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Reviewed, UniProtKB/Swiss-Prot O60294 (LCMT2_HUMAN)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Leucine carboxyl methyltransferase 2
    EC=2.1.1.-
Alternative name(s):
    p21WAF1/CIP1 promoter-interacting protein
    tRNA wybutosine-synthesizing protein 4 homolog
    tRNA yW-synthesizing protein 4 homolog
Gene names
Name: LCMT2
Synonyms: KIAA0547, TYW4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA By similarity. May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues.

Pathway

tRNA modification; wybutosine-tRNA(Phe) biosynthesis.

Subunit structure

Interacts with RNF144B/IBRDC2. Ref.6

Sequence similarities

Belongs to the methyltransferase superfamily. LCMT family.

Ontologies

Keywords
   Biological processtRNA processing
   Coding sequence diversityPolymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmethyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.6

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 686686Leucine carboxyl methyltransferase 2
PRO_0000204423

Regions

Region161 – 1622S-adenosyl-L-methionine binding By similarity

Sites

Binding site591S-adenosyl-L-methionine By similarity
Binding site891S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1141S-adenosyl-L-methionine By similarity
Binding site1881S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Natural variations

Natural variant671V → L: dbSNP rs45552436. Ref.2
VAR_023378
Natural variant1411R → S: dbSNP rs3742970. Ref.2
VAR_022081
Natural variant1491C → Y Ref.2
VAR_023379
Natural variant5181T → A Ref.2
VAR_023380

Experimental info

Sequence conflict164 – 1652QL → HV in AAF75774. Ref.4
Sequence conflict2021L → F in AAF75774. Ref.4
Sequence conflict2711M → I in BAA25473. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O60294-1 [UniParc].

Last modified May 24, 2004. Version 3.
Checksum: 146F1C44F541059F

FASTA68675,602
        10         20         30         40         50         60 
MGPRSRERRA GAVQNTNDSS ALSKRSLAAR GYVQDPFAAL LVPGAARRAP LIHRGYYVRA 

        70         80         90        100        110        120 
RAVRHCVRAF LEQIGAPQAA LRAQILSLGA GFDSLYFRLK TAGRLARAAV WEVDFPDVAR 

       130        140        150        160        170        180 
RKAERIGETP ELCALTGPFE RGEPASALCF ESADYCILGL DLRQLQRVEE ALGAAGLDAA 

       190        200        210        220        230        240 
SPTLLLAEAV LTYLEPESAA ALIAWAAQRF PNALFVVYEQ MRPQDAFGQF MLQHFRQLNS 

       250        260        270        280        290        300 
PLHGLERFPD VEAQRRRFLQ AGWTACGAVD MNEFYHCFLP AEERRRVENI EPFDEFEEWH 

       310        320        330        340        350        360 
LKCAHYFILA ASRGDTLSHT LVFPSSEAFP RVNPASPSGV FPASVVSSEG QVPNLKRYGH 

       370        380        390        400        410        420 
ASVFLSPDVI LSAGGFGEQE GRHCRVSQFH LLSRDCDSEW KGSQIGSCGT GVQWDGRLYH 

       430        440        450        460        470        480 
TMTRLSESRV LVLGGRLSPV SPALGVLQLH FFKSEDNNTE DLKVTITKAG RKDDSTLCCW 

       490        500        510        520        530        540 
RHSTTEVSCQ NQEYLFVYGG RSVVEPVLSD WHFLHVGTMA WVRIPVEGEV PEARHSHSAC 

       550        560        570        580        590        600 
TWQGGALIAG GLGASEEPLN SVLFLRPISC GFLWESVDIQ PPITPRYSHT AHVLNGKLLL 

       610        620        630        640        650        660 
VGGIWIHSSS FPGVTVINLT TGLSSEYQID TTYVPWPLML HNHTSILLPE EQQLLLLGGG 

       670        680 
GNCFSFGTYF NPHTVTLDLS SLSAGQ 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed: 9628581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-67; SER-141; TYR-149 AND ALA-518.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[4]"Isolation of genes coding for p21WAF1/CIP1 promoter-interacting proteins using the yeast one-hybrid system."
Li S., Zhang B., Li X.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-686.
[5]"Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue."
De Baere I., Derua R., Janssens V., Van Hoof C., Waelkens E., Merlevede W., Goris J.
Biochemistry 38:16539-16547(1999) [PubMed: 10600115] [Abstract]
Cited for: FUNCTION.
[6]"p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1."
Ng C.-C., Arakawa H., Fukuda S., Kondoh H., Nakamura Y.
Oncogene 22:4449-4458(2003) [PubMed: 12853982] [Abstract]
Cited for: INTERACTION WITH RNF144B.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

AB011119 mRNA. Translation: BAA25473.2. Different initiation.
DQ102852 Genomic DNA. Translation: AAY88744.1.
BC015949 mRNA. Translation: AAH15949.1.
AF265443 mRNA. Translation: AAF75774.1.
IPIIPI00171712.
RefSeqNP_055608.2.
UniGeneHs.200596

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEO60294.

Genome annotation databases

EnsemblENSG00000168806. Homo sapiens. [Contig view]
GeneID9836.
KEGGhsa:9836.
NMPDRfig|9606.3.peg.10594.

Organism-specific databases

GeneCardsGC15M041407.
H-InvDBHIX0012182.
HGNCHGNC:17558. LCMT2.
MIM611246. gene.
PharmGKBPA134878443.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMO60294.
HOVERGENO60294.
OMAO60294. DGRLYHT.

Gene expression databases

ArrayExpressO60294.
BgeeO60294.
CleanExHS_LCMT2.
GermOnlineENSG00000168806. Homo sapiens.

Family and domain databases

InterProIPR015915. Kelch-typ_b-propeller.
IPR011498. Kelch_2.
IPR007213. LCM_MeTrfase.
[Graphical view]
Gene3DG3DSA:2.120.10.80. Kelch-typ_b-propeller. 1 hit.
PANTHERPTHR13600. LCM_mtfrase. 1 hit.
PfamPF07646. Kelch_2. 1 hit.
PF04072. LCM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00149. L-Leucine.
NextBio37062.
SOURCESearch...

Entry information

Entry nameLCMT2_HUMAN
AccessionPrimary (citable) accession number: O60294
Secondary accession number(s): Q4JFT6, Q96B55, Q9NR10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: June 16, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents