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Small glutamine-rich tetratricopeptide repeat-containing protein alpha (Alpha-SGT) (Vpu-binding protein) (UBP)

 SGTA_HUMAN              Reviewed;         313 AA.
O43765; D6W610; Q6FIA9; Q9BTZ9;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
AltName: Full=Alpha-SGT;
AltName: Full=Vpu-binding protein;
Short=UBP;
Name=SGTA; Synonyms=SGT, SGT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9740675; DOI=10.1006/geno.1998.5385;
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]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
"Specific interaction of the 70-kDa heat shock cognate protein with
the tetratricopeptide repeats.";
J. Biol. Chem. 274:34425-34432(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HIV-1V PU AND GAG
(MICROBIAL INFECTION).
PubMed=9573291;
Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W.,
Panganiban A.T.;
"Functional interaction of human immunodeficiency virus type 1 Vpu and
Gag with a novel member of the tetratricopeptide repeat protein
family.";
J. Virol. 72:5189-5197(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Tobaben S., Stahl B.;
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 138-160; 165-174 AND 185-196.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
SUBUNIT, AND INTERACTION WITH HSP90AA1 AND SLC2A1.
PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
Liou S.T., Wang C.;
"Small glutamine-rich tetratricopeptide repeat-containing protein is
composed of three structural units with distinct functions.";
Arch. Biochem. Biophys. 435:253-263(2005).
[12]
INTERACTION WITH HSP90AB1, AND SUBCELLULAR LOCATION.
PubMed=16580629; DOI=10.1016/j.bbrc.2006.03.090;
Yin H., Wang H., Zong H., Chen X., Wang Y., Yun X., Wu Y., Wang J.,
Gu J.;
"SGT, a Hsp90beta binding partner, is accumulated in the nucleus
during cell apoptosis.";
Biochem. Biophys. Res. Commun. 343:1153-1158(2006).
[13]
INTERACTION WITH SARS-COV ACCESSORY PROTEIN 7A (MICROBIAL INFECTION).
PubMed=16580632; DOI=10.1016/j.bbrc.2006.03.091;
Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S.,
Lim S.G., Hong W., Tan Y.-J.;
"Severe acute respiratory syndrome coronavirus protein 7a interacts
with hSGT.";
Biochem. Biophys. Res. Commun. 343:1201-1208(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
INTERACTION WITH DNAJC5 AND DNAJC5B.
PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
"Cysteine-string protein isoform beta (Cspbeta) is targeted to the
trans-Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
Biochim. Biophys. Acta 1773:109-119(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301;
THR-303 AND SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
FUNCTION, AND INTERACTION WITH BAG6.
PubMed=23129660; DOI=10.1073/pnas.1209997109;
Leznicki P., High S.;
"SGTA antagonizes BAG6-mediated protein triage.";
Proc. Natl. Acad. Sci. U.S.A. 109:19214-19219(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-301,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
FUNCTION, AND INTERACTION WITH BAG6.
PubMed=25179605; DOI=10.1242/jcs.155648;
Wunderley L., Leznicki P., Payapilly A., High S.;
"SGTA regulates the cytosolic quality control of hydrophobic
substrates.";
J. Cell Sci. 127:4728-4739(2014).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81; THR-303 AND SER-305,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
FUNCTION (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX WITH
DNAJB12 AND DNAJB14, AND INTERACTION WITH HSPA8.
PubMed=24675744; DOI=10.1371/journal.ppat.1004007;
Walczak C.P., Ravindran M.S., Inoue T., Tsai B.;
"A cytosolic chaperone complexes with dynamic membrane J-proteins and
mobilizes a nonenveloped virus out of the endoplasmic reticulum.";
PLoS Pathog. 10:E1004007-E1004007(2014).
[27]
FUNCTION, AND INTERACTION WITH BAG6.
PubMed=27193484; DOI=10.1038/srep26433;
Krysztofinska E.M., Martinez-Lumbreras S., Thapaliya A., Evans N.J.,
High S., Isaacson R.L.;
"Structural and functional insights into the E3 ligase, RNF126.";
Sci. Rep. 6:26433-26433(2016).
[28]
FUNCTION.
PubMed=28104892; DOI=10.1126/science.aah6130;
Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
"Mechanistic basis for a molecular triage reaction.";
Science 355:298-302(2017).
[29]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-210, SUBUNIT (MICROBIAL
INFECTION), AND FUNCTION.
PubMed=18759457; DOI=10.1021/bi800758a;
Dutta S., Tan Y.J.;
"Structural and functional characterization of human SGT and its
interaction with Vpu of the human immunodeficiency virus type 1.";
Biochemistry 47:10123-10131(2008).
-!- FUNCTION: Co-chaperone that binds misfolded and hydrophobic
patches-containing client proteins in the cytosol. Mediates their
targeting to the endoplasmic reticulum but also regulates their
sorting to the proteasome when targeting fails (PubMed:28104892).
Functions in tail-anchored/type II transmembrane proteins membrane
insertion constituting with ASNA1 and the BAG6 complex a targeting
module (PubMed:28104892). Probably functions upstream of the BAG6
complex and ASNA1, binding more rapidly the transmembrane domain
of newly synthesized proteins (PubMed:28104892). It is also
involved in the regulation of the endoplasmic reticulum-associated
misfolded protein catabolic process via its interaction with BAG6:
collaborates with the BAG6 complex to maintain hydrophobic
substrates in non-ubiquitinated states (PubMed:23129660,
PubMed:25179605). Competes with RNF126 for interaction with BAG6,
preventing the ubiquitination of client proteins associated with
the BAG6 complex (PubMed:27193484). Binds directly to HSC70 and
HSP70 and regulates their ATPase activity (PubMed:18759457).
{ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:23129660,
ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:27193484,
ECO:0000269|PubMed:28104892}.
-!- FUNCTION: (Microbial infection) In case of infection by
polyomavirus, involved in the virus endoplasmic reticulum membrane
penetration and infection via interaction with DNAJB12, DNAJB14
and HSPA8/Hsc70 (PubMed:24675744). {ECO:0000269|PubMed:24675744}.
-!- SUBUNIT: Homodimer (PubMed:15708368). Homooligomer (By
similarity). Interacts with DNAJC5 and DNAJC5B. Interacts (via TPR
repeats) with HSP90AA1 (PubMed:15708368). Interacts (via Gln-rich
region) with SLC2A1 (PubMed:15708368). Interacts with HSP90AB1
(PubMed:16580629). Interacts (via TPR repeats) with HSPA8/Hsc70;
the interaction is direct (PubMed:24675744). Interacts with BAG6
(via ubiquitin-like domain); interaction prevents interaction
between BAG6 and RNF126 (PubMed:23129660, PubMed:25179605,
PubMed:27193484). Forms a multiprotein complex, at least composed
of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with
DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744).
{ECO:0000250|UniProtKB:O70593, ECO:0000269|PubMed:15708368,
ECO:0000269|PubMed:16580629, ECO:0000269|PubMed:17034881,
ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:23129660,
ECO:0000269|PubMed:24675744, ECO:0000269|PubMed:25179605,
ECO:0000269|PubMed:27193484}.
-!- SUBUNIT: (Microbial infection) Interacts with NS1 from parvovirus
H-1, with Vpu and Gag from HIV-1. Interacts with SARS-CoV
accessory protein 7a. {ECO:0000269|PubMed:16580632,
ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:9573291}.
-!- INTERACTION:
A8K660:ADIPOQ; NbExp=3; IntAct=EBI-347996, EBI-10174479;
Q15848:ADIPOQ; NbExp=5; IntAct=EBI-347996, EBI-10827839;
Q8TD06:AGR3; NbExp=5; IntAct=EBI-347996, EBI-3925742;
O95816:BAG2; NbExp=2; IntAct=EBI-347996, EBI-355275;
P46379:BAG6; NbExp=5; IntAct=EBI-347996, EBI-347552;
P35070:BTC; NbExp=5; IntAct=EBI-347996, EBI-6590057;
Q9BXJ1:C1QTNF1; NbExp=4; IntAct=EBI-347996, EBI-750200;
Q9BXI9:C1QTNF6; NbExp=3; IntAct=EBI-347996, EBI-10301084;
Q8N6L0:CCDC155; NbExp=9; IntAct=EBI-347996, EBI-749265;
P40259:CD79B; NbExp=6; IntAct=EBI-347996, EBI-2873732;
P55291:CDH15; NbExp=5; IntAct=EBI-347996, EBI-10215061;
P08123:COL1A2; NbExp=5; IntAct=EBI-347996, EBI-983038;
Q4VAQ0:COL8A2; NbExp=3; IntAct=EBI-347996, EBI-10241815;
P09603:CSF1; NbExp=5; IntAct=EBI-347996, EBI-2872294;
P01037:CST1; NbExp=3; IntAct=EBI-347996, EBI-1056240;
P78358:CTAG1B; NbExp=4; IntAct=EBI-347996, EBI-1188472;
P07711:CTSL; NbExp=3; IntAct=EBI-347996, EBI-1220160;
Q12805:EFEMP1; NbExp=9; IntAct=EBI-347996, EBI-536772;
O95967:EFEMP2; NbExp=6; IntAct=EBI-347996, EBI-743414;
Q96DN0:ERP27; NbExp=5; IntAct=EBI-347996, EBI-953772;
Q9NVM1:EVA1B; NbExp=5; IntAct=EBI-347996, EBI-10314666;
Q9Y624:F11R; NbExp=9; IntAct=EBI-347996, EBI-742600;
Q96RJ6:FERD3L; NbExp=3; IntAct=EBI-347996, EBI-10183007;
Q9Y680:FKBP7; NbExp=3; IntAct=EBI-347996, EBI-3918971;
P58549:FXYD7; NbExp=7; IntAct=EBI-347996, EBI-10216171;
P22466:GAL; NbExp=3; IntAct=EBI-347996, EBI-6624768;
P09681:GIP; NbExp=7; IntAct=EBI-347996, EBI-8588553;
Q14440:GPErik; NbExp=3; IntAct=EBI-347996, EBI-10232920;
Q96SL4:GPX7; NbExp=5; IntAct=EBI-347996, EBI-749411;
P28799:GRN; NbExp=6; IntAct=EBI-347996, EBI-747754;
Q02747:GUCA2A; NbExp=4; IntAct=EBI-347996, EBI-12244272;
A0A0C4DFT7:GYPA; NbExp=3; IntAct=EBI-347996, EBI-12044847;
B8Q183:GYPA; NbExp=4; IntAct=EBI-347996, EBI-10176190;
P48723:HSPA13; NbExp=5; IntAct=EBI-347996, EBI-750892;
P46695:IER3; NbExp=4; IntAct=EBI-347996, EBI-1748945;
Q6PIQ7:IGL@; NbExp=3; IntAct=EBI-347996, EBI-6677651;
Q8N355:IGL@; NbExp=4; IntAct=EBI-347996, EBI-748681;
Q14653:IRF3; NbExp=3; IntAct=EBI-347996, EBI-2650369;
Q13568:IRF5; NbExp=3; IntAct=EBI-347996, EBI-3931258;
Q6GPH6:ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-953819;
P02538:KRT6A; NbExp=3; IntAct=EBI-347996, EBI-702198;
Q86UP2:KTN1; NbExp=3; IntAct=EBI-347996, EBI-359761;
Q6ISS4:LAIR2; NbExp=5; IntAct=EBI-347996, EBI-10250491;
O43561:LAT; NbExp=3; IntAct=EBI-347996, EBI-1222766;
P80188:LCN2; NbExp=4; IntAct=EBI-347996, EBI-11911016;
P08118:MSMB; NbExp=3; IntAct=EBI-347996, EBI-10195681;
Q969H8:MYDGF; NbExp=5; IntAct=EBI-347996, EBI-718622;
Q8IW45:NAXD; NbExp=6; IntAct=EBI-347996, EBI-8650724;
Q13232:NME3; NbExp=8; IntAct=EBI-347996, EBI-713684;
C3PTT6:PAUF; NbExp=3; IntAct=EBI-347996, EBI-3505892;
Q96AQ6:PBXIP1; NbExp=3; IntAct=EBI-347996, EBI-740845;
Q9UN74:PCDHA4; NbExp=3; IntAct=EBI-347996, EBI-712273;
P23284:PPIB; NbExp=5; IntAct=EBI-347996, EBI-359252;
P45877:PPIC; NbExp=5; IntAct=EBI-347996, EBI-953909;
Q96NZ9:PRAP1; NbExp=5; IntAct=EBI-347996, EBI-2116102;
Q9UL19:RARRES3; NbExp=3; IntAct=EBI-347996, EBI-10323452;
Q96K19-5:RNF170; NbExp=4; IntAct=EBI-347996, EBI-12055631;
P04843:RPN1; NbExp=5; IntAct=EBI-347996, EBI-355963;
P31431:SDC4; NbExp=5; IntAct=EBI-347996, EBI-3913237;
P05121:SERPINE1; NbExp=5; IntAct=EBI-347996, EBI-953978;
Q16586:SGCA; NbExp=9; IntAct=EBI-347996, EBI-5663553;
P03973:SLPI; NbExp=3; IntAct=EBI-347996, EBI-355293;
Q0VAQ4:SMAGP; NbExp=3; IntAct=EBI-347996, EBI-10226799;
Q71RC9:SMIM5; NbExp=4; IntAct=EBI-347996, EBI-12334905;
P08294:SOD3; NbExp=3; IntAct=EBI-347996, EBI-10195782;
P10451:SPP1; NbExp=8; IntAct=EBI-347996, EBI-723648;
Q8TCT8:SPPL2A; NbExp=6; IntAct=EBI-347996, EBI-750784;
P10124:SRGN; NbExp=8; IntAct=EBI-347996, EBI-744915;
Q9BT88:SYT11; NbExp=6; IntAct=EBI-347996, EBI-751770;
Q9H2B2:SYT4; NbExp=6; IntAct=EBI-347996, EBI-751132;
Q07654:TFF3; NbExp=3; IntAct=EBI-347996, EBI-10224676;
P02786:TFRC; NbExp=5; IntAct=EBI-347996, EBI-355727;
P01135:TGFA; NbExp=3; IntAct=EBI-347996, EBI-1034374;
Q8WUU8:TMEM174; NbExp=5; IntAct=EBI-347996, EBI-10276729;
Q5JXX7:TMEM31; NbExp=3; IntAct=EBI-347996, EBI-10244617;
Q71RG4:TMUB2; NbExp=3; IntAct=EBI-347996, EBI-2820477;
O14836:TNFRSF13B; NbExp=3; IntAct=EBI-347996, EBI-519160;
O14836-2:TNFRSF13B; NbExp=5; IntAct=EBI-347996, EBI-12023110;
Q5BVD1:TTMP; NbExp=5; IntAct=EBI-347996, EBI-10243654;
Q9GZX9:TWSG1; NbExp=3; IntAct=EBI-347996, EBI-10304067;
O95881:TXNDC12; NbExp=3; IntAct=EBI-347996, EBI-2564581;
P11441:UBL4A; NbExp=4; IntAct=EBI-347996, EBI-356983;
O75631:UPK3A; NbExp=3; IntAct=EBI-347996, EBI-10188907;
P01282:VIP; NbExp=3; IntAct=EBI-347996, EBI-751454;
Q9NX94:WBP1L; NbExp=3; IntAct=EBI-347996, EBI-10316321;
O60844:ZG16; NbExp=8; IntAct=EBI-347996, EBI-746479;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629}.
Nucleus {ECO:0000269|PubMed:16580629}. Note=Co-localizes with
HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen
during cell apoptosis. {ECO:0000269|PubMed:16580629}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The second tetratricopeptide repeat (TPR 2) mediates the
interaction with SARS-CoV accessory protein 7a.
-!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ223828; CAA11565.1; -; mRNA.
EMBL; AJ133129; CAB39725.1; -; mRNA.
EMBL; AF408399; AAL01051.1; -; mRNA.
EMBL; AF368279; AAP29457.1; -; mRNA.
EMBL; AL050156; CAB43297.2; -; mRNA.
EMBL; CR533517; CAG38548.1; -; mRNA.
EMBL; CR542282; CAG47077.1; -; mRNA.
EMBL; AC006538; AAD13117.1; -; Genomic_DNA.
EMBL; CH471139; EAW69366.1; -; Genomic_DNA.
EMBL; CH471139; EAW69367.1; -; Genomic_DNA.
EMBL; CH471139; EAW69368.1; -; Genomic_DNA.
EMBL; BC000390; AAH00390.1; -; mRNA.
EMBL; BC002989; AAH02989.2; -; mRNA.
EMBL; BC005165; AAH05165.1; -; mRNA.
EMBL; BC008885; AAH08885.1; -; mRNA.
CCDS; CCDS12094.1; -.
RefSeq; NP_003012.1; NM_003021.3.
RefSeq; XP_011526480.1; XM_011528178.2.
UniGene; Hs.203910; -.
PDB; 2VYI; X-ray; 2.40 A; A/B=84-210.
PDB; 4CPG; NMR; -; A/B=1-69.
PDB; 4GOD; X-ray; 1.40 A; A/B=4-54.
PDB; 4GOE; X-ray; 1.45 A; A/B=4-54.
PDB; 4GOF; X-ray; 1.35 A; A/B=4-54.
PDBsum; 2VYI; -.
PDBsum; 4CPG; -.
PDBsum; 4GOD; -.
PDBsum; 4GOE; -.
PDBsum; 4GOF; -.
ProteinModelPortal; O43765; -.
SMR; O43765; -.
BioGrid; 112347; 139.
IntAct; O43765; 186.
MINT; MINT-1035135; -.
STRING; 9606.ENSP00000221566; -.
iPTMnet; O43765; -.
PhosphoSitePlus; O43765; -.
BioMuta; SGTA; -.
EPD; O43765; -.
MaxQB; O43765; -.
PaxDb; O43765; -.
PeptideAtlas; O43765; -.
PRIDE; O43765; -.
TopDownProteomics; O43765; -.
DNASU; 6449; -.
Ensembl; ENST00000221566; ENSP00000221566; ENSG00000104969.
GeneID; 6449; -.
KEGG; hsa:6449; -.
UCSC; uc002lwi.2; human.
CTD; 6449; -.
DisGeNET; 6449; -.
EuPathDB; HostDB:ENSG00000104969.9; -.
GeneCards; SGTA; -.
HGNC; HGNC:10819; SGTA.
HPA; HPA056309; -.
MIM; 603419; gene.
neXtProt; NX_O43765; -.
OpenTargets; ENSG00000104969; -.
PharmGKB; PA35727; -.
eggNOG; KOG0553; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00730000110724; -.
HOGENOM; HOG000208193; -.
HOVERGEN; HBG000885; -.
InParanoid; O43765; -.
KO; K16365; -.
OMA; EAVVYYK; -.
OrthoDB; EOG091G0C0Q; -.
PhylomeDB; O43765; -.
TreeFam; TF313092; -.
ChiTaRS; SGTA; human.
EvolutionaryTrace; O43765; -.
GeneWiki; SGTA; -.
GenomeRNAi; 6449; -.
PRO; PR:O43765; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104969; -.
CleanEx; HS_SGTA; -.
ExpressionAtlas; O43765; baseline and differential.
Genevisible; O43765; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1904288; F:BAT3 complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR032374; SGTA_dimer.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
Pfam; PF16546; SGTA_dimer; 1.
Pfam; PF00515; TPR_1; 2.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Nucleus;
Phosphoprotein; Reference proteome; Repeat; TPR repeat.
CHAIN 1 313 Small glutamine-rich tetratricopeptide
repeat-containing protein alpha.
/FTId=PRO_0000106365.
REPEAT 91 124 TPR 1.
REPEAT 125 158 TPR 2.
REPEAT 159 192 TPR 3.
COMPBIAS 275 287 Gln-rich.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 81 81 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 84 84 Phosphoserine.
{ECO:0000250|UniProtKB:O70593}.
MOD_RES 137 137 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 303 303 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
HELIX 5 21 {ECO:0000244|PDB:4GOF}.
HELIX 26 43 {ECO:0000244|PDB:4GOF}.
HELIX 48 51 {ECO:0000244|PDB:4CPG}.
HELIX 58 65 {ECO:0000244|PDB:4CPG}.
HELIX 87 103 {ECO:0000244|PDB:2VYI}.
HELIX 107 120 {ECO:0000244|PDB:2VYI}.
HELIX 125 137 {ECO:0000244|PDB:2VYI}.
HELIX 141 154 {ECO:0000244|PDB:2VYI}.
HELIX 159 171 {ECO:0000244|PDB:2VYI}.
HELIX 175 188 {ECO:0000244|PDB:2VYI}.
HELIX 193 206 {ECO:0000244|PDB:2VYI}.
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


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