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O43765

- SGTA_HUMAN

UniProt

O43765 - SGTA_HUMAN

Protein

Small glutamine-rich tetratricopeptide repeat-containing protein alpha

Gene

SGTA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Host-virus interaction

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small glutamine-rich tetratricopeptide repeat-containing protein alpha
    Alternative name(s):
    Alpha-SGT
    Vpu-binding protein
    Short name:
    UBP
    Gene namesi
    Name:SGTA
    Synonyms:SGT, SGT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10819. SGTA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35727.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Small glutamine-rich tetratricopeptide repeat-containing protein alphaPRO_0000106365Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphoserine2 Publications
    Modified residuei81 – 811Phosphothreonine2 Publications
    Modified residuei137 – 1371N6-acetyllysine1 Publication
    Modified residuei301 – 3011Phosphoserine2 Publications
    Modified residuei303 – 3031Phosphothreonine2 Publications
    Modified residuei305 – 3051Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43765.
    PaxDbiO43765.
    PeptideAtlasiO43765.
    PRIDEiO43765.

    PTM databases

    PhosphoSiteiO43765.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO43765.
    BgeeiO43765.
    CleanExiHS_SGTA.
    GenevestigatoriO43765.

    Organism-specific databases

    HPAiHPA056309.

    Interactioni

    Subunit structurei

    Homooligomerize By similarity. Interacts with NS1 from parvovirus H-1, with Vpu and Gag from HIV-1. Interacts with SARS-CoV accessory protein 7a. Interacts with DNAJC5 and DNAJC5B.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BAG2O958162EBI-347996,EBI-355275
    IRF3Q146533EBI-347996,EBI-2650369
    IRF5Q135683EBI-347996,EBI-3931258

    Protein-protein interaction databases

    BioGridi112347. 64 interactions.
    IntActiO43765. 62 interactions.
    MINTiMINT-1035135.
    STRINGi9606.ENSP00000221566.

    Structurei

    Secondary structure

    1
    313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 2117
    Helixi26 – 4318
    Helixi87 – 10317
    Helixi107 – 12014
    Helixi125 – 13713
    Helixi141 – 15414
    Helixi159 – 17113
    Helixi175 – 18814
    Helixi193 – 20614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VYIX-ray2.40A/B84-210[»]
    4GODX-ray1.40A/B4-54[»]
    4GOEX-ray1.45A/B4-54[»]
    4GOFX-ray1.35A/B4-54[»]
    ProteinModelPortaliO43765.
    SMRiO43765. Positions 4-54, 86-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43765.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati91 – 12434TPR 1Add
    BLAST
    Repeati125 – 15834TPR 2Add
    BLAST
    Repeati159 – 19234TPR 3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi275 – 28713Gln-richAdd
    BLAST

    Domaini

    The second tetratricopeptide repeat (TPR 2) mediates the interaction with SARS-CoV accessory protein 7a.

    Sequence similaritiesi

    Belongs to the SGT family.Curated
    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000208193.
    HOVERGENiHBG000885.
    InParanoidiO43765.
    KOiK16365.
    OMAiASGQHEK.
    OrthoDBiEOG78SQJJ.
    PhylomeDBiO43765.
    TreeFamiTF313092.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 3 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 3 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43765-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS    50
    DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE 100
    QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER 150
    AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK 200
    IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM 250
    ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR 300
    SRTPSASNDD QQE 313
    Length:313
    Mass (Da):34,063
    Last modified:June 1, 1998 - v1
    Checksum:i80B3C71B41F3CB55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223828 mRNA. Translation: CAA11565.1.
    AJ133129 mRNA. Translation: CAB39725.1.
    AF408399 mRNA. Translation: AAL01051.1.
    AF368279 mRNA. Translation: AAP29457.1.
    AL050156 mRNA. Translation: CAB43297.2.
    CR533517 mRNA. Translation: CAG38548.1.
    CR542282 mRNA. Translation: CAG47077.1.
    AC006538 Genomic DNA. Translation: AAD13117.1.
    CH471139 Genomic DNA. Translation: EAW69366.1.
    CH471139 Genomic DNA. Translation: EAW69367.1.
    CH471139 Genomic DNA. Translation: EAW69368.1.
    BC000390 mRNA. Translation: AAH00390.1.
    BC002989 mRNA. Translation: AAH02989.2.
    BC005165 mRNA. Translation: AAH05165.1.
    BC008885 mRNA. Translation: AAH08885.1.
    CCDSiCCDS12094.1.
    RefSeqiNP_003012.1. NM_003021.3.
    UniGeneiHs.203910.

    Genome annotation databases

    EnsembliENST00000221566; ENSP00000221566; ENSG00000104969.
    GeneIDi6449.
    KEGGihsa:6449.
    UCSCiuc002lwi.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223828 mRNA. Translation: CAA11565.1 .
    AJ133129 mRNA. Translation: CAB39725.1 .
    AF408399 mRNA. Translation: AAL01051.1 .
    AF368279 mRNA. Translation: AAP29457.1 .
    AL050156 mRNA. Translation: CAB43297.2 .
    CR533517 mRNA. Translation: CAG38548.1 .
    CR542282 mRNA. Translation: CAG47077.1 .
    AC006538 Genomic DNA. Translation: AAD13117.1 .
    CH471139 Genomic DNA. Translation: EAW69366.1 .
    CH471139 Genomic DNA. Translation: EAW69367.1 .
    CH471139 Genomic DNA. Translation: EAW69368.1 .
    BC000390 mRNA. Translation: AAH00390.1 .
    BC002989 mRNA. Translation: AAH02989.2 .
    BC005165 mRNA. Translation: AAH05165.1 .
    BC008885 mRNA. Translation: AAH08885.1 .
    CCDSi CCDS12094.1.
    RefSeqi NP_003012.1. NM_003021.3.
    UniGenei Hs.203910.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VYI X-ray 2.40 A/B 84-210 [» ]
    4GOD X-ray 1.40 A/B 4-54 [» ]
    4GOE X-ray 1.45 A/B 4-54 [» ]
    4GOF X-ray 1.35 A/B 4-54 [» ]
    ProteinModelPortali O43765.
    SMRi O43765. Positions 4-54, 86-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112347. 64 interactions.
    IntActi O43765. 62 interactions.
    MINTi MINT-1035135.
    STRINGi 9606.ENSP00000221566.

    PTM databases

    PhosphoSitei O43765.

    Proteomic databases

    MaxQBi O43765.
    PaxDbi O43765.
    PeptideAtlasi O43765.
    PRIDEi O43765.

    Protocols and materials databases

    DNASUi 6449.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221566 ; ENSP00000221566 ; ENSG00000104969 .
    GeneIDi 6449.
    KEGGi hsa:6449.
    UCSCi uc002lwi.1. human.

    Organism-specific databases

    CTDi 6449.
    GeneCardsi GC19M002754.
    HGNCi HGNC:10819. SGTA.
    HPAi HPA056309.
    MIMi 603419. gene.
    neXtProti NX_O43765.
    PharmGKBi PA35727.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000208193.
    HOVERGENi HBG000885.
    InParanoidi O43765.
    KOi K16365.
    OMAi ASGQHEK.
    OrthoDBi EOG78SQJJ.
    PhylomeDBi O43765.
    TreeFami TF313092.

    Miscellaneous databases

    EvolutionaryTracei O43765.
    GeneWikii SGTA.
    GenomeRNAii 6449.
    NextBioi 25065.
    PROi O43765.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43765.
    Bgeei O43765.
    CleanExi HS_SGTA.
    Genevestigatori O43765.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 3 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 3 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of human SGT and identification of homologues in Saccharomyces cerevisiae and Caenorhabditis elegans."
      Kordes E., Savelyeva L., Schwab M., Rommelaere J., Jauniaux J.-C., Cziepluch C.
      Genomics 52:90-94(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats."
      Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.
      J. Biol. Chem. 274:34425-34432(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family."
      Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W., Panganiban A.T.
      J. Virol. 72:5189-5197(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Tobaben S., Stahl B.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung, Muscle and Uterus.
    10. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 138-160; 165-174 AND 185-196.
      Tissue: Fetal brain cortex.
    11. "Severe acute respiratory syndrome coronavirus protein 7a interacts with hSGT."
      Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S., Lim S.G., Hong W., Tan Y.-J.
      Biochem. Biophys. Res. Commun. 343:1201-1208(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SARS-COV ACCESSORY PROTEIN 7A.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Cysteine-string protein isoform beta (Cspbeta) is targeted to the trans-Golgi network as a non-palmitoylated CSP in clonal beta-cells."
      Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.
      Biochim. Biophys. Acta 1773:109-119(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC5 AND DNAJC5B.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301; THR-303 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Structural and functional characterization of human SGT and its interaction with Vpu of the human immunodeficiency virus type 1."
      Dutta S., Tan Y.J.
      Biochemistry 47:10123-10131(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-210, SUBUNIT, FUNCTION.

    Entry informationi

    Entry nameiSGTA_HUMAN
    AccessioniPrimary (citable) accession number: O43765
    Secondary accession number(s): D6W610, Q6FIA9, Q9BTZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3