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Q09892 (HOG1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase sty1

Short name=MAP kinase sty1
EC=2.7.11.24
Alternative name(s):
MAP kinase spc1
Gene names
Name:sty1
Synonyms:hog1, phh1, spc1
ORF Names:SPAC24B11.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes. Involved in osmoregulation and stress response pathways leading to an efficient start of sexual differentiation. Supports translation initiation and facilitates adaptation to environmental stress in part through reducing eIF2-alpha phosphorylation. Links the cell-cycle G2/M control with changes in the extracellular environment that affect cell physiology. Phosphorylates atf1 and mkp1. In conjunction with hal4, has a role in the cellular resistance to toxic cations such as Na+, Li+ and Ca2+. Involved in resistance to arsenite, methylglyoxal and hydrogen peroxide. Involved in induction of thermotolerance in mRNA export, as well as in vacuolar fission. Ref.1 Ref.2 Ref.3 Ref.5 Ref.9 Ref.10 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by the MAPK kinase wisl, and negatively regulated by pypl and pyp2 tyrosine phosphatases. Ref.2 Ref.6 Ref.8 Ref.13 Ref.14 Ref.22

Subunit structure

Interacts with cdc37, cmk2, hal4, sin1 and srk1. Ref.12 Ref.14 Ref.15 Ref.20

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation. Ref.7 Ref.11 Ref.12 Ref.13 Ref.19 Ref.23

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme By similarity. Phosphorylated by wis1 in response to osmotic stress, nutrient limitation, hydrogen peroxide and arsenite. Dephosphorylated by pyp1 and pyp2. Ref.2 Ref.6 Ref.8 Ref.9 Ref.12 Ref.17 Ref.19 Ref.22

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1 cell cycle arrest in response to nitrogen starvation

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

G1 to G0 transition

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

MAPK cascade in response to starvation

Inferred from mutant phenotype Ref.2. Source: PomBase

MAPK cascade involved in osmosensory signaling pathway

Inferred from mutant phenotype Ref.2. Source: PomBase

activation of bipolar cell growth

Inferred from mutant phenotype PubMed 20501954. Source: PomBase

cell cycle arrest in response to nitrogen starvation

Inferred from mutant phenotype Ref.5. Source: PomBase

cellular response to arsenic-containing substance

Inferred from mutant phenotype Ref.17. Source: PomBase

cellular response to cation stress

Inferred from genetic interaction Ref.20. Source: PomBase

cellular response to nitrogen starvation

Inferred from mutant phenotype PubMed 15448137. Source: PomBase

mRNA export from nucleus in response to heat stress

Inferred from mutant phenotype Ref.16. Source: PomBase

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.2. Source: PomBase

positive regulation of transcription factor import into nucleus in response to oxidative stress

Inferred from mutant phenotype Ref.10. Source: PomBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15164362. Source: PomBase

positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from mutant phenotype PubMed 17016471Ref.10. Source: PomBase

protein phosphorylation

Inferred from genetic interaction Ref.7. Source: PomBase

regulation of DNA binding

Inferred from direct assay PubMed 9819443. Source: PomBase

regulation of cAMP-mediated signaling

Inferred from mutant phenotype PubMed 15448137. Source: PomBase

regulation of cAMP-mediated signaling by regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15448137. Source: PomBase

regulation of cell shape involved in G1 to G0 transition

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

regulation of chromatin assembly

Inferred from mutant phenotype PubMed 15448137. Source: PomBase

regulation of chromatin disassembly

Inferred from mutant phenotype PubMed 15448137. Source: PomBase

regulation of histone acetylation

Inferred from mutant phenotype PubMed 14988732. Source: PomBase

regulation of mRNA stability involved in cellular response to UV

Inferred from mutant phenotype PubMed 10954610. Source: PomBase

regulation of meiotic cell cycle

Inferred from mutant phenotype PubMed 9819443. Source: PomBase

regulation of reciprocal meiotic recombination

Inferred from mutant phenotype PubMed 9819443. Source: PomBase

regulation of translation in response to nitrogen starvation

Inferred from direct assay PubMed 18065650. Source: PomBase

regulation of translation in response to osmotic stress

Inferred from direct assay PubMed 18065650. Source: PomBase

regulation of translation in response to oxidative stress

Inferred from direct assay PubMed 18065650. Source: PomBase

response to methylglyoxal

Inferred from direct assay Ref.19. Source: PomBase

stress granule assembly

Inferred from mutant phenotype PubMed 21098141. Source: PomBase

stress granule disassembly

Inferred from mutant phenotype PubMed 21098141. Source: PomBase

stress-activated MAPK cascade

Inferred from mutant phenotype Ref.6PubMed 9718372. Source: PomBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay Ref.23. Source: PomBase

nucleus

Inferred from direct assay Ref.23PubMed 19672306. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from direct assay Ref.12PubMed 12135491Ref.15Ref.2Ref.7. Source: PomBase

MAP kinase activity involved in osmosensory signaling pathway

Inferred from direct assay Ref.5. Source: PomBase

protein binding

Inferred from physical interaction Ref.12PubMed 22139357. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Mitogen-activated protein kinase sty1
PRO_0000186342

Regions

Domain20 – 299280Protein kinase
Nucleotide binding26 – 349ATP By similarity
Motif171 – 1733TXY
Motif176 – 1783TXY

Sites

Active site1411Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1711Phosphothreonine Ref.26
Modified residue1731Phosphotyrosine Ref.26
Modified residue1751Phosphoserine Ref.26
Modified residue1761Phosphothreonine Ref.26

Sequences

Sequence LengthMass (Da)Tools
Q09892 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9A10835FFD381AC0

FASTA34940,222
        10         20         30         40         50         60 
MAEFIRTQIF GTCFEITTRY SDLQPIGMGA FGLVCSAKDQ LTGMNVAVKK IMKPFSTPVL 

        70         80         90        100        110        120 
AKRTYRELKL LKHLRHENII SLSDIFISPF EDIYFVTELL GTDLHRLLTS RPLETQFIQY 

       130        140        150        160        170        180 
FLYQILRGLK FVHSAGVIHR DLKPSNILIN ENCDLKICDF GLARIQDPQM TGYVSTRYYR 

       190        200        210        220        230        240 
APEIMLTWQK YNVEVDIWSA GCIFAEMIEG KPLFPGRDHV NQFSIITELL GTPPMEVIET 

       250        260        270        280        290        300 
ICSKNTLRFV QSLPQKEKVP FAEKFKNADP DAIDLLEKML VFDPRKRISA ADALAHNYLA 

       310        320        330        340 
PYHDPTDEPV ADEVFDWSFQ DNDLPVETWK VMMYSEVLSF HNMDNELQS 

« Hide

References

« Hide 'large scale' references
[1]"Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast."
Millar J.B.A., Buck V., Wilkinson M.G.
Genes Dev. 9:2117-2130(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast."
Shiozaki K., Russell P.
Nature 378:739-743(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, ENZYME REGULATION.
[3]"Stress signal, mediated by a Hog1-like MAP kinase, controls sexual development in fission yeast."
Kato T. Jr., Okazaki K., Murakami H., Stettler S., Fantes P.A., Okayama H.
FEBS Lett. 378:207-212(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[5]"Conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast."
Shiozaki K., Russell P.
Genes Dev. 10:2276-2288(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 972 / ATCC 24843.
[6]"Activation and regulation of the Spc1 stress-activated protein kinase in Schizosaccharomyces pombe."
Degols G., Shiozaki K., Russell P.
Mol. Cell. Biol. 16:2870-2877(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION.
[7]"Stress-activated protein kinase pathway in cell cycle control of fission yeast."
Shiozaki K., Russell P.
Methods Enzymol. 283:506-520(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Mcs4 mitotic catastrophe suppressor regulates the fission yeast cell cycle through the Wik1-Wis1-Spc1 kinase cascade."
Shiozaki K., Shiozaki M., Russell P.
Mol. Biol. Cell 8:409-419(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION.
[9]"Regulated vacuole fusion and fission in Schizosaccharomyces pombe: an osmotic response dependent on MAP kinases."
Bone N., Millar J.B.A., Toda T., Armstrong J.
Curr. Biol. 8:135-144(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[10]"Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (Exportin) and the stress-activated MAP kinase Sty1/Spc1."
Toone W.M., Kuge S., Samuels M., Morgan B.A., Toda T., Jones N.
Genes Dev. 12:1453-1463(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast."
Gaits F., Degols G., Shiozaki K., Russell P.
Genes Dev. 12:1464-1473(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast."
Smith D.A., Toone W.M., Chen D., Baehler J., Jones N., Morgan B.A., Quinn J.
J. Biol. Chem. 277:33411-33421(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH SRK1.
[13]"Cytoplasmic localization of Wis1 MAPKK by nuclear export signal is important for nuclear targeting of Spc1/Sty1 MAPK in fission yeast."
Nguyen A.N., Ikner A.D., Shiozaki M., Warren S.M., Shiozaki K.
Mol. Biol. Cell 13:2651-2663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
[14]"Identification of cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinase."
Tatebe H., Shiozaki K.
Mol. Cell. Biol. 23:5132-5142(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC37, ENZYME REGULATION.
[15]"Mkp1 and Mkp2, two MAPKAP-kinase homologues in Schizosaccharomyces pombe, interact with the MAP kinase Sty1."
Asp E., Sunnerhagen P.
Mol. Genet. Genomics 268:585-597(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CMK2 AND SRK1.
[16]"Hsp16p is required for thermotolerance in nuclear mRNA export in fission yeast Schizosaccharomyces pombe."
Yoshida J., Tani T.
Cell Struct. Funct. 29:125-138(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Distinct signaling pathways respond to arsenite and reactive oxygen species in Schizosaccharomyces pombe."
Rodriguez-Gabriel M.A., Russell P.
Eukaryot. Cell 4:1396-1402(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[18]"Stress-activated protein kinase pathway functions to support protein synthesis and translational adaptation in response to environmental stress in fission yeast."
Dunand-Sauthier I., Walker C.A., Narasimhan J., Pearce A.K., Wek R.C., Humphrey T.C.
Eukaryot. Cell 4:1785-1793(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe."
Zuin A., Vivancos A.P., Sanso M., Takatsume Y., Ayte J., Inoue Y., Hidalgo E.
J. Biol. Chem. 280:36708-36713(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[20]"Response of fission yeast to toxic cations involves cooperative action of the stress-activated protein kinase Spc1/Sty1 and the Hal4 protein kinase."
Wang L.-Y., Shimada K., Morishita M., Shiozaki K.
Mol. Cell. Biol. 25:3945-3955(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HAL4.
[21]"The fission yeast stress MAPK cascade regulates the pmp3+ gene that encodes a highly conserved plasma membrane protein."
Wang L.-Y., Shiozaki K.
FEBS Lett. 580:2409-2413(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Methylglyoxal as a signal initiator for activation of the stress-activated protein kinase cascade in the fission yeast Schizosaccharomyces pombe."
Takatsume Y., Izawa S., Inoue Y.
J. Biol. Chem. 281:9086-9092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, ENZYME REGULATION.
[23]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[24]"Regulation of Schizosaccharomyces pombe Atf1 protein levels by Sty1-mediated phosphorylation and heterodimerization with Pcr1."
Lawrence C.L., Maekawa H., Worthington J.L., Reiter W., Wilkinson C.R.M., Jones N.
J. Biol. Chem. 282:5160-5170(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Rad4TopBP1 associates with Srr2, an Spc1 MAPK-regulated protein, in response to environmental stress."
Taricani L., Wang T.S.F.
J. Biol. Chem. 282:8793-8800(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[26]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-171; TYR-173; SER-175 AND THR-176, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89262 Genomic DNA. Translation: CAA61537.1.
U26739 mRNA. Translation: AAA91020.1.
CU329670 Genomic DNA. Translation: CAA91771.1.
PIRS68675.
RefSeqNP_592843.1. NM_001018244.2.

3D structure databases

ProteinModelPortalQ09892.
SMRQ09892. Positions 3-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278148. 296 interactions.
IntActQ09892. 5 interactions.
MINTMINT-4696085.
STRING4896.SPAC24B11.06c-1.

Proteomic databases

MaxQBQ09892.
PaxDbQ09892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC24B11.06c.1; SPAC24B11.06c.1:pep; SPAC24B11.06c.
GeneID2541652.
KEGGspo:SPAC24B11.06c.

Organism-specific databases

PomBaseSPAC24B11.06c.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04441.
OMAPDDVIHT.
OrthoDBEOG7K3TWD.
PhylomeDBQ09892.

Enzyme and pathway databases

BRENDA2.7.11.24. 5615.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01773. P38MAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802745.
PROQ09892.

Entry information

Entry nameHOG1_SCHPO
AccessionPrimary (citable) accession number: Q09892
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names