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 27-MAR-2024, entry version 229. 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}, CCNA GN {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=18; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7MKX; X-ray; 3.08 A; B/D=171-432. DR PDB; 7QHL; X-ray; 1.70 A; B/D=175-432. DR PDB; 8B54; X-ray; 2.60 A; B/D=175-432. DR PDB; 8BYA; EM; 3.38 A; B=1-432. DR PDB; 8BZO; EM; 3.50 A; B=1-432. 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 PDBsum; 7MKX; -. DR PDBsum; 7QHL; -. DR PDBsum; 8B54; -. DR PDBsum; 8BYA; -. DR PDBsum; 8BZO; -. DR AlphaFoldDB; P20248; -. DR EMDB; EMD-12037; -. DR EMDB; EMD-12048; -. DR EMDB; EMD-16325; -. DR EMDB; EMD-16344; -. DR EMDB; EMD-4465; -. DR EMDB; EMD-4466; -. DR EMDB; EMD-4467; -. DR SMR; P20248; -. DR BioGRID; 107331; 181. 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.ENSP00000481380; -. 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; 9606-ENSP00000274026; -. DR PeptideAtlas; P20248; -. DR ProteomicsDB; 53735; -. DR Pumba; P20248; -. DR Antibodypedia; 3665; 863 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 AGR; HGNC:1578; -. 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 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; HQPFSIH; -. DR OrthoDB; 5474295at2759; -. 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; 802 hits in 1170 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 cell types or tissues. DR GO; GO:0097122; C:cyclin A2-CDK1 complex; ISO:ComplexPortal. 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:0006351; P:DNA-templated transcription; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl. DR GO; GO:0043687; P:post-translational protein modification; IDA:CAFA. DR GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL. DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl. DR CDD; cd20561; CYCLIN_CCNA2_rpt1; 1. DR CDD; cd20564; CYCLIN_CCNA2_rpt2; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR IDEAL; IID00032; -. DR InterPro; IPR039361; Cyclin. DR InterPro; IPR032447; Cyclin-A_N. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR046965; Cyclin_A/B-like. DR InterPro; IPR004367; Cyclin_C-dom. DR InterPro; IPR006671; Cyclin_N. DR InterPro; IPR048258; Cyclins_cyclin-box. DR PANTHER; PTHR10177:SF444; CYCLIN-A2; 1. DR PANTHER; PTHR10177; CYCLINS; 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; Cyclin-like; 2. DR PROSITE; PS00292; CYCLINS; 1. DR Genevisible; P20248; HS. 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 STRAND 348..350 FT /evidence="ECO:0007829|PDB:8BYA" 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 STRAND 404..406 FT /evidence="ECO:0007829|PDB:8BYA" 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 //