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UniProtKB/Swiss-Prot entry P49777


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ABP1_SCHPO
Primary accession number P49777
Secondary accession number Q9URU7
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on August 14, 2001 (Sequence version 2)
Annotations were last modified on    May 5, 2009 (Entry version 71)
Name and origin of the protein
Protein name ARS-binding protein 1
Synonyms None
Gene name
Name: abp1
ORFNames: SPBC1105.04c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1073/pnas.93.1.502; PubMed=8552670 [NCBI, ExPASy, EBI, Israel, Japan]
Murakami Y., Huberman J.A., Hurwitz J.;
"Identification, purification, and molecular cloning of autonomously replicating sequence-binding protein 1 from fission yeast Schizosaccharomyces pombe.";
Proc. Natl. Acad. Sci. U.S.A. 93:502-507(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
INTERACTION WITH ABP1.
DOI=10.1186/1747-1028-1-27; PubMed=17112379 [NCBI, ExPASy, EBI, Israel, Japan]
Locovei A.M., Spiga M.-G., Tanaka K., Murakami Y., D'Urso G.;
"The CENP-B homolog, Abp1, interacts with the initiation protein Cdc23 (MCM10) and is required for efficient DNA replication in fission yeast.";
Cell Div. 1:27-27(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U39079; AAB01537.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAB50967.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39281; T39281.
RefSeq NP_596460.1; -.
3D structure databases
PDB
1IUF; NMR; -; A=1-141.[ExPASy / RCSB / EBI]
PDBsum 1IUF; -.
ModBase P49777.
Protein-protein interaction databases
IntAct P49777; 2.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004461-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC1105.04c; -.
Gene expression databases
ArrayExpress P49777; -.
Ontologies
GO
GO:0000780; Cellular component: condensed nuclear chromosome, centromeric region (inferred from direct assay from GeneDB_SPombe).
GO:0000790; Cellular component: nuclear chromatin (inferred by curator from GeneDB_SPombe).
GO:0019237; Molecular function: centromeric DNA binding (inferred from direct assay from GeneDB_SPombe).
GO:0046983; Molecular function: protein dimerization activity (non-traceable author statement from GeneDB_SPombe).
GO:0030702; Biological process: chromatin silencing at centromere (inferred from mutant phenotype from GeneDB_SPombe).
GO:0007059; Biological process: chromosome segregation (inferred from genetic interaction from GeneDB_SPombe).
GO:0006270; Biological process: DNA replication initiation (inferred from genetic interaction from GeneDB_SPombe).
GO:0016570; Biological process: histone modification (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR015175; Centromere_CenpB_DNA-db_2.
IPR006600; Centromere_CenpB_HTH.
IPR004875; DDE_SF_endonuclease_CENPB-like.
IPR012287; Homeodomain-rel.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.60; Homeodomain-rel; 2.
Pfam PF09091; CenpB-DNA-bind; 1.
PF03184; DDE; 1.
Pfam graphical view of domain structure.
SMART SM00674; CENPB; 1.
SMART graphical view of domain structure.
PROSITE PS51253; HTH_CENPB; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 2539971; -.
KEGG spo:SPBC1105.04c; -.
NMPDR fig|4896.1.peg.2326; -.
Phylogenomic databases
OMA P49777; ANTHARM.
Other
ProtoNet P49777.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; DNA-binding; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   522  522     ARS-binding protein 1. PRO_0000126133
DOMAIN   70   144  75     HTH CENPB-type. 
MOD_RES   460   460        Phosphothreonine. 
CONFLICT   336   336        C -> S (in Ref. 1; AAB01537). 
STRAND   5     7  3      
HELIX   12    22  11      
STRAND   23    26  4      
HELIX   30    41  12      
STRAND   46    49  4      
HELIX   52    60  9      
TURN   61    63  3      
STRAND   66    72  7      
HELIX   80    92  13      
HELIX   102   114  13      
STRAND   116   119  4      
HELIX   129   137  9      
Sequence information
Length: 522 AA [This is the length of the unprocessed precursor] Molecular weight: 59840 Da [This is the MW of the unprocessed precursor] CRC64: 8D50078EA9E2233F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGKIKRRAIT EHEKRALRHY FFQLQNRSGQ QDLIEWFREK FGKDISQPSV SQILSSKYSY 

        70         80         90        100        110        120 
LDNTVEKPWD VKRNRPPKYP LLEAALFEWQ VQQGDDATLS GETIKRAAAI LWHKIPEYQD 

       130        140        150        160        170        180 
QPVPNFSNGW LEGFRKRHIL HAINEQPTES VVLNNTEPPN DPLSRVYDVT RLTNINDIFT 

       190        200        210        220        230        240 
MQETGLFWKL VPNGTPEVED IKGITRFKAR ITLTVCCNAS GTERLPLWVI GYSQSPRVFR 

       250        260        270        280        290        300 
AANVKPEVMN FKWRSNGKAS MTTAIMEEWL RWFDACMEGR KVILLIDSYT PHLRAVENIR 

       310        320        330        340        350        360 
NSGNDLRNTT VITLPSTSAS ISQPCSEGVI YALKACYRKH WVQYILEQNE LGRNPYNTTN 

       370        380        390        400        410        420 
VLRAILWLVK AWTTDISPEI IENAFNLSGV LGLFNESAVT SRALDEMIHP LRELVSEFSV 

       430        440        450        460        470        480 
QAAMRIEDFI SPSEENIVDS SEDIINQIAS QYMDDRAFET DEEESTEFQI TTKDAMKAIE 

       490        500        510        520 
LLLNYEAQQP DGNPAITISL LNYQKLLEAR GGNVNLSRLR ST 

P49777 in FASTA format

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