Reviewed, UniProtKB/Swiss-Prot P28829 (BYR2_SCHPO)

Names and origin

Protein names

Recommended name:
    Protein kinase byr2
    EC=2.7.11.25
Alternative name(s):
    Protein kinase ste8
    MAPK kinase kinase
      Short name=MAPKKK

Gene names

Name:	byr2
Synonyms:	ste8
ORF Names:	SPBC1D7.05, SPBC2F12.01

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	659 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serine/threonine protein kinase involved in conjugation and sporulation. It is thought that it phosphorylates the byr1 protein kinase which itself phosphorylate the spk1 kinase.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Conjugation Sporulation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle arrest in response to pheromone Traceable author statement. Source: GeneDB_SPombe induction of conjugation upon nitrogen starvation Traceable author statement. Source: GeneDB_SPombe protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction involved in conjugation with cellular fusion Traceable author statement. Source: GeneDB_SPombe sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: GeneDB_SPombe plasma membrane Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase activity Traceable author statement. Source: GeneDB_SPombe protein binding Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HRAS	P01112	1	EBI-1032333,EBI-350145	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 659

659

Protein kinase byr2

PRO_0000085689

Regions

Domain

4 – 67

64

SAM

Domain

394 – 658

265

Protein kinase

Nucleotide binding

400 – 408

9

ATP By similarity

Sites

Active site

522

1

Proton acceptor By similarity

Binding site

423

1

ATP By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

659

Helix Strand Turn

Details...

Beta strand

72 – 76

5

Beta strand

82 – 86

5

Helix

91 – 102

12

Beta strand

109 – 115

7

Beta strand

117 – 122

6

Beta strand

143 – 150

8

Helix

155 – 160

6

Sequences

	Sequence		Length	Mass (Da)
	P28829-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 18CD78F1D1FABBCD	FASTA	659	73,633
	10 20 30 40 50 60 MEYYTSKEVA EWLKSIGLEK YIEQFSQNNI EGRHLNHLTL PLLKDLGIEN TAKGKQFLKQ 70 80 90 100 110 120 RDYLREFPRP CILRFIACNG QTRAVQSRGD YQKTLAIALK KFSLEDASKF IVCVSQSSRI 130 140 150 160 170 180 KLITEEEFKQ ICFNSSSPER DRLIIVPKEK PCPSFEDLRR SWEIELAQPA ALSSQSSLSP 190 200 210 220 230 240 KLSSVLPTST QKRSVRSNNA KPFESYQRPP SELINSRISD FFPDHQPKLL EKTISNSLRR 250 260 270 280 290 300 NLSIRTSQGH NLGNFGQEIL PRSSRRARPS ELVCPLSSLR ISVAEDVNRL PRIDRGFDPP 310 320 330 340 350 360 LTVSSTQRIS RPPSLQKSIT MVGVEPLYQS NGNEKSSKYN VFSESAHGNH QVLSFSPGSS 370 380 390 400 410 420 PSFIEQPSPI SPTSTTSEDT NTLEEDTDDQ SIKWIRGALI GSGSFGQVYL GMNASSGELM 430 440 450 460 470 480 AVKQVILDSV SESKDRHAKL LDALAGEIAL LQELSHEHIV QYLGSNLNSD HLNIFLEYVP 490 500 510 520 530 540 GGSVAGLLTM YGSFEETLVK NFIKQTLKGL EYLHSRGIVH RDIKGANILV DNKGKIKISD 550 560 570 580 590 600 FGISKKLELN STSTKTGGAR PSFQGSSFWM APEVVKQTMH TEKTDIWSLG CLVIEMLTSK 610 620 630 640 650 HPYPNCDQMQ AIFRIGENIL PEFPSNISSS AIDFLEKTFA IDCNLRPTAS ELLSHPFVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype." Wang Y., Xu H.P., Riggs M., Rodgers L., Wigler M. Mol. Cell. Biol. 11:3554-3563(1991) [PubMed: 2046669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Functional conservation between Schizosaccharomyces pombe ste8 and Saccharomyces cerevisiae STE11 protein kinases in yeast signal transduction." Styrkarsdottir U., Egel R., Nielsen O. Mol. Gen. Genet. 235:122-130(1992) [PubMed: 1435723] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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.
[4]	"Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings." Gronwald W., Brunner E., Huber F., Wenzler M., Herrmann C., Kalbitzer H.R. Protein Sci. 10:1260-1263(2001) [PubMed: 11369865] [Abstract] Cited for: STRUCTURE BY NMR OF 71-165.
[5]	"The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast." Scheffzek K., Grunewald P., Wohlgemuth S., Kabsch W., Tu H., Wigler M., Wittinghofer A., Herrmann C. Structure 9:1043-1050(2001) [PubMed: 11709168] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 81-180.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M74293 Genomic DNA. Translation: AAA35289.1.
X68851 Genomic DNA. Translation: CAA48731.1.
CU329671 Genomic DNA. Translation: CAB10150.1.

PIR

A39723.

RefSeq

NP_595714.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I35	NMR	-	A	71-165	[»]
1K8R	X-ray	3.00	B	71-180	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:136N.

IntAct

P28829. 1 interaction.

STRING

P28829.

Genome annotation databases

GeneID

2540612.

GenomeReviews

Gene locus byr2 in contig CU329671_GR.

KEGG

spo:SPBC1D7.05.

Organism-specific databases

GeneDB_Spombe

SPBC1D7.05.

Phylogenomic databases

OMA

RIGENIL.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-004863-MON.

BRENDA

2.7.11.25. 653.

Gene expression databases

ArrayExpress

P28829.

Family and domain databases

InterPro

IPR015748. MAPKKK3.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR011510. SAM_2.
IPR013761. SAM_type.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

Gene3D

G3DSA:1.10.150.50. SAM_type. 1 hit.

PANTHER

PTHR22986:SF64. MAPKKK3. 1 hit.

Pfam

PF00069. Pkinase. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00220. S_TKc. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BYR2_SCHPO

Accession

Primary (citable) accession number: P28829
Secondary accession number(s): Q7LGJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	November 3, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)