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

Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial

Gene

GATC

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

GO - Biological processi

  • glutaminyl-tRNAGln biosynthesis via transamidation Source: UniProtKB
  • mitochondrial translation Source: UniProtKB
  • regulation of translational fidelity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.5.7. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrialUniRule annotation (EC:6.3.5.-UniRule annotation)
Short name:
Glu-AdT subunit CUniRule annotation
Alternative name(s):
Protein 15E1.2
Gene namesi
Name:GATCUniRule annotation
Synonyms:15E1.2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:25068. GATC.

Subcellular locationi

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

PharmGKBiPA162389278.

Polymorphism and mutation databases

BioMutaiGATC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 136Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrialPRO_0000105365
Transit peptidei1 – ?MitochondrionUniRule annotation

Proteomic databases

EPDiO43716.
MaxQBiO43716.
PaxDbiO43716.
PRIDEiO43716.

PTM databases

PhosphoSiteiO43716.

Expressioni

Gene expression databases

BgeeiO43716.
CleanExiHS_GATC.
ExpressionAtlasiO43716. baseline and differential.
GenevisibleiO43716. HS.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SRSF11Q055193EBI-6929453,EBI-1051785

Protein-protein interaction databases

BioGridi129569. 22 interactions.
DIPiDIP-48969N.
IntActiO43716. 5 interactions.
STRINGi9606.ENSP00000446872.

Structurei

3D structure databases

ProteinModelPortaliO43716.
SMRiO43716. Positions 31-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GatC family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4247. Eukaryota.
ENOG4111XXR. LUCA.
GeneTreeiENSGT00390000018351.
HOGENOMiHOG000043885.
HOVERGENiHBG095154.
InParanoidiO43716.
KOiK02435.
OMAiCVEDLLQ.
PhylomeDBiO43716.

Family and domain databases

HAMAPiMF_00122. GatC.
InterProiIPR003837. Asp/Glu-ADT_csu.
[Graphical view]
PfamiPF02686. Glu-tRNAGln. 1 hit.
[Graphical view]
SUPFAMiSSF141000. SSF141000. 1 hit.
TIGRFAMsiTIGR00135. gatC. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O43716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWSRLVWLGL RAPLGGRQGF TSKADPQGSG RITAAVIEHL ERLALVDFGS
60 70 80 90 100
REAVARLEKA IAFADRLRAV DTDGVEPMES VLEDRCLYLR SDNVVEGNCA
110 120 130
DELLQNSHRV VEEYFVAPPG NISLPKLDEQ EPFPHS
Length:136
Mass (Da):15,086
Last modified:June 1, 1998 - v1
Checksum:i113118E9507234E4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31S → L.
Corresponds to variant rs17431446 [ dbSNP | Ensembl ].
VAR_049129

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094319 mRNA. Translation: BAG52859.1.
AL021546 Genomic DNA. Translation: CAA16496.1.
BC107145 mRNA. Translation: AAI07146.1.
BC107146 mRNA. Translation: AAI07147.1.
CCDSiCCDS31911.1.
PIRiT09477.
RefSeqiNP_789788.1. NM_176818.2.
UniGeneiHs.706889.

Genome annotation databases

EnsembliENST00000551765; ENSP00000446872; ENSG00000257218.
GeneIDi283459.
KEGGihsa:283459.
UCSCiuc010szi.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094319 mRNA. Translation: BAG52859.1.
AL021546 Genomic DNA. Translation: CAA16496.1.
BC107145 mRNA. Translation: AAI07146.1.
BC107146 mRNA. Translation: AAI07147.1.
CCDSiCCDS31911.1.
PIRiT09477.
RefSeqiNP_789788.1. NM_176818.2.
UniGeneiHs.706889.

3D structure databases

ProteinModelPortaliO43716.
SMRiO43716. Positions 31-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129569. 22 interactions.
DIPiDIP-48969N.
IntActiO43716. 5 interactions.
STRINGi9606.ENSP00000446872.

PTM databases

PhosphoSiteiO43716.

Polymorphism and mutation databases

BioMutaiGATC.

Proteomic databases

EPDiO43716.
MaxQBiO43716.
PaxDbiO43716.
PRIDEiO43716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000551765; ENSP00000446872; ENSG00000257218.
GeneIDi283459.
KEGGihsa:283459.
UCSCiuc010szi.3. human.

Organism-specific databases

CTDi283459.
GeneCardsiGATC.
HGNCiHGNC:25068. GATC.
neXtProtiNX_O43716.
PharmGKBiPA162389278.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4247. Eukaryota.
ENOG4111XXR. LUCA.
GeneTreeiENSGT00390000018351.
HOGENOMiHOG000043885.
HOVERGENiHBG095154.
InParanoidiO43716.
KOiK02435.
OMAiCVEDLLQ.
PhylomeDBiO43716.

Enzyme and pathway databases

BRENDAi6.3.5.7. 2681.

Miscellaneous databases

ChiTaRSiGATC. human.
GenomeRNAii283459.
PROiO43716.

Gene expression databases

BgeeiO43716.
CleanExiHS_GATC.
ExpressionAtlasiO43716. baseline and differential.
GenevisibleiO43716. HS.

Family and domain databases

HAMAPiMF_00122. GatC.
InterProiIPR003837. Asp/Glu-ADT_csu.
[Graphical view]
PfamiPF02686. Glu-tRNAGln. 1 hit.
[Graphical view]
SUPFAMiSSF141000. SSF141000. 1 hit.
TIGRFAMsiTIGR00135. gatC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Cerebellum.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
  4. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGATC_HUMAN
AccessioniPrimary (citable) accession number: O43716
Secondary accession number(s): B3KSU7, Q3B824, Q3KNR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 111 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 12
    Human chromosome 12: 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. 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.