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

Translation initiation factor IF-3, mitochondrial

Gene

MTIF3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

IF-3 binds to the 28S ribosomal subunit and shifts the equilibrum between 55S ribosomes and their 39S and 28S subunits in favor of the free subunits, thus enhancing the availability of 28S subunits on which protein synthesis initiation begins.1 Publication

GO - Molecular functioni

  • ribosomal small subunit binding Source: BHF-UCL
  • translation factor activity, RNA binding Source: BHF-UCL
  • translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  • mitochondrial translation Source: Reactome
  • mitochondrial translational initiation Source: SGD
  • organelle organization Source: Reactome
  • ribosome disassembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-HSA-5368286. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor IF-3, mitochondrial
Short name:
IF-3(Mt)
Short name:
IF-3Mt
Short name:
IF3(mt)
Short name:
IF3mt
Gene namesi
Name:MTIF3
ORF Names:DC38
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:29788. MTIF3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162396264.

Polymorphism and mutation databases

BioMutaiMTIF3.
DMDMi317373570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131MitochondrionAdd
BLAST
Chaini32 – 278247Translation initiation factor IF-3, mitochondrialPRO_0000280037Add
BLAST

Proteomic databases

EPDiQ9H2K0.
MaxQBiQ9H2K0.
PaxDbiQ9H2K0.
PRIDEiQ9H2K0.

Expressioni

Gene expression databases

BgeeiQ9H2K0.
CleanExiHS_MTIF3.
GenevisibleiQ9H2K0. HS.

Organism-specific databases

HPAiHPA039791.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SIAH1Q8IUQ43EBI-3923617,EBI-747107

Protein-protein interaction databases

BioGridi128525. 3 interactions.
IntActiQ9H2K0. 2 interactions.
STRINGi9606.ENSP00000370508.

Structurei

3D structure databases

ProteinModelPortaliQ9H2K0.
SMRiQ9H2K0. Positions 149-250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IF-3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IXD5. Eukaryota.
COG0290. LUCA.
GeneTreeiENSGT00390000014424.
HOGENOMiHOG000264227.
HOVERGENiHBG080563.
InParanoidiQ9H2K0.
KOiK02520.
OMAiQTMPGIA.
OrthoDBiEOG7DZ8KV.
PhylomeDBiQ9H2K0.
TreeFamiTF332326.

Family and domain databases

Gene3Di3.10.20.80. 1 hit.
3.30.110.10. 1 hit.
InterProiIPR001288. Translation_initiation_fac_3.
IPR019815. Translation_initiation_fac_3_C.
IPR019814. Translation_initiation_fac_3_N.
[Graphical view]
PANTHERiPTHR10938. PTHR10938. 1 hit.
PfamiPF00707. IF3_C. 1 hit.
PF05198. IF3_N. 1 hit.
[Graphical view]
SUPFAMiSSF54364. SSF54364. 1 hit.
SSF55200. SSF55200. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9H2K0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALFLKRLT LQTVKSENSC IRCFGKHILQ KTAPAQLSPI ASAPRLSFLI
60 70 80 90 100
HAKAFSTAED TQNEGKKTKK NKTAFSNVGR KISQRVIHLF DEKGNDLGNM
110 120 130 140 150
HRANVIRLMD ERDLRLVQRN TSTEPAEYQL MTGLQILQER QRLREMEKAN
160 170 180 190 200
PKTGPTLRKE LILSSNIGQH DLDTKTKQIQ QWIKKKHLVQ ITIKKGKNVD
210 220 230 240 250
VSENEMEEIF HQILQTMPGI ATFSSRPQAV QGGKALMCVL RAFSKNEEKA
260 270
YKETQETQER DTLNKDHGND KESNVLHQ
Length:278
Mass (Da):31,725
Last modified:January 11, 2011 - v4
Checksum:iE0CA6D5F547DD6E3
GO

Sequence cautioni

The sequence AAH39599.1 differs from that shown. Reason: Frameshift at position 246. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681T → I.1 Publication
Corresponds to variant rs17857314 [ dbSNP | Ensembl ].
VAR_031045
Natural varianti243 – 2431F → L.3 Publications
Corresponds to variant rs1218825 [ dbSNP | Ensembl ].
VAR_031046

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF410851 mRNA. Translation: AAL04150.1.
AF265440 mRNA. Translation: AAG44698.1.
AL137059 Genomic DNA. Translation: CAH70316.1.
BC039599 mRNA. Translation: AAH39599.1. Frameshift.
BC046166 mRNA. Translation: AAH46166.1.
CCDSiCCDS9322.1.
RefSeqiNP_001159733.1. NM_001166261.1.
NP_001159734.1. NM_001166262.1.
NP_001159735.1. NM_001166263.1.
NP_690876.3. NM_152912.4.
XP_005266340.1. XM_005266283.2.
XP_006719834.1. XM_006719771.2.
XP_006719835.1. XM_006719772.2.
XP_011533259.1. XM_011534957.1.
XP_011533260.1. XM_011534958.1.
XP_011533261.1. XM_011534959.1.
XP_011533262.1. XM_011534960.1.
XP_011533263.1. XM_011534961.1.
XP_011533264.1. XM_011534962.1.
XP_011533265.1. XM_011534963.1.
UniGeneiHs.534582.

Genome annotation databases

EnsembliENST00000381116; ENSP00000370508; ENSG00000122033.
ENST00000381120; ENSP00000370512; ENSG00000122033.
ENST00000405591; ENSP00000384659; ENSG00000122033.
GeneIDi219402.
KEGGihsa:219402.
UCSCiuc001urh.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF410851 mRNA. Translation: AAL04150.1.
AF265440 mRNA. Translation: AAG44698.1.
AL137059 Genomic DNA. Translation: CAH70316.1.
BC039599 mRNA. Translation: AAH39599.1. Frameshift.
BC046166 mRNA. Translation: AAH46166.1.
CCDSiCCDS9322.1.
RefSeqiNP_001159733.1. NM_001166261.1.
NP_001159734.1. NM_001166262.1.
NP_001159735.1. NM_001166263.1.
NP_690876.3. NM_152912.4.
XP_005266340.1. XM_005266283.2.
XP_006719834.1. XM_006719771.2.
XP_006719835.1. XM_006719772.2.
XP_011533259.1. XM_011534957.1.
XP_011533260.1. XM_011534958.1.
XP_011533261.1. XM_011534959.1.
XP_011533262.1. XM_011534960.1.
XP_011533263.1. XM_011534961.1.
XP_011533264.1. XM_011534962.1.
XP_011533265.1. XM_011534963.1.
UniGeneiHs.534582.

3D structure databases

ProteinModelPortaliQ9H2K0.
SMRiQ9H2K0. Positions 149-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128525. 3 interactions.
IntActiQ9H2K0. 2 interactions.
STRINGi9606.ENSP00000370508.

Polymorphism and mutation databases

BioMutaiMTIF3.
DMDMi317373570.

Proteomic databases

EPDiQ9H2K0.
MaxQBiQ9H2K0.
PaxDbiQ9H2K0.
PRIDEiQ9H2K0.

Protocols and materials databases

DNASUi219402.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381116; ENSP00000370508; ENSG00000122033.
ENST00000381120; ENSP00000370512; ENSG00000122033.
ENST00000405591; ENSP00000384659; ENSG00000122033.
GeneIDi219402.
KEGGihsa:219402.
UCSCiuc001urh.4. human.

Organism-specific databases

CTDi219402.
GeneCardsiMTIF3.
H-InvDBHIX0011193.
HGNCiHGNC:29788. MTIF3.
HPAiHPA039791.
neXtProtiNX_Q9H2K0.
PharmGKBiPA162396264.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXD5. Eukaryota.
COG0290. LUCA.
GeneTreeiENSGT00390000014424.
HOGENOMiHOG000264227.
HOVERGENiHBG080563.
InParanoidiQ9H2K0.
KOiK02520.
OMAiQTMPGIA.
OrthoDBiEOG7DZ8KV.
PhylomeDBiQ9H2K0.
TreeFamiTF332326.

Enzyme and pathway databases

ReactomeiR-HSA-5368286. Mitochondrial translation initiation.

Miscellaneous databases

ChiTaRSiMTIF3. human.
GenomeRNAii219402.
NextBioi90583.
PROiQ9H2K0.

Gene expression databases

BgeeiQ9H2K0.
CleanExiHS_MTIF3.
GenevisibleiQ9H2K0. HS.

Family and domain databases

Gene3Di3.10.20.80. 1 hit.
3.30.110.10. 1 hit.
InterProiIPR001288. Translation_initiation_fac_3.
IPR019815. Translation_initiation_fac_3_C.
IPR019814. Translation_initiation_fac_3_N.
[Graphical view]
PANTHERiPTHR10938. PTHR10938. 1 hit.
PfamiPF00707. IF3_C. 1 hit.
PF05198. IF3_N. 1 hit.
[Graphical view]
SUPFAMiSSF54364. SSF54364. 1 hit.
SSF55200. SSF55200. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of mammalian mitochondrial translational initiation factor 3 and examination of its role in initiation complex formation with natural mRNAs."
    Koc E.C., Spremulli L.L.
    J. Biol. Chem. 277:35541-35549(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 98-104, FUNCTION, VARIANT LEU-243.
    Tissue: Melanocyte.
  2. "A novel gene from human dendritic cells."
    Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-243.
    Tissue: Dendritic cell.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS ILE-68 AND LEU-243.
    Tissue: Cervix and Colon.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF3M_HUMAN
AccessioniPrimary (citable) accession number: Q9H2K0
Secondary accession number(s): Q05BL8, Q5W0V0, Q86X68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: January 11, 2011
Last modified: March 16, 2016
This is version 105 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. Translation initiation factors
    List of translation initiation factor entries
  5. 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.