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Q969S9 (RRF2M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosome-releasing factor 2, mitochondrial

Short name=RRF2mt
Alternative name(s):
Elongation factor G 2, mitochondrial
Short name=EF-G2mt
Short name=mEF-G 2
Elongation factor G2
Short name=hEFG2
Gene names
Name:GFM2
Synonyms:EFG2
ORF Names:MSTP027
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. Ref.7

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandGTP-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitochondrial translation

Inferred from direct assay Ref.7. Source: UniProtKB

ribosome disassembly

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q969S9-1)

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: Q969S9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     361-407: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q969S9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     608-609: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q969S9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     530-531: TV → IP
     532-709: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q969S9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     504-513: DLEHALKCLQ → GINGLSVSTN
     514-779: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 779Ribosome-releasing factor 2, mitochondrialPRO_0000007450

Regions

Nucleotide binding77 – 848GTP By similarity
Nucleotide binding141 – 1455GTP By similarity
Nucleotide binding195 – 1984GTP By similarity

Natural variations

Alternative sequence361 – 40747Missing in isoform 2.
VSP_001363
Alternative sequence504 – 51310DLEHALKCLQ → GINGLSVSTN in isoform 5.
VSP_038190
Alternative sequence514 – 779266Missing in isoform 5.
VSP_038191
Alternative sequence530 – 5312TV → IP in isoform 4.
VSP_038192
Alternative sequence532 – 709178Missing in isoform 4.
VSP_038193
Alternative sequence608 – 6092Missing in isoform 3.
VSP_038194
Natural variant641N → S.
Corresponds to variant rs957680 [ dbSNP | Ensembl ].
VAR_053983
Natural variant3001S → C.
Corresponds to variant rs16872235 [ dbSNP | Ensembl ].
VAR_053984
Natural variant4251P → H. Ref.6
Corresponds to variant rs17852780 [ dbSNP | Ensembl ].
VAR_060200
Natural variant5941E → G. Ref.6
Corresponds to variant rs17856872 [ dbSNP | Ensembl ].
VAR_060201
Natural variant7351E → G. Ref.6
Corresponds to variant rs17856871 [ dbSNP | Ensembl ].
VAR_060202
Natural variant7741R → Q.
Corresponds to variant rs1048167 [ dbSNP | Ensembl ].
VAR_053985

Experimental info

Sequence conflict591L → I in AAH30612. Ref.6
Sequence conflict2011G → V in AAS49035. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 856B4E26FD9DD94E

FASTA77986,601
        10         20         30         40         50         60 
MLTNLRIFAM SHQTIPSVYI NNICCYKIRA SLKRLKPHVP LGRNCSSLPG LIGNDIKSLH 

        70         80         90        100        110        120 
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG 

       130        140        150        160        170        180 
ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW 

       190        200        210        220        230        240 
RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVM 

       250        260        270        280        290        300 
KEKLLWNCNS NDGKDFERKP LLEMNDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS 

       310        320        330        340        350        360 
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEERNYEFL 

       370        380        390        400        410        420 
QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NINGNCTERI SRLLLPFADQ 

       430        440        450        460        470        480 
HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNNEAERLLL 

       490        500        510        520        530        540 
AGVEIPEPVF FCTIEPPSLS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI 

       550        560        570        580        590        600 
EIIHDRIKRE YGLETYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPIET 

       610        620        630        640        650        660 
SSVMPVIEFE YAESINEGLL KVSQEAIENG IHSACLQGPL LGSPIQDVAI TLHSLTIHPG 

       670        680        690        700        710        720 
TSTTMISACV SRCVQKALKK ADKQVLEPLM NLEVTVARDY LSPVLADLAQ RRGNIQEIQT 

       730        740        750        760        770 
RQDNKVVIGF VPLAEIMGYS TVLRTLTSGS ATFALELSTY QAMNPQDQNT LLNRRSGLT 

« Hide

Isoform 2 [UniParc].

Checksum: 15869E090CB0848A
Show »

FASTA73281,200
Isoform 3 [UniParc].

Checksum: 539970B070FB4904
Show »

FASTA77786,324
Isoform 4 [UniParc].

Checksum: C712D5773F21E83E
Show »

FASTA60167,068
Isoform 5 [UniParc].

Checksum: 81B3AF2019E9D71F
Show »

FASTA51357,060

References

« Hide 'large scale' references
[1]"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), TISSUE SPECIFICITY.
[2]"Cloning of elongation factor G isoform."
Zheng M., Xie Y., Mao Y.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[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. expand/collapse author list , 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 5).
Tissue: Colon.
[4]Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., Jiang Y.X., Zhao X.W., Liu S. expand/collapse author list , Liu L.S., Ding J.F., Gao R.L., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Aorta.
[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. expand/collapse author list , 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 (JUL-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] (ISOFORMS 1 AND 3), VARIANTS HIS-425; GLY-594 AND GLY-735.
Tissue: Brain and Skin.
[7]"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.
[8]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF367997 mRNA. Translation: AAK53401.1.
AY453587 mRNA. Translation: AAS49035.1.
AK025314 mRNA. Translation: BAB15109.1.
AF111808 mRNA. Translation: AAL39010.1.
CH471084 Genomic DNA. Translation: EAW95744.1.
BC015712 mRNA. Translation: AAH15712.1.
BC030612 mRNA. Translation: AAH30612.1.
IPIIPI00071703.
IPI00172648.
IPI00216419.
IPI00945410.
IPI00946969.
RefSeqNP_115756.2. NM_032380.3.
NP_733781.1. NM_170681.1.
NP_733792.1. NM_170691.1.
UniGeneHs.277154.

3D structure databases

ProteinModelPortalQ969S9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ969S9. 2 interactions.
STRING9606.ENSP00000296805.

PTM databases

PhosphoSiteQ969S9.

Polymorphism databases

DMDM28201798.

Proteomic databases

PaxDbQ969S9.
PRIDEQ969S9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296805; ENSP00000296805; ENSG00000164347.
ENST00000345239; ENSP00000296804; ENSG00000164347.
ENST00000427854; ENSP00000405808; ENSG00000164347.
ENST00000509430; ENSP00000427004; ENSG00000164347.
GeneID84340.
KEGGhsa:84340.
UCSCuc003kdh.1. human.
uc003kdi.1. human.
uc003kdj.1. human.

Organism-specific databases

CTD84340.
GeneCardsGC05M074052.
HGNCHGNC:29682. GFM2.
HPAHPA036863.
MIM606544. gene.
neXtProtNX_Q969S9.
PharmGKBPA134949527.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0480.
HOGENOMHOG000231585.
InParanoidQ969S9.
KOK02355.
OMARKATINM.
OrthoDBEOG4NKBV3.
PhylomeDBQ969S9.

Gene expression databases

ArrayExpressQ969S9.
BgeeQ969S9.
CleanExHS_GFM2.
GenevestigatorQ969S9.
GermOnlineENSG00000164347. Homo sapiens.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
InterProIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00679. EFG_C. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SMARTSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMSSF54980. EFG_III_V. 2 hits.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGFM2. human.
GenomeRNAi84340.
NextBio74121.
SOURCESearch...

Entry information

Entry nameRRF2M_HUMAN
AccessionPrimary (citable) accession number: Q969S9
Secondary accession number(s): A0AR28 expand/collapse secondary AC list , Q8N6D8, Q8WYI0, Q9H6Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families