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Protein

ARS-binding protein 1

Gene

abp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds, preferentially, to the Maundrell ARS consensus sequence within ARS3002.

GO - Molecular functioni

  • centromeric DNA binding Source: PomBase
  • sequence-specific DNA binding Source: PomBase

GO - Biological processi

  • chromatin silencing at centromere Source: PomBase
  • donor selection Source: PomBase
  • mitotic sister chromatid segregation Source: PomBase
  • protein localization to mating-type region heterochromatin Source: PomBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ARS-binding protein 1
Gene namesi
Name:abp1
ORF Names:SPBC1105.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1105.04c.
PomBaseiSPBC1105.04c.

Subcellular locationi

GO - Cellular componenti

  • condensed nuclear chromosome, centromeric region Source: PomBase
  • mating-type region heterochromatin Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522ARS-binding protein 1PRO_0000126133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei460 – 4601Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49777.

PTM databases

iPTMnetiP49777.

Interactioni

Subunit structurei

Interacts with mcm10.1 Publication

Protein-protein interaction databases

BioGridi276515. 128 interactions.
IntActiP49777. 2 interactions.
MINTiMINT-4690563.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi12 – 2211Combined sources
Beta strandi23 – 264Combined sources
Helixi30 – 4112Combined sources
Beta strandi46 – 494Combined sources
Helixi52 – 609Combined sources
Turni61 – 633Combined sources
Beta strandi66 – 727Combined sources
Helixi80 – 9213Combined sources
Helixi102 – 11413Combined sources
Beta strandi116 – 1194Combined sources
Helixi129 – 1379Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IUFNMR-A1-141[»]
ProteinModelPortaliP49777.
SMRiP49777. Positions 1-141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49777.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 14475HTH CENPB-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH CENPB-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000033772.
InParanoidiP49777.
OMAiIFTHAFR.
OrthoDBiEOG7N905B.
PhylomeDBiP49777.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR004875. DDE_SF_endonuclease_dom.
IPR009057. Homeodomain-like.
IPR006600. HTH_CenpB_DNA-bd_dom.
[Graphical view]
PfamiPF03184. DDE_1. 1 hit.
PF03221. HTH_Tnp_Tc5. 1 hit.
[Graphical view]
SMARTiSM00674. CENPB. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51253. HTH_CENPB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKIKRRAIT EHEKRALRHY FFQLQNRSGQ QDLIEWFREK FGKDISQPSV
60 70 80 90 100
SQILSSKYSY LDNTVEKPWD VKRNRPPKYP LLEAALFEWQ VQQGDDATLS
110 120 130 140 150
GETIKRAAAI LWHKIPEYQD QPVPNFSNGW LEGFRKRHIL HAINEQPTES
160 170 180 190 200
VVLNNTEPPN DPLSRVYDVT RLTNINDIFT MQETGLFWKL VPNGTPEVED
210 220 230 240 250
IKGITRFKAR ITLTVCCNAS GTERLPLWVI GYSQSPRVFR AANVKPEVMN
260 270 280 290 300
FKWRSNGKAS MTTAIMEEWL RWFDACMEGR KVILLIDSYT PHLRAVENIR
310 320 330 340 350
NSGNDLRNTT VITLPSTSAS ISQPCSEGVI YALKACYRKH WVQYILEQNE
360 370 380 390 400
LGRNPYNTTN VLRAILWLVK AWTTDISPEI IENAFNLSGV LGLFNESAVT
410 420 430 440 450
SRALDEMIHP LRELVSEFSV QAAMRIEDFI SPSEENIVDS SEDIINQIAS
460 470 480 490 500
QYMDDRAFET DEEESTEFQI TTKDAMKAIE LLLNYEAQQP DGNPAITISL
510 520
LNYQKLLEAR GGNVNLSRLR ST
Length:522
Mass (Da):59,840
Last modified:August 14, 2001 - v2
Checksum:i8D50078EA9E2233F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361C → S in AAB01537 (PubMed:8552670).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39079 Genomic DNA. Translation: AAB01537.1.
CU329671 Genomic DNA. Translation: CAB50967.1.
PIRiT39281.
RefSeqiNP_596460.1. NM_001022379.2.

Genome annotation databases

EnsemblFungiiSPBC1105.04c.1; SPBC1105.04c.1:pep; SPBC1105.04c.
GeneIDi2539971.
KEGGispo:SPBC1105.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39079 Genomic DNA. Translation: AAB01537.1.
CU329671 Genomic DNA. Translation: CAB50967.1.
PIRiT39281.
RefSeqiNP_596460.1. NM_001022379.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IUFNMR-A1-141[»]
ProteinModelPortaliP49777.
SMRiP49777. Positions 1-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276515. 128 interactions.
IntActiP49777. 2 interactions.
MINTiMINT-4690563.

PTM databases

iPTMnetiP49777.

Proteomic databases

MaxQBiP49777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1105.04c.1; SPBC1105.04c.1:pep; SPBC1105.04c.
GeneIDi2539971.
KEGGispo:SPBC1105.04c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1105.04c.
PomBaseiSPBC1105.04c.

Phylogenomic databases

HOGENOMiHOG000033772.
InParanoidiP49777.
OMAiIFTHAFR.
OrthoDBiEOG7N905B.
PhylomeDBiP49777.

Miscellaneous databases

EvolutionaryTraceiP49777.
PROiP49777.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR004875. DDE_SF_endonuclease_dom.
IPR009057. Homeodomain-like.
IPR006600. HTH_CenpB_DNA-bd_dom.
[Graphical view]
PfamiPF03184. DDE_1. 1 hit.
PF03221. HTH_Tnp_Tc5. 1 hit.
[Graphical view]
SMARTiSM00674. CENPB. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51253. HTH_CENPB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, purification, and molecular cloning of autonomously replicating sequence-binding protein 1 from fission yeast Schizosaccharomyces pombe."
    Murakami Y., Huberman J.A., Hurwitz J.
    Proc. Natl. Acad. Sci. U.S.A. 93:502-507(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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.
    , 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.
  3. "The CENP-B homolog, Abp1, interacts with the initiation protein Cdc23 (MCM10) and is required for efficient DNA replication in fission yeast."
    Locovei A.M., Spiga M.-G., Tanaka K., Murakami Y., D'Urso G.
    Cell Div. 1:27-27(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABP1.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiABP1_SCHPO
AccessioniPrimary (citable) accession number: P49777
Secondary accession number(s): Q9URU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 14, 2001
Last modified: June 8, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.