Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribosome-associated molecular chaperone SSB1

Gene

SSB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.8 Publications

Miscellaneous

Present with 170000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM potassium acetate) and 0.81 min(-1) with ATP as substrate (at 100 mM potassium acetate).1 Publication
  1. KM=270 µM for ATP (at 2.5 mM potassium acetate)1 Publication
  2. KM=147 µM for ATP (at 100 mM potassium acetate)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei73ATPBy similarity1
    Binding sitei342ATP; via amide nitrogenBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi16 – 18ATPBy similarity3
    Nucleotide bindingi205 – 207ATPBy similarity3
    Nucleotide bindingi271 – 278ATPBy similarity8

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • ATPase activity Source: SGD
    • ATPase activity, coupled Source: GO_Central
    • ATP binding Source: GO_Central
    • calmodulin binding Source: SGD
    • heat shock protein binding Source: GO_Central
    • misfolded protein binding Source: GO_Central
    • protein binding involved in protein folding Source: GO_Central
    • unfolded protein binding Source: SGD

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionChaperone, Hydrolase
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:G3O-29608-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-3371453 Regulation of HSF1-mediated heat shock response

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Ribosome-associated molecular chaperone SSB11 Publication (EC:3.6.4.101 Publication)
    Alternative name(s):
    Cold-inducible protein YG1011 Publication
    Heat shock protein SSB11 Publication
    Hsp70 chaperone Ssb1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:SSB11 Publication
    Synonyms:YG1011 Publication
    Ordered Locus Names:YDL229WImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000002388 SSB1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi73K → A: Unable to hydrolyze ATP and moderately reduces ribosome binding. 1 Publication1
    Mutagenesisi567 – 568KR → EE in SSB1-L(BC): Reduces ribosome-binding to less than 50%. 1 Publication2
    Mutagenesisi596 – 597RK → DD in SSB1-D1: Reduces ribosome-binding to less than 50%. 1 Publication2
    Mutagenesisi603 – 604KR → DD in SSB1-D2: Reduces ribosome-binding to less than 50%. 1 Publication2

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000783892 – 613Ribosome-associated molecular chaperone SSB1Add BLAST612

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanine1 Publication1
    Modified residuei47PhosphothreonineCombined sources1
    Modified residuei431PhosphothreonineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P11484

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P11484

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11484

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    P11484

    2D gel databases

    2-DE database at Universidad Complutense de Madrid

    More...
    COMPLUYEAST-2DPAGEi
    P11484

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P11484

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P11484

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P11484

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P11484

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression decreases after heat shock or during growth to stationary phase (PubMed:6761581, PubMed:2651414). Degraded during heat shock treatment (at protein level) (PubMed:7646503). Up-regulated upon carbon upshift and down-regulated upon amino acid limitation in an HSF1-dependent manner (PubMed:10322015).4 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Binds to ribosomes (PubMed:9670014, PubMed:1394434, PubMed:27917864). Binds close to the ribosomal tunnel exit via contacts with both ribosomal proteins RPL35, RPL39 and RPL19, and rRNA (PubMed:27882919). Directly interacts with nascent polypeptides. This interaction is dependent on the ribosome-associated complex (RAC) (PubMed:11929994, PubMed:23332755). Interacts with SSE1 (PubMed:16219770, PubMed:16221677, PubMed:23332755). Interacts with FES1 (PubMed:17132105). Interacts with NAP1 (PubMed:18086883).10 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    31882, 803 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-2254N

    Protein interaction database and analysis system

    More...
    IntActi
    P11484, 777 interactors

    Molecular INTeraction database

    More...
    MINTi
    P11484

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YDL229W

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1613
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3GL1X-ray1.92A/B1-384[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P11484

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P11484

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P11484

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 391Nucleotide binding domain (NBD)By similarityAdd BLAST390
    Regioni392 – 402Inter-domain linkerBy similarityAdd BLAST11
    Regioni403 – 613Substrate binding domain (SBD)By similarityAdd BLAST211
    Regioni516 – 612Lid domain (SBDalpha)By similarityAdd BLAST97
    Regioni601 – 613Required for interaction with ribosomes1 PublicationAdd BLAST13

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi428 – 430Contributes to ribosome binding1 Publication3
    Motifi574 – 582Nuclear export signal1 Publication9

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000154813

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000228135

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P11484

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DFSARHE

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.20.1270.10, 1 hit
    2.60.34.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR018181 Heat_shock_70_CS
    IPR029048 HSP70_C_sf
    IPR029047 HSP70_peptide-bd_sf
    IPR013126 Hsp_70_fam

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR19375 PTHR19375, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00012 HSP70, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00301 HEATSHOCK70

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF100920 SSF100920, 1 hit
    SSF100934 SSF100934, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00297 HSP70_1, 1 hit
    PS00329 HSP70_2, 1 hit
    PS01036 HSP70_3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P11484-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE
    60 70 80 90 100
    RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD
    110 120 130 140 150
    GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA
    160 170 180 190 200
    YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI
    210 220 230 240 250
    FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK
    260 270 280 290 300
    KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
    310 320 330 340 350
    TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ
    360 370 380 390 400
    KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV
    410 420 430 440 450
    APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE
    460 470 480 490 500
    RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG
    510 520 530 540 550
    KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV
    560 570 580 590 600
    ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
    610
    GLKRVVTKAM SSR
    Length:613
    Mass (Da):66,602
    Last modified:January 23, 2007 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF16FA7C25A40321A
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti180 – 184AAAIA → VVVIV in AAA34692 (PubMed:6761581).Curated5
    Sequence conflicti189A → V in AAA34692 (PubMed:6761581).Curated1
    Sequence conflicti192S → F in AAA34692 (PubMed:6761581).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X13713 Genomic DNA Translation: CAA31995.1
    M25395 mRNA Translation: AAA35099.1
    Z74277 Genomic DNA Translation: CAA98807.1
    M17585 Genomic DNA Translation: AAA34692.1
    BK006938 Genomic DNA Translation: DAA11637.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S20149

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_010052.1, NM_001180289.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YDL229W_mRNA; YDL229W_mRNA; YDL229W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    851369

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YDL229W

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13713 Genomic DNA Translation: CAA31995.1
    M25395 mRNA Translation: AAA35099.1
    Z74277 Genomic DNA Translation: CAA98807.1
    M17585 Genomic DNA Translation: AAA34692.1
    BK006938 Genomic DNA Translation: DAA11637.1
    PIRiS20149
    RefSeqiNP_010052.1, NM_001180289.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3GL1X-ray1.92A/B1-384[»]
    ProteinModelPortaliP11484
    SMRiP11484
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31882, 803 interactors
    DIPiDIP-2254N
    IntActiP11484, 777 interactors
    MINTiP11484
    STRINGi4932.YDL229W

    PTM databases

    CarbonylDBiP11484
    iPTMnetiP11484

    2D gel databases

    COMPLUYEAST-2DPAGEiP11484
    SWISS-2DPAGEiP11484
    UCD-2DPAGEiP11484

    Proteomic databases

    MaxQBiP11484
    PaxDbiP11484
    PRIDEiP11484
    TopDownProteomicsiP11484

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDL229W_mRNA; YDL229W_mRNA; YDL229W
    GeneIDi851369
    KEGGisce:YDL229W

    Organism-specific databases

    SGDiS000002388 SSB1

    Phylogenomic databases

    GeneTreeiENSGT00940000154813
    HOGENOMiHOG000228135
    InParanoidiP11484
    OMAiDFSARHE

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29608-MONOMER
    ReactomeiR-SCE-3371453 Regulation of HSF1-mediated heat shock response

    Miscellaneous databases

    EvolutionaryTraceiP11484

    Protein Ontology

    More...
    PROi
    PR:P11484

    Family and domain databases

    Gene3Di1.20.1270.10, 1 hit
    2.60.34.10, 1 hit
    InterProiView protein in InterPro
    IPR018181 Heat_shock_70_CS
    IPR029048 HSP70_C_sf
    IPR029047 HSP70_peptide-bd_sf
    IPR013126 Hsp_70_fam
    PANTHERiPTHR19375 PTHR19375, 1 hit
    PfamiView protein in Pfam
    PF00012 HSP70, 1 hit
    PRINTSiPR00301 HEATSHOCK70
    SUPFAMiSSF100920 SSF100920, 1 hit
    SSF100934 SSF100934, 1 hit
    PROSITEiView protein in PROSITE
    PS00297 HSP70_1, 1 hit
    PS00329 HSP70_2, 1 hit
    PS01036 HSP70_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSSB1_YEAST
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11484
    Secondary accession number(s): D6VRC7, Q05834
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: January 16, 2019
    This is version 191 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again