ESS2_SCHPO
ID ESS2_SCHPO Reviewed; 384 AA.
AC O59793;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Stress response protein bis1;
DE AltName: Full=Splicing factor ESS-2 homolog;
GN Name=bis1; ORFNames=SPCC364.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH ISH1, AND SUBCELLULAR LOCATION.
RX PubMed=11751918; DOI=10.1074/jbc.m110686200;
RA Taricani L., Tejada M.L., Young P.G.;
RT "The fission yeast ES2 homologue, Bis1, interacts with the Ish1 stress-
RT responsive nuclear envelope protein.";
RL J. Biol. Chem. 277:10562-10572(2002).
CC -!- FUNCTION: Has a role in maintaining cell viability during stationary
CC phase induced by stress response (PubMed:11751918). May be involved in
CC pre-mRNA splicing. {ECO:0000250|UniProtKB:P34420,
CC ECO:0000269|PubMed:11751918}.
CC -!- SUBUNIT: Heterodimer with ish1. {ECO:0000269|PubMed:11751918}.
CC -!- INTERACTION:
CC O59793; Q9Y7X6: ish1; NbExp=4; IntAct=EBI-1559662, EBI-1559673;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11751918}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:11751918}. Note=During
CC mitosis associates with the spindle microtubules.
CC -!- SIMILARITY: Belongs to the ESS2 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA18284.1; -; Genomic_DNA.
DR PIR; T41334; T41334.
DR RefSeq; NP_587842.1; NM_001022835.2.
DR AlphaFoldDB; O59793; -.
DR BioGRID; 275368; 45.
DR IntAct; O59793; 24.
DR STRING; 4896.SPCC364.02c.1; -.
DR iPTMnet; O59793; -.
DR MaxQB; O59793; -.
DR PaxDb; O59793; -.
DR PRIDE; O59793; -.
DR EnsemblFungi; SPCC364.02c.1; SPCC364.02c.1:pep; SPCC364.02c.
DR GeneID; 2538787; -.
DR KEGG; spo:SPCC364.02c; -.
DR PomBase; SPCC364.02c; bis1.
DR VEuPathDB; FungiDB:SPCC364.02c; -.
DR eggNOG; KOG2627; Eukaryota.
DR HOGENOM; CLU_719929_0_0_1; -.
DR InParanoid; O59793; -.
DR OMA; IAWKERP; -.
DR PhylomeDB; O59793; -.
DR PRO; PR:O59793; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR InterPro; IPR019148; Nuclear_protein_DGCR14_ESS-2.
DR PANTHER; PTHR12940; PTHR12940; 2.
DR Pfam; PF09751; Es2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Reference proteome.
FT CHAIN 1..384
FT /note="Stress response protein bis1"
FT /id="PRO_0000064936"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 43023 MW; 0DC9D851B655C695 CRC64;
MSLAKKIDDD EKQLVKPVNK EQTYKKPIPL EEDDYIEGLS YIIQQQYFPD LPKLKAEVVL
ESEEVGSFDA QNESRDEKLK YLIAKNSEDP LRKRLPSLAI HEITKAQLDG ENKPISVASY
QNKFTSEDNA SFGELMEDES RLRAEQHKRR FGVHSQQPSN SIQTIGYSNS DAIKSIAWKE
KDKSIKTWNY QPKNALMYTP ETNHSSSLSQ IKKQSTEIQA DATGLSQSFL EAANQPSTDP
IVPPSVNETD ASVNGYPLVD VNFGQAVGSS SKSYFNIPER PRRERLHAMR VRDIRSHSTN
TTITSVDSAS TALNSYSTPN SVSRKLTNLT PAARRLVARS YLRSPLHGSS PSASRHTALR
TSIPKFSWTP TPRVKSTAPT PKRV
