CCNA2_HUMAN
ID CCNA2_HUMAN Reviewed; 432 AA.
AC P20248; A8K7B6; Q2M3U6; Q4W5P4; Q6LER8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Cyclin-A2 {ECO:0000312|HGNC:HGNC:1578};
DE Short=Cyclin-A {ECO:0000303|PubMed:1967822};
DE AltName: Full=Cyclin A {ECO:0000303|PubMed:1967822};
GN Name=CCNA2 {ECO:0000312|HGNC:HGNC:1578};
GN Synonyms=CCN1 {ECO:0000312|HGNC:HGNC:1578},
GN CCNA {ECO:0000312|HGNC:HGNC:1578};
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], AND VARIANT VAL-163.
RX PubMed=1967822; DOI=10.1038/343555a0;
RA Wang J., Chenivesse X., Henglein B., Brechot C.;
RT "Hepatitis B virus integration in a cyclin A gene in a hepatocellular
RT carcinoma.";
RL Nature 343:555-557(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=8202514; DOI=10.1073/pnas.91.12.5490;
RA Henglein B., Chenivesse X., Wang D., Eick D., Brechot C.;
RT "Structure and cell cycle-regulated transcription of the human cyclin A
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5490-5494(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-163.
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-163.
RG NIEHS SNPs program;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-163.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-163.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-163.
RC TISSUE=Brain;
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 [9]
RP FUNCTION, INTERACTION WITH CDK1 AND CDK2, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=1312467; DOI=10.1002/j.1460-2075.1992.tb05135.x;
RA Pagano M., Pepperkok R., Verde F., Ansorge W., Draetta G.;
RT "Cyclin A is required at two points in the human cell cycle.";
RL EMBO J. 11:961-971(1992).
RN [10]
RP INTERACTION WITH SCAPER, AND SUBCELLULAR LOCATION.
RX PubMed=17698606; DOI=10.1083/jcb.200701166;
RA Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.;
RT "SCAPER, a novel cyclin A-interacting protein that regulates cell cycle
RT progression.";
RL J. Cell Biol. 178:621-633(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5 AND SER-55, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
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 [13]
RP INTERACTION WITH INCA1.
RX PubMed=21540187; DOI=10.1074/jbc.m110.203471;
RA Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S.,
RA Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G.,
RA Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.;
RT "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1
RT (INCA1) regulates proliferation and is repressed by oncogenic signaling.";
RL J. Biol. Chem. 286:28210-28222(2011).
RN [14]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP37.
RX PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027;
RA Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,
RA Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.;
RT "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and
RT promote S phase entry.";
RL Mol. Cell 42:511-523(2011).
RN [15]
RP IDENTIFICATION BY MASS 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [17]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS UL32 (MICROBIAL INFECTION).
RX PubMed=24101496; DOI=10.1073/pnas.1312235110;
RA Bogdanow B., Weisbach H., von Einem J., Straschewski S., Voigt S.,
RA Winkler M., Hagemeier C., Wiebusch L.;
RT "Human cytomegalovirus tegument protein pp150 acts as a cyclin A2-CDK-
RT dependent sensor of the host cell cycle and differentiation state.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17510-17515(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN COMPLEX WITH CDK2.
RX PubMed=7630397; DOI=10.1038/376313a0;
RA Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J.,
RA Pavletich N.P.;
RT "Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2
RT complex.";
RL Nature 376:313-320(1995).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN COMPLEX WITH CDK2 AND
RP CDKN1B.
RX PubMed=8684460; DOI=10.1038/382325a0;
RA Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
RT "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound
RT to the cyclin A-Cdk2 complex.";
RL Nature 382:325-331(1996).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 IN COMPLEX WITH CDK2.
RX PubMed=8756328; DOI=10.1038/nsb0896-696;
RA Russo A.A., Jeffrey P.D., Pavletich N.P.;
RT "Structural basis of cyclin-dependent kinase activation by
RT phosphorylation.";
RL Nat. Struct. Biol. 3:696-700(1996).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-163, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
CC -!- FUNCTION: Cyclin which controls both the G1/S and the G2/M transition
CC phases of the cell cycle. Functions through the formation of specific
CC serine/threonine protein kinase holoenzyme complexes with the cyclin-
CC dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the
CC substrate specificity of these complexes and differentially interacts
CC with and activates CDK1 and CDK2 throughout the cell cycle.
CC {ECO:0000269|PubMed:1312467}.
CC -!- SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form
CC serine/threonine kinase holoenzyme complexes (PubMed:1312467,
CC PubMed:7630397, PubMed:8684460, PubMed:8756328). Interacts with CDK1
CC (hyperphosphorylated form in G1 and underphosphorylated forms in S and
CC G2) (PubMed:1312467). Interacts with CDK2; the interaction increases
CC from G1 to G2 (PubMed:1312467). Interacts (associated with CDK2 but not
CC with CDK1) with SCAPER; regulates the activity of CCNA2/CDK2 by
CC transiently maintaining CCNA2 in the cytoplasm (PubMed:17698606). Forms
CC a ternary complex with CDK2 and CDKN1B; CDKN1B inhibits the kinase
CC activity of CDK2 through conformational rearrangements
CC (PubMed:8684460). Interacts with INCA1 (PubMed:21540187).
CC {ECO:0000269|PubMed:1312467, ECO:0000269|PubMed:17698606,
CC ECO:0000269|PubMed:21540187, ECO:0000269|PubMed:7630397,
CC ECO:0000269|PubMed:8684460, ECO:0000269|PubMed:8756328}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL32. {ECO:0000269|PubMed:24101496}.
CC -!- INTERACTION:
CC P20248; P31749: AKT1; NbExp=2; IntAct=EBI-457097, EBI-296087;
CC P20248; P24941: CDK2; NbExp=28; IntAct=EBI-457097, EBI-375096;
CC P20248; P38936: CDKN1A; NbExp=5; IntAct=EBI-457097, EBI-375077;
CC P20248; P46527: CDKN1B; NbExp=17; IntAct=EBI-457097, EBI-519280;
CC P20248; Q96PU4: UHRF2; NbExp=2; IntAct=EBI-457097, EBI-625304;
CC P20248; P03129: E7; Xeno; NbExp=2; IntAct=EBI-457097, EBI-866453;
CC P20248; P03070; Xeno; NbExp=2; IntAct=EBI-457097, EBI-617698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1312467,
CC ECO:0000269|PubMed:17698606}. Cytoplasm {ECO:0000269|PubMed:1312467,
CC ECO:0000269|PubMed:17698606}. Note=Exclusively nuclear during
CC interphase (PubMed:1312467). Detected in the nucleus and the cytoplasm
CC at prophase (PubMed:1312467). Cytoplasmic when associated with SCAPER
CC (PubMed:17698606). {ECO:0000269|PubMed:1312467,
CC ECO:0000269|PubMed:17698606}.
CC -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC destroyed at mitosis. Not detected during the G1 phase of the cell
CC cycle. It accumulates during the DNA synthesis/S phase and disappears
CC as cells progress into mitosis, between prophase and metaphase (at
CC protein level). {ECO:0000269|PubMed:1312467}.
CC -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-
CC promoting complex (APC/C), leading to its degradation by the
CC proteasome. Deubiquitinated and stabilized by USP37 enables entry into
CC S phase. {ECO:0000269|PubMed:21596315}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccna2/";
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DR EMBL; X51688; CAA35986.1; -; mRNA.
DR EMBL; X68303; CAA48375.1; -; Genomic_DNA.
DR EMBL; CR407692; CAG28620.1; -; mRNA.
DR EMBL; AF518006; AAM54042.1; -; Genomic_DNA.
DR EMBL; AK291931; BAF84620.1; -; mRNA.
DR EMBL; AC079341; AAY40969.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05246.1; -; Genomic_DNA.
DR EMBL; BC104783; AAI04784.1; -; mRNA.
DR EMBL; BC104787; AAI04788.1; -; mRNA.
DR CCDS; CCDS3723.1; -.
DR PIR; S08277; S08277.
DR RefSeq; NP_001228.1; NM_001237.4.
DR PDB; 1E9H; X-ray; 2.50 A; B/D=175-432.
DR PDB; 1FIN; X-ray; 2.30 A; B/D=173-432.
DR PDB; 1FVV; X-ray; 2.80 A; B/D=173-432.
DR PDB; 1GY3; X-ray; 2.70 A; B/D=175-432.
DR PDB; 1H1P; X-ray; 2.10 A; B/D=175-432.
DR PDB; 1H1Q; X-ray; 2.50 A; B/D=175-432.
DR PDB; 1H1R; X-ray; 2.00 A; B/D=175-432.
DR PDB; 1H1S; X-ray; 2.00 A; B/D=175-432.
DR PDB; 1H24; X-ray; 2.50 A; B/D=174-432.
DR PDB; 1H25; X-ray; 2.50 A; B/D=174-432.
DR PDB; 1H26; X-ray; 2.24 A; B/D=174-432.
DR PDB; 1H27; X-ray; 2.20 A; B/D=174-432.
DR PDB; 1H28; X-ray; 2.80 A; B/D=174-432.
DR PDB; 1JST; X-ray; 2.60 A; B/D=175-432.
DR PDB; 1JSU; X-ray; 2.30 A; B=173-432.
DR PDB; 1OGU; X-ray; 2.60 A; B/D=174-432.
DR PDB; 1OI9; X-ray; 2.10 A; B/D=174-432.
DR PDB; 1OIU; X-ray; 2.00 A; B/D=174-432.
DR PDB; 1OIY; X-ray; 2.40 A; B/D=174-432.
DR PDB; 1OKV; X-ray; 2.40 A; B/D=173-432.
DR PDB; 1OKW; X-ray; 2.50 A; B/D=173-432.
DR PDB; 1OL1; X-ray; 2.90 A; B/D=173-432.
DR PDB; 1OL2; X-ray; 2.60 A; B/D=173-432.
DR PDB; 1P5E; X-ray; 2.22 A; B/D=175-432.
DR PDB; 1PKD; X-ray; 2.30 A; B/D=175-432.
DR PDB; 1QMZ; X-ray; 2.20 A; B/D=174-432.
DR PDB; 1URC; X-ray; 2.60 A; B/D=173-432.
DR PDB; 1VYW; X-ray; 2.30 A; B/D=174-432.
DR PDB; 2BKZ; X-ray; 2.60 A; B/D=174-432.
DR PDB; 2BPM; X-ray; 2.40 A; B/D=174-432.
DR PDB; 2C4G; X-ray; 2.70 A; B/D=173-432.
DR PDB; 2C5N; X-ray; 2.10 A; B/D=174-432.
DR PDB; 2C5O; X-ray; 2.10 A; B/D=173-432.
DR PDB; 2C5V; X-ray; 2.90 A; B/D=174-432.
DR PDB; 2C5X; X-ray; 2.90 A; B/D=174-432.
DR PDB; 2C6T; X-ray; 2.61 A; B/D=175-432.
DR PDB; 2CCH; X-ray; 1.70 A; B/D=173-432.
DR PDB; 2CCI; X-ray; 2.70 A; B/D=175-432.
DR PDB; 2CJM; X-ray; 2.30 A; B/D=175-432.
DR PDB; 2I40; X-ray; 2.80 A; B/D=173-432.
DR PDB; 2IW6; X-ray; 2.30 A; B/D=174-432.
DR PDB; 2IW8; X-ray; 2.30 A; B/D=174-432.
DR PDB; 2IW9; X-ray; 2.00 A; B/D=174-432.
DR PDB; 2UUE; X-ray; 2.06 A; B/D=174-432.
DR PDB; 2UZB; X-ray; 2.70 A; B/D=175-432.
DR PDB; 2UZD; X-ray; 2.72 A; B/D=175-432.
DR PDB; 2UZE; X-ray; 2.40 A; B/D=175-432.
DR PDB; 2UZL; X-ray; 2.40 A; B/D=175-432.
DR PDB; 2V22; X-ray; 2.60 A; B/D=174-432.
DR PDB; 2WEV; X-ray; 2.30 A; B/D=173-432.
DR PDB; 2WFY; X-ray; 2.53 A; B/D=173-432.
DR PDB; 2WHB; X-ray; 2.90 A; B/D=173-432.
DR PDB; 2WIH; X-ray; 2.50 A; B/D=173-432.
DR PDB; 2WIP; X-ray; 2.80 A; B/D=173-432.
DR PDB; 2WMA; X-ray; 2.80 A; B/D=174-432.
DR PDB; 2WMB; X-ray; 2.60 A; B/D=174-432.
DR PDB; 2WPA; X-ray; 2.51 A; B/D=173-432.
DR PDB; 2WXV; X-ray; 2.60 A; B/D=173-432.
DR PDB; 2X1N; X-ray; 2.75 A; B/D=172-432.
DR PDB; 3EID; X-ray; 3.15 A; B/D=173-432.
DR PDB; 3EJ1; X-ray; 3.22 A; B/D=173-432.
DR PDB; 3EOC; X-ray; 3.20 A; B/D=173-432.
DR PDB; 3F5X; X-ray; 2.40 A; B/D=177-432.
DR PDB; 4BCK; X-ray; 2.05 A; B/D=171-432.
DR PDB; 4BCM; X-ray; 2.45 A; B/D=171-432.
DR PDB; 4BCN; X-ray; 2.10 A; B=171-432, D=171-431.
DR PDB; 4BCP; X-ray; 2.26 A; B/D=171-432.
DR PDB; 4CFM; X-ray; 2.85 A; B/D=175-432.
DR PDB; 4CFN; X-ray; 2.20 A; B/D=175-432.
DR PDB; 4CFU; X-ray; 2.20 A; B=172-432, D=173-432.
DR PDB; 4CFV; X-ray; 2.00 A; B/D=172-432.
DR PDB; 4CFW; X-ray; 2.45 A; B/D=175-432.
DR PDB; 4CFX; X-ray; 3.50 A; B/D=173-432.
DR PDB; 4EOI; X-ray; 2.00 A; B/D=175-432.
DR PDB; 4EOJ; X-ray; 1.65 A; B/D=175-432.
DR PDB; 4EOK; X-ray; 2.57 A; B/D=175-432.
DR PDB; 4EOL; X-ray; 2.40 A; B/D=175-432.
DR PDB; 4EOM; X-ray; 2.10 A; B/D=175-432.
DR PDB; 4EON; X-ray; 2.40 A; B/D=175-432.
DR PDB; 4EOO; X-ray; 2.10 A; B/D=175-432.
DR PDB; 4EOP; X-ray; 1.99 A; B/D=175-432.
DR PDB; 4EOQ; X-ray; 2.15 A; B/D=175-432.
DR PDB; 4EOR; X-ray; 2.20 A; B/D=175-432.
DR PDB; 4EOS; X-ray; 2.57 A; B/D=175-432.
DR PDB; 4FX3; X-ray; 2.75 A; B/D=175-432.
DR PDB; 5CYI; X-ray; 2.00 A; B/D=174-432.
DR PDB; 5IF1; X-ray; 2.61 A; B/D=174-432.
DR PDB; 5LMK; X-ray; 2.40 A; B/D=175-432.
DR PDB; 5NEV; X-ray; 2.97 A; B/D=174-432.
DR PDB; 6ATH; X-ray; 1.82 A; B=173-432.
DR PDB; 6GVA; X-ray; 2.15 A; B=175-432.
DR PDB; 6P3W; X-ray; 2.54 A; B/D=176-432.
DR PDB; 6Q6G; EM; 3.20 A; S=1-432.
DR PDB; 6Q6H; EM; 3.20 A; S=1-432.
DR PDB; 6RIJ; X-ray; 2.20 A; B/D=175-432.
DR PDB; 6SG4; X-ray; 2.43 A; B/D=174-432.
DR PDB; 7ACK; X-ray; 1.80 A; B/D=175-432.
DR PDB; 7B5L; EM; 3.80 A; Y=1-432.
DR PDB; 7B5R; EM; 3.80 A; Y=1-432.
DR PDB; 7B7S; X-ray; 2.54 A; B/D=175-432.
DR PDB; 7LUO; X-ray; 3.17 A; A/C=174-432.
DR PDBsum; 1E9H; -.
DR PDBsum; 1FIN; -.
DR PDBsum; 1FVV; -.
DR PDBsum; 1GY3; -.
DR PDBsum; 1H1P; -.
DR PDBsum; 1H1Q; -.
DR PDBsum; 1H1R; -.
DR PDBsum; 1H1S; -.
DR PDBsum; 1H24; -.
DR PDBsum; 1H25; -.
DR PDBsum; 1H26; -.
DR PDBsum; 1H27; -.
DR PDBsum; 1H28; -.
DR PDBsum; 1JST; -.
DR PDBsum; 1JSU; -.
DR PDBsum; 1OGU; -.
DR PDBsum; 1OI9; -.
DR PDBsum; 1OIU; -.
DR PDBsum; 1OIY; -.
DR PDBsum; 1OKV; -.
DR PDBsum; 1OKW; -.
DR PDBsum; 1OL1; -.
DR PDBsum; 1OL2; -.
DR PDBsum; 1P5E; -.
DR PDBsum; 1PKD; -.
DR PDBsum; 1QMZ; -.
DR PDBsum; 1URC; -.
DR PDBsum; 1VYW; -.
DR PDBsum; 2BKZ; -.
DR PDBsum; 2BPM; -.
DR PDBsum; 2C4G; -.
DR PDBsum; 2C5N; -.
DR PDBsum; 2C5O; -.
DR PDBsum; 2C5V; -.
DR PDBsum; 2C5X; -.
DR PDBsum; 2C6T; -.
DR PDBsum; 2CCH; -.
DR PDBsum; 2CCI; -.
DR PDBsum; 2CJM; -.
DR PDBsum; 2I40; -.
DR PDBsum; 2IW6; -.
DR PDBsum; 2IW8; -.
DR PDBsum; 2IW9; -.
DR PDBsum; 2UUE; -.
DR PDBsum; 2UZB; -.
DR PDBsum; 2UZD; -.
DR PDBsum; 2UZE; -.
DR PDBsum; 2UZL; -.
DR PDBsum; 2V22; -.
DR PDBsum; 2WEV; -.
DR PDBsum; 2WFY; -.
DR PDBsum; 2WHB; -.
DR PDBsum; 2WIH; -.
DR PDBsum; 2WIP; -.
DR PDBsum; 2WMA; -.
DR PDBsum; 2WMB; -.
DR PDBsum; 2WPA; -.
DR PDBsum; 2WXV; -.
DR PDBsum; 2X1N; -.
DR PDBsum; 3EID; -.
DR PDBsum; 3EJ1; -.
DR PDBsum; 3EOC; -.
DR PDBsum; 3F5X; -.
DR PDBsum; 4BCK; -.
DR PDBsum; 4BCM; -.
DR PDBsum; 4BCN; -.
DR PDBsum; 4BCP; -.
DR PDBsum; 4CFM; -.
DR PDBsum; 4CFN; -.
DR PDBsum; 4CFU; -.
DR PDBsum; 4CFV; -.
DR PDBsum; 4CFW; -.
DR PDBsum; 4CFX; -.
DR PDBsum; 4EOI; -.
DR PDBsum; 4EOJ; -.
DR PDBsum; 4EOK; -.
DR PDBsum; 4EOL; -.
DR PDBsum; 4EOM; -.
DR PDBsum; 4EON; -.
DR PDBsum; 4EOO; -.
DR PDBsum; 4EOP; -.
DR PDBsum; 4EOQ; -.
DR PDBsum; 4EOR; -.
DR PDBsum; 4EOS; -.
DR PDBsum; 4FX3; -.
DR PDBsum; 5CYI; -.
DR PDBsum; 5IF1; -.
DR PDBsum; 5LMK; -.
DR PDBsum; 5NEV; -.
DR PDBsum; 6ATH; -.
DR PDBsum; 6GVA; -.
DR PDBsum; 6P3W; -.
DR PDBsum; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR PDBsum; 6RIJ; -.
DR PDBsum; 6SG4; -.
DR PDBsum; 7ACK; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5R; -.
DR PDBsum; 7B7S; -.
DR PDBsum; 7LUO; -.
DR AlphaFoldDB; P20248; -.
DR SMR; P20248; -.
DR BioGRID; 107331; 157.
DR ComplexPortal; CPX-2004; Cyclin A2-CDK1 complex.
DR ComplexPortal; CPX-2006; Cyclin A2-CDK2 complex.
DR CORUM; P20248; -.
DR DIP; DIP-638N; -.
DR ELM; P20248; -.
DR IntAct; P20248; 81.
DR MINT; P20248; -.
DR STRING; 9606.ENSP00000274026; -.
DR BindingDB; P20248; -.
DR ChEMBL; CHEMBL2582; -.
DR DrugBank; DB08463; (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol.
DR DrugBank; DB08285; (2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol.
DR DrugBank; DB07137; (2S)-N-[(3E)-5-Cyclopropyl-3H-pyrazol-3-ylidene]-2-[4-(2-oxo-1-imidazolidinyl)phenyl]propanamide.
DR DrugBank; DB07852; 1-(3,5-DICHLOROPHENYL)-5-METHYL-1H-1,2,4-TRIAZOLE-3-CARBOXYLIC ACID.
DR DrugBank; DB08527; 1-[4-(AMINOSULFONYL)PHENYL]-1,6-DIHYDROPYRAZOLO[3,4-E]INDAZOLE-3-CARBOXAMIDE.
DR DrugBank; DB08355; 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid.
DR DrugBank; DB06948; 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE.
DR DrugBank; DB08248; 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE.
DR DrugBank; DB08309; 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL.
DR DrugBank; DB02915; 4-(2,4-Dimethyl-1,3-thiazol-5-yl)-N-[4-(trifluoromethyl)phenyl]-2-pyrimidinamine.
DR DrugBank; DB02091; 4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamine.
DR DrugBank; DB08178; 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine.
DR DrugBank; DB08182; 4-(4-propoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine.
DR DrugBank; DB08241; 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE.
DR DrugBank; DB06844; 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE.
DR DrugBank; DB08219; 4-Methyl-5-[(2Z)-2-{[4-(4-morpholinyl)phenyl]imino}-2,5-dihydro-4-pyrimidinyl]-1,3-thiazol-2-amine.
DR DrugBank; DB07533; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]-2-FURYL}-N-METHYLBENZENESULFONAMIDE.
DR DrugBank; DB07538; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}-2-(TRIFLUOROMETHYL)BENZENESULFONAMIDE.
DR DrugBank; DB07534; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE.
DR DrugBank; DB07539; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID.
DR DrugBank; DB08572; 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE.
DR DrugBank; DB07688; 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE.
DR DrugBank; DB07471; 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE.
DR DrugBank; DB07203; 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE.
DR DrugBank; DB08233; 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE.
DR DrugBank; DB02407; 6-O-Cyclohexylmethyl Guanine.
DR DrugBank; DB02833; [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine.
DR DrugBank; DB08218; HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)AMMONIUM.
DR DrugBank; DB06944; N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide.
DR DrugBank; DB07562; N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4-DIAMINE.
DR DrugBank; DB07164; N-cyclopropyl-4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amine.
DR DrugBank; DB07126; O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE.
DR DrugBank; DB08694; Variolin B.
DR DrugCentral; P20248; -.
DR iPTMnet; P20248; -.
DR MetOSite; P20248; -.
DR PhosphoSitePlus; P20248; -.
DR BioMuta; CCNA2; -.
DR DMDM; 311033358; -.
DR EPD; P20248; -.
DR jPOST; P20248; -.
DR MassIVE; P20248; -.
DR MaxQB; P20248; -.
DR PaxDb; P20248; -.
DR PeptideAtlas; P20248; -.
DR PRIDE; P20248; -.
DR ProteomicsDB; 53735; -.
DR Antibodypedia; 3665; 787 antibodies from 44 providers.
DR DNASU; 890; -.
DR Ensembl; ENST00000274026.10; ENSP00000274026.5; ENSG00000145386.11.
DR GeneID; 890; -.
DR KEGG; hsa:890; -.
DR MANE-Select; ENST00000274026.10; ENSP00000274026.5; NM_001237.5; NP_001228.2.
DR UCSC; uc003iec.5; human.
DR CTD; 890; -.
DR DisGeNET; 890; -.
DR GeneCards; CCNA2; -.
DR HGNC; HGNC:1578; CCNA2.
DR HPA; ENSG00000145386; Tissue enhanced (bone marrow, lymphoid tissue, retina).
DR MalaCards; CCNA2; -.
DR MIM; 123835; gene.
DR neXtProt; NX_P20248; -.
DR OpenTargets; ENSG00000145386; -.
DR PharmGKB; PA94; -.
DR VEuPathDB; HostDB:ENSG00000145386; -.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00940000155372; -.
DR HOGENOM; CLU_020695_3_2_1; -.
DR InParanoid; P20248; -.
DR OMA; QDLHQTY; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; P20248; -.
DR TreeFam; TF101002; -.
DR PathwayCommons; P20248; -.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-170145; Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-68911; G2 Phase.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR SignaLink; P20248; -.
DR SIGNOR; P20248; -.
DR BioGRID-ORCS; 890; 770 hits in 1091 CRISPR screens.
DR EvolutionaryTrace; P20248; -.
DR GeneWiki; Cyclin_A2; -.
DR GenomeRNAi; 890; -.
DR Pharos; P20248; Tchem.
DR PRO; PR:P20248; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P20248; protein.
DR Bgee; ENSG00000145386; Expressed in ventricular zone and 161 other tissues.
DR Genevisible; P20248; HS.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IDA:UniProtKB.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
DR GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0044843; P:cell cycle G1/S phase transition; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071314; P:cellular response to cocaine; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0016572; P:histone phosphorylation; IDA:CAFA.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR CDD; cd00043; CYCLIN; 2.
DR IDEAL; IID00032; -.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR032447; Cyclin-A_N.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF16500; Cyclin_N2; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm;
KW Host-virus interaction; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..432
FT /note="Cyclin-A2"
FT /id="PRO_0000080338"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VARIANT 163
FT /note="I -> V (in dbSNP:rs769242)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1967822,
FT ECO:0000269|PubMed:8202514, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:18691976"
FT /id="VAR_018819"
FT CONFLICT 156
FT /note="H -> R (in Ref. 3; CAG28620)"
FT /evidence="ECO:0000305"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4CFV"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6ATH"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 253..268
FT /evidence="ECO:0007829|PDB:4EOJ"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2C5N"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:4EOJ"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:4EOJ"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:4EOJ"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1H1P"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 352..368
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 384..400
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:4EOJ"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1OL1"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4EOJ"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4EOJ"
SQ SEQUENCE 432 AA; 48551 MW; 97763A2897DD35F4 CRC64;
MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL AVLKSGNPRG
LAQQQRPKTR RVAPLKDLPV NDEHVTVPPW KANSKQPAFT IHVDEAEKEA QKKPAESQKI
EREDALAFNS AISLPGPRKP LVPLDYPMDG SFESPHTMDM SIILEDEKPV SVNEVPDYHE
DIHTYLREME VKCKPKVGYM KKQPDITNSM RAILVDWLVE VGEEYKLQNE TLHLAVNYID
RFLSSMSVLR GKLQLVGTAA MLLASKFEEI YPPEVAEFVY ITDDTYTKKQ VLRMEHLVLK
VLTFDLAAPT VNQFLTQYFL HQQPANCKVE SLAMFLGELS LIDADPYLKY LPSVIAGAAF
HLALYTVTGQ SWPESLIRKT GYTLESLKPC LMDLHQTYLK APQHAQQSIR EKYKNSKYHG
VSLLNPPETL NL
