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Protein

Elongation factor G, mitochondrial

Gene

GFM1

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

Functioni

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.UniRule annotation1 Publication

Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi53 – 608GTPUniRule annotation
Nucleotide bindingi120 – 1245GTPUniRule annotation
Nucleotide bindingi174 – 1774GTPUniRule annotation

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-HAMAP
  • poly(A) RNA binding Source: UniProtKB
  • translation elongation factor activity Source: UniProtKB

GO - Biological processi

  • mitochondrial translational elongation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-5389840. Mitochondrial translation elongation.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor G, mitochondrialUniRule annotation
Short name:
EF-GmtUniRule annotation
Alternative name(s):
Elongation factor G 1, mitochondrialUniRule annotation
Short name:
mEF-G 1UniRule annotation
Elongation factor G1UniRule annotation
Short name:
hEFG1
Gene namesi
Name:GFM1UniRule annotation
Synonyms:EFG, EFG1UniRule annotation, GFM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:13780. GFM1.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 1 (COXPD1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA mitochondrial disease resulting in early rapidly progressive hepatoencephalopathy.
See also OMIM:609060
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741N → S in COXPD1. 1 Publication
Corresponds to variant rs28939098 [ dbSNP | Ensembl ].
VAR_021512
Natural varianti496 – 4961M → R in COXPD1. 1 Publication
Corresponds to variant rs119470020 [ dbSNP | Ensembl ].
VAR_031901

Organism-specific databases

MalaCardsiGFM1.
MIMi609060. phenotype.
Orphaneti137681. Hepatoencephalopathy due to combined oxidative phosphorylation deficiency type 1.
PharmGKBiPA134971637.

Polymorphism and mutation databases

BioMutaiGFM1.
DMDMi116241346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636MitochondrionUniRule annotationAdd
BLAST
Chaini37 – 751715Elongation factor G, mitochondrialPRO_0000007440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911PhosphoserineCombined sources
Modified residuei175 – 1751N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96RP9.
MaxQBiQ96RP9.
PaxDbiQ96RP9.
PeptideAtlasiQ96RP9.
PRIDEiQ96RP9.

PTM databases

iPTMnetiQ96RP9.
PhosphoSiteiQ96RP9.

Expressioni

Gene expression databases

BgeeiQ96RP9.
CleanExiHS_GFM1.
ExpressionAtlasiQ96RP9. baseline and differential.
GenevisibleiQ96RP9. HS.

Organism-specific databases

HPAiHPA034764.
HPA034765.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TRIM63Q969Q12EBI-2255048,EBI-5661333

Protein-protein interaction databases

BioGridi124551. 16 interactions.
IntActiQ96RP9. 9 interactions.
STRINGi9606.ENSP00000419038.

Structurei

3D structure databases

ProteinModelPortaliQ96RP9.
SMRiQ96RP9. Positions 42-732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 321278tr-type GAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0465. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00550000074911.
HOGENOMiHOG000231585.
InParanoidiQ96RP9.
KOiK02355.
OMAiGDTFCDP.
OrthoDBiEOG7VDXNM.
PhylomeDBiQ96RP9.
TreeFamiTF105631.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00054_B. EF_G_EF_2_B.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96RP9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG
60 70 80 90 100
ISAHIDSGKT TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI
110 120 130 140 150
TIQSAATYTM WKDVNINIID TPGHVDFTIE VERALRVLDG AVLVLCAVGG
160 170 180 190 200
VQCQTMTVNR QMKRYNVPFL TFINKLDRMG SNPARALQQM RSKLNHNAAF
210 220 230 240 250
MQIPMGLEGN FKGIVDLIEE RAIYFDGDFG QIVRYGEIPA ELRAAATDHR
260 270 280 290 300
QELIECVANS DEQLGEMFLE EKIPSISDLK LAIRRATLKR SFTPVFLGSA
310 320 330 340 350
LKNKGVQPLL DAVLEYLPNP SEVQNYAILN KEDDSKEKTK ILMNSSRDNS
360 370 380 390 400
HPFVGLAFKL EVGRFGQLTY VRSYQGELKK GDTIYNTRTR KKVRLQRLAR
410 420 430 440 450
MHADMMEDVE EVYAGDICAL FGIDCASGDT FTDKANSGLS MESIHVPDPV
460 470 480 490 500
ISIAMKPSNK NDLEKFSKGI GRFTREDPTF KVYFDTENKE TVISGMGELH
510 520 530 540 550
LEIYAQRLER EYGCPCITGK PKVAFRETIT APVPFDFTHK KQSGGAGQYG
560 570 580 590 600
KVIGVLEPLD PEDYTKLEFS DETFGSNIPK QFVPAVEKGF LDACEKGPLS
610 620 630 640 650
GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAN ATLCILEPIM
660 670 680 690 700
AVEVVAPNEF QGQVIAGINR RHGVITGQDG VEDYFTLYAD VPLNDMFGYS
710 720 730 740 750
TELRSCTEGK GEYTMEYSRY QPCLPSTQED VINKYLEATG QLPVKKGKAK

N
Length:751
Mass (Da):83,471
Last modified:October 17, 2006 - v2
Checksum:i5937FFB24A089E2E
GO
Isoform 2 (identifier: Q96RP9-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:770
Mass (Da):85,869
Checksum:i02D5772EF01F8208
GO

Sequence cautioni

The sequence EAW78682.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti373 – 3731S → C in AAK58877 (PubMed:11374907).Curated
Sequence conflicti578 – 5781I → M in AAK58877 (PubMed:11374907).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741N → S in COXPD1. 1 Publication
Corresponds to variant rs28939098 [ dbSNP | Ensembl ].
VAR_021512
Natural varianti215 – 2151V → I.1 Publication
Corresponds to variant rs2303909 [ dbSNP | Ensembl ].
VAR_028303
Natural varianti496 – 4961M → R in COXPD1. 1 Publication
Corresponds to variant rs119470020 [ dbSNP | Ensembl ].
VAR_031901

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei230 – 2301G → GHFLRDFLPLLWNWDRRSGS in isoform 2. 1 PublicationVSP_038189

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33885.1. [Q96RP9-1]
CCDS77851.1. [Q96RP9-2]
RefSeqiNP_001295093.1. NM_001308164.1. [Q96RP9-2]
NP_001295095.1. NM_001308166.1.
NP_079272.4. NM_024996.5. [Q96RP9-1]
UniGeneiHs.518355.

Genome annotation databases

EnsembliENST00000264263; ENSP00000264263; ENSG00000168827. [Q96RP9-2]
ENST00000486715; ENSP00000419038; ENSG00000168827. [Q96RP9-1]
GeneIDi85476.
KEGGihsa:85476.
UCSCiuc003fce.4. human. [Q96RP9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33885.1. [Q96RP9-1]
CCDS77851.1. [Q96RP9-2]
RefSeqiNP_001295093.1. NM_001308164.1. [Q96RP9-2]
NP_001295095.1. NM_001308166.1.
NP_079272.4. NM_024996.5. [Q96RP9-1]
UniGeneiHs.518355.

3D structure databases

ProteinModelPortaliQ96RP9.
SMRiQ96RP9. Positions 42-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124551. 16 interactions.
IntActiQ96RP9. 9 interactions.
STRINGi9606.ENSP00000419038.

PTM databases

iPTMnetiQ96RP9.
PhosphoSiteiQ96RP9.

Polymorphism and mutation databases

BioMutaiGFM1.
DMDMi116241346.

Proteomic databases

EPDiQ96RP9.
MaxQBiQ96RP9.
PaxDbiQ96RP9.
PeptideAtlasiQ96RP9.
PRIDEiQ96RP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264263; ENSP00000264263; ENSG00000168827. [Q96RP9-2]
ENST00000486715; ENSP00000419038; ENSG00000168827. [Q96RP9-1]
GeneIDi85476.
KEGGihsa:85476.
UCSCiuc003fce.4. human. [Q96RP9-1]

Organism-specific databases

CTDi85476.
GeneCardsiGFM1.
HGNCiHGNC:13780. GFM1.
HPAiHPA034764.
HPA034765.
MalaCardsiGFM1.
MIMi606639. gene.
609060. phenotype.
neXtProtiNX_Q96RP9.
Orphaneti137681. Hepatoencephalopathy due to combined oxidative phosphorylation deficiency type 1.
PharmGKBiPA134971637.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0465. Eukaryota.
COG0480. LUCA.
GeneTreeiENSGT00550000074911.
HOGENOMiHOG000231585.
InParanoidiQ96RP9.
KOiK02355.
OMAiGDTFCDP.
OrthoDBiEOG7VDXNM.
PhylomeDBiQ96RP9.
TreeFamiTF105631.

Enzyme and pathway databases

UniPathwayiUPA00345.
ReactomeiR-HSA-5389840. Mitochondrial translation elongation.

Miscellaneous databases

ChiTaRSiGFM1. human.
GeneWikiiGFM1.
GenomeRNAii85476.
PROiQ96RP9.
SOURCEiSearch...

Gene expression databases

BgeeiQ96RP9.
CleanExiHS_GFM1.
ExpressionAtlasiQ96RP9. baseline and differential.
GenevisibleiQ96RP9. HS.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00054_B. EF_G_EF_2_B.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR004540. Transl_elong_EFG/EF2.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00484. EF-G. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT COXPD1 SER-174.
  15. "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.

Entry informationi

Entry nameiEFGM_HUMAN
AccessioniPrimary (citable) accession number: Q96RP9
Secondary accession number(s): A6NCI9
, B2RCB9, B3KRW1, Q6GTN2, Q96T39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: October 17, 2006
Last modified: July 6, 2016
This is version 136 of the entry and version 2 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 3
    Human chromosome 3: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.