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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial

Gene

GATB

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

Functioni

Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).UniRule annotation1 Publication

Catalytic activityi

ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.UniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Source: UniProtKB
  • translation factor activity, RNA binding Source: ProtInc

GO - Biological processi

  • glutaminyl-tRNAGln biosynthesis via transamidation Source: UniProtKB
  • mitochondrial translation Source: UniProtKB
  • translation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00732-MONOMER.
BRENDAi6.3.5.7. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrialUniRule annotation (EC:6.3.5.-UniRule annotation)
Short name:
Glu-AdT subunit BUniRule annotation
Alternative name(s):
Cytochrome c oxidase assembly factor PET112 homolog
Gene namesi
Name:GATBUniRule annotationImported
Synonyms:PET112UniRule annotation, PET112LUniRule annotation
ORF Names:HSPC199
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:8849. GATB.

Subcellular locationi

  • Mitochondrion UniRule annotation1 Publication

GO - Cellular componenti

  • glutamyl-tRNA(Gln) amidotransferase complex Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi5188.
OpenTargetsiENSG00000059691.
PharmGKBiPA33191.

Chemistry databases

DrugBankiDB00130. L-Glutamine.

Polymorphism and mutation databases

BioMutaiPET112.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30MitochondrionUniRule annotation1 PublicationAdd BLAST30
ChainiPRO_000001071031 – 557Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrialAdd BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei529N6-succinyllysineBy similarity1

Proteomic databases

EPDiO75879.
PaxDbiO75879.
PeptideAtlasiO75879.
PRIDEiO75879.

PTM databases

iPTMnetiO75879.
PhosphoSitePlusiO75879.

Expressioni

Tissue specificityi

Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle and heart.1 Publication

Gene expression databases

BgeeiENSG00000059691.
CleanExiHS_PET112L.
ExpressionAtlasiO75879. baseline and differential.
GenevisibleiO75879. HS.

Organism-specific databases

HPAiHPA042610.

Interactioni

Subunit structurei

Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.

Protein-protein interaction databases

BioGridi111211. 9 interactors.
DIPiDIP-48968N.
STRINGi9606.ENSP00000263985.

Structurei

3D structure databases

ProteinModelPortaliO75879.
SMRiO75879.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GatB/GatE family. GatB subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2438. Eukaryota.
COG0064. LUCA.
GeneTreeiENSGT00390000016644.
HOGENOMiHOG000223743.
HOVERGENiHBG003160.
InParanoidiO75879.
KOiK02434.
OMAiRAMRTKE.
OrthoDBiEOG091G099P.
PhylomeDBiO75879.
TreeFamiTF314355.

Family and domain databases

HAMAPiMF_00121. GatB. 1 hit.
InterProiIPR004413. Apn/Gln-ADT_bsu.
IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
IPR018027. Asn/Gln_amidotransferase.
IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]
PANTHERiPTHR11659. PTHR11659. 1 hit.
PfamiPF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTiSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMiSSF89095. SSF89095. 1 hit.
TIGRFAMsiTIGR00133. gatB. 1 hit.
PROSITEiPS01234. GATB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPMLRWGC RGRRWAFARV DGGSCHRRGA PTGSTSNQIR GESSVAQQPL
60 70 80 90 100
HTAQKTRKGE HKWAAVVGLE IHAQISSNSK LFSGSQVRFS APPNSLVSFF
110 120 130 140 150
DASLPGTLPV LNRRCVEAAV MTGLALNCHI NKKSLFDRKH YFYADLPAGY
160 170 180 190 200
QITQQRLPIA VNGSLIYGVC AGKKQSQVIP KTVRIKQIQL EQDSGKSLHD
210 220 230 240 250
NLRSQTLIDL NRAGVGLLEV VLEPDMSCGE EAATAVRELQ LILQALGTSQ
260 270 280 290 300
ANMAEGQLRV DANISVHHPG EPLGVRTEVK NLNSIRFLAK AIDYEIQRQI
310 320 330 340 350
NELENGGEIL NETRSFHHKL GCTMSMRDKE GKQDYRFMPE PNLPPLVLYD
360 370 380 390 400
ATSLPAGADP QQVINIDQIR ETLPELPSVT REKLVQQYGM LLEHSFTLLN
410 420 430 440 450
EVGLLEFFQN VIKETRAEPK KVTSWVLNTF LGYLKQQNLA VSESPVTPSA
460 470 480 490 500
LAELLDLLDS RTISSSAAKQ VFEELWKREG KTPGQIVSEK QLELMQDQGA
510 520 530 540 550
LEQLCHSVME AHPQVVMDVK NRNPRAINKL IGLVRKATQS RADPVMIKEI

LEKKLSL
Length:557
Mass (Da):61,864
Last modified:November 1, 1998 - v1
Checksum:i449EB3EA2FD4769D
GO

Sequence cautioni

The sequence AAF36119 differs from that shown. Reason: Frameshift at position 420.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti317H → R in BAD96607 (Ref. 4) Curated1
Sequence conflicti418 – 419EP → DK in AAF36119 (PubMed:11042152).Curated2
Sequence conflicti521N → D in BAD96607 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04912830A → D.Corresponds to variant rs11556167dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026851 mRNA. Translation: AAD08640.1.
AF151033 mRNA. Translation: AAF36119.1. Frameshift.
AK312957 mRNA. Translation: BAG35796.1.
AK222887 mRNA. Translation: BAD96607.1.
AC092611 Genomic DNA. Translation: AAY40897.1.
CH471056 Genomic DNA. Translation: EAX04981.1.
BC130348 mRNA. Translation: AAI30349.1.
BC136547 mRNA. Translation: AAI36548.1.
AB019410 mRNA. No translation available.
CCDSiCCDS3776.1.
RefSeqiNP_004555.1. NM_004564.2.
UniGeneiHs.119316.
Hs.636045.

Genome annotation databases

EnsembliENST00000263985; ENSP00000263985; ENSG00000059691.
GeneIDi5188.
KEGGihsa:5188.
UCSCiuc003iml.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026851 mRNA. Translation: AAD08640.1.
AF151033 mRNA. Translation: AAF36119.1. Frameshift.
AK312957 mRNA. Translation: BAG35796.1.
AK222887 mRNA. Translation: BAD96607.1.
AC092611 Genomic DNA. Translation: AAY40897.1.
CH471056 Genomic DNA. Translation: EAX04981.1.
BC130348 mRNA. Translation: AAI30349.1.
BC136547 mRNA. Translation: AAI36548.1.
AB019410 mRNA. No translation available.
CCDSiCCDS3776.1.
RefSeqiNP_004555.1. NM_004564.2.
UniGeneiHs.119316.
Hs.636045.

3D structure databases

ProteinModelPortaliO75879.
SMRiO75879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111211. 9 interactors.
DIPiDIP-48968N.
STRINGi9606.ENSP00000263985.

Chemistry databases

DrugBankiDB00130. L-Glutamine.

PTM databases

iPTMnetiO75879.
PhosphoSitePlusiO75879.

Polymorphism and mutation databases

BioMutaiPET112.

Proteomic databases

EPDiO75879.
PaxDbiO75879.
PeptideAtlasiO75879.
PRIDEiO75879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263985; ENSP00000263985; ENSG00000059691.
GeneIDi5188.
KEGGihsa:5188.
UCSCiuc003iml.5. human.

Organism-specific databases

CTDi5188.
DisGeNETi5188.
GeneCardsiGATB.
HGNCiHGNC:8849. GATB.
HPAiHPA042610.
MIMi603645. gene.
neXtProtiNX_O75879.
OpenTargetsiENSG00000059691.
PharmGKBiPA33191.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2438. Eukaryota.
COG0064. LUCA.
GeneTreeiENSGT00390000016644.
HOGENOMiHOG000223743.
HOVERGENiHBG003160.
InParanoidiO75879.
KOiK02434.
OMAiRAMRTKE.
OrthoDBiEOG091G099P.
PhylomeDBiO75879.
TreeFamiTF314355.

Enzyme and pathway databases

BioCyciZFISH:HS00732-MONOMER.
BRENDAi6.3.5.7. 2681.

Miscellaneous databases

GenomeRNAii5188.
PROiO75879.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000059691.
CleanExiHS_PET112L.
ExpressionAtlasiO75879. baseline and differential.
GenevisibleiO75879. HS.

Family and domain databases

HAMAPiMF_00121. GatB. 1 hit.
InterProiIPR004413. Apn/Gln-ADT_bsu.
IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
IPR018027. Asn/Gln_amidotransferase.
IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]
PANTHERiPTHR11659. PTHR11659. 1 hit.
PfamiPF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTiSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMiSSF89095. SSF89095. 1 hit.
TIGRFAMsiTIGR00133. gatB. 1 hit.
PROSITEiPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGATB_HUMAN
AccessioniPrimary (citable) accession number: O75879
Secondary accession number(s): Q4W5M8
, Q53GP4, Q9P0S6, Q9Y2B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 139 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.