Q96RP9 (EFGM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor G, mitochondrial
Short name=EF-Gmt

Alternative name(s):
Elongation factor G 1, mitochondrial
Short name=mEF-G 1
Elongation factor G1
Short name=hEFG1

Gene names

Name:	GFM1
Synonyms:	EFG, EFG1, GFM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	751 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Ref.8
Pathway	Protein biosynthesis; polypeptide chain elongation. Ref.8
Subcellular location	Mitochondrion By similarity.
Involvement in disease	Combined oxidative phosphorylation deficiency 1 (COXPD1) [MIM:609060]: A mitochondrial disease resulting in early rapidly progressive hepatoencephalopathy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
Sequence caution	The sequence EAW78682.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial translational elongation Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay Ref.8. Source: UniProtKB translation elongation factor activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96RP9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q96RP9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     230-230: G → GHFLRDFLPLLWNWDRRSGS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 35	35	Mitochondrion Potential
	Chain	36 – 751	716	Elongation factor G, mitochondrial		PRO_0000007440
Regions
	Nucleotide binding	53 – 60	8	GTP By similarity
	Nucleotide binding	120 – 124	5	GTP By similarity
	Nucleotide binding	174 – 177	4	GTP By similarity
Amino acid modifications
	Modified residue	175	1	N6-acetyllysine Ref.9
Natural variations
	Alternative sequence	230	1	G → GHFLRDFLPLLWNWDRRSGS in isoform 2.		VSP_038189
	Natural variant	174	1	N → S in COXPD1. Ref.11 Corresponds to variant rs28939098 [ dbSNP | Ensembl ].		VAR_021512
	Natural variant	215	1	V → I. Ref.3 Corresponds to variant rs2303909 [ dbSNP | Ensembl ].		VAR_028303
	Natural variant	496	1	M → R in COXPD1. Ref.12		VAR_031901
Experimental info
	Sequence conflict	373	1	S → C in AAK58877. Ref.1
	Sequence conflict	578	1	I → M in AAK58877. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 5937FFB24A089E2E	FASTA	751	83,471
	10 20 30 40 50 60 MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG ISAHIDSGKT 70 80 90 100 110 120 TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI TIQSAATYTM WKDVNINIID 130 140 150 160 170 180 TPGHVDFTIE VERALRVLDG AVLVLCAVGG VQCQTMTVNR QMKRYNVPFL TFINKLDRMG 190 200 210 220 230 240 SNPARALQQM RSKLNHNAAF MQIPMGLEGN FKGIVDLIEE RAIYFDGDFG QIVRYGEIPA 250 260 270 280 290 300 ELRAAATDHR QELIECVANS DEQLGEMFLE EKIPSISDLK LAIRRATLKR SFTPVFLGSA 310 320 330 340 350 360 LKNKGVQPLL DAVLEYLPNP SEVQNYAILN KEDDSKEKTK ILMNSSRDNS HPFVGLAFKL 370 380 390 400 410 420 EVGRFGQLTY VRSYQGELKK GDTIYNTRTR KKVRLQRLAR MHADMMEDVE EVYAGDICAL 430 440 450 460 470 480 FGIDCASGDT FTDKANSGLS MESIHVPDPV ISIAMKPSNK NDLEKFSKGI GRFTREDPTF 490 500 510 520 530 540 KVYFDTENKE TVISGMGELH LEIYAQRLER EYGCPCITGK PKVAFRETIT APVPFDFTHK 550 560 570 580 590 600 KQSGGAGQYG KVIGVLEPLD PEDYTKLEFS DETFGSNIPK QFVPAVEKGF LDACEKGPLS 610 620 630 640 650 660 GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAN ATLCILEPIM AVEVVAPNEF 670 680 690 700 710 720 QGQVIAGINR RHGVITGQDG VEDYFTLYAD VPLNDMFGYS TELRSCTEGK GEYTMEYSRY 730 740 750 QPCLPSTQED VINKYLEATG QLPVKKGKAK N
	Isoform 2 [UniParc]. Checksum: 02D5772EF01F8208	FASTA	770	85,869
	10 20 30 40 50 60 MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG ISAHIDSGKT 70 80 90 100 110 120 TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI TIQSAATYTM WKDVNINIID 130 140 150 160 170 180 TPGHVDFTIE VERALRVLDG AVLVLCAVGG VQCQTMTVNR QMKRYNVPFL TFINKLDRMG 190 200 210 220 230 240 SNPARALQQM RSKLNHNAAF MQIPMGLEGN FKGIVDLIEE RAIYFDGDFG HFLRDFLPLL 250 260 270 280 290 300 WNWDRRSGSQ IVRYGEIPAE LRAAATDHRQ ELIECVANSD EQLGEMFLEE KIPSISDLKL 310 320 330 340 350 360 AIRRATLKRS FTPVFLGSAL KNKGVQPLLD AVLEYLPNPS EVQNYAILNK EDDSKEKTKI 370 380 390 400 410 420 LMNSSRDNSH PFVGLAFKLE VGRFGQLTYV RSYQGELKKG DTIYNTRTRK KVRLQRLARM 430 440 450 460 470 480 HADMMEDVEE VYAGDICALF GIDCASGDTF TDKANSGLSM ESIHVPDPVI SIAMKPSNKN 490 500 510 520 530 540 DLEKFSKGIG RFTREDPTFK VYFDTENKET VISGMGELHL EIYAQRLERE YGCPCITGKP 550 560 570 580 590 600 KVAFRETITA PVPFDFTHKK QSGGAGQYGK VIGVLEPLDP EDYTKLEFSD ETFGSNIPKQ 610 620 630 640 650 660 FVPAVEKGFL DACEKGPLSG HKLSGLRFVL QDGAHHMVDS NEISFIRAGE GALKQALANA 670 680 690 700 710 720 TLCILEPIMA VEVVAPNEFQ GQVIAGINRR HGVITGQDGV EDYFTLYADV PLNDMFGYST 730 740 750 760 770 ELRSCTEGKG EYTMEYSRYQ PCLPSTQEDV INKYLEATGQ LPVKKGKAKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human and mouse mitochondrial elongation factor G, GFM and gfm, and mapping of GFM to human chromosome 3q25.1-q26.2." Gao J., Yu L., Zhang P., Jiang J., Chen J., Peng J., Wei Y., Zhao S. Genomics 74:109-114(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Identification and characterization of two novel human mitochondrial elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved through evolution." Hammarsund M., Wilson W., Corcoran M., Merup M., Einhorn S., Grander D., Sangfelt O. Hum. Genet. 109:542-550(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-751 (ISOFORM 2), VARIANT ILE-215. Tissue: Placenta and Tongue.
[4]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1). Tissue: Duodenum.
[7]	"Expression and characterization of isoform 1 of human mitochondrial elongation factor G." Bhargava K., Templeton P., Spremulli L.L. Protein Expr. Purif. 37:368-376(2004) [PubMed] [Europe PMC] [Abstract] Cited for: POTENTIAL TRANSIT PEPTIDE.
[8]	"EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis." Tsuboi M., Morita H., Nozaki Y., Akama K., Ueda T., Ito K., Nierhaus K.H., Takeuchi N. Mol. Cell 35:502-510(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PATHWAY.
[9]	"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-175, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Mutant mitochondrial elongation factor G1 and combined oxidative phosphorylation deficiency." Coenen M.J.H., Antonicka H., Ugalde C., Sasarman F., Rossi R., Angelien Heister J.G.A.M., Newbold R.F., Trijbels F.J.M.F., van den Heuvel L.P., Shoubridge E.A., Smeitink J.A.M. N. Engl. J. Med. 351:2080-2086(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT COXPD1 SER-174.
[12]	"Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu." Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E., Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C., Comi G.P., Savasta S., Ferrero I., Zeviani M. Am. J. Hum. Genet. 80:44-58(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT COXPD1 ARG-496.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF309777 mRNA. Translation: AAK58877.1. AF367998 mRNA. Translation: AAK53402.1. AK092293 mRNA. Translation: BAG52523.1. AK315031 mRNA. Translation: BAG37516.1. AC080013 Genomic DNA. No translation available. CH471052 Genomic DNA. Translation: EAW78677.1. CH471052 Genomic DNA. Translation: EAW78682.1. Sequence problems. BC049210 mRNA. Translation: AAH49210.1.
IPI	IPI00154473. IPI00945964.
RefSeq	NP_079272.4. NM_024996.5.
UniGene	Hs.518355.
3D structure databases
ProteinModelPortal	Q96RP9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96RP9. 3 interactions.
STRING	9606.ENSP00000419038.
PTM databases
PhosphoSite	Q96RP9.
Polymorphism databases
DMDM	116241346.
Proteomic databases
PaxDb	Q96RP9.
PRIDE	Q96RP9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264263; ENSP00000264263; ENSG00000168827. ENST00000486715; ENSP00000419038; ENSG00000168827.
GeneID	85476.
KEGG	hsa:85476.
UCSC	uc003fce.3. human. uc003fcg.3. human.
Organism-specific databases
CTD	85476.
GeneCards	GC03P158362.
HGNC	HGNC:13780. GFM1.
HPA	HPA034765.
MIM	606639. gene. 609060. phenotype.
neXtProt	NX_Q96RP9.
Orphanet	137681. Hepatoencephalopathy due to combined oxidative phosphorylation deficiency type 1.
PharmGKB	PA134971637.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0480.
HOGENOM	HOG000231585.
InParanoid	Q96RP9.
KO	K02355.
OMA	FMGSAYK.
OrthoDB	EOG4D52X3.
Enzyme and pathway databases
UniPathway	UPA00345.
Gene expression databases
ArrayExpress	Q96RP9.
Bgee	Q96RP9.
CleanEx	HS_GFM1.
Genevestigator	Q96RP9.
GermOnline	ENSG00000168827. Homo sapiens.
Family and domain databases
Gene3D	3.30.230.10. 1 hit. 3.30.70.240. 1 hit.
InterPro	IPR000795. EF_GTP-bd_dom. IPR009022. EFG_III-V. IPR000640. EFG_V. IPR027417. P-loop_NTPase. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR005225. Small_GTP-bd_dom. IPR004540. Transl_elong_EFG/EF2. IPR005517. Transl_elong_EFG/EF2_IV. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
Pfam	PF00679. EFG_C. 1 hit. PF03764. EFG_IV. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SMART	SM00838. EFG_C. 1 hit. SM00889. EFG_IV. 1 hit. [Graphical view]
SUPFAM	SSF54980. EFG_III_V. 2 hits. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF52540. SSF52540. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00484. EF-G. 1 hit. TIGR00231. small_GTP. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GFM1. human.
GenomeRNAi	85476.
NextBio	76132.
SOURCE	Search...

Entry information

Entry name

EFGM_HUMAN

Accession

Primary (citable) accession number: Q96RP9
Secondary accession number(s): A6NCI9 , B2RCB9, B3KRW1, Q6GTN2, Q96T39

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.