Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Small glutamine-rich tetratricopeptide repeat-containing protein alpha

Gene

SGTA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10819. SGTA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35727.

Polymorphism and mutation databases

BioMutaiSGTA.

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 – 811Phosphothreonine3 Publications
Modified residuei137 – 1371N6-acetyllysine1 Publication
Modified residuei301 – 3011Phosphoserine2 Publications
Modified residuei303 – 3031Phosphothreonine3 Publications
Modified residuei305 – 3051Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO43765.
PaxDbiO43765.
PeptideAtlasiO43765.
PRIDEiO43765.

PTM databases

PhosphoSiteiO43765.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO43765.
CleanExiHS_SGTA.
ExpressionAtlasiO43765. baseline and differential.
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
ADIPOQA8K6603EBI-347996,EBI-10174479
AGR3Q8TD063EBI-347996,EBI-3925742
BAG2O958162EBI-347996,EBI-355275
BAG6P463795EBI-347996,EBI-347552
C19orf10Q969H83EBI-347996,EBI-718622
C1QTNF1Q9BXJ14EBI-347996,EBI-750200
C1QTNF6Q9BXI93EBI-347996,EBI-10301084
CARKDQ8IW454EBI-347996,EBI-8650724
CCDC155Q8N6L03EBI-347996,EBI-749265
CD79BP402593EBI-347996,EBI-2873732
CDH15P552913EBI-347996,EBI-10215061
COL1A2P081233EBI-347996,EBI-983038
COL8A2Q4VAQ03EBI-347996,EBI-10241815
CSF1P096033EBI-347996,EBI-2872294
CST1P010373EBI-347996,EBI-1056240
CTSLP077113EBI-347996,EBI-1220160
EFEMP1Q128054EBI-347996,EBI-536772
EFEMP2O959674EBI-347996,EBI-743414
ERP27Q96DN03EBI-347996,EBI-953772
EVA1BQ9NVM13EBI-347996,EBI-10314666
F11RQ9Y6245EBI-347996,EBI-742600
FERD3LQ96RJ63EBI-347996,EBI-10183007
FKBP7Q9Y6803EBI-347996,EBI-3918971
FXYD7P585495EBI-347996,EBI-10216171
GALP224663EBI-347996,EBI-6624768
GIPP096813EBI-347996,EBI-8588553
GPErikQ144403EBI-347996,EBI-10232920
GRNP287993EBI-347996,EBI-747754
GYPAB8Q1834EBI-347996,EBI-10176190
HSPA13P487233EBI-347996,EBI-750892
IGL@Q6PIQ73EBI-347996,EBI-6677651
IGL@Q8N3554EBI-347996,EBI-748681
IRF3Q146533EBI-347996,EBI-2650369
IRF5Q135683EBI-347996,EBI-3931258
ITPRIPL1Q6GPH63EBI-347996,EBI-953819
KRT6AP025383EBI-347996,EBI-702198
KTN1Q86UP23EBI-347996,EBI-359761
LAIR2Q6ISS43EBI-347996,EBI-10250491
LATO435613EBI-347996,EBI-1222766
MSMBP081183EBI-347996,EBI-10195681
NME3Q132324EBI-347996,EBI-713684
PAUFC3PTT63EBI-347996,EBI-3505892
PBXIP1Q96AQ63EBI-347996,EBI-740845
PCDHA4Q9UN743EBI-347996,EBI-712273
PPIBP232843EBI-347996,EBI-359252
PPICP458773EBI-347996,EBI-953909
PRAP1Q96NZ93EBI-347996,EBI-2116102
RARRES3Q9UL193EBI-347996,EBI-10323452
RPN1P048433EBI-347996,EBI-355963
SDC4P314313EBI-347996,EBI-3913237
SERPINE1P051213EBI-347996,EBI-953978
SGCAQ165864EBI-347996,EBI-5663553
SLPIP039733EBI-347996,EBI-355293
SMAGPQ0VAQ43EBI-347996,EBI-10226799
SOD3P082943EBI-347996,EBI-10195782
SPP1P104515EBI-347996,EBI-723648
SPPL2AQ8TCT84EBI-347996,EBI-750784
SRGNP101244EBI-347996,EBI-744915
SYT11Q9BT884EBI-347996,EBI-751770
SYT4Q9H2B24EBI-347996,EBI-751132
TFF3Q076543EBI-347996,EBI-10224676
TFRCP027863EBI-347996,EBI-355727
TGFAP011353EBI-347996,EBI-1034374
TMEM174Q8WUU83EBI-347996,EBI-10276729
TMEM31Q5JXX73EBI-347996,EBI-10244617
TMUB2Q71RG43EBI-347996,EBI-2820477
TNFRSF13BO148363EBI-347996,EBI-519160
TTMPQ5BVD13EBI-347996,EBI-10243654
TWSG1Q9GZX93EBI-347996,EBI-10304067
TXNDC12O958813EBI-347996,EBI-2564581
UPK3AO756313EBI-347996,EBI-10188907
VIPP012823EBI-347996,EBI-751454
WBP1LQ9NX943EBI-347996,EBI-10316321
ZG16O608444EBI-347996,EBI-746479

Protein-protein interaction databases

BioGridi112347. 128 interactions.
IntActiO43765. 118 interactions.
MINTiMINT-1035135.
STRINGi9606.ENSP00000221566.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2117Combined sources
Helixi26 – 4318Combined sources
Helixi48 – 514Combined sources
Helixi58 – 658Combined sources
Helixi87 – 10317Combined sources
Helixi107 – 12014Combined sources
Helixi125 – 13713Combined sources
Helixi141 – 15414Combined sources
Helixi159 – 17113Combined sources
Helixi175 – 18814Combined sources
Helixi193 – 20614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYIX-ray2.40A/B84-210[»]
4CPGNMR-A/B1-69[»]
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.
GeneTreeiENSGT00730000110724.
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_dom.
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

        10         20         30         40         50
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS
60 70 80 90 100
DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE
110 120 130 140 150
QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER
160 170 180 190 200
AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK
210 220 230 240 250
IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM
260 270 280 290 300
ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR
310
SRTPSASNDD QQE
Length:313
Mass (Da):34,063
Last modified:June 1, 1998 - v1
Checksum:i80B3C71B41F3CB55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Polymorphism and mutation databases

BioMutaiSGTA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VYIX-ray2.40A/B84-210[»]
4CPGNMR-A/B1-69[»]
4GODX-ray1.40A/B4-54[»]
4GOEX-ray1.45A/B4-54[»]
4GOFX-ray1.35A/B4-54[»]
ProteinModelPortaliO43765.
SMRiO43765. Positions 4-54, 86-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112347. 128 interactions.
IntActiO43765. 118 interactions.
MINTiMINT-1035135.
STRINGi9606.ENSP00000221566.

PTM databases

PhosphoSiteiO43765.

Polymorphism and mutation databases

BioMutaiSGTA.

Proteomic databases

MaxQBiO43765.
PaxDbiO43765.
PeptideAtlasiO43765.
PRIDEiO43765.

Protocols and materials databases

DNASUi6449.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6449.
GeneCardsiGC19M002754.
HGNCiHGNC:10819. SGTA.
HPAiHPA056309.
MIMi603419. gene.
neXtProtiNX_O43765.
PharmGKBiPA35727.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00730000110724.
HOGENOMiHOG000208193.
HOVERGENiHBG000885.
InParanoidiO43765.
KOiK16365.
OMAiASGQHEK.
OrthoDBiEOG78SQJJ.
PhylomeDBiO43765.
TreeFamiTF313092.

Miscellaneous databases

ChiTaRSiSGTA. human.
EvolutionaryTraceiO43765.
GeneWikiiSGTA.
GenomeRNAii6449.
NextBioi25065.
PROiO43765.
SOURCEiSearch...

Gene expression databases

BgeeiO43765.
CleanExiHS_SGTA.
ExpressionAtlasiO43765. baseline and differential.
GenevestigatoriO43765.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81; THR-303 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "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: April 29, 2015
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.