P30290 (MIK1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitosis inhibitor protein kinase mik1
EC=2.7.11.1

Gene names

Name:	mik1
ORF Names:	SPBC660.14

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Protein kinase that acts both on serines and on tyrosines. It acts as a negative regulator of entry into mitosis (G2 to M transition). Phosphorylates and inhibits cdc2.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of mitotic cell cycle Inferred from genetic interaction Ref.1. Source: PomBase
Cellular_component	cytosol Inferred from direct assay PubMed 16823372. Source: PomBase nucleus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	ATP binding Inferred from sequence model. Source: PomBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay PubMed 1297355Ref.1. Source: PomBase protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 581	581	Mitosis inhibitor protein kinase mik1		PRO_0000086327
Regions
	Domain	289 – 561	273	Protein kinase
	Nucleotide binding	295 – 303	9	ATP By similarity
Sites
	Active site	417	1	Proton acceptor By similarity
	Metal binding	422	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	435	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	320	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30290 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 371E0CEDB2CA1CE3	FASTA	581	65,934
	10 20 30 40 50 60 MDSSTTIPIT PTRTPCFFNI SSSFNEHSPL NFYDEPIYNF SSGHEENQSH KSSKLTFFKP 70 80 90 100 110 120 SNTKRSPHTP MQNNAKAIRL STTVRHGIFK NSDLDGCSKP FAFSSGLKLS KKIVDASTPI 130 140 150 160 170 180 DLKRKRAVTS LSTGLLSKRE KWSLWEGNLT NPRSEQPHTP CKKGTKIKLK PPQSPLSPTT 190 200 210 220 230 240 SLLARKCKHI DLDTFSRLDH PNSDSSDETF EMEELPSLSY GSEDLLEFCE TPCKSQPIFL 250 260 270 280 290 300 SSSHVNNWDE KDVPSSLSWT PTSPIFLNIN SADDYEEEED WTSDLRIRFQ QVKPIHESDF 310 320 330 340 350 360 SFVYHVSSIN PPTETVYVVK MLKKNAAKFT GKERHLQEVS ILQRLQACPF VVNLVNVWSY 370 380 390 400 410 420 NDNIFLQLDY CENGDLSLFL SELGLLQVMD PFRVWKMLFQ LTQALNFIHL LEFVHLDVKP 430 440 450 460 470 480 SNVLITRDGN LKLGDFGLAT SLPVSSMVDL EGDRVYIAPE ILASHNYGKP ADVYSLGLSM 490 500 510 520 530 540 IEAATNVVLP ENGVEWQRLR SGDYSNLPNL KDLLLSKEKV QINKVRCAES LQCLLQRMTH 550 560 570 580 PYVDCRPTTQ DLLAMPEMIF ISEHSQKAAI IYEDHNSWLE T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of cdc2." Lundgren K., Walworth N., Booher R., Dembski M., Kirschner M., Beach D. Cell 64:1111-1122(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." 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. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60834 Genomic DNA. Translation: AAA91278.1. CU329671 Genomic DNA. Translation: CAA22534.1.
PIR	A37913.
RefSeq	NP_595093.1. NM_001021000.2.
3D structure databases
ProteinModelPortal	P30290.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC660.14-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC660.14.1; SPBC660.14.1:pep; SPBC660.14.
GeneID	2540885.
KEGG	spo:SPBC660.14.
Organism-specific databases
PomBase	SPBC660.14.
Phylogenomic databases
eggNOG	COG0515.
OrthoDB	EOG486CN1.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802001.

Entry information

Entry name

MIK1_SCHPO

Accession

Primary (citable) accession number: P30290

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program