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Protein

Transcription factor prr1

Gene

prr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in oxidative stress. Transcription factor that acts upon trr1 and ctt1.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi7 – 111105By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • positive regulation of transcription from RNA polymerase II promoter Source: GOC
  • regulation of cellular response to oxidative stress by regulation of transcription from RNA polymerase II promoter Source: PomBase
  • regulation of conjugation with cellular fusion by regulation of transcription from RNA polymerase II promoter Source: PomBase
  • response to stress Source: InterPro
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor prr1
Alternative name(s):
Pombe response regulator 1
Gene namesi
Name:prr1
ORF Names:SPAC8C9.14
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC8C9.14.
PomBaseiSPAC8C9.14. prr1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Transcription factor prr1PRO_0000124594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei221 – 2211Phosphothreonine1 Publication
Modified residuei223 – 2231Phosphoserine1 Publication
Modified residuei418 – 41814-aspartylphosphatePROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14283.

PTM databases

iPTMnetiO14283.

Interactioni

Protein-protein interaction databases

BioGridi278250. 11 interactions.
MINTiMINT-4671965.

Structurei

3D structure databases

ProteinModelPortaliO14283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 483115Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the HSF family.Curated
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO14283.
KOiK15859.
OMAiNWQSPGQ.
OrthoDBiEOG7ZKSNN.
PhylomeDBiO14283.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR014402. Sig_transdc_resp-reg_Skn7.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFiPIRSF002595. RR_SKN7. 1 hit.
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSSNGSSDF VRKLFNMLEE PEYRHILRWS DSGDSFIVLD TNEFTKTILP
60 70 80 90 100
RHFKHSNFAS FVRQLNKYDF HKVRHEEGAP SIYGEGAWEF RHDDFQLHHK
110 120 130 140 150
DLLDNIKRKA PSKRNLANEN TAPVIENLKQ QVDSILDFQK LLDRNLSGLA
160 170 180 190 200
TSYQTILLKM FELKRGIESR DLLMSSIISY LCDLEGSTQR QANPGAMFVP
210 220 230 240 250
SHPLQELLNA YQALAKGQVA TTSPQQIPNQ IQQASAATTA SSKMTVDTNL
260 270 280 290 300
GTAQPSLYNT PSSDYELANQ EKPADSMASA ASLNTPLSSN DHSLNPHAHG
310 320 330 340 350
SYPMYEKFQP IQHPNPGSFT THLDSNASMA KSFSQISNDS LAKASSVATS
360 370 380 390 400
MSQMGAAVPT TGLWKRQPRI LLVEDDELSR RMTIKFLTSF DCQVDVAVDG
410 420 430 440 450
IGAVNKANAG GFDLILMDFI LPNLDGLSVT CLIRQYDHNT PILAITSNIS
460 470 480 490 500
MNDAVTYFNH GVTDLLVKPF TKLTLLQLLK KQLLNLLQAD NSINMSDVPS
510 520 530
TKEAKDDKAP VTFYLENDAP MYPQQMLQDP IQADLQHPH
Length:539
Mass (Da):60,046
Last modified:January 1, 1999 - v2
Checksum:iF3B4945C595B2871
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041768 mRNA. Translation: BAB16722.1.
CU329670 Genomic DNA. Translation: CAB16301.1.
AB027943 Genomic DNA. Translation: BAA87247.1.
PIRiT39150.
RefSeqiNP_594284.1. NM_001019707.2.

Genome annotation databases

EnsemblFungiiSPAC8C9.14.1; SPAC8C9.14.1:pep; SPAC8C9.14.
GeneIDi2541756.
KEGGispo:SPAC8C9.14.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041768 mRNA. Translation: BAB16722.1.
CU329670 Genomic DNA. Translation: CAB16301.1.
AB027943 Genomic DNA. Translation: BAA87247.1.
PIRiT39150.
RefSeqiNP_594284.1. NM_001019707.2.

3D structure databases

ProteinModelPortaliO14283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278250. 11 interactions.
MINTiMINT-4671965.

PTM databases

iPTMnetiO14283.

Proteomic databases

MaxQBiO14283.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC8C9.14.1; SPAC8C9.14.1:pep; SPAC8C9.14.
GeneIDi2541756.
KEGGispo:SPAC8C9.14.

Organism-specific databases

EuPathDBiFungiDB:SPAC8C9.14.
PomBaseiSPAC8C9.14. prr1.

Phylogenomic databases

InParanoidiO14283.
KOiK15859.
OMAiNWQSPGQ.
OrthoDBiEOG7ZKSNN.
PhylomeDBiO14283.

Miscellaneous databases

PROiO14283.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR000232. HSF_DNA-bd.
IPR027725. HSF_fam.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR014402. Sig_transdc_resp-reg_Skn7.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10015. PTHR10015. 2 hits.
PfamiPF00447. HSF_DNA-bind. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PIRSFiPIRSF002595. RR_SKN7. 1 hit.
PRINTSiPR00056. HSFDOMAIN.
SMARTiSM00415. HSF. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS00434. HSF_DOMAIN. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A fission yeast gene (prr1(+)) that encodes a response regulator implicated in oxidative stress response."
    Ohmiya R., Kato C., Yamada H., Aiba H., Mizuno T.
    J. Biochem. 125:1061-1066(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  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. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 224-413.
    Strain: ATCC 38364 / 968.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPRR1_SCHPO
AccessioniPrimary (citable) accession number: O14283
Secondary accession number(s): Q9UTX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: January 1, 1999
Last modified: June 8, 2016
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.