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Reviewed, UniProtKB/Swiss-Prot O13919 (PST2_SCHPO)

Last modified September 22, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Paired amphipathic helix protein pst2
Alternative name(s):
    SIN3 homolog 2
Gene names
Name: pst2
ORF Names: SPAC23C11.15
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1075 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones. Ref.3

Subunit structure

Heterotetramer of alp13, clr6, prw1 and pst2. Ref.3

Subcellular location

Nucleus. Ref.3

Sequence similarities

Contains 3 PAH (paired amphipathic helix) repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   Molecular functionChromatin regulator
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processchromatin remodeling

Inferred by curator. Source: GeneDB_SPombe

chromosome condensation Ref.3

Inferred from mutant phenotype. Source: GeneDB_SPombe

histone deacetylation Ref.3

Inferred from mutant phenotype. Source: GeneDB_SPombe

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentRpd3S complex Ref.3

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionprotein binding Ref.3

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10751075Paired amphipathic helix protein pst2
PRO_0000121542

Regions

Repeat54 – 10047PAH 1
Repeat160 – 20647PAH 2
Repeat271 – 31747PAH 3

Amino acid modifications

Modified residue6411Phosphoserine Ref.4
Modified residue6431Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O13919-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1AD301DB4EB1AFFB

FASTA1,075124,849
        10         20         30         40         50         60 
MEQTLAILKN DNSTLVAEMQ NQLVHDFSPN GTALPELDIK AFVQKLGQRL CHRPYVYSAF 

        70         80         90        100        110        120 
MDVVKALHNE IVDFPGFIER ISVILRDYPD LLEYLNIFLP SSYKYLLSNS GANFTLQFTT 

       130        140        150        160        170        180 
PSGPVSTPST YVATYNDLPC TYHRAIGFVS RVRRALLSNP EQFFKLQDSL RKFKNSECSL 

       190        200        210        220        230        240 
SELQTIVTSL LAEHPSLAHE FHNFLPSSIF FGSKPPLGSF PLRGIQSSQF TLSNISDLLS 

       250        260        270        280        290        300 
QSRPDNLSPF SHLSNESSDF FKNVKNVLTD VETYHEFLKL LNLYVQGIID RNILVSRGFG 

       310        320        330        340        350        360 
FLKSNSGLWR SFLSLTSLSP EEFLSVYNSA CSDFPECGPS YRLLPVEERN ISCSGRDDFA 

       370        380        390        400        410        420 
WGILNDDWVS HPTWASEESG FIVQRKTPYE EAMTKLEEER YEFDRHIEAT SWTIKSLKKI 

       430        440        450        460        470        480 
QNRINELPEE ERETYTLEEG LGLPSKSIYK KTIKLVYTSE HAEEMFKALE RMPCLTLPLV 

       490        500        510        520        530        540 
ISRLEEKNEE WKSVKRSLQP GWRSIEFKNY DKSLDSQCVY FKARDKKNVS SKFLLAEADI 

       550        560        570        580        590        600 
LRSQAKLHFP LRSRSAFEFS FVYDNEIVLF DTCYMVCTYI VCNSPSGLKK VEHFFKNILP 

       610        620        630        640        650        660 
LHFGLEKDKF SIFLDQVFRG PDYDVNAPNI VGNKPVRRKR SNSITQLTEF VKQPKINGQR 

       670        680        690        700        710        720 
ESRSAAAARK KEESGNKSQS NSQNSLSDES GNVTPVSKKQ LSQPAAAIKA SLKYPSHPDS 

       730        740        750        760        770        780 
LLEHQDHAGD TENEMHDDVD KEQFGYSSMY VFFRLFNLLY ERLYELQRLE DQVSIIQQRI 

       790        800        810        820        830        840 
IPNPVSQKQK IWRDRWNDLS DVPDEKTHYE NTYVMILRLI YGIVDQSAFE DYLRFYYGNK 

       850        860        870        880        890        900 
AYKIYTIDKL VWSAAKQVHH IVSDGKYKFV TSLVEQNSSA SPKKNYDDFL YRLEIEKLLN 

       910        920        930        940        950        960 
PDEILFRFCW INKFKSFGIK IMKRANLIVD QSLDTQRRVW KKYVQNYRIQ KLTEEISYKN 

       970        980        990       1000       1010       1020 
YRCPFLCRNI EKERTVEQLV SRLQTKLLRS AELVSGLQAK LCLDSFKLLY LPRTEDSYID 

      1030       1040       1050       1060       1070 
ASYLRLRDTD FLDCQNKRKQ RWRNRWESLL KSVRGTSDNT AEVNFDADIN ALFIP 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: ATCC 38366 / 972.
[2]"A new member of the Sin3 family of corepressors is essential for cell viability and required for retroelement propagation in fission yeast."
Dang V.D., Benedik M.J., Ekwall K., Choi J., Allshire R.C., Levin H.L.
Mol. Cell. Biol. 19:2351-2365(1999) [PubMed: 10022921] [Abstract]
Cited for: GENE NAME.
[3]"Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity."
Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K., Kobayashi R., Grewal S.I.S.
EMBO J. 22:2776-2787(2003) [PubMed: 12773392] [Abstract]
Cited for: PROTEIN SEQUENCE OF 87-104; 280-291; 386-395; 424-446; 608-637; 678-709; 780-788; 819-834; 869-883; 925-937 AND 1055-1075, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[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 SER-641 AND SER-643, MASS SPECTROMETRY.

Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAB11171.1.
PIRT38253.
RefSeqNP_593646.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO13919. 3 interactions.
STRINGO13919.

Genome annotation databases

GeneID2541624.
GenomeReviewsGene locus pst2 in contig CU329670_GR.
KEGGspo:SPAC23C11.15.
NMPDRfig|4896.1.peg.3616.

Organism-specific databases

GeneDB_SpombeSPAC23C11.15.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001315-MON.

Gene expression databases

ArrayExpressO13919.

Family and domain databases

InterProIPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]
Gene3DG3DSA:1.20.1160.11. PAH. 2 hits.
PfamPF08295. HDAC_interact. 1 hit.
PF02671. PAH. 3 hits.
[Graphical view]
SMARTSM00761. HDAC_interact. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePST2_SCHPO
AccessionPrimary (citable) accession number: O13919
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: September 22, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents