Reviewed, UniProtKB/Swiss-Prot P10506 (BYR1_SCHPO)

Names and origin

Protein names

Recommended name:
    Protein kinase byr1
    EC=2.7.12.2
Alternative name(s):
    MAPK kinase
      Short name=MAPKK

Gene names

Name:	byr1
Synonyms:	ste1
ORF Names:	SPAC1D4.13

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serine/threonine protein kinase involved in conjugation and sporulation. It is thought that it is phosphorylated by the byr2 protein kinase and that it can phosphorylate the spk1 kinase. When bound to bob1, is involved in the regulation of sexual differentiation. Ref.1 Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with bob1 and spk1. Ref.3
Subcellular location	Cytoplasm. Note: Localizes to the cell tips and septum forming regions. Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Conjugation Sporulation
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle arrest in response to pheromone Traceable author statement. Source: GeneDB_SPombe cellular response to nitrogen starvation Inferred from genetic interaction. Source: GeneDB_SPombe protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction involved in conjugation with cellular fusion Inferred from genetic interaction. Source: GeneDB_SPombe sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Ref.3 Traceable author statement. Source: GeneDB_SPombe protein binding Ref.3 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
bob1	O94307	1	EBI-2042633,EBI-2042611
spk1	P27638	1	EBI-2042633,EBI-2104356

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 340	340	Protein kinase byr1		PRO_0000085688
Regions
	Domain	66 – 320	255	Protein kinase
	Nucleotide binding	72 – 80	9	ATP By similarity
Sites
	Active site	186	1	Proton acceptor By similarity
	Binding site	93	1	ATP By similarity
Amino acid modifications
	Modified residue	214	1	Phosphoserine By similarity
	Modified residue	218	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10506-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 2AC885AEE971DB8A	FASTA	340	38,189
	10 20 30 40 50 60 MFKRRRNPKG LVLNPNASVK SSDNDHKEEL INNQKSFESN VEAFMEQCAH MNRRPAWISD 70 80 90 100 110 120 LDNSSLEVVR HLGEGNGGAV SLVKHRNIFM ARKTVYVGSD SKLQKQILRE LGVLHHCRSP 130 140 150 160 170 180 YIVGFYGAFQ YKNNISLCME YMDCGSLDAI LREGGPIPLD ILGKIINSMV KGLIYLYNVL 190 200 210 220 230 240 HIIHRDLKPS NVVVNSRGEI KLCDFGVSGE LVNSVAQTFV GTSTYMSPER IRGGKYTVKS 250 260 270 280 290 300 DIWSLGISII ELATQELPWS FSNIDDSIGI LDLLHCIVQE EPPRLPSSFP EDLRLFVDAC 310 320 330 340 LHKDPTLRAS PQQLCAMPYF QQALMINVDL ASWASNFRSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A gene which encodes a predicted protein kinase can restore some functions of the ras gene in fission yeast." Nadin-Davis S.A., Nasim A. EMBO J. 7:985-993(1988) [PubMed: 3042386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Bob1, a Gim5/MM-1/Pfd5 homolog, interacts with the MAP kinase kinase byr1 to regulate sexual differentiation in the fission yeast, Schizosaccharomyces pombe." Henkel J., Du H., Yang P., Qyang Y., Kansra S., Ko M., Kim H., Marcus S. Differentiation 67:98-106(2001) [PubMed: 11683500] [Abstract] Cited for: FUNCTION, INTERACTION WITH BOB1 AND SPK1, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07445 Genomic DNA. Translation: CAA30326.1. CU329670 Genomic DNA. Translation: CAA93222.1.
PIR	OKBYR1. S00473.
RefSeq	NP_593026.1.
3D structure databases
SMR	P10506. Positions 58-336.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10506. 2 interactions.
STRING	P10506.
Genome annotation databases
GeneID	2542137.
GenomeReviews	Gene locus byr1 in contig CU329670_GR.
KEGG	spo:SPAC1D4.13.
NMPDR	fig|4896.1.peg.2996.
Organism-specific databases
GeneDB_Spombe	SPAC1D4.13.
Phylogenomic databases
eggNOG	fuNOG07450.
HOGENOM	HBG755340.
OMA	DREISIC.
OrthoDB	EOG9615MC.
PhylomeDB	P10506.
Enzyme and pathway databases
BRENDA	2.7.12.2. 653.
Gene expression databases
ArrayExpress	P10506.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BYR1_SCHPO

Accession

Primary (citable) accession number: P10506

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 19, 2010
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)