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Cyclin-A2 (Cyclin-A) (Cyclin A)

 CCNA2_HUMAN             Reviewed;         432 AA.
P20248; A8K7B6; Q2M3U6; Q4W5P4; Q6LER8;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
12-AUG-2020, entry version 211.
RecName: Full=Cyclin-A2 {ECO:0000312|HGNC:HGNC:1578};
Short=Cyclin-A {ECO:0000303|PubMed:1967822};
AltName: Full=Cyclin A {ECO:0000303|PubMed:1967822};
Name=CCNA2 {ECO:0000312|HGNC:HGNC:1578};
Synonyms=CCN1 {ECO:0000312|HGNC:HGNC:1578},
CCNA {ECO:0000312|HGNC:HGNC:1578};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-163.
PubMed=1967822; DOI=10.1038/343555a0;
Wang J., Chenivesse X., Henglein B., Brechot C.;
"Hepatitis B virus integration in a cyclin A gene in a hepatocellular
carcinoma.";
Nature 343:555-557(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-163, AND DEVELOPMENTAL
STAGE.
PubMed=8202514; DOI=10.1073/pnas.91.12.5490;
Henglein B., Chenivesse X., Wang D., Eick D., Brechot C.;
"Structure and cell cycle-regulated transcription of the human cyclin A
gene.";
Proc. Natl. Acad. Sci. U.S.A. 91:5490-5494(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-163.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-163.
NIEHS SNPs program;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-163.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-163.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-163.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, INTERACTION WITH CDK1 AND CDK2, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=1312467; DOI=10.1002/j.1460-2075.1992.tb05135.x;
Pagano M., Pepperkok R., Verde F., Ansorge W., Draetta G.;
"Cyclin A is required at two points in the human cell cycle.";
EMBO J. 11:961-971(1992).
[10]
INTERACTION WITH SCAPER, AND SUBCELLULAR LOCATION.
PubMed=17698606; DOI=10.1083/jcb.200701166;
Tsang W.Y., Wang L., Chen Z., Sanchez I., Dynlacht B.D.;
"SCAPER, a novel cyclin A-interacting protein that regulates cell cycle
progression.";
J. Cell Biol. 178:621-633(2007).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-5 AND SER-55, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH INCA1.
PubMed=21540187; DOI=10.1074/jbc.m110.203471;
Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S.,
Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G.,
Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.;
"Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1
(INCA1) regulates proliferation and is repressed by oncogenic signaling.";
J. Biol. Chem. 286:28210-28222(2011).
[14]
UBIQUITINATION, AND DEUBIQUITINATION BY USP37.
PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027;
Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,
Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.;
"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and
promote S phase entry.";
Mol. Cell 42:511-523(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS UL32 (MICROBIAL INFECTION).
PubMed=24101496; DOI=10.1073/pnas.1312235110;
Bogdanow B., Weisbach H., von Einem J., Straschewski S., Voigt S.,
Winkler M., Hagemeier C., Wiebusch L.;
"Human cytomegalovirus tegument protein pp150 acts as a cyclin A2-CDK-
dependent sensor of the host cell cycle and differentiation state.";
Proc. Natl. Acad. Sci. U.S.A. 110:17510-17515(2013).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN COMPLEX WITH CDK2.
PubMed=7630397; DOI=10.1038/376313a0;
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J.,
Pavletich N.P.;
"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2
complex.";
Nature 376:313-320(1995).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 173-432 IN COMPLEX WITH CDK2 AND
CDKN1B.
PubMed=8684460; DOI=10.1038/382325a0;
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound
to the cyclin A-Cdk2 complex.";
Nature 382:325-331(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 173-432 IN COMPLEX WITH CDK2.
PubMed=8756328; DOI=10.1038/nsb0896-696;
Russo A.A., Jeffrey P.D., Pavletich N.P.;
"Structural basis of cyclin-dependent kinase activation by
phosphorylation.";
Nat. Struct. Biol. 3:696-700(1996).
[21]
VARIANT [LARGE SCALE ANALYSIS] VAL-163, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
-!- FUNCTION: Cyclin which controls both the G1/S and the G2/M transition
phases of the cell cycle. Functions through the formation of specific
serine/threonine protein kinase holoenzyme complexes with the cyclin-
dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the
substrate specificity of these complexes and differentially interacts
with and activates CDK1 and CDK2 throughout the cell cycle.
{ECO:0000269|PubMed:1312467}.
-!- SUBUNIT: Interacts with the CDK1 and CDK2 protein kinases to form
serine/threonine kinase holoenzyme complexes (PubMed:1312467,
PubMed:7630397, PubMed:8684460, PubMed:8756328). Interacts with CDK1
(hyperphosphorylated form in G1 and underphosphorylated forms in S and
G2) (PubMed:1312467). Interacts with CDK2; the interaction increases
from G1 to G2 (PubMed:1312467). Interacts (associated with CDK2 but not
with CDK1) with SCAPER; regulates the activity of CCNA2/CDK2 by
transiently maintaining CCNA2 in the cytoplasm (PubMed:17698606). Forms
a ternary complex with CDK2 and CDKN1B; CDKN1B inhibits the kinase
activity of CDK2 through conformational rearrangements
(PubMed:8684460). Interacts with INCA1 (PubMed:21540187).
{ECO:0000269|PubMed:1312467, ECO:0000269|PubMed:17698606,
ECO:0000269|PubMed:21540187, ECO:0000269|PubMed:7630397,
ECO:0000269|PubMed:8684460, ECO:0000269|PubMed:8756328}.
-!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
protein UL32. {ECO:0000269|PubMed:24101496}.
-!- INTERACTION:
P20248; P31749: AKT1; NbExp=2; IntAct=EBI-457097, EBI-296087;
P20248; P24941: CDK2; NbExp=27; IntAct=EBI-457097, EBI-375096;
P20248; P38936: CDKN1A; NbExp=5; IntAct=EBI-457097, EBI-375077;
P20248; P46527: CDKN1B; NbExp=17; IntAct=EBI-457097, EBI-519280;
P20248; Q96PU4: UHRF2; NbExp=2; IntAct=EBI-457097, EBI-625304;
P20248; P03129: E7; Xeno; NbExp=2; IntAct=EBI-457097, EBI-866453;
P20248; P03070; Xeno; NbExp=2; IntAct=EBI-457097, EBI-617698;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1312467,
ECO:0000269|PubMed:17698606}. Cytoplasm {ECO:0000269|PubMed:1312467,
ECO:0000269|PubMed:17698606}. Note=Exclusively nuclear during
interphase (PubMed:1312467). Detected in the nucleus and the cytoplasm
at prophase (PubMed:1312467). Cytoplasmic when associated with SCAPER
(PubMed:17698606). {ECO:0000269|PubMed:1312467,
ECO:0000269|PubMed:17698606}.
-!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
destroyed at mitosis. Not detected during the G1 phase of the cell
cycle. It accumulates during the DNA synthesis/S phase and disappears
as cells progress into mitosis, between prophase and metaphase (at
protein level). {ECO:0000269|PubMed:1312467}.
-!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-
promoting complex (APC/C), leading to its degradation by the
proteasome. Deubiquitinated and stabilized by USP37 enables entry into
S phase. {ECO:0000269|PubMed:21596315}.
-!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ccna2/";
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EMBL; X51688; CAA35986.1; -; mRNA.
EMBL; X68303; CAA48375.1; -; Genomic_DNA.
EMBL; CR407692; CAG28620.1; -; mRNA.
EMBL; AF518006; AAM54042.1; -; Genomic_DNA.
EMBL; AK291931; BAF84620.1; -; mRNA.
EMBL; AC079341; AAY40969.1; -; Genomic_DNA.
EMBL; CH471056; EAX05246.1; -; Genomic_DNA.
EMBL; BC104783; AAI04784.1; -; mRNA.
EMBL; BC104787; AAI04788.1; -; mRNA.
CCDS; CCDS3723.1; -.
PIR; S08277; S08277.
RefSeq; NP_001228.1; NM_001237.4.
PDB; 1E9H; X-ray; 2.50 A; B/D=175-432.
PDB; 1FIN; X-ray; 2.30 A; B/D=173-432.
PDB; 1FVV; X-ray; 2.80 A; B/D=173-432.
PDB; 1GY3; X-ray; 2.70 A; B/D=175-432.
PDB; 1H1P; X-ray; 2.10 A; B/D=175-432.
PDB; 1H1Q; X-ray; 2.50 A; B/D=175-432.
PDB; 1H1R; X-ray; 2.00 A; B/D=175-432.
PDB; 1H1S; X-ray; 2.00 A; B/D=175-432.
PDB; 1H24; X-ray; 2.50 A; B/D=174-432.
PDB; 1H25; X-ray; 2.50 A; B/D=174-432.
PDB; 1H26; X-ray; 2.24 A; B/D=174-432.
PDB; 1H27; X-ray; 2.20 A; B/D=174-432.
PDB; 1H28; X-ray; 2.80 A; B/D=174-432.
PDB; 1JST; X-ray; 2.60 A; B/D=175-432.
PDB; 1JSU; X-ray; 2.30 A; B=173-432.
PDB; 1OGU; X-ray; 2.60 A; B/D=174-432.
PDB; 1OI9; X-ray; 2.10 A; B/D=174-432.
PDB; 1OIU; X-ray; 2.00 A; B/D=174-432.
PDB; 1OIY; X-ray; 2.40 A; B/D=174-432.
PDB; 1OKV; X-ray; 2.40 A; B/D=173-432.
PDB; 1OKW; X-ray; 2.50 A; B/D=173-432.
PDB; 1OL1; X-ray; 2.90 A; B/D=173-432.
PDB; 1OL2; X-ray; 2.60 A; B/D=173-432.
PDB; 1P5E; X-ray; 2.22 A; B/D=175-432.
PDB; 1PKD; X-ray; 2.30 A; B/D=175-432.
PDB; 1QMZ; X-ray; 2.20 A; B/D=174-432.
PDB; 1URC; X-ray; 2.60 A; B/D=173-432.
PDB; 1VYW; X-ray; 2.30 A; B/D=174-432.
PDB; 2BKZ; X-ray; 2.60 A; B/D=174-432.
PDB; 2BPM; X-ray; 2.40 A; B/D=174-432.
PDB; 2C4G; X-ray; 2.70 A; B/D=173-432.
PDB; 2C5N; X-ray; 2.10 A; B/D=174-432.
PDB; 2C5O; X-ray; 2.10 A; B/D=173-432.
PDB; 2C5V; X-ray; 2.90 A; B/D=174-432.
PDB; 2C5X; X-ray; 2.90 A; B/D=174-432.
PDB; 2C6T; X-ray; 2.61 A; B/D=175-432.
PDB; 2CCH; X-ray; 1.70 A; B/D=173-432.
PDB; 2CCI; X-ray; 2.70 A; B/D=175-432.
PDB; 2CJM; X-ray; 2.30 A; B/D=175-432.
PDB; 2I40; X-ray; 2.80 A; B/D=173-432.
PDB; 2IW6; X-ray; 2.30 A; B/D=174-432.
PDB; 2IW8; X-ray; 2.30 A; B/D=174-432.
PDB; 2IW9; X-ray; 2.00 A; B/D=174-432.
PDB; 2UUE; X-ray; 2.06 A; B/D=174-432.
PDB; 2UZB; X-ray; 2.70 A; B/D=175-432.
PDB; 2UZD; X-ray; 2.72 A; B/D=175-432.
PDB; 2UZE; X-ray; 2.40 A; B/D=175-432.
PDB; 2UZL; X-ray; 2.40 A; B/D=175-432.
PDB; 2V22; X-ray; 2.60 A; B/D=174-432.
PDB; 2WEV; X-ray; 2.30 A; B/D=173-432.
PDB; 2WFY; X-ray; 2.53 A; B/D=173-432.
PDB; 2WHB; X-ray; 2.90 A; B/D=173-432.
PDB; 2WIH; X-ray; 2.50 A; B/D=173-432.
PDB; 2WIP; X-ray; 2.80 A; B/D=173-432.
PDB; 2WMA; X-ray; 2.80 A; B/D=174-432.
PDB; 2WMB; X-ray; 2.60 A; B/D=174-432.
PDB; 2WPA; X-ray; 2.51 A; B/D=173-432.
PDB; 2WXV; X-ray; 2.60 A; B/D=173-432.
PDB; 2X1N; X-ray; 2.75 A; B/D=172-432.
PDB; 3EID; X-ray; 3.15 A; B/D=173-432.
PDB; 3EJ1; X-ray; 3.22 A; B/D=173-432.
PDB; 3EOC; X-ray; 3.20 A; B/D=173-432.
PDB; 3F5X; X-ray; 2.40 A; B/D=177-432.
PDB; 4BCK; X-ray; 2.05 A; B/D=171-432.
PDB; 4BCM; X-ray; 2.45 A; B/D=171-432.
PDB; 4BCN; X-ray; 2.10 A; B=171-432, D=171-431.
PDB; 4BCP; X-ray; 2.26 A; B/D=171-432.
PDB; 4CFM; X-ray; 2.85 A; B/D=175-432.
PDB; 4CFN; X-ray; 2.20 A; B/D=175-432.
PDB; 4CFU; X-ray; 2.20 A; B=172-432, D=173-432.
PDB; 4CFV; X-ray; 2.00 A; B/D=172-432.
PDB; 4CFW; X-ray; 2.45 A; B/D=175-432.
PDB; 4CFX; X-ray; 3.50 A; B/D=173-432.
PDB; 4EOI; X-ray; 2.00 A; B/D=175-432.
PDB; 4EOJ; X-ray; 1.65 A; B/D=175-432.
PDB; 4EOK; X-ray; 2.57 A; B/D=175-432.
PDB; 4EOL; X-ray; 2.40 A; B/D=175-432.
PDB; 4EOM; X-ray; 2.10 A; B/D=175-432.
PDB; 4EON; X-ray; 2.40 A; B/D=175-432.
PDB; 4EOO; X-ray; 2.10 A; B/D=175-432.
PDB; 4EOP; X-ray; 1.99 A; B/D=175-432.
PDB; 4EOQ; X-ray; 2.15 A; B/D=175-432.
PDB; 4EOR; X-ray; 2.20 A; B/D=175-432.
PDB; 4EOS; X-ray; 2.57 A; B/D=175-432.
PDB; 4FX3; X-ray; 2.75 A; B/D=175-432.
PDB; 5CYI; X-ray; 2.00 A; B/D=174-432.
PDB; 5IF1; X-ray; 2.61 A; B/D=174-432.
PDB; 5LMK; X-ray; 2.40 A; B/D=175-432.
PDB; 5NEV; X-ray; 2.97 A; B/D=174-432.
PDB; 6ATH; X-ray; 1.82 A; B=173-432.
PDB; 6GVA; X-ray; 2.15 A; B=175-432.
PDB; 6P3W; X-ray; 2.54 A; B/D=176-432.
PDB; 6Q6G; EM; 3.20 A; S=1-432.
PDB; 6Q6H; EM; 3.20 A; S=1-432.
PDBsum; 1E9H; -.
PDBsum; 1FIN; -.
PDBsum; 1FVV; -.
PDBsum; 1GY3; -.
PDBsum; 1H1P; -.
PDBsum; 1H1Q; -.
PDBsum; 1H1R; -.
PDBsum; 1H1S; -.
PDBsum; 1H24; -.
PDBsum; 1H25; -.
PDBsum; 1H26; -.
PDBsum; 1H27; -.
PDBsum; 1H28; -.
PDBsum; 1JST; -.
PDBsum; 1JSU; -.
PDBsum; 1OGU; -.
PDBsum; 1OI9; -.
PDBsum; 1OIU; -.
PDBsum; 1OIY; -.
PDBsum; 1OKV; -.
PDBsum; 1OKW; -.
PDBsum; 1OL1; -.
PDBsum; 1OL2; -.
PDBsum; 1P5E; -.
PDBsum; 1PKD; -.
PDBsum; 1QMZ; -.
PDBsum; 1URC; -.
PDBsum; 1VYW; -.
PDBsum; 2BKZ; -.
PDBsum; 2BPM; -.
PDBsum; 2C4G; -.
PDBsum; 2C5N; -.
PDBsum; 2C5O; -.
PDBsum; 2C5V; -.
PDBsum; 2C5X; -.
PDBsum; 2C6T; -.
PDBsum; 2CCH; -.
PDBsum; 2CCI; -.
PDBsum; 2CJM; -.
PDBsum; 2I40; -.
PDBsum; 2IW6; -.
PDBsum; 2IW8; -.
PDBsum; 2IW9; -.
PDBsum; 2UUE; -.
PDBsum; 2UZB; -.
PDBsum; 2UZD; -.
PDBsum; 2UZE; -.
PDBsum; 2UZL; -.
PDBsum; 2V22; -.
PDBsum; 2WEV; -.
PDBsum; 2WFY; -.
PDBsum; 2WHB; -.
PDBsum; 2WIH; -.
PDBsum; 2WIP; -.
PDBsum; 2WMA; -.
PDBsum; 2WMB; -.
PDBsum; 2WPA; -.
PDBsum; 2WXV; -.
PDBsum; 2X1N; -.
PDBsum; 3EID; -.
PDBsum; 3EJ1; -.
PDBsum; 3EOC; -.
PDBsum; 3F5X; -.
PDBsum; 4BCK; -.
PDBsum; 4BCM; -.
PDBsum; 4BCN; -.
PDBsum; 4BCP; -.
PDBsum; 4CFM; -.
PDBsum; 4CFN; -.
PDBsum; 4CFU; -.
PDBsum; 4CFV; -.
PDBsum; 4CFW; -.
PDBsum; 4CFX; -.
PDBsum; 4EOI; -.
PDBsum; 4EOJ; -.
PDBsum; 4EOK; -.
PDBsum; 4EOL; -.
PDBsum; 4EOM; -.
PDBsum; 4EON; -.
PDBsum; 4EOO; -.
PDBsum; 4EOP; -.
PDBsum; 4EOQ; -.
PDBsum; 4EOR; -.
PDBsum; 4EOS; -.
PDBsum; 4FX3; -.
PDBsum; 5CYI; -.
PDBsum; 5IF1; -.
PDBsum; 5LMK; -.
PDBsum; 5NEV; -.
PDBsum; 6ATH; -.
PDBsum; 6GVA; -.
PDBsum; 6P3W; -.
PDBsum; 6Q6G; -.
PDBsum; 6Q6H; -.
SMR; P20248; -.
BioGRID; 107331; 131.
ComplexPortal; CPX-2004; Cyclin A2-CDK1 complex.
ComplexPortal; CPX-2006; Cyclin A2-CDK2 complex.
CORUM; P20248; -.
DIP; DIP-638N; -.
ELM; P20248; -.
IntAct; P20248; 77.
MINT; P20248; -.
STRING; 9606.ENSP00000274026; -.
BindingDB; P20248; -.
ChEMBL; CHEMBL2582; -.
DrugBank; DB08463; (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol.
DrugBank; DB08285; (2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol.
DrugBank; DB07137; (2S)-N-[(3E)-5-Cyclopropyl-3H-pyrazol-3-ylidene]-2-[4-(2-oxo-1-imidazolidinyl)phenyl]propanamide.
DrugBank; DB07852; 1-(3,5-DICHLOROPHENYL)-5-METHYL-1H-1,2,4-TRIAZOLE-3-CARBOXYLIC ACID.
DrugBank; DB08527; 1-[4-(AMINOSULFONYL)PHENYL]-1,6-DIHYDROPYRAZOLO[3,4-E]INDAZOLE-3-CARBOXAMIDE.
DrugBank; DB08355; 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid.
DrugBank; DB06948; 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE.
DrugBank; DB08248; 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE.
DrugBank; DB08309; 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL.
DrugBank; DB02915; 4-(2,4-Dimethyl-1,3-thiazol-5-yl)-N-[4-(trifluoromethyl)phenyl]-2-pyrimidinamine.
DrugBank; DB02091; 4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamine.
DrugBank; DB08178; 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine.
DrugBank; DB08182; 4-(4-propoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine.
DrugBank; DB08241; 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE.
DrugBank; DB06844; 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE.
DrugBank; DB08219; 4-Methyl-5-[(2Z)-2-{[4-(4-morpholinyl)phenyl]imino}-2,5-dihydro-4-pyrimidinyl]-1,3-thiazol-2-amine.
DrugBank; DB07533; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]-2-FURYL}-N-METHYLBENZENESULFONAMIDE.
DrugBank; DB07538; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}-2-(TRIFLUOROMETHYL)BENZENESULFONAMIDE.
DrugBank; DB07534; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE.
DrugBank; DB07539; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID.
DrugBank; DB08572; 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE.
DrugBank; DB07688; 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE.
DrugBank; DB07471; 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE.
DrugBank; DB07203; 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE.
DrugBank; DB08233; 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE.
DrugBank; DB02407; 6-O-Cyclohexylmethyl Guanine.
DrugBank; DB02833; [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine.
DrugBank; DB08218; HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)AMMONIUM.
DrugBank; DB06944; N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide.
DrugBank; DB07562; N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4-DIAMINE.
DrugBank; DB07164; N-cyclopropyl-4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amine.
DrugBank; DB07126; O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE.
DrugBank; DB08694; Variolin B.
DrugCentral; P20248; -.
iPTMnet; P20248; -.
MetOSite; P20248; -.
PhosphoSitePlus; P20248; -.
BioMuta; CCNA2; -.
DMDM; 311033358; -.
EPD; P20248; -.
jPOST; P20248; -.
MassIVE; P20248; -.
MaxQB; P20248; -.
PaxDb; P20248; -.
PeptideAtlas; P20248; -.
PRIDE; P20248; -.
ProteomicsDB; 53735; -.
Antibodypedia; 3665; 760 antibodies.
Ensembl; ENST00000274026; ENSP00000274026; ENSG00000145386.
Ensembl; ENST00000618014; ENSP00000481380; ENSG00000145386.
GeneID; 890; -.
KEGG; hsa:890; -.
UCSC; uc003iec.5; human.
CTD; 890; -.
DisGeNET; 890; -.
EuPathDB; HostDB:ENSG00000145386.9; -.
GeneCards; CCNA2; -.
HGNC; HGNC:1578; CCNA2.
HPA; ENSG00000145386; Tissue enriched (lymphoid).
MIM; 123835; gene.
neXtProt; NX_P20248; -.
OpenTargets; ENSG00000145386; -.
PharmGKB; PA94; -.
eggNOG; KOG0654; Eukaryota.
GeneTree; ENSGT00940000155372; -.
HOGENOM; CLU_020695_3_2_1; -.
InParanoid; P20248; -.
KO; K06627; -.
OMA; LMPCVED; -.
OrthoDB; 993640at2759; -.
PhylomeDB; P20248; -.
TreeFam; TF101002; -.
PathwayCommons; P20248; -.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-170145; Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-68911; G2 Phase.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
SignaLink; P20248; -.
SIGNOR; P20248; -.
BioGRID-ORCS; 890; 733 hits in 881 CRISPR screens.
EvolutionaryTrace; P20248; -.
GeneWiki; Cyclin_A2; -.
GenomeRNAi; 890; -.
Pharos; P20248; Tchem.
PRO; PR:P20248; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; P20248; protein.
Bgee; ENSG00000145386; Expressed in ventricular zone and 205 other tissues.
Genevisible; P20248; HS.
GO; GO:0097124; C:cyclin A2-CDK2 complex; IDA:UniProtKB.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0044843; P:cell cycle G1/S phase transition; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071314; P:cellular response to cocaine; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0090102; P:cochlea development; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0016572; P:histone phosphorylation; IDA:CAFA.
GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00043; CYCLIN; 2.
IDEAL; IID00032; -.
InterPro; IPR039361; Cyclin.
InterPro; IPR032447; Cyclin-A_N.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR004367; Cyclin_C-dom.
InterPro; IPR006671; Cyclin_N.
PANTHER; PTHR10177; PTHR10177; 1.
Pfam; PF02984; Cyclin_C; 1.
Pfam; PF00134; Cyclin_N; 1.
Pfam; PF16500; Cyclin_N2; 1.
PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
SMART; SM00385; CYCLIN; 2.
SMART; SM01332; Cyclin_C; 1.
SUPFAM; SSF47954; SSF47954; 2.
PROSITE; PS00292; CYCLINS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm;
Host-virus interaction; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1..432
/note="Cyclin-A2"
/id="PRO_0000080338"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 5
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163"
MOD_RES 55
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
VARIANT 163
/note="I -> V (in dbSNP:rs769242)"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1967822, ECO:0000269|PubMed:8202514,
ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.7"
/id="VAR_018819"
CONFLICT 156
/note="H -> R (in Ref. 3; CAG28620)"
/evidence="ECO:0000305"
TURN 30..32
/evidence="ECO:0000244|PDB:6Q6G"
STRAND 54..56
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 172..174
/evidence="ECO:0000244|PDB:4CFV"
TURN 176..178
/evidence="ECO:0000244|PDB:6ATH"
HELIX 179..192
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 199..202
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 208..224
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 229..243
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 250..252
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 253..268
/evidence="ECO:0000244|PDB:4EOJ"
STRAND 269..271
/evidence="ECO:0000244|PDB:2C5N"
HELIX 275..281
/evidence="ECO:0000244|PDB:4EOJ"
TURN 282..284
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 288..301
/evidence="ECO:0000244|PDB:4EOJ"
TURN 302..304
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 311..319
/evidence="ECO:0000244|PDB:4EOJ"
STRAND 322..324
/evidence="ECO:0000244|PDB:1H1P"
HELIX 327..342
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 344..347
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 352..368
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 374..380
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 384..400
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 401..403
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 408..412
/evidence="ECO:0000244|PDB:4EOJ"
STRAND 413..415
/evidence="ECO:0000244|PDB:1OL1"
HELIX 416..418
/evidence="ECO:0000244|PDB:4EOJ"
HELIX 421..423
/evidence="ECO:0000244|PDB:4EOJ"
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


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EIAAB06184 CCNT1,Cyclin-T,Cyclin-T1,CycT1,Homo sapiens,Human
bs-12060R-Cy5 Rabbit Anti-Cyclin Y-Cyclin X Polyclonal Antibody, Cy5 Conjugated 100ul
'AP09132PU-N Cyclin L1 (+ Cyclin L2, Isoform 2) antibody Isotype IgG Host Rabbit 0.5 mg
bs-12060R-Cy7 Rabbit Anti-Cyclin Y-Cyclin X Polyclonal Antibody, Cy7 Conjugated 100ul
bs-12060R-A488 Rabbit Anti-Cyclin Y-Cyclin X Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-12060R-A555 Rabbit Anti-Cyclin Y-Cyclin X Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-12060R-A647 Rabbit Anti-Cyclin Y-Cyclin X Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-12060R-A350 Rabbit Anti-Cyclin Y-Cyclin X Polyclonal Antibody, ALEXA FLUOR 350 Conjugated 100ul
Pathways :
WP1403: AMPK signaling
WP2361: Gastric cancer network 1
WP656: p53 signal pathway
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP655: p53 pathway
WP215: noncanonical wnt pathway
WP654: ATM

Related Genes :
[CCNA2 CCN1 CCNA] Cyclin-A2 (Cyclin-A) (Cyclin A)
[cye-1 C37A2.4] G1/S-specific cyclin-E
[Cdkn2a P16ink4a] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16-INK4)
[botA atx bna bonT CLM_0897] Botulinum neurotoxin type A2 (BoNT/A) (Bontoxilysin-A) (BOTOX) [Cleaved into: Botulinum neurotoxin A2 light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin A2 heavy chain (HC)]
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK5R1 CDK5R NCK5A] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[Cdk5r1 Cdk5r Nck5a] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[CDK5R1 CDK5R NCK5A] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[CDKN2A CDKN2 MTS1] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (Multiple tumor suppressor 1) (MTS-1) (p16-INK4a) (p16-INK4) (p16INK4A)
[Cdkn2a P16ink4a] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16) (p16-INK4)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDKN2A CDKN2 MLM] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p14ARF)
[SCAPER KIAA1454 ZNF291 MSTP063] S phase cyclin A-associated protein in the endoplasmic reticulum (S phase cyclin A-associated protein in the ER) (Zinc finger protein 291)
[nimX cdk1 AN4182] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (Never in mitosis protein X)
[CDKA-1 CDC2 CDC2A At3g48750 T21J18.20] Cyclin-dependent kinase A-1 (CDKA;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog A) (CDC2aAt)
[CDK11A CDC2L2 CDC2L3 PITSLREB] Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)
[cdk1-a cdc2-a cdc2x1.1] Cyclin-dependent kinase 1-A (CDK1-A) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 1) (Cell division control protein 2-A) (Cell division protein kinase 1-A) (p34 protein kinase 1)
[Cdk5r1 Cdk5r] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[CDKN1A CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1] Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein 6) (MDA-6) (p21)
[Cdkn1a Cip1 Waf1] Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein) (p21)
[CDKN1A CIP1 WAF1] Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (p21)
[PHO85 SSG3 YPL031C P7102.18A] Cyclin-dependent protein kinase PHO85 (EC 2.7.11.22) (Negative regulator of the PHO system) (Serine/threonine-protein kinase PHO85)
[Mnat1 Mat1] CDK-activating kinase assembly factor MAT1 (CDK7/cyclin-H assembly factor) (Menage a trois) (RING finger protein MAT1) (p35) (p36)
[PCL1 HCS26 YNL289W N0536] PHO85 cyclin-1 (Cyclin HCS26) (G1/S-specific cyclin PCL1)
[PCL2 CLN4 YDL127W D2223] PHO85 cyclin-2 (Cyclin HCS26 homolog) (G1/S-specific cyclin PCL2)
[INCA1 HSD45] Protein INCA1 (Inhibitor of CDK interacting with cyclin A1)
[CDKN3 CDI1 CIP2 KAP] Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Cyclin-dependent kinase interactor 1) (Cyclin-dependent kinase-interacting protein 2) (Kinase-associated phosphatase)

Bibliography :
[32930475] Inorganic arsenic-mediated upregulation of AS3MT promotes proliferation of nonsmall cell lung cancer cells by regulating cell cycle genes.
[32901501] Simulated microgravity reduces proliferation and reorganizes the cytoskeleton of human umbilical cord mesenchymal stem cells.
[32888357] Ribosome Assembly Factor URB1 Contributes to Colorectal Cancer Proliferation via Transcriptional Activation of ATF4.
[32840291] Quercetin promotes human epidermal stem cell proliferation through the estrogen receptor/β-catenin/c-Myc/cyclin A2 signaling pathway.
[32818521] Methylprednisolone potentiates tetrandrine pharmacodynamics against human T lymphoblastoid leukemia MOLT-4 cells via regulation of NF-κB activation and cell cycle transition.
[32799868] Magnetic targeting enhances the cutaneous wound healing effects of human mesenchymal stem cell-derived iron oxide exosomes.
[32794202] Yap is crucial for CAR-driven hepatocyte proliferation, but not for induction of drug metabolism genes in mice.
[32752095] Standardized Saponin Extract from Baiye No.1 Tea () Flowers Induced S Phase Cell Cycle Arrest and Apoptosis via AKT-MDM2-p53 Signaling Pathway in Ovarian Cancer Cells.
[32724412] Identification of hub genes involved in the occurrence and development of hepatocellular carcinoma via bioinformatics analysis.
[32626933] High expression of FUSE binding protein 1 in breast cancer stimulates cell proliferation and diminishes drug sensitivity.