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Protein

G2/mitotic-specific cyclin-A

Gene

CycA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the Cdk1 and Cdk2 protein kinases to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase regulator activity Source: UniProtKB

GO - Biological processi

  • asymmetric neuroblast division Source: FlyBase
  • G2/M transition of mitotic cell cycle Source: FlyBase
  • lateral inhibition Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • mitotic sister chromatid segregation Source: FlyBase
  • negative regulation of mitotic metaphase/anaphase transition Source: FlyBase
  • neurogenesis Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • regulation of chromatin binding Source: FlyBase
  • regulation of exit from mitosis Source: FlyBase
  • regulation of mitotic cell cycle, embryonic Source: FlyBase
  • regulation of mitotic nuclear division Source: UniProtKB
  • regulation of protein kinase activity Source: GOC
  • sensory perception of pain Source: FlyBase
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-DME-113510. E2F mediated regulation of DNA replication.
R-DME-1538133. G0 and Early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-DME-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-DME-5693607. Processing of DNA double-strand break ends.
R-DME-68911. G2 Phase.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69205. G1/S-Specific Transcription.
R-DME-69273. Cyclin A/B1 associated events during G2/M transition.
R-DME-69656. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP14785.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-A
Gene namesi
Name:CycA
ORF Names:CG5940
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000404. CycA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • fusome Source: FlyBase
  • nuclear cyclin-dependent protein kinase holoenzyme complex Source: FlyBase
  • nucleus Source: UniProtKB
  • spectrosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491G2/mitotic-specific cyclin-APRO_0000080345Add
BLAST

Proteomic databases

PaxDbiP14785.

Expressioni

Gene expression databases

BgeeiP14785.
ExpressionAtlasiP14785. differential.
GenevisibleiP14785. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Z600P224694EBI-240333,EBI-7376821

Protein-protein interaction databases

BioGridi64701. 50 interactions.
DIPiDIP-22019N.
IntActiP14785. 24 interactions.
MINTiMINT-301152.
STRINGi7227.FBpp0075807.

Structurei

3D structure databases

ProteinModelPortaliP14785.
SMRiP14785. Positions 199-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0654. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
InParanoidiP14785.
KOiK06627.
OMAiRESEKKH.
OrthoDBiEOG7G7KQ0.
PhylomeDBiP14785.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P14785-1) [UniParc]FASTAAdd to basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASFQIHQDM SNKENPGIKI PAGVKNTKQP LAVIGGKAEK NALAPRANFA
60 70 80 90 100
VLNGNNNVPR PAGKVQVFRD VRNLNVDENV EYGAKKSNVV PVVEQFKTFS
110 120 130 140 150
VYEDNNDTQV APSGKSLASL VDKENHDVKF GAGQKELVDY DLDSTPMSVT
160 170 180 190 200
DVQSPMSVDR SILGVIQSSD ISVGTETGVS PTGRVKELPP RNDRQRFLEV
210 220 230 240 250
VQYQMDILEY FRESEKKHRP KPLYMRRQKD ISHNMRSILI DWLVEVSEEY
260 270 280 290 300
KLDTETLYLS VFYLDRFLSQ MAVVRSKLQL VGTAAMYIAA KYEEIYPPEV
310 320 330 340 350
GEFVFLTDDS YTKAQVLRME QVILKILSFD LCTPTAYVFI NTYAVLCDMP
360 370 380 390 400
EKLKYMTLYI SELSLMEGET YLQYLPSLMS SASVALARHI LGMEMWTPRL
410 420 430 440 450
EEITTYKLED LKTVVLHLCH THKTAKELNT QAMREKYNRD TYKKVAMMES
460 470 480 490
VEMSKDDFDQ LCEAYNCKQK EDEHQQPDIN TKSNVNLFYK F
Length:491
Mass (Da):56,152
Last modified:May 4, 2001 - v3
Checksum:i6B700EB48A18ED99
GO
Isoform B (identifier: P14785-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.

Note: No experimental confirmation available.
Show »
Length:345
Mass (Da):40,305
Checksum:i176915AA7416E1C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471M → I in BAA01629 (PubMed:1332913).Curated
Sequence conflicti179 – 1791V → A in BAA01628 (PubMed:1332913).Curated
Sequence conflicti179 – 1791V → A in BAA01629 (PubMed:1332913).Curated
Sequence conflicti200 – 2001V → M in BAA01629 (PubMed:1332913).Curated
Sequence conflicti220 – 2201P → A in AAN71390 (PubMed:12537569).Curated
Sequence conflicti223 – 2231L → R in AAA28435 (PubMed:2564316).Curated
Sequence conflicti474 – 4741H → Q in BAA01629 (PubMed:1332913).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 146146Missing in isoform B. 1 PublicationVSP_001249Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10857 Genomic DNA. Translation: BAA01628.1.
D10858 mRNA. Translation: BAA01629.1.
M24841 Genomic RNA. Translation: AAA28435.1.
AE014296 Genomic DNA. Translation: AAF49999.2.
AE014296 Genomic DNA. Translation: AAF50000.3.
AY058712 mRNA. Translation: AAL13941.1.
BT001635 mRNA. Translation: AAN71390.1.
PIRiJC1390.
RefSeqiNP_524030.2. NM_079306.4. [P14785-1]
UniGeneiDm.2549.

Genome annotation databases

EnsemblMetazoaiFBtr0076075; FBpp0075807; FBgn0000404. [P14785-1]
GeneIDi39340.
KEGGidme:Dmel_CG5940.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10857 Genomic DNA. Translation: BAA01628.1.
D10858 mRNA. Translation: BAA01629.1.
M24841 Genomic RNA. Translation: AAA28435.1.
AE014296 Genomic DNA. Translation: AAF49999.2.
AE014296 Genomic DNA. Translation: AAF50000.3.
AY058712 mRNA. Translation: AAL13941.1.
BT001635 mRNA. Translation: AAN71390.1.
PIRiJC1390.
RefSeqiNP_524030.2. NM_079306.4. [P14785-1]
UniGeneiDm.2549.

3D structure databases

ProteinModelPortaliP14785.
SMRiP14785. Positions 199-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64701. 50 interactions.
DIPiDIP-22019N.
IntActiP14785. 24 interactions.
MINTiMINT-301152.
STRINGi7227.FBpp0075807.

Proteomic databases

PaxDbiP14785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076075; FBpp0075807; FBgn0000404. [P14785-1]
GeneIDi39340.
KEGGidme:Dmel_CG5940.

Organism-specific databases

CTDi39340.
FlyBaseiFBgn0000404. CycA.

Phylogenomic databases

eggNOGiKOG0654. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
InParanoidiP14785.
KOiK06627.
OMAiRESEKKH.
OrthoDBiEOG7G7KQ0.
PhylomeDBiP14785.

Enzyme and pathway databases

ReactomeiR-DME-113510. E2F mediated regulation of DNA replication.
R-DME-1538133. G0 and Early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-DME-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-DME-5693607. Processing of DNA double-strand break ends.
R-DME-68911. G2 Phase.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69205. G1/S-Specific Transcription.
R-DME-69273. Cyclin A/B1 associated events during G2/M transition.
R-DME-69656. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP14785.

Miscellaneous databases

ChiTaRSiCycA. fly.
GenomeRNAii39340.
PROiP14785.

Gene expression databases

BgeeiP14785.
ExpressionAtlasiP14785. differential.
GenevisibleiP14785. DM.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Drosophila melanogaster gene encoding cyclin A."
    Takahisa M., Togashi S., Ueda R., Mikuni M., Tsurumura S., Kondo K., Miyake T.
    Gene 121:343-346(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
    Strain: Canton-S.
  2. "Expression and function of Drosophila cyclin A during embryonic cell cycle progression."
    Lehner C.F., O'Farrell P.H.
    Cell 56:957-968(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Transcripts of one of two Drosophila cyclin genes become localized in pole cells during embryogenesis."
    Whitfield W.G.F., Gonzalez C., Sanchez-Herrero E., Glover D.M.
    Nature 338:337-340(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 235-247 AND 288-300.

Entry informationi

Entry nameiCCNA_DROME
AccessioniPrimary (citable) accession number: P14785
Secondary accession number(s): Q8IGR7, Q9VTP6, Q9VTP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 4, 2001
Last modified: June 8, 2016
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.