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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial

Gene

Gatb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 annotation

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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 annotation
Synonyms:Pet112UniRule annotation, Pet112lUniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2442496. Gatb.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionUniRule annotationAdd
BLAST
Chaini31 – 557527Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrialPRO_0000010711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei529 – 5291N6-succinyllysineCombined sources

Proteomic databases

EPDiQ99JT1.
MaxQBiQ99JT1.
PaxDbiQ99JT1.
PeptideAtlasiQ99JT1.
PRIDEiQ99JT1.

PTM databases

iPTMnetiQ99JT1.
PhosphoSiteiQ99JT1.

Expressioni

Gene expression databases

BgeeiQ99JT1.
CleanExiMM_PET112L.
ExpressionAtlasiQ99JT1. baseline and differential.
GenevisibleiQ99JT1. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000119949.

Structurei

3D structure databases

ProteinModelPortaliQ99JT1.
SMRiQ99JT1. Positions 62-555.
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.
InParanoidiQ99JT1.
KOiK02434.
OMAiESADYRY.
OrthoDBiEOG769ZJB.
PhylomeDBiQ99JT1.
TreeFamiTF314355.

Family and domain databases

HAMAPiMF_00121. GatB.
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.

Q99JT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPMLRLGF PGRRWALTWL DGGSRHRSGS QTGPTSNWAR RQSSVAQPSL
60 70 80 90 100
HTAQKPRKGE HKWAAVVGLE IHAQISSNSK LFSGAQVCFA APPNSLVSYF
110 120 130 140 150
DASLPGTLPV LNRRCVEAAV MTGLALNCHI NKKSLFDRKH YFYSDLPAGY
160 170 180 190 200
QITQQRLPIA ANGHLTYCIY LGKKPSQVTT KTVRIKQIQL EQDSGKSLHD
210 220 230 240 250
DLRSQTLIDL NRAGIGLLEV VLEPDLCCGE EAALAVRELQ LILQALGTSQ
260 270 280 290 300
ANMAEGQLRV DANISVHHPG EPLGVRTEVK NLNSLRFLAK AIDYEIQRQI
310 320 330 340 350
TELENGGEIL NETRSFDYKL GCTMPMRDKE GKQDYRFMPE PNLPPLVLYD
360 370 380 390 400
DTSLPRGADS QQVINIDQLR DMLPELPSAT RERLVQQYGM LPEHSFALLN
410 420 430 440 450
EVGLLEFFQN VIKETRTEPK KVTNWVLNTF LCYLKQQNLA VSESPVTPSA
460 470 480 490 500
LAELLNLLDR KAISSSAAKQ VFEELWKGEG KTAAQIVSEQ QLELMQDQEA
510 520 530 540 550
LEKLCQTTID GHPQVVMDVK KRNPKAINKL IGLVRKASHS RADPALIKKI

LERKLSL
Length:557
Mass (Da):62,118
Last modified:June 1, 2001 - v1
Checksum:iCD8D0EDFE595B1B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111N → S in BAC38336 (PubMed:16141072).Curated
Sequence conflicti508 – 5081T → P in BAC25803 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028193 mRNA. Translation: BAC25803.1.
AK034702 mRNA. Translation: BAC28801.1.
AK081800 mRNA. Translation: BAC38336.1.
BC005709 mRNA. Translation: AAH05709.1.
CCDSiCCDS17441.1.
RefSeqiNP_659145.1. NM_144896.4.
UniGeneiMm.393738.
Mm.52275.

Genome annotation databases

EnsembliENSMUST00000127348; ENSMUSP00000119949; ENSMUSG00000028085.
GeneIDi229487.
KEGGimmu:229487.
UCSCiuc008pqs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028193 mRNA. Translation: BAC25803.1.
AK034702 mRNA. Translation: BAC28801.1.
AK081800 mRNA. Translation: BAC38336.1.
BC005709 mRNA. Translation: AAH05709.1.
CCDSiCCDS17441.1.
RefSeqiNP_659145.1. NM_144896.4.
UniGeneiMm.393738.
Mm.52275.

3D structure databases

ProteinModelPortaliQ99JT1.
SMRiQ99JT1. Positions 62-555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000119949.

PTM databases

iPTMnetiQ99JT1.
PhosphoSiteiQ99JT1.

Proteomic databases

EPDiQ99JT1.
MaxQBiQ99JT1.
PaxDbiQ99JT1.
PeptideAtlasiQ99JT1.
PRIDEiQ99JT1.

Protocols and materials databases

DNASUi229487.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000127348; ENSMUSP00000119949; ENSMUSG00000028085.
GeneIDi229487.
KEGGimmu:229487.
UCSCiuc008pqs.1. mouse.

Organism-specific databases

CTDi5188.
MGIiMGI:2442496. Gatb.

Phylogenomic databases

eggNOGiKOG2438. Eukaryota.
COG0064. LUCA.
GeneTreeiENSGT00390000016644.
HOGENOMiHOG000223743.
HOVERGENiHBG003160.
InParanoidiQ99JT1.
KOiK02434.
OMAiESADYRY.
OrthoDBiEOG769ZJB.
PhylomeDBiQ99JT1.
TreeFamiTF314355.

Miscellaneous databases

PROiQ99JT1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JT1.
CleanExiMM_PET112L.
ExpressionAtlasiQ99JT1. baseline and differential.
GenevisibleiQ99JT1. MM.

Family and domain databases

HAMAPiMF_00121. GatB.
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...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiGATB_MOUSE
AccessioniPrimary (citable) accession number: Q99JT1
Secondary accession number(s): Q8BMU3, Q8BUY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.