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P10506 (BYR1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

bob1O943072EBI-2042633,EBI-2042611

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Protein kinase byr1
PRO_0000085688

Regions

Domain66 – 320255Protein kinase
Nucleotide binding72 – 809ATP By similarity

Sites

Active site1861Proton acceptor By similarity
Binding site931ATP By similarity

Amino acid modifications

Modified residue2141Phosphoserine By similarity
Modified residue2181Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P10506 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 2AC885AEE971DB8A

FASTA34038,189
        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

« Hide

References

« Hide '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. expand/collapse author list , 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: 972 / ATCC 24843.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07445 Genomic DNA. Translation: CAA30326.1.
CU329670 Genomic DNA. Translation: CAA93222.1.
PIROKBYR1. S00473.
RefSeqNP_593026.1. NM_001018425.1.

3D structure databases

ProteinModelPortalP10506.
ModBaseSearch...

Protein-protein interaction databases

IntActP10506. 2 interactions.
STRINGP10506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1D4.13.1; SPAC1D4.13.1:pep; SPAC1D4.13.
GeneID2542137.
GenomeReviewsGene locus byr1 in contig CU329670_GR.
KEGGspo:SPAC1D4.13.
NMPDRfig|4896.1.peg.2996.

Organism-specific databases

GeneDB_SpombeSPAC1D4.13.

Phylogenomic databases

eggNOGfuNOG07450.
GeneTreeEFGT00050000000597.
HOGENOMHBG755340.
OMAKVIQLNI.
OrthoDBEOG43V342.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000747-MONOMER.
BRENDA2.7.12.2. 5615.

Gene expression databases

ArrayExpressP10506.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
KOK00924.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBYR1_SCHPO
AccessionPrimary (citable) accession number: P10506
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 14, 2011
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents