ABP2_SCHPO
ID ABP2_SCHPO Reviewed; 527 AA.
AC Q9USY4; P78967;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=ARS-binding protein 2;
GN Name=abp2; ORFNames=SPBC1861.02;
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 [MRNA], PROTEIN SEQUENCE OF 154-171; 302-308; 312-328;
RP 377-384 AND 419-431, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-331; GLY-332 AND ARG-333.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9488484; DOI=10.1128/mcb.18.3.1670;
RA Sanchez J.P., Murakami Y., Huberman J.A., Hurwitz J.;
RT "Isolation, characterization, and molecular cloning of a protein (Abp2)
RT that binds to a Schizosaccharomyces pombe origin of replication
RT (ars3002).";
RL Mol. Cell. Biol. 18:1670-1681(1998).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-298 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Binds, preferentially, to the Maundrell ARS consensus
CC sequence within ARS3002. {ECO:0000269|PubMed:9488484}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9488484}.
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DR EMBL; U73044; AAC49930.1; -; mRNA.
DR EMBL; CU329671; CAB52738.1; -; Genomic_DNA.
DR PIR; T39741; T39741.
DR RefSeq; NP_596719.1; NM_001022644.2.
DR AlphaFoldDB; Q9USY4; -.
DR SMR; Q9USY4; -.
DR BioGRID; 276376; 10.
DR IntAct; Q9USY4; 1.
DR STRING; 4896.SPBC1861.02.1; -.
DR iPTMnet; Q9USY4; -.
DR SwissPalm; Q9USY4; -.
DR MaxQB; Q9USY4; -.
DR PaxDb; Q9USY4; -.
DR PRIDE; Q9USY4; -.
DR EnsemblFungi; SPBC1861.02.1; SPBC1861.02.1:pep; SPBC1861.02.
DR GeneID; 2539827; -.
DR KEGG; spo:SPBC1861.02; -.
DR PomBase; SPBC1861.02; abp2.
DR VEuPathDB; FungiDB:SPBC1861.02; -.
DR eggNOG; ENOG502QV85; Eukaryota.
DR HOGENOM; CLU_039335_0_0_1; -.
DR InParanoid; Q9USY4; -.
DR OMA; CLCCNPW; -.
DR PRO; PR:Q9USY4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:PomBase.
DR InterPro; IPR018562; ARS-binding_2.
DR PANTHER; PTHR42048; PTHR42048; 2.
DR Pfam; PF09441; Abp2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..527
FT /note="ARS-binding protein 2"
FT /id="PRO_0000064430"
FT REGION 160..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 331
FT /note="R->A: 40-fold decrease in DNA-binding."
FT /evidence="ECO:0000269|PubMed:9488484"
FT MUTAGEN 332
FT /note="G->A: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:9488484"
FT MUTAGEN 333
FT /note="R->A: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:9488484"
FT CONFLICT 260
FT /note="A -> P (in Ref. 1; AAC49930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59629 MW; 2860AE683999B9F4 CRC64;
MNFYSLLPSR HDVSADNITE KFCQFCLCCN PWYAGADTRQ LANAFNMIPK SEGQKFEIWV
LFLLVRQYHQ KIINSWSKLV GFLGVERKDE QSTQKIQQYV VRLKRWMSQT HVDAFFDYLL
NKPNPYYLEI PETQPQVRCN VNVTDDLVIK SLRAGLMSHP DVNSSSISTM RTSTSPSNWI
HSASASLDDN THNLGSFVTN PHADSQECPT PQSLLMRASH HMSERGSQQA HQTTPQNHSL
PHPPNMFEPP DEDHQLPSAA NNSHNHDHAF QTAEAVGVAD SIDPDWHQWP DDLRDVSSPK
ESDGLNDSWS RQTNQVETEN VENEAGVPRK RGRPPGARNK IKRLRSEPSV SLTLSISWYE
RFEKLMHAQN TMLRSAFSHV ARLPMETVSQ LLSHYTETIS QYLPPSETSP IPKTPNFKFI
SSTLLALVSS HSEILEASTD RLIWTVHQGP LTATICHAFN LEKAPSMHSL AEAQMIPDVP
ISHSNSMEPL DTVSSLKLEI AKLNAALKEK NLELENLKRK IMNAVFD
