739784, EBI-11977115;
CC Q9BW66; Q9H3L0: MMADHC; NbExp=3; IntAct=EBI-739784, EBI-11111575;
CC Q9BW66; Q08AG7: MZT1; NbExp=5; IntAct=EBI-739784, EBI-2637198;
CC Q9BW66; P17568: NDUFB7; NbExp=3; IntAct=EBI-739784, EBI-1246238;
CC Q9BW66; P26367: PAX6; NbExp=3; IntAct=EBI-739784, EBI-747278;
CC Q9BW66; P78424: POU6F2; NbExp=3; IntAct=EBI-739784, EBI-12029004;
CC Q9BW66; O43663: PRC1; NbExp=3; IntAct=EBI-739784, EBI-741137;
CC Q9BW66; P54821: PRRX1; NbExp=3; IntAct=EBI-739784, EBI-12828023;
CC Q9BW66; P25786: PSMA1; NbExp=3; IntAct=EBI-739784, EBI-359352;
CC Q9BW66; Q04864: REL; NbExp=3; IntAct=EBI-739784, EBI-307352;
CC Q9BW66; Q04864-2: REL; NbExp=3; IntAct=EBI-739784, EBI-10829018;
CC Q9BW66; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-739784, EBI-748601;
CC Q9BW66; P62316: SNRPD2; NbExp=3; IntAct=EBI-739784, EBI-297993;
CC Q9BW66; Q02086-2: SP2; NbExp=3; IntAct=EBI-739784, EBI-9088579;
CC Q9BW66; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-739784, EBI-6872807;
CC Q9BW66; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-739784, EBI-11139477;
CC Q9BW66; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-739784, EBI-18122152;
CC Q9BW66; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-739784, EBI-12287587;
CC Q9BW66; P17023: ZNF19; NbExp=3; IntAct=EBI-739784, EBI-12884200;
CC Q9BW66; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-739784, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19889979}. Note=Binds
CC to nuclear under G1 conditions, and dissociates from chromatin with the
CC start of DNA replication. {ECO:0000269|PubMed:19889979}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BW66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BW66-2; Sequence=VSP_045342, VSP_045343;
CC Name=3;
CC IsoId=Q9BW66-3; Sequence=VSP_046386;
CC -!- PTM: Phosphorylated by CDC7 but not by CDK2.
CC {ECO:0000269|PubMed:16082200}.
CC -!- SIMILARITY: Belongs to the CINP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BU174070; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF228148; AAF44747.1; -; mRNA.
DR EMBL; AF228149; AAF44748.1; -; mRNA.
DR EMBL; AK056112; BAB71095.1; -; mRNA.
DR EMBL; DA167716; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR457178; CAG33459.1; -; mRNA.
DR EMBL; AL137229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81785.1; -; Genomic_DNA.
DR EMBL; BC000600; AAH00600.1; -; mRNA.
DR EMBL; BU174070; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS53915.1; -. [Q9BW66-2]
DR CCDS; CCDS9972.1; -. [Q9BW66-1]
DR RefSeq; NP_001306975.1; NM_001320046.1. [Q9BW66-2]
DR RefSeq; NP_116019.1; NM_032630.2. [Q9BW66-1]
DR AlphaFoldDB; Q9BW66; -.
DR SMR; Q9BW66; -.
DR BioGRID; 119604; 62.
DR DIP; DIP-49011N; -.
DR IntAct; Q9BW66; 48.
DR STRING; 9606.ENSP00000216756; -.
DR iPTMnet; Q9BW66; -.
DR PhosphoSitePlus; Q9BW66; -.
DR BioMuta; CINP; -.
DR DMDM; 74733401; -.
DR EPD; Q9BW66; -.
DR jPOST; Q9BW66; -.
DR MassIVE; Q9BW66; -.
DR MaxQB; Q9BW66; -.
DR PaxDb; Q9BW66; -.
DR PeptideAtlas; Q9BW66; -.
DR PRIDE; Q9BW66; -.
DR ProteomicsDB; 27547; -.
DR ProteomicsDB; 27731; -.
DR ProteomicsDB; 79257; -. [Q9BW66-1]
DR Antibodypedia; 27836; 130 antibodies from 21 providers.
DR DNASU; 51550; -.
DR Ensembl; ENST00000216756.11; ENSP00000216756.6; ENSG00000100865.15. [Q9BW66-1]
DR Ensembl; ENST00000536961.6; ENSP00000442057.2; ENSG00000100865.15. [Q9BW66-3]
DR Ensembl; ENST00000541568.6; ENSP00000442377.2; ENSG00000100865.15. [Q9BW66-2]
DR Ensembl; ENST00000559514.5; ENSP00000453839.1; ENSG00000100865.15. [Q9BW66-1]
DR GeneID; 51550; -.
DR KEGG; hsa:51550; -.
DR MANE-Select; ENST00000216756.11; ENSP00000216756.6; NM_032630.3; NP_116019.1.
DR UCSC; uc001ylv.2; human. [Q9BW66-1]
DR CTD; 51550; -.
DR DisGeNET; 51550; -.
DR GeneCards; CINP; -.
DR HGNC; HGNC:23789; CINP.
DR HPA; ENSG00000100865; Low tissue specificity.
DR MIM; 613362; gene.
DR neXtProt; NX_Q9BW66; -.
DR OpenTargets; ENSG00000100865; -.
DR PharmGKB; PA165478684; -.
DR VEuPathDB; HostDB:ENSG00000100865; -.
DR eggNOG; ENOG502S092; Eukaryota.
DR GeneTree; ENSGT00390000015784; -.
DR HOGENOM; CLU_077982_0_0_1; -.
DR InParanoid; Q9BW66; -.
DR OMA; DQDLMMV; -.
DR PhylomeDB; Q9BW66; -.
DR TreeFam; TF329462; -.
DR PathwayCommons; Q9BW66; -.
DR SignaLink; Q9BW66; -.
DR BioGRID-ORCS; 51550; 693 hits in 1103 CRISPR screens.
DR GenomeRNAi; 51550; -.
DR Pharos; Q9BW66; Tbio.
DR PRO; PR:Q9BW66; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BW66; protein.
DR Bgee; ENSG00000100865; Expressed in C1 segment of cervical spinal cord and 119 other tissues.
DR ExpressionAtlas; Q9BW66; baseline and differential.
DR Genevisible; Q9BW66; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990275; F:preribosome binding; IDA: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; IDA:UniProtKB.
DR InterPro; IPR023250; Cyclin-dep_Kinase_2_interact.
DR PRINTS; PR02040; CDK2IP.
PE 1: Evidence at protein 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_0000326055"
FT COILED 73..107
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..3
FT /note="MEA -> MNGTIYANECQQIRHPNS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046386"
FT VAR_SEQ 103..118
FT /note="TKIQVKMEKLSSTTKG -> MRFRISSWRCTGRSCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045342"
FT VAR_SEQ 119..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045343"
FT VARIANT 164
FT /note="R -> H (in dbSNP:rs7011)"
FT /id="VAR_039979"
FT VARIANT 177
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039980"
FT CONFLICT 157
FT /note="R -> K (in Ref. 1; AAF44747/AAF44748)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="D -> N (in Ref. 1; AAF44747/AAF44748)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..197
FT /note="SDSR -> NDNK (in Ref. 1; AAF44747/AAF44748)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="S -> R (in Ref. 6; BU174070)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="S -> N (in Ref. 1; AAF44747/AAF44748)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..212
FT /note="RAL -> PSSLTS (in Ref. 6; BU174070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24324 MW; 3678E123B8C206B1 CRC64;
MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN
KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC
ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL
SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL
