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Protein

Small glutamine-rich tetratricopeptide repeat-containing protein beta

Gene

SGTB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.By similarity

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Small glutamine-rich tetratricopeptide repeat-containing protein beta
Alternative name(s):
Beta-SGT
Small glutamine-rich protein with tetratricopeptide repeats 2
Gene namesi
Name:SGTB
Synonyms:SGT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:23567. SGTB.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134957805.

Polymorphism and mutation databases

BioMutaiSGTB.
DMDMi41018109.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Small glutamine-rich tetratricopeptide repeat-containing protein betaPRO_0000106368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei293 – 2931PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei297 – 2971PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96EQ0.
MaxQBiQ96EQ0.
PaxDbiQ96EQ0.
PeptideAtlasiQ96EQ0.
PRIDEiQ96EQ0.

PTM databases

iPTMnetiQ96EQ0.
PhosphoSiteiQ96EQ0.

Expressioni

Gene expression databases

BgeeiQ96EQ0.
CleanExiHS_SGTB.
ExpressionAtlasiQ96EQ0. baseline and differential.
GenevisibleiQ96EQ0. HS.

Organism-specific databases

HPAiHPA044689.
HPA063674.

Interactioni

Subunit structurei

Homooligomerize.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EFEMP2O959674EBI-744081,EBI-743414
IL6STQ17RA03EBI-744081,EBI-10238517
RAI2Q9Y5P34EBI-744081,EBI-746228
SERPINE1P051213EBI-744081,EBI-953978
TXNDC12O958813EBI-744081,EBI-2564581

Protein-protein interaction databases

BioGridi120042. 86 interactions.
IntActiQ96EQ0. 85 interactions.
MINTiMINT-1471872.
STRINGi9606.ENSP00000370395.

Structurei

3D structure databases

ProteinModelPortaliQ96EQ0.
SMRiQ96EQ0. Positions 5-49, 80-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati15 – 4935TPR 1Add
BLAST
Repeati85 – 11834TPR 2Add
BLAST
Repeati119 – 15234TPR 3Add
BLAST
Repeati153 – 18634TPR 4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 27913Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the SGT family.Curated
Contains 4 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0553. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00730000110724.
HOGENOMiHOG000208193.
HOVERGENiHBG000885.
InParanoidiQ96EQ0.
OMAiGMMSNAI.
OrthoDBiEOG78SQJJ.
PhylomeDBiQ96EQ0.
TreeFamiTF313092.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR032374. SGTA_dimer.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF16546. SGTA_dimer. 1 hit.
PF00515. TPR_1. 1 hit.
PF13414. TPR_11. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96EQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIKHLVYA VIRFLREQSQ MDTYTSDEQE SLEVAIQCLE TVFKISPEDT
60 70 80 90 100
HLAVSQPLTE MFTSSFCKND VLPLSNSVPE DVGKADQLKD EGNNHMKEEN
110 120 130 140 150
YAAAVDCYTQ AIELDPNNAV YYCNRAAAQS KLGHYTDAIK DCEKAIAIDS
160 170 180 190 200
KYSKAYGRMG LALTALNKFE EAVTSYQKAL DLDPENDSYK SNLKIAEQKL
210 220 230 240 250
REVSSPTGTG LSFDMASLIN NPAFISMAAS LMQNPQVQQL MSGMMTNAIG
260 270 280 290 300
GPAAGVGGLT DLSSLIQAGQ QFAQQIQQQN PELIEQLRNH IRSRSFSSSA

EEHS
Length:304
Mass (Da):33,429
Last modified:December 1, 2001 - v1
Checksum:i10819155C4E150FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368281 mRNA. Translation: AAP29459.1.
AK096321 mRNA. Translation: BAC04761.1.
BC012044 mRNA. Translation: AAH12044.1.
CCDSiCCDS3988.1.
RefSeqiNP_061945.1. NM_019072.2.
XP_005248605.1. XM_005248548.2.
UniGeneiHs.482301.
Hs.707786.

Genome annotation databases

EnsembliENST00000381007; ENSP00000370395; ENSG00000197860.
GeneIDi54557.
KEGGihsa:54557.
UCSCiuc003jud.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368281 mRNA. Translation: AAP29459.1.
AK096321 mRNA. Translation: BAC04761.1.
BC012044 mRNA. Translation: AAH12044.1.
CCDSiCCDS3988.1.
RefSeqiNP_061945.1. NM_019072.2.
XP_005248605.1. XM_005248548.2.
UniGeneiHs.482301.
Hs.707786.

3D structure databases

ProteinModelPortaliQ96EQ0.
SMRiQ96EQ0. Positions 5-49, 80-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120042. 86 interactions.
IntActiQ96EQ0. 85 interactions.
MINTiMINT-1471872.
STRINGi9606.ENSP00000370395.

PTM databases

iPTMnetiQ96EQ0.
PhosphoSiteiQ96EQ0.

Polymorphism and mutation databases

BioMutaiSGTB.
DMDMi41018109.

Proteomic databases

EPDiQ96EQ0.
MaxQBiQ96EQ0.
PaxDbiQ96EQ0.
PeptideAtlasiQ96EQ0.
PRIDEiQ96EQ0.

Protocols and materials databases

DNASUi54557.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381007; ENSP00000370395; ENSG00000197860.
GeneIDi54557.
KEGGihsa:54557.
UCSCiuc003jud.4. human.

Organism-specific databases

CTDi54557.
GeneCardsiSGTB.
HGNCiHGNC:23567. SGTB.
HPAiHPA044689.
HPA063674.
neXtProtiNX_Q96EQ0.
PharmGKBiPA134957805.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0553. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00730000110724.
HOGENOMiHOG000208193.
HOVERGENiHBG000885.
InParanoidiQ96EQ0.
OMAiGMMSNAI.
OrthoDBiEOG78SQJJ.
PhylomeDBiQ96EQ0.
TreeFamiTF313092.

Miscellaneous databases

GenomeRNAii54557.
PROiQ96EQ0.

Gene expression databases

BgeeiQ96EQ0.
CleanExiHS_SGTB.
ExpressionAtlasiQ96EQ0. baseline and differential.
GenevisibleiQ96EQ0. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR032374. SGTA_dimer.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF16546. SGTA_dimer. 1 hit.
PF00515. TPR_1. 1 hit.
PF13414. TPR_11. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Tobaben S., Stahl B.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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: Uterus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiSGTB_HUMAN
AccessioniPrimary (citable) accession number: Q96EQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.