O43765 (SGTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Host-virus interaction
Domain	Repeat TPR repeat
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: LIFEdb
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IRF3	Q14653	3	EBI-347996,EBI-2650369
IRF5	Q13568	3	EBI-347996,EBI-3931258

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

Small glutamine-rich tetratricopeptide repeat-containing protein alpha

PRO_0000106365

Regions

Repeat

91 – 124

34

TPR 1

Repeat

125 – 158

34

TPR 2

Repeat

159 – 192

34

TPR 3

Compositional bias

275 – 287

13

Gln-rich

Amino acid modifications

Modified residue

77

1

Phosphoserine Ref.14 Ref.15

Modified residue

81

1

Phosphothreonine Ref.14 Ref.15

Modified residue

137

1

N6-acetyllysine Ref.16

Modified residue

301

1

Phosphoserine Ref.14 Ref.19

Modified residue

303

1

Phosphothreonine Ref.14 Ref.17

Modified residue

305

1

Phosphoserine Ref.12 Ref.14 Ref.15 Ref.19

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

313

Helix Strand Turn

Details...

Helix

5 – 21

17

Helix

26 – 43

18

Helix

87 – 103

17

Helix

107 – 120

14

Helix

125 – 137

13

Helix

141 – 154

14

Helix

159 – 171

13

Helix

175 – 188

14

Helix

193 – 206

14

Sequences

	Sequence		Length	Mass (Da)
	O43765 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 80B3C71B41F3CB55	FASTA	313	34,063
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00013949.

RefSeq

NP_003012.1. NM_003021.3.

UniGene

Hs.203910.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O43765.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43765. 32 interactions.

MINT

MINT-1035135.

STRING

9606.ENSP00000221566.

PTM databases

PhosphoSite

O43765.

Proteomic databases

PaxDb

O43765.

PeptideAtlas

O43765.

PRIDE

O43765.

Protocols and materials databases

DNASU

6449.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221566; ENSP00000221566; ENSG00000104969.

GeneID

6449.

KEGG

hsa:6449.

UCSC

uc002lwi.1. human.

Organism-specific databases

CTD

6449.

GeneCards

GC19M002754.

HGNC

HGNC:10819. SGTA.

HPA

HPA056309.

MIM

603419. gene.

neXtProt

NX_O43765.

PharmGKB

PA35727.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0457.

HOGENOM

HOG000208193.

HOVERGEN

HBG000885.

InParanoid

O43765.

KO

K16365.

OMA

VRDCERA.

OrthoDB

EOG4DJJWZ.

PhylomeDB

O43765.

Gene expression databases

Bgee

O43765.

CleanEx

HS_SGTA.

Genevestigator

O43765.

GermOnline

ENSG00000104969. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF00515. TPR_1. 3 hits.
[Graphical view]

SMART

SM00028. TPR. 3 hits.
[Graphical view]

PROSITE

PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O43765.

GenomeRNAi

6449.

NextBio

25065.

SOURCE

Search...

Entry information

Entry name

SGTA_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.