[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-67. DOI=10.1016/0378-1119(84)90203-8; PubMed=6526270 [NCBI, ExPASy, EBI, Israel, Japan] Hindley J., Phear G.A.; "Sequence of the cell division gene CDC2 from Schizosaccharomyces pombe; patterns of splicing and homology to protein kinases."; Gene 31:129-134(1984).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 38366 / 972; DOI=10.1002/(SICI)1097-0061(20000115)16:1<71::AID-YEA505>3.0.CO;2-5; PubMed=10620777 [NCBI, ExPASy, EBI, Israel, Japan] Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.; "A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment."; Yeast 16:71-80(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 38366 / 972; DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan] Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; "The genome sequence of Schizosaccharomyces pombe."; Nature 415:871-880(2002).
[4]	ASSOCIATION WITH SUC1. PubMed=3322810 [NCBI, ExPASy, EBI, Israel, Japan] Brizuela L., Draetta G., Beach D.; "p13suc1 acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase."; EMBO J. 6:3507-3515(1987).
[5]	PHOSPHORYLATION AT TYR-15. DOI=10.1038/342039a0; PubMed=2682257 [NCBI, ExPASy, EBI, Israel, Japan] Gould K.L., Nurse P.; "Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis."; Nature 342:39-45(1989).
[6]	INTERACTION WITH CIG2. PubMed=8455610 [NCBI, ExPASy, EBI, Israel, Japan] Bueno A., Russell P.; "Two fission yeast B-type cyclins, cig2 and Cdc13, have different functions in mitosis."; Mol. Cell. Biol. 13:2286-2297(1993).
[7]	MUTAGENESIS OF TYR-15. DOI=10.1007/BF00277142; PubMed=8437586 [NCBI, ExPASy, EBI, Israel, Japan] McNeill S.A., Nurse P.; "Mutational analysis of the fission yeast p34cdc2 protein kinase gene."; Mol. Gen. Genet. 236:415-426(1993).
[8]	FUNCTION. DOI=10.1016/S0092-8674(94)90542-8; PubMed=8087848 [NCBI, ExPASy, EBI, Israel, Japan] Hayles J., Fisher D., Woollard A., Nurse P.; "Temporal order of S phase and mitosis in fission yeast is determined by the state of the p34cdc2-mitotic B cyclin complex."; Cell 78:813-822(1994).
[9]	REVIEW. DOI=10.1016/0168-9525(96)10036-6; PubMed=8855663 [NCBI, ExPASy, EBI, Israel, Japan] Stern B., Nurse P.; "A quantitative model for the cdc2 control of S phase and mitosis in fission yeast."; Trends Genet. 12:345-350(1996).
[10]	FUNCTION. PubMed=9042863 [NCBI, ExPASy, EBI, Israel, Japan] Rhind N., Furnari B., Russell P.; "Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast."; Genes Dev. 11:504-511(1997).
[11]	INTERACTION WITH CIG2. DOI=10.1016/S1097-2765(00)00135-0; PubMed=11163211 [NCBI, ExPASy, EBI, Israel, Japan] Yamano H., Kitamura K., Kominami K., Lehmann A., Hunt T., Toda T.; "The spike of S phase cyclin Cig2 expression at the G1-S border in fission yeast requires both APC and SCF ubiquitin ligases."; Mol. Cell 6:1377-1387(2000).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND THR-167, AND MASS SPECTROMETRY. DOI=10.1073/pnas.122231399; PubMed=12060738 [NCBI, ExPASy, EBI, Israel, Japan] MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M., Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I., Yates J.R. III; "Shotgun identification of protein modifications from protein complexes and lens tissue."; Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002).
[13]	FUNCTION. DOI=10.1074/jbc.M504746200; PubMed=16049013 [NCBI, ExPASy, EBI, Israel, Japan] Shimada M., Namikawa-Yamada C., Nakanishi M., Murakami H.; "Regulation of Cdc2p and Cdc13p is required for cell cycle arrest induced by defective RNA splicing in fission yeast."; J. Biol. Chem. 280:32640-32648(2005).
[14]	FUNCTION. DOI=10.1016/j.cub.2006.06.065; PubMed=16920624 [NCBI, ExPASy, EBI, Israel, Japan] Aoki K., Nakaseko Y., Kinoshita K., Goshima G., Yanagida M.; "CDC2 phosphorylation of the fission yeast dis1 ensures accurate chromosome segregation."; Curr. Biol. 16:1627-1635(2006).
[15]	INTERACTION WITH CDC13 AND CDC37. DOI=10.1242/jcs.02729; PubMed=16390871 [NCBI, ExPASy, EBI, Israel, Japan] Turnbull E.L., Martin I.V., Fantes P.A.; "Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe."; J. Cell Sci. 119:292-302(2006).
[16]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan] Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.; "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."; Nat. Biotechnol. 24:841-847(2006).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND THR-167, AND MASS SPECTROMETRY. DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan] Wilson-Grady J.T., Villen J., Gygi S.P.; "Phosphoproteome analysis of fission yeast."; J. Proteome Res. 7:1088-1097(2008).

Comments

FUNCTION: Plays a key role in the control of the eukaryotic cell cycle. It is required for entry into S-phase and mitosis. When complexed with cig2, plays a role in G1-S phase transition. When activated and complexed with the cyclin cdc13, it leads to the onset of mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II. Involved in cell cycle arrest induced by defective RNA splicing. Required for phosphorylation of dis1 to ensure accurate chromosome segregation and for the DNA damage checkpoint.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-167 activates it (By similarity).
SUBUNIT: Forms a stable but non-covalent complex with a regulatory subunit suc1 and with the cyclin cdc13. Also associates with cdc37 and cig2.
INTERACTION:
P10815:cdc13; NbExp=1; IntAct=EBI-1187862, EBI-1187843;
O94740:cdc37; NbExp=1; IntAct=EBI-1187862, EBI-1209056;
P36630:cig2; NbExp=1; IntAct=EBI-1187862, EBI-1149212;
P40380:rum1; NbExp=1; IntAct=EBI-1187862, EBI-1187892;
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M12912; AAA35293.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB004534; BAA21379.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAC37513.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23359; TVZP2.

RefSeq

NP_595629.1; -.

3D structure databases

HSSP

P24941; 1H00. [HSSP ENTRY / PDB]

SMR

P04551; 1-295.

ModBase

P04551.

Protein-protein interaction databases

DIP

DIP:1076N; -.

IntAct

P04551; -.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-003661-MON; -.

Organism-specific databases

GeneDB_Spombe

SPBC11B10.09; -.

Gene expression databases

ArrayExpress

P04551; -.

GermOnline

SPACTOKYO_453.34; Schizosaccharomyces pombe.

Ontologies

GO:0000307;	Cellular component: cyclin-dependent protein kinase holoenzyme complex (inferred by curator from GeneDB_SPombe).
GO:0005829;	Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0004693;	Molecular function: cyclin-dependent protein kinase activity (traceable author statement from GeneDB_SPombe).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0000077;	Biological process: DNA damage checkpoint (traceable author statement from GeneDB_SPombe).
GO:0000076;	Biological process: DNA replication checkpoint (traceable author statement from GeneDB_SPombe).
GO:0000082;	Biological process: G1/S transition of mitotic cell cycle (traceable author statement from GeneDB_SPombe).
GO:0000086;	Biological process: G2/M transition of mitotic cell cycle (traceable author statement from GeneDB_SPombe).
GO:0007089;	Biological process: traversing start control point of mitotic cell cycle (non-traceable author statement from GeneDB_SPombe).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

2539869; -.

fig|4896.1.peg.1495; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm; Kinase; Mitosis; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 297`	`297`	`Cell division control protein 2.`	`PRO_0000085720`
`DOMAIN`	`4 293`	`290`	`Protein kinase.`
`NP_BIND`	`10 18`	`9`	`ATP (By similarity).`
`ACT_SITE`	`134 134`		`Proton acceptor (By similarity).`
`BINDING`	`33 33`		`ATP (By similarity).`
`MOD_RES`	`14 14`		`Phosphothreonine (By similarity).`
`MOD_RES`	`15 15`		`Phosphotyrosine.`
`MOD_RES`	`167 167`		`Phosphothreonine.`
`MUTAGEN`	`15 15`		`Y->F: Premature entry into mitosis.`
`MUTAGEN`	`67 67`		`C->F: In cdc2-4W.`
`MUTAGEN`	`67 67`		`C->Y: In cdc2-3W.`

Sequence information

Length: 297 AA [This is the length of the unprocessed precursor]

Molecular weight: 34359 Da [This is the MW of the unprocessed precursor]

CRC64: D04EF14BA1492875 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENYQKVEKI GEGTYGVVYK ARHKLSGRIV AMKKIRLEDE SEGVPSTAIR EISLLKEVND 

        70         80         90        100        110        120 
ENNRSNCVRL LDILHAESKL YLVFEFLDMD LKKYMDRISE TGATSLDPRL VQKFTYQLVN 

       130        140        150        160        170        180 
GVNFCHSRRI IHRDLKPQNL LIDKEGNLKL ADFGLARSFG VPLRNYTHEI VTLWYRAPEV 

       190        200        210        220        230        240 
LLGSRHYSTG VDIWSVGCIF AEMIRRSPLF PGDSEIDEIF KIFQVLGTPN EEVWPGVTLL 

       250        260        270        280        290 
QDYKSTFPRW KRMDLHKVVP NGEEDAIELL SAMLVYDPAH RISAKRALQQ NYLRDFH

P04551 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools