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Reviewed, UniProtKB/Swiss-Prot Q9UNQ2 (DIMT1_HUMAN)

Last modified June 16, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable dimethyladenosine transferase
    EC=2.1.1.-
Alternative name(s):
    S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase
    18S rRNA dimethylase
    DIM1 dimethyladenosine transferase 1-like
Gene names
Name: DIMT1L
Synonyms: DIMT1
ORF Names: HUSSY-05
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle By similarity.

Subcellular location

Nucleus › nucleolus. Ref.5

Sequence similarities

Belongs to the rRNA adenine N(6)-methyltransferase family.

Sequence caution

The sequence AAC72947.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Sequence of unknown origin in the N-terminal part.

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Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentNucleus
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processrRNA modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

rRNA (adenine-N6,N6-)-dimethyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Probable dimethyladenosine transferase
PRO_0000101465

Sites

Binding site371S-adenosyl-L-methionine; via carbonyl oxygen
Binding site391S-adenosyl-L-methionine; via amide nitrogen
Binding site641S-adenosyl-L-methionine; via carbonyl oxygen
Binding site851S-adenosyl-L-methionine
Binding site1131S-adenosyl-L-methionine
Binding site1281S-adenosyl-L-methionine

Experimental info

Sequence conflict157 – 1582RE → EN in CAA08815. Ref.3
Sequence conflict265 – 27511IIPEDFSIADK → VSAAVYPVKQI in AAH02841. Ref.2
Sequence conflict276 – 31338Missing in AAH02841. Ref.2

Secondary structure

1 ............................................. 313
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9UNQ2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 306B9D4A4F9494A6

FASTA31335,236
        10         20         30         40         50         60 
MPKVKSGAIG RRRGRQEQRR ELKSAGGLMF NTGIGQHILK NPLIINSIID KAALRPTDVV 

        70         80         90        100        110        120 
LEVGPGTGNM TVKLLEKAKK VVACELDPRL VAELHKRVQG TPVASKLQVL VGDVLKTDLP 

       130        140        150        160        170        180 
FFDTCVANLP YQISSPFVFK LLLHRPFFRC AILMFQREFA LRLVAKPGDK LYCRLSINTQ 

       190        200        210        220        230        240 
LLARVDHLMK VGKNNFRPPP KVESSVVRIE PKNPPPPINF QEWDGLVRIT FVRKNKTLSA 

       250        260        270        280        290        300 
AFKSSAVQQL LEKNYRIHCS VHNIIIPEDF SIADKIQQIL TSTGFSDKRA RSMDIDDFIR 

       310 
LLHGFNAEGI HFS

« Hide

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References

« Hide 'large scale' references
[1]Wei Y.J., Ding J.F., Liu Y.Q., Xu Y.Y., Hui R.T., Sheng H., Zhao X.W., Jiang Y.X., Liu D.Q., Zhao Y., Cao H.Q., Meng X.M., Liu S.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Aorta.
[2]"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: Lung and Placenta.
[3]"Characterization of 16 novel human genes showing high similarity to yeast sequences."
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
Yeast 18:69-80(2001) [PubMed: 11124703] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 157-313.
Tissue: Brain.
[4]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-313.
[5]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed: 12429849] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]"Crystal structure of human dimethyladenosine transferase with SAM."
Structural genomics consortium (SGC)
Submitted (MAY-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 31-313 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

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Cross-references

Sequence databases

AF102147 mRNA. Translation: AAC97955.1.
BC002841 mRNA. Translation: AAH02841.1.
BC010874 mRNA. Translation: AAH10874.1.
AJ009761 mRNA. Translation: CAA08815.1.
AF091078 mRNA. Translation: AAC72947.1. Sequence problems.
IPIIPI00004459.
RefSeqNP_055288.1.
UniGeneHs.714754

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ZQ9X-ray1.90A/B31-313[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UNQ2. 3 interactions.

2-D gel databases

SWISS-2DPAGEQ9UNQ2.

Proteomic databases

PeptideAtlasQ9UNQ2.
PRIDEQ9UNQ2.

Genome annotation databases

EnsemblENSG00000086189. Homo sapiens. [Contig view]
GeneID27292.
KEGGhsa:27292.

Organism-specific databases

GeneCardsGC05M061721.
HGNCHGNC:30217. DIMT1L.
MIM612499. gene.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9UNQ2.
OMAQ9UNQ2. FMPQPNV.

Gene expression databases

ArrayExpressQ9UNQ2.
BgeeQ9UNQ2.
CleanExHS_DIMT1L.
GermOnlineENSG00000086189. Homo sapiens.

Family and domain databases

InterProIPR001737. RRNA_Ade_Mease_Trfase.
IPR011530. rRNA_adenine_dimethylase.
[Graphical view]
PANTHERPTHR11727. RRNA_meth_trans. 1 hit.
PfamPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTSM00650. rADc. 1 hit.
[Graphical view]
TIGRFAMsTIGR00755. ksgA. 1 hit.
PROSITEPS01131. RRNA_A_DIMETH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio50248.
SOURCESearch...

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Entry information

Entry nameDIMT1_HUMAN
AccessionPrimary (citable) accession number: Q9UNQ2
Secondary accession number(s): O76025, Q9BU77, Q9UES1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 5

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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