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Protein

DNA repair and recombination protein rad22

Gene

rad22

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

Active in the repair of DNA damage and in mating-type switching. Probably involved in the repair of DNA double-strands breaks. Has a role in promoting S phase completion.

GO - Molecular functioni

  • damaged DNA binding Source: PomBase
  • DNA end binding Source: PomBase
  • single-stranded DNA binding Source: PomBase

GO - Biological processi

  • DNA recombinase assembly Source: InterPro
  • double-strand break repair via homologous recombination Source: PomBase
  • double-strand break repair via single-strand annealing Source: InterPro
  • homologous recombination-dependent replication fork processing Source: PomBase
  • mating type switching Source: PomBase
  • mitotic recombination Source: PomBase
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Enzyme and pathway databases

ReactomeiR-SPO-3108214. SUMOylation of DNA damage response and repair proteins.
R-SPO-5685938. HDR through Single Strand Annealing (SSA).

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair and recombination protein rad22
Gene namesi
Name:rad22
ORF Names:SPAC30D11.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC30D11.10.
PomBaseiSPAC30D11.10.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
  • site of double-strand break Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469DNA repair and recombination protein rad22PRO_0000173891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961Phosphoserine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36592.

PTM databases

iPTMnetiP36592.

Interactioni

Subunit structurei

Interacts with rhp51.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
pmt3O133514EBI-966242,EBI-966336
rhp51P366014EBI-966242,EBI-926960
ssb1Q923722EBI-966242,EBI-966394

Protein-protein interaction databases

BioGridi279519. 51 interactions.
IntActiP36592. 5 interactions.
MINTiMINT-239306.

Structurei

3D structure databases

ProteinModelPortaliP36592.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RAD52 family.Curated

Phylogenomic databases

InParanoidiP36592.
KOiK10873.
OrthoDBiEOG7F7WMJ.
PhylomeDBiP36592.

Family and domain databases

InterProiIPR004585. DNA_recomb/repair_Rad52.
IPR007232. Rad52_Rad59_Rad22.
[Graphical view]
PANTHERiPTHR12132. PTHR12132. 1 hit.
PTHR12132:SF1. PTHR12132:SF1. 1 hit.
PfamiPF04098. Rad52_Rad22. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00607. rad52. 1 hit.

Sequencei

Sequence statusi: Complete.

P36592-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFEQKQHVA SEDQGHFNTA YSHEEFNFLQ SSLTRKLGPE YVSRRSGPGG
60 70 80 90 100
FSVSYIESWK AIELANEIFG FNGWSSSIRS INVDFMDENK ENGRISLGLS
110 120 130 140 150
VIVRVTIKDG AYHEDIGYGS IDNCRGKASA FEKCKKEGTT DALKRALRNF
160 170 180 190 200
GNSLGNCMYD KYYLREVGKM KPPTYHFDSG DLFRKTDPAA RESFIKKQKT
210 220 230 240 250
LNSTRTVNNQ PLVNKGEQLA PRRAAELNDE QTREIEMYAD EELDNIFVED
260 270 280 290 300
DIIAHLAVAE DTAHPAANNH HSEKAGTQIN NKDKGSHNSA KPVQRSHTYP
310 320 330 340 350
VAVPQNTSDS VGNAVTDTSP KTLFDPLKPN TGTPSPKFIS ARAAAAAEGV
360 370 380 390 400
VSAPFTNNFN PRLDSPSIRK TSIIDHSKSL PVQRASVLPI IKQSSQTSPV
410 420 430 440 450
SNNSMIRDSE SIINERKENI GLIGVKRSLH DSTTSHNKSD LMRTNSDPQS
460
AMRSRENYDA TVDKKAKKG
Length:469
Mass (Da):51,961
Last modified:February 1, 1996 - v2
Checksum:iE6B8B538D28B899D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341T → S in CAA51021 (PubMed:8290356).Curated
Sequence conflicti84 – 841D → E in CAA51021 (PubMed:8290356).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72220 Genomic DNA. Translation: CAA51021.1.
CU329670 Genomic DNA. Translation: CAA91896.1.
PIRiS41496.
RefSeqiNP_593207.1. NM_001018603.2.

Genome annotation databases

EnsemblFungiiSPAC30D11.10.1; SPAC30D11.10.1:pep; SPAC30D11.10.
GeneIDi2543086.
KEGGispo:SPAC30D11.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72220 Genomic DNA. Translation: CAA51021.1.
CU329670 Genomic DNA. Translation: CAA91896.1.
PIRiS41496.
RefSeqiNP_593207.1. NM_001018603.2.

3D structure databases

ProteinModelPortaliP36592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279519. 51 interactions.
IntActiP36592. 5 interactions.
MINTiMINT-239306.

PTM databases

iPTMnetiP36592.

Proteomic databases

MaxQBiP36592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC30D11.10.1; SPAC30D11.10.1:pep; SPAC30D11.10.
GeneIDi2543086.
KEGGispo:SPAC30D11.10.

Organism-specific databases

EuPathDBiFungiDB:SPAC30D11.10.
PomBaseiSPAC30D11.10.

Phylogenomic databases

InParanoidiP36592.
KOiK10873.
OrthoDBiEOG7F7WMJ.
PhylomeDBiP36592.

Enzyme and pathway databases

ReactomeiR-SPO-3108214. SUMOylation of DNA damage response and repair proteins.
R-SPO-5685938. HDR through Single Strand Annealing (SSA).

Miscellaneous databases

NextBioi20804114.
PROiP36592.

Family and domain databases

InterProiIPR004585. DNA_recomb/repair_Rad52.
IPR007232. Rad52_Rad59_Rad22.
[Graphical view]
PANTHERiPTHR12132. PTHR12132. 1 hit.
PTHR12132:SF1. PTHR12132:SF1. 1 hit.
PfamiPF04098. Rad52_Rad22. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00607. rad52. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The fission yeast rad22 gene, having a function in mating-type switching and repair of DNA damages, encodes a protein homolog to Rad52 of Saccharomyces cerevisiae."
    Ostermann K., Lorentz A., Schmidt H.
    Nucleic Acids Res. 21:5940-5944(1993) [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. "Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair meiotic double-strand breaks."
    Catlett M.G., Forsburg S.L.
    Mol. Biol. Cell 14:4707-4720(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHP51.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-319, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRAD22_SCHPO
AccessioniPrimary (citable) accession number: P36592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 118 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.