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O43765 (SGTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Alternative name(s):
Alpha-SGT
Vpu-binding protein
Short name=UBP
Gene names
Name:SGTA
Synonyms:SGT, SGT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. Ref.20

Subunit structure

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. Ref.11 Ref.13 Ref.20

Tissue specificity

Ubiquitous.

Domain

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

Sequence similarities

Belongs to the SGT family.

Contains 3 TPR repeats.

Ontologies

Keywords
   Biological processHost-virus interaction
   DomainRepeat
TPR repeat
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processviral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: LIFEdb

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Small glutamine-rich tetratricopeptide repeat-containing protein alpha
PRO_0000106365

Regions

Repeat91 – 12434TPR 1
Repeat125 – 15834TPR 2
Repeat159 – 19234TPR 3
Compositional bias275 – 28713Gln-rich

Amino acid modifications

Modified residue771Phosphoserine Ref.14 Ref.15
Modified residue811Phosphothreonine Ref.14 Ref.15
Modified residue1371N6-acetyllysine Ref.16
Modified residue3011Phosphoserine Ref.14 Ref.19
Modified residue3031Phosphothreonine Ref.14 Ref.17
Modified residue3051Phosphoserine Ref.12 Ref.14 Ref.15 Ref.19

Secondary structure

................... 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43765 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 80B3C71B41F3CB55

FASTA31334,063
        10         20         30         40         50         60 
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE 

        70         80         90        100        110        120 
IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL 

       130        140        150        160        170        180 
NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA 

       190        200        210        220        230        240 
YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN 

       250        260        270        280        290        300 
PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR 

       310 
SRTPSASNDD QQE 

« Hide

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003012.1. NM_003021.3.
UniGeneHs.203910.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYIX-ray2.40A/B84-210[»]
4GODX-ray1.40A/B4-54[»]
4GOEX-ray1.45A/B4-54[»]
4GOFX-ray1.35A/B4-54[»]
ProteinModelPortalO43765.
SMRO43765. Positions 4-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112347. 66 interactions.
IntActO43765. 36 interactions.
MINTMINT-1035135.
STRING9606.ENSP00000221566.

PTM databases

PhosphoSiteO43765.

Proteomic databases

PaxDbO43765.
PeptideAtlasO43765.
PRIDEO43765.

Protocols and materials databases

DNASU6449.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221566; ENSP00000221566; ENSG00000104969.
GeneID6449.
KEGGhsa:6449.
UCSCuc002lwi.1. human.

Organism-specific databases

CTD6449.
GeneCardsGC19M002754.
HGNCHGNC:10819. SGTA.
HPAHPA056309.
MIM603419. gene.
neXtProtNX_O43765.
PharmGKBPA35727.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000208193.
HOVERGENHBG000885.
InParanoidO43765.
KOK16365.
OMAASGQHEK.
OrthoDBEOG78SQJJ.
PhylomeDBO43765.
TreeFamTF313092.

Gene expression databases

ArrayExpressO43765.
BgeeO43765.
CleanExHS_SGTA.
GenevestigatorO43765.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 3 hits.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43765.
GeneWikiSGTA.
GenomeRNAi6449.
NextBio25065.
PROO43765.
SOURCESearch...

Entry information

Entry nameSGTA_HUMAN
AccessionPrimary (citable) accession number: O43765
Secondary accession number(s): D6W610, Q6FIA9, Q9BTZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: March 19, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM