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Q9BV20 (MTNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylthioribose-1-phosphate isomerase

Short name=M1Pi
Short name=MTR-1-P isomerase
EC=5.3.1.23
Alternative name(s):
Mediator of RhoA-dependent invasion
S-methyl-5-thioribose-1-phosphate isomerase
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
Gene names
Name:MRI1
Synonyms:MRDI
ORF Names:UNQ6390/PRO21135
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover. Ref.5

Catalytic activity

S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate. HAMAP-Rule MF_03119

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6. HAMAP-Rule MF_03119

Subcellular location

Nucleus. Cytoplasm. Cell projection. Note: Primarily nuclear, but cytoplasmic in cancer cells, with enrichment at leading edge of the plasma membrane in late stage tumor cells. Ref.5

Induction

By RhoA activation in cancer cells (at protein level). Ref.5

Sequence similarities

Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-747381,EBI-747381

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BV20-1)

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: Q9BV20-2)

The sequence of this isoform differs from the canonical sequence as follows:
     125-200: VICCTEDMLE...LGRLEHAFCT → RETELCEHWEEHTRQRELPLRGPLGGTVL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Methylthioribose-1-phosphate isomerase HAMAP-Rule MF_03119
PRO_0000317325

Sites

Active site2481Proton donor Ref.5
Site1681Transition state stabilizer

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7

Natural variations

Alternative sequence125 – 20076VICCT…HAFCT → RETELCEHWEEHTRQRELPL RGPLGGTVL in isoform 2.
VSP_030935
Natural variant2351M → V.
Corresponds to variant rs35098252 [ dbSNP | Ensembl ].
VAR_059253
Natural variant3191G → A.
Corresponds to variant rs10402855 [ dbSNP | Ensembl ].
VAR_059254

Experimental info

Mutagenesis1681C → S: Abolishes enzymatic activity. Ref.5
Mutagenesis2481D → A: Abolishes enzymatic activity. Ref.5

Secondary structure

.................................................................... 369
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: A6A1B5EC76632F4F

FASTA36939,150
        10         20         30         40         50         60 
MTLEAIRYSR GSLQILDQLL LPKQSRYEAV GSVHQAWEAI RAMKVRGAPA IALVGCLSLA 

        70         80         90        100        110        120 
VELQAGAGGP GLAALVAFVR DKLSFLVTAR PTAVNMARAA RDLADVAARE AEREGATEEA 

       130        140        150        160        170        180 
VRERVICCTE DMLEKDLRDN RSIGDLGARH LLERVAPSGG KVTVLTHCNT GALATAGYGT 

       190        200        210        220        230        240 
ALGVIRSLHS LGRLEHAFCT ETRPYNQGAR LTAFELVYEQ IPATLITDSM VAAAMAHRGV 

       250        260        270        280        290        300 
SAVVVGADRV VANGDTANKV GTYQLAIVAK HHGIPFYVAA PSSSCDLRLE TGKEIIIEER 

       310        320        330        340        350        360 
PGQELTDVNG VRIAAPGIGV WNPAFDVTPH DLITGGIITE LGVFAPEELR TALTTTISSR 


DGTLDGPQM 

« Hide

Isoform 2 [UniParc].

Checksum: B9C6A0C26615AA76
Show »

FASTA32234,529

References

« Hide 'large scale' references
[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]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].
[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] (ISOFORM 1).
Tissue: Brain.
[5]"A mediator of Rho-dependent invasion moonlights as a methionine salvage enzyme."
Kabuyama Y., Litman E.S., Templeton P.D., Metzner S.I., Witze E.S., Argast G.M., Langer S.J., Polvinen K., Shellman Y., Chan D., Shabb J.B., Fitzpatrick J.E., Resing K.A., Sousa M.C., Ahn N.G.
Mol. Cell. Proteomics 8:2308-2320(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, ACTIVE SITE, INDUCTION BY RHOA, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-168 AND ASP-248.
[6]"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].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY358176 mRNA. Translation: AAQ88543.1.
AL834276 mRNA. Translation: CAD38951.1.
CH471106 Genomic DNA. Translation: EAW84370.1.
CH471106 Genomic DNA. Translation: EAW84371.1.
BC001703 mRNA. Translation: AAH01703.1.
CCDSCCDS12297.1. [Q9BV20-2]
CCDS32923.1. [Q9BV20-1]
RefSeqNP_001026897.1. NM_001031727.2. [Q9BV20-1]
NP_115661.1. NM_032285.2. [Q9BV20-2]
UniGeneHs.439370.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LDQX-ray2.50A/B1-369[»]
4LDRX-ray2.29A/B1-369[»]
ProteinModelPortalQ9BV20.
SMRQ9BV20. Positions 2-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123973. 6 interactions.
IntActQ9BV20. 1 interaction.
MINTMINT-1197605.
STRING9606.ENSP00000040663.

PTM databases

PhosphoSiteQ9BV20.

Polymorphism databases

DMDM74733279.

Proteomic databases

MaxQBQ9BV20.
PaxDbQ9BV20.
PeptideAtlasQ9BV20.
PRIDEQ9BV20.

Protocols and materials databases

DNASU84245.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000040663; ENSP00000040663; ENSG00000037757. [Q9BV20-1]
ENST00000319545; ENSP00000314871; ENSG00000037757. [Q9BV20-2]
GeneID84245.
KEGGhsa:84245.
UCSCuc002mxe.3. human. [Q9BV20-1]
uc002mxf.3. human. [Q9BV20-2]

Organism-specific databases

CTD84245.
GeneCardsGC19P013875.
HGNCHGNC:28469. MRI1.
HPACAB045988.
HPA042744.
MIM615105. gene.
neXtProtNX_Q9BV20.
PharmGKBPA164723110.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0182.
HOGENOMHOG000224730.
InParanoidQ9BV20.
KOK08963.
OMAAPGINCW.
OrthoDBEOG7SBNP2.
PhylomeDBQ9BV20.
TreeFamTF300852.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00904; UER00874.

Gene expression databases

ArrayExpressQ9BV20.
BgeeQ9BV20.
GenevestigatorQ9BV20.

Family and domain databases

Gene3D1.20.120.420. 1 hit.
HAMAPMF_01678. Salvage_MtnA.
InterProIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.
ProtoNetSearch...

Other

GeneWikiMGC3207.
GenomeRNAi84245.
NextBio73721.
PROQ9BV20.
SOURCESearch...

Entry information

Entry nameMTNA_HUMAN
AccessionPrimary (citable) accession number: Q9BV20
Secondary accession number(s): Q8NDC9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 108 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM