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Q96DP5 (FMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 103. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase, mitochondrial

Short name=MtFMT
EC=2.1.2.9
Gene names
Name:MTFMT
Synonyms:FMT, FMT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism By similarity.

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).

Subcellular location

Mitochondrion By similarity.

Domain

Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.

Sequence similarities

Belongs to the Fmt family.

Sequence caution

The sequence AAH16630.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAH33687.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB70984.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranslational initiation

Inferred from electronic annotation. Source: GOC

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: EC

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 389Methionyl-tRNA formyltransferase, mitochondrialPRO_0000010093

Natural variations

Natural variant51V → A.
Corresponds to variant rs2946655 [ dbSNP | Ensembl ].
VAR_059289

Sequences

Sequence LengthMass (Da)Tools
Q96DP5 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: EBBE92142AB954E0

FASTA38943,832
        10         20         30         40         50         60 
MRVLVRRCWG PPLAHGARRG RPSPQWRALA RLGWEDCRDS RVREKPPWRV LFFGTDQFAR 

        70         80         90        100        110        120 
EALRALHAAR ENKEEELIDK LEVVTMPSPS PKGLPVKQYA VQSQLPVYEW PDVGSGEYDV 

       130        140        150        160        170        180 
GVVASFGRLL NEALILKFPY GILNVHPSCL PRWRGPAPVI HTVLHGDTVT GVTIMQIRPK 

       190        200        210        220        230        240 
RFDVGPILKQ ETVPVPPKST AKELEAVLSR LGANMLISVL KNLPESLSNG RQQPMEGATY 

       250        260        270        280        290        300 
APKISAGTSC IKWEEQTSEQ IFRLYRAIGN IIPLQTLWMA NTIKLLDLVE VNSSVLADPK 

       310        320        330        340        350        360 
LTGQALIPGS VIYHKQSQIL LVYCKDGWIG VRSVMLKKSL TATDFYNGYL HPWYQKNSQA 

       370        380 
QPSQCRFQTL RLPTKKKQKK TVAMQQCIE 

« Hide

References

[1]"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].
Tissue: Brain and Mammary gland.
[2]"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] OF 11-389.
Tissue: Neuroblastoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC016630 mRNA. Translation: AAH16630.2. Different initiation.
BC033687 mRNA. Translation: AAH33687.1. Different initiation.
AK055688 mRNA. Translation: BAB70984.1. Different initiation.
IPIIPI00055753.
RefSeqNP_640335.2. NM_139242.3.
UniGeneHs.531615.

3D structure databases

ProteinModelPortalQ96DP5.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000220058.

PTM databases

PhosphoSiteQ96DP5.

Polymorphism databases

DMDM27923776.

Proteomic databases

PaxDbQ96DP5.
PRIDEQ96DP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220058; ENSP00000220058; ENSG00000103707.
ENST00000558460; ENSP00000452646; ENSG00000103707.
GeneID123263.
KEGGhsa:123263.
UCSCuc002aof.4. human.

Organism-specific databases

CTD123263.
GeneCardsGC15M065293.
HGNCHGNC:29666. MTFMT.
HPAHPA040710.
MIM611766. gene.
neXtProtNX_Q96DP5.
Orphanet319524. Combined oxidative phosphorylation defect type 15.
2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBPA142671304.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
HOVERGENHBG031552.
InParanoidQ96DP5.
KOK00604.
OMADWNKSAR.
OrthoDBEOG45TCN8.
PhylomeDBQ96DP5.

Gene expression databases

ArrayExpressQ96DP5.
BgeeQ96DP5.
CleanExHS_MTFMT.
GenevestigatorQ96DP5.
GermOnlineENSG00000103707. Homo sapiens.

Family and domain databases

Gene3D3.40.50.170. 1 hit.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
ProtoNetSearch...

Other

DrugBankDB00116. Tetrahydrofolic acid.
GenomeRNAi123263.
NextBio81093.
SOURCESearch...

Entry information

Entry nameFMT_HUMAN
AccessionPrimary (citable) accession number: Q96DP5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: May 29, 2013
This is version 103 of the entry and version 2 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 15

Human chromosome 15: 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