P49777 (ABP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ARS-binding protein 1

Gene names

Name:	abp1
ORF Names:	SPBC1105.04c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds, preferentially, to the Maundrell ARS consensus sequence within ARS3002.
Subunit structure	Interacts with mcm10. Ref.3
Subcellular location	Nucleus.
Sequence similarities	Contains 1 HTH CENPB-type DNA-binding domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA-dependent DNA replication initiation Inferred from mutant phenotype. Source: GeneDB_Spombe chromatin silencing at centromere Inferred from mutant phenotype. Source: GeneDB_Spombe histone modification Inferred from mutant phenotype. Source: GeneDB_Spombe mitotic sister chromatid segregation Inferred from genetic interaction. Source: GeneDB_Spombe
Cellular component	condensed nuclear chromosome, centromeric region Inferred from direct assay. Source: GeneDB_Spombe nuclear chromatin Inferred by curator. Source: GeneDB_Spombe
Molecular function	centromeric DNA binding Inferred from direct assay. Source: GeneDB_Spombe protein dimerization activity Non-traceable author statement. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

ARS-binding protein 1

PRO_0000126133

Regions

Domain

70 – 144

75

HTH CENPB-type

Amino acid modifications

Modified residue

460

1

Phosphothreonine Ref.4

Experimental info

Sequence conflict

336

1

C → S in AAB01537. Ref.1

Secondary structure

1

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522

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Helix

12 – 22

11

Beta strand

23 – 26

4

Helix

30 – 41

12

Beta strand

46 – 49

4

Helix

52 – 60

9

Turn

61 – 63

3

Beta strand

66 – 72

7

Helix

80 – 92

13

Helix

102 – 114

13

Beta strand

116 – 119

4

Helix

129 – 137

9

Sequences

	Sequence		Length	Mass (Da)
	P49777 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 8D50078EA9E2233F	FASTA	522	59,840
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8552670] [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: 11859360] [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: 17112379] [Abstract] Cited for: INTERACTION WITH ABP1.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U39079 Genomic DNA. Translation: AAB01537.1.
CU329671 Genomic DNA. Translation: CAB50967.1.

PIR

T39281.

RefSeq

NP_596460.1. NM_001022379.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IUF	NMR	-	A	1-141	[»]

ProteinModelPortal

P49777.

SMR

P49777. Positions 1-141.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49777. 2 interactions.

STRING

P49777.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

SPBC1105.04c.1; SPBC1105.04c.1:pep; SPBC1105.04c.

GeneID

2539971.

GenomeReviews

Gene locus abp1 in contig CU329671_GR.

KEGG

spo:SPBC1105.04c.

NMPDR

fig|4896.1.peg.2326.

Organism-specific databases

GeneDB_Spombe

SPBC1105.04c.

Phylogenomic databases

eggNOG

fuNOG05144.

GeneTree

EFGT00050000007452.

HOGENOM

HBG207912.

OMA

ANTHARM.

OrthoDB

EOG4DRDN0.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-004461-MONOMER.

Gene expression databases

ArrayExpress

P49777.

Family and domain databases

InterPro

IPR004875. DDE_SF_endonuclease_CENPB-like.
IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR006600. Pogo/CenpB/PDC2_DNA-bd_HTH.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 2 hits.

Pfam

PF03184. DDE_1. 1 hit.
PF03221. HTH_Tnp_Tc5. 1 hit.
[Graphical view]

SMART

SM00674. CENPB. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51253. HTH_CENPB. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ABP1_SCHPO

Accession

Primary (citable) accession number: P49777
Secondary accession number(s): Q9URU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	August 14, 2001
Last modified:	December 14, 2011
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program