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Protein

Probable heat shock protein ssa2

Gene

ssa2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • chaperone-mediated protein folding Source: PomBase
  • negative regulation of cellular response to heat Source: PomBase
  • protein folding Source: PomBase
  • protein refolding Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-3371453. Regulation of HSF1-mediated heat shock response.
R-SPO-3371568. Attenuation phase.
R-SPO-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable heat shock protein ssa2
Gene namesi
Name:ssa2
ORF Names:SPCC1739.13
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1739.13.
PomBaseiSPCC1739.13. ssa2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 647646Probable heat shock protein ssa2PRO_0000078380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei36 – 361Phosphothreonine1 Publication
Modified residuei339 – 3391Phosphothreonine1 Publication
Modified residuei417 – 4171Phosphothreonine1 Publication
Modified residuei546 – 5461Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO59855.
PRIDEiO59855.

PTM databases

iPTMnetiO59855.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi275795. 14 interactions.
IntActiO59855. 3 interactions.
MINTiMINT-4676637.

Structurei

3D structure databases

ProteinModelPortaliO59855.
SMRiO59855. Positions 4-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

HOGENOMiHOG000228135.
InParanoidiO59855.
KOiK03283.
OMAiKESSRIG.
OrthoDBiEOG728916.
PhylomeDBiO59855.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59855-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSIGIDLG TTYSCVGHFS NNRVEIIAND QGNRTTPSYV AFTDTERLIG
60 70 80 90 100
DAAKNQVAMN PHNTIFDAKR LIGRKFDDPE VQSDMKHWPF KVISKDGKPV
110 120 130 140 150
LQVEYKGETK TFTPEEISSM VLMKMRETAE AYLGGKVTDA VVTVPAYFND
160 170 180 190 200
SQRQATKDAG LIAGLNVLRI INEPTAAAIA YGLDRSNQGE SNVLIFDLGG
210 220 230 240 250
GTFDVSLLTI EEGIFEVKAT AGDTHLGGED FDSRLVNHFI QEFKRKNKKD
260 270 280 290 300
ITGNARAVRR LRTACERAKR TLSSSAQASI EIDSLFEGID FYTSITRARF
310 320 330 340 350
EELCADLFRK TMEPVERVLR DSKVDKASVN EIVLVGGSTR IPRVQKLVSD
360 370 380 390 400
FFNGKEPCKS INPDEAVAYG AAVQAAVLTG DTSEKTQDLL LLDVAPLSMG
410 420 430 440 450
IETAGGVMTP LIKRNTTIPT KKSEIFSTYS DNQPGVLIQV FEGERARTKD
460 470 480 490 500
CNLLGKFELS GIPPAPRGVP QIEVTFDVDA NGILNVSALE KGTGKTQKIT
510 520 530 540 550
ITNDKGRLSK EEIDRMVAEA EKYKAEDEAE SGRIQAKNHL ESYAYSLRNS
560 570 580 590 600
LDDPNLKDKV DASDKETVDK AVKETIEWLD SNTTAAKDEF EAKQKELESV
610 620 630 640
ANPIMAKIYQ AGGAPGGMPG AAPGAAPGAA PGAAPGGDNG PEVEEVD
Length:647
Mass (Da):70,233
Last modified:January 23, 2007 - v3
Checksum:i02CAFB9E80516362
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012387 mRNA. Translation: BAA25322.1.
CU329672 Genomic DNA. Translation: CAA20787.1.
PIRiT41121.
RefSeqiNP_588421.1. NM_001023412.2.

Genome annotation databases

EnsemblFungiiSPCC1739.13.1; SPCC1739.13.1:pep; SPCC1739.13.
GeneIDi2539225.
KEGGispo:SPCC1739.13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012387 mRNA. Translation: BAA25322.1.
CU329672 Genomic DNA. Translation: CAA20787.1.
PIRiT41121.
RefSeqiNP_588421.1. NM_001023412.2.

3D structure databases

ProteinModelPortaliO59855.
SMRiO59855. Positions 4-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275795. 14 interactions.
IntActiO59855. 3 interactions.
MINTiMINT-4676637.

PTM databases

iPTMnetiO59855.

Proteomic databases

MaxQBiO59855.
PRIDEiO59855.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1739.13.1; SPCC1739.13.1:pep; SPCC1739.13.
GeneIDi2539225.
KEGGispo:SPCC1739.13.

Organism-specific databases

EuPathDBiFungiDB:SPCC1739.13.
PomBaseiSPCC1739.13. ssa2.

Phylogenomic databases

HOGENOMiHOG000228135.
InParanoidiO59855.
KOiK03283.
OMAiKESSRIG.
OrthoDBiEOG728916.
PhylomeDBiO59855.

Enzyme and pathway databases

ReactomeiR-SPO-3371453. Regulation of HSF1-mediated heat shock response.
R-SPO-3371568. Attenuation phase.
R-SPO-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiO59855.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S.pombe heat shock protein of HSP70 family."
    Kawamukai M.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36; THR-339; THR-417 AND SER-546, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiHSP72_SCHPO
AccessioniPrimary (citable) accession number: O59855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 115 of the entry and version 3 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.