Full text data of SGTA
SGTA
(SGT, SGT1)
[Confidence: low (only semi-automatic identification from reviews)]
Small glutamine-rich tetratricopeptide repeat-containing protein alpha (Alpha-SGT; Vpu-binding protein; UBP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Small glutamine-rich tetratricopeptide repeat-containing protein alpha (Alpha-SGT; Vpu-binding protein; UBP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43765
ID SGTA_HUMAN Reviewed; 313 AA.
AC O43765; D6W610; Q6FIA9; Q9BTZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE AltName: Full=Alpha-SGT;
DE AltName: Full=Vpu-binding protein;
DE Short=UBP;
GN Name=SGTA; Synonyms=SGT, SGT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9740675; DOI=10.1006/geno.1998.5385;
RA Kordes E., Savelyeva L., Schwab M., Rommelaere J., Jauniaux J.-C.,
RA Cziepluch C.;
RT "Isolation and characterization of human SGT and identification of
RT homologues in Saccharomyces cerevisiae and Caenorhabditis elegans.";
RL Genomics 52:90-94(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT "Specific interaction of the 70-kDa heat shock cognate protein with
RT the tetratricopeptide repeats.";
RL J. Biol. Chem. 274:34425-34432(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9573291;
RA Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W.,
RA Panganiban A.T.;
RT "Functional interaction of human immunodeficiency virus type 1 Vpu and
RT Gag with a novel member of the tetratricopeptide repeat protein
RT family.";
RL J. Virol. 72:5189-5197(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tobaben S., Stahl B.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 138-160; 165-174 AND 185-196.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP INTERACTION WITH SARS-COV ACCESSORY PROTEIN 7A.
RX PubMed=16580632; DOI=10.1016/j.bbrc.2006.03.091;
RA Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S.,
RA Lim S.G., Hong W., Tan Y.-J.;
RT "Severe acute respiratory syndrome coronavirus protein 7a interacts
RT with hSGT.";
RL Biochem. Biophys. Res. Commun. 343:1201-1208(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP INTERACTION WITH DNAJC5 AND DNAJC5B.
RX PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
RA Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
RT "Cysteine-string protein isoform beta (Cspbeta) is targeted to the
RT trans-Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
RL Biochim. Biophys. Acta 1773:109-119(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301;
RP THR-303 AND SER-305, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-210, SUBUNIT, AND
RP FUNCTION.
RX PubMed=18759457; DOI=10.1021/bi800758a;
RA Dutta S., Tan Y.J.;
RT "Structural and functional characterization of human SGT and its
RT interaction with Vpu of the human immunodeficiency virus type 1.";
RL Biochemistry 47:10123-10131(2008).
CC -!- FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and
CC regulates their ATPase activity.
CC -!- SUBUNIT: Homooligomerize (By similarity). Interacts with NS1 from
CC parvovirus H-1, with Vpu and Gag from HIV-1. Interacts with SARS-
CC CoV accessory protein 7a. Interacts with DNAJC5 and DNAJC5B.
CC -!- INTERACTION:
CC Q14653:IRF3; NbExp=3; IntAct=EBI-347996, EBI-2650369;
CC Q13568:IRF5; NbExp=3; IntAct=EBI-347996, EBI-3931258;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The second tetratricopeptide repeat (TPR 2) mediates the
CC interaction with SARS-CoV accessory protein 7a.
CC -!- SIMILARITY: Belongs to the SGT family.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; AJ223828; CAA11565.1; -; mRNA.
DR EMBL; AJ133129; CAB39725.1; -; mRNA.
DR EMBL; AF408399; AAL01051.1; -; mRNA.
DR EMBL; AF368279; AAP29457.1; -; mRNA.
DR EMBL; AL050156; CAB43297.2; -; mRNA.
DR EMBL; CR533517; CAG38548.1; -; mRNA.
DR EMBL; CR542282; CAG47077.1; -; mRNA.
DR EMBL; AC006538; AAD13117.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69366.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69367.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69368.1; -; Genomic_DNA.
DR EMBL; BC000390; AAH00390.1; -; mRNA.
DR EMBL; BC002989; AAH02989.2; -; mRNA.
DR EMBL; BC005165; AAH05165.1; -; mRNA.
DR EMBL; BC008885; AAH08885.1; -; mRNA.
DR RefSeq; NP_003012.1; NM_003021.3.
DR UniGene; Hs.203910; -.
DR PDB; 2VYI; X-ray; 2.40 A; A/B=84-210.
DR PDB; 4GOD; X-ray; 1.40 A; A/B=4-54.
DR PDB; 4GOE; X-ray; 1.45 A; A/B=4-54.
DR PDB; 4GOF; X-ray; 1.35 A; A/B=4-54.
DR PDBsum; 2VYI; -.
DR PDBsum; 4GOD; -.
DR PDBsum; 4GOE; -.
DR PDBsum; 4GOF; -.
DR ProteinModelPortal; O43765; -.
DR SMR; O43765; 4-54, 86-210.
DR IntAct; O43765; 36.
DR MINT; MINT-1035135; -.
DR STRING; 9606.ENSP00000221566; -.
DR PhosphoSite; O43765; -.
DR PaxDb; O43765; -.
DR PeptideAtlas; O43765; -.
DR PRIDE; O43765; -.
DR DNASU; 6449; -.
DR Ensembl; ENST00000221566; ENSP00000221566; ENSG00000104969.
DR GeneID; 6449; -.
DR KEGG; hsa:6449; -.
DR UCSC; uc002lwi.1; human.
DR CTD; 6449; -.
DR GeneCards; GC19M002754; -.
DR HGNC; HGNC:10819; SGTA.
DR HPA; HPA056309; -.
DR MIM; 603419; gene.
DR neXtProt; NX_O43765; -.
DR PharmGKB; PA35727; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000208193; -.
DR HOVERGEN; HBG000885; -.
DR InParanoid; O43765; -.
DR KO; K16365; -.
DR OMA; ASGQHEK; -.
DR OrthoDB; EOG78SQJJ; -.
DR PhylomeDB; O43765; -.
DR EvolutionaryTrace; O43765; -.
DR GeneWiki; SGTA; -.
DR GenomeRNAi; 6449; -.
DR NextBio; 25065; -.
DR PRO; PR:O43765; -.
DR ArrayExpress; O43765; -.
DR Bgee; O43765; -.
DR CleanEx; HS_SGTA; -.
DR Genevestigator; O43765; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 3.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Complete proteome;
KW Direct protein sequencing; Host-virus interaction; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 313 Small glutamine-rich tetratricopeptide
FT repeat-containing protein alpha.
FT /FTId=PRO_0000106365.
FT REPEAT 91 124 TPR 1.
FT REPEAT 125 158 TPR 2.
FT REPEAT 159 192 TPR 3.
FT COMPBIAS 275 287 Gln-rich.
FT MOD_RES 77 77 Phosphoserine.
FT MOD_RES 81 81 Phosphothreonine.
FT MOD_RES 137 137 N6-acetyllysine.
FT MOD_RES 301 301 Phosphoserine.
FT MOD_RES 303 303 Phosphothreonine.
FT MOD_RES 305 305 Phosphoserine.
FT HELIX 5 21
FT HELIX 26 43
FT HELIX 87 103
FT HELIX 107 120
FT HELIX 125 137
FT HELIX 141 154
FT HELIX 159 171
FT HELIX 175 188
FT HELIX 193 206
SQ SEQUENCE 313 AA; 34063 MW; 80B3C71B41F3CB55 CRC64;
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE
IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL
NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA
YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN
PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR
SRTPSASNDD QQE
//
ID SGTA_HUMAN Reviewed; 313 AA.
AC O43765; D6W610; Q6FIA9; Q9BTZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE AltName: Full=Alpha-SGT;
DE AltName: Full=Vpu-binding protein;
DE Short=UBP;
GN Name=SGTA; Synonyms=SGT, SGT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9740675; DOI=10.1006/geno.1998.5385;
RA Kordes E., Savelyeva L., Schwab M., Rommelaere J., Jauniaux J.-C.,
RA Cziepluch C.;
RT "Isolation and characterization of human SGT and identification of
RT homologues in Saccharomyces cerevisiae and Caenorhabditis elegans.";
RL Genomics 52:90-94(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT "Specific interaction of the 70-kDa heat shock cognate protein with
RT the tetratricopeptide repeats.";
RL J. Biol. Chem. 274:34425-34432(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9573291;
RA Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W.,
RA Panganiban A.T.;
RT "Functional interaction of human immunodeficiency virus type 1 Vpu and
RT Gag with a novel member of the tetratricopeptide repeat protein
RT family.";
RL J. Virol. 72:5189-5197(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tobaben S., Stahl B.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 138-160; 165-174 AND 185-196.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP INTERACTION WITH SARS-COV ACCESSORY PROTEIN 7A.
RX PubMed=16580632; DOI=10.1016/j.bbrc.2006.03.091;
RA Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S.,
RA Lim S.G., Hong W., Tan Y.-J.;
RT "Severe acute respiratory syndrome coronavirus protein 7a interacts
RT with hSGT.";
RL Biochem. Biophys. Res. Commun. 343:1201-1208(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP INTERACTION WITH DNAJC5 AND DNAJC5B.
RX PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
RA Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
RT "Cysteine-string protein isoform beta (Cspbeta) is targeted to the
RT trans-Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
RL Biochim. Biophys. Acta 1773:109-119(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301;
RP THR-303 AND SER-305, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-210, SUBUNIT, AND
RP FUNCTION.
RX PubMed=18759457; DOI=10.1021/bi800758a;
RA Dutta S., Tan Y.J.;
RT "Structural and functional characterization of human SGT and its
RT interaction with Vpu of the human immunodeficiency virus type 1.";
RL Biochemistry 47:10123-10131(2008).
CC -!- FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and
CC regulates their ATPase activity.
CC -!- SUBUNIT: Homooligomerize (By similarity). Interacts with NS1 from
CC parvovirus H-1, with Vpu and Gag from HIV-1. Interacts with SARS-
CC CoV accessory protein 7a. Interacts with DNAJC5 and DNAJC5B.
CC -!- INTERACTION:
CC Q14653:IRF3; NbExp=3; IntAct=EBI-347996, EBI-2650369;
CC Q13568:IRF5; NbExp=3; IntAct=EBI-347996, EBI-3931258;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The second tetratricopeptide repeat (TPR 2) mediates the
CC interaction with SARS-CoV accessory protein 7a.
CC -!- SIMILARITY: Belongs to the SGT family.
CC -!- SIMILARITY: Contains 3 TPR repeats.
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DR EMBL; AJ223828; CAA11565.1; -; mRNA.
DR EMBL; AJ133129; CAB39725.1; -; mRNA.
DR EMBL; AF408399; AAL01051.1; -; mRNA.
DR EMBL; AF368279; AAP29457.1; -; mRNA.
DR EMBL; AL050156; CAB43297.2; -; mRNA.
DR EMBL; CR533517; CAG38548.1; -; mRNA.
DR EMBL; CR542282; CAG47077.1; -; mRNA.
DR EMBL; AC006538; AAD13117.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69366.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69367.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69368.1; -; Genomic_DNA.
DR EMBL; BC000390; AAH00390.1; -; mRNA.
DR EMBL; BC002989; AAH02989.2; -; mRNA.
DR EMBL; BC005165; AAH05165.1; -; mRNA.
DR EMBL; BC008885; AAH08885.1; -; mRNA.
DR RefSeq; NP_003012.1; NM_003021.3.
DR UniGene; Hs.203910; -.
DR PDB; 2VYI; X-ray; 2.40 A; A/B=84-210.
DR PDB; 4GOD; X-ray; 1.40 A; A/B=4-54.
DR PDB; 4GOE; X-ray; 1.45 A; A/B=4-54.
DR PDB; 4GOF; X-ray; 1.35 A; A/B=4-54.
DR PDBsum; 2VYI; -.
DR PDBsum; 4GOD; -.
DR PDBsum; 4GOE; -.
DR PDBsum; 4GOF; -.
DR ProteinModelPortal; O43765; -.
DR SMR; O43765; 4-54, 86-210.
DR IntAct; O43765; 36.
DR MINT; MINT-1035135; -.
DR STRING; 9606.ENSP00000221566; -.
DR PhosphoSite; O43765; -.
DR PaxDb; O43765; -.
DR PeptideAtlas; O43765; -.
DR PRIDE; O43765; -.
DR DNASU; 6449; -.
DR Ensembl; ENST00000221566; ENSP00000221566; ENSG00000104969.
DR GeneID; 6449; -.
DR KEGG; hsa:6449; -.
DR UCSC; uc002lwi.1; human.
DR CTD; 6449; -.
DR GeneCards; GC19M002754; -.
DR HGNC; HGNC:10819; SGTA.
DR HPA; HPA056309; -.
DR MIM; 603419; gene.
DR neXtProt; NX_O43765; -.
DR PharmGKB; PA35727; -.
DR eggNOG; COG0457; -.
DR HOGENOM; HOG000208193; -.
DR HOVERGEN; HBG000885; -.
DR InParanoid; O43765; -.
DR KO; K16365; -.
DR OMA; ASGQHEK; -.
DR OrthoDB; EOG78SQJJ; -.
DR PhylomeDB; O43765; -.
DR EvolutionaryTrace; O43765; -.
DR GeneWiki; SGTA; -.
DR GenomeRNAi; 6449; -.
DR NextBio; 25065; -.
DR PRO; PR:O43765; -.
DR ArrayExpress; O43765; -.
DR Bgee; O43765; -.
DR CleanEx; HS_SGTA; -.
DR Genevestigator; O43765; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 3.
DR SMART; SM00028; TPR; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Complete proteome;
KW Direct protein sequencing; Host-virus interaction; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 313 Small glutamine-rich tetratricopeptide
FT repeat-containing protein alpha.
FT /FTId=PRO_0000106365.
FT REPEAT 91 124 TPR 1.
FT REPEAT 125 158 TPR 2.
FT REPEAT 159 192 TPR 3.
FT COMPBIAS 275 287 Gln-rich.
FT MOD_RES 77 77 Phosphoserine.
FT MOD_RES 81 81 Phosphothreonine.
FT MOD_RES 137 137 N6-acetyllysine.
FT MOD_RES 301 301 Phosphoserine.
FT MOD_RES 303 303 Phosphothreonine.
FT MOD_RES 305 305 Phosphoserine.
FT HELIX 5 21
FT HELIX 26 43
FT HELIX 87 103
FT HELIX 107 120
FT HELIX 125 137
FT HELIX 141 154
FT HELIX 159 171
FT HELIX 175 188
FT HELIX 193 206
SQ SEQUENCE 313 AA; 34063 MW; 80B3C71B41F3CB55 CRC64;
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE
IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL
NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA
YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN
PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR
SRTPSASNDD QQE
//
MIM
603419
*RECORD*
*FIELD* NO
603419
*FIELD* TI
*603419 SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN,
ALPHA; SGTA
read more;;SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN;
SGT
*FIELD* TX
CLONING
The SGT protein interacts with the parvovirus nonstructural protein NS1.
Kordes et al. (1998) used yeast 2-hybrid screening to isolate a human
SGT cDNA from a placenta library. The SGT gene encodes a 313-amino acid
polypeptide containing 3 tetratricopeptide repeat (TPR) protein-protein
interaction motifs. Northern blot analysis revealed SGT expression as a
2.4-kb mRNA at comparable levels in all human tissues tested.
GENE FUNCTION
Tobaben et al. (2001) showed that rat Csp (DNAJC5; 611203) interacted
with Sgt and Hsc70 (HSPA8; 600816) in a complex located on the synaptic
vesicle surface. The complex functioned as an ATP-dependent chaperone
that reactivated a denatured substrate. Sgt overexpression in cultured
rat hippocampal neurons inhibited neurotransmitter release, suggesting
that the Csp/Sgt/Hsc70 complex is important for maintenance of a normal
synapse.
MAPPING
Kordes et al. (1998) used fluorescence in situ hybridization to map the
SGTA gene to human chromosome 19p13.
*FIELD* RF
1. Kordes, E.; Savelyeva, L.; Schwab, M.; Rommelaere, J.; Jauniaux,
J.-C.; Cziepluch, C.: Isolation and characterization of human SGT
and identification of homologues in Saccharomyces cerevisiae and Caenorhabditis
elegans. Genomics 52: 90-94, 1998.
2. Tobaben, S.; Thakur, P.; Fernandez-Chacon, R.; Sudhof, T. C.; Rettig,
J.; Stahl, B.: A trimeric protein complex functions as a synaptic
chaperone machine. Neuron 31: 987-999, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 07/16/2007
*FIELD* CD
Jennifer P. Macke: 1/12/1999
*FIELD* ED
mgross: 07/16/2007
alopez: 3/28/2006
alopez: 1/12/1999
*RECORD*
*FIELD* NO
603419
*FIELD* TI
*603419 SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN,
ALPHA; SGTA
read more;;SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN;
SGT
*FIELD* TX
CLONING
The SGT protein interacts with the parvovirus nonstructural protein NS1.
Kordes et al. (1998) used yeast 2-hybrid screening to isolate a human
SGT cDNA from a placenta library. The SGT gene encodes a 313-amino acid
polypeptide containing 3 tetratricopeptide repeat (TPR) protein-protein
interaction motifs. Northern blot analysis revealed SGT expression as a
2.4-kb mRNA at comparable levels in all human tissues tested.
GENE FUNCTION
Tobaben et al. (2001) showed that rat Csp (DNAJC5; 611203) interacted
with Sgt and Hsc70 (HSPA8; 600816) in a complex located on the synaptic
vesicle surface. The complex functioned as an ATP-dependent chaperone
that reactivated a denatured substrate. Sgt overexpression in cultured
rat hippocampal neurons inhibited neurotransmitter release, suggesting
that the Csp/Sgt/Hsc70 complex is important for maintenance of a normal
synapse.
MAPPING
Kordes et al. (1998) used fluorescence in situ hybridization to map the
SGTA gene to human chromosome 19p13.
*FIELD* RF
1. Kordes, E.; Savelyeva, L.; Schwab, M.; Rommelaere, J.; Jauniaux,
J.-C.; Cziepluch, C.: Isolation and characterization of human SGT
and identification of homologues in Saccharomyces cerevisiae and Caenorhabditis
elegans. Genomics 52: 90-94, 1998.
2. Tobaben, S.; Thakur, P.; Fernandez-Chacon, R.; Sudhof, T. C.; Rettig,
J.; Stahl, B.: A trimeric protein complex functions as a synaptic
chaperone machine. Neuron 31: 987-999, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 07/16/2007
*FIELD* CD
Jennifer P. Macke: 1/12/1999
*FIELD* ED
mgross: 07/16/2007
alopez: 3/28/2006
alopez: 1/12/1999