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Protein

Probable dimethyladenosine transferase

Gene

DIMT1

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

Functioni

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

Catalytic activityi

4 S-adenosyl-L-methionine + adenine(1779)/adenine(1780) in 18S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1779)/N(6)-dimethyladenine(1780) in 18S rRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1 Publication
Binding sitei39 – 391S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication
Binding sitei64 – 641S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1 Publication
Binding sitei85 – 851S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Binding sitei113 – 1131S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
Binding sitei128 – 1281S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dimethyladenosine transferase (EC:2.1.1.183)
Alternative name(s):
DIM1 dimethyladenosine transferase 1 homolog
DIM1 dimethyladenosine transferase 1-like
Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase
Probable 18S rRNA dimethylase
Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase
Gene namesi
Name:DIMT1
Synonyms:DIMT1L
ORF Names:HUSSY-05
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:30217. DIMT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162383599.

Polymorphism and mutation databases

BioMutaiDIMT1.
DMDMi27151492.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Probable dimethyladenosine transferasePRO_0000101465Add
BLAST

Proteomic databases

EPDiQ9UNQ2.
MaxQBiQ9UNQ2.
PaxDbiQ9UNQ2.
PeptideAtlasiQ9UNQ2.
PRIDEiQ9UNQ2.

2D gel databases

SWISS-2DPAGEQ9UNQ2.

PTM databases

iPTMnetiQ9UNQ2.
PhosphoSiteiQ9UNQ2.

Expressioni

Gene expression databases

BgeeiENSG00000086189.
CleanExiHS_DIMT1L.
ExpressionAtlasiQ9UNQ2. baseline and differential.
GenevisibleiQ9UNQ2. HS.

Organism-specific databases

HPAiHPA042944.

Interactioni

Protein-protein interaction databases

BioGridi118116. 45 interactions.
IntActiQ9UNQ2. 13 interactions.
MINTiMINT-3082856.
STRINGi9606.ENSP00000199320.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 5110Combined sources
Beta strandi59 – 635Combined sources
Helixi71 – 777Combined sources
Beta strandi78 – 869Combined sources
Helixi88 – 9811Combined sources
Helixi104 – 1063Combined sources
Beta strandi107 – 1126Combined sources
Turni114 – 1163Combined sources
Beta strandi123 – 1286Combined sources
Helixi131 – 1333Combined sources
Helixi134 – 14310Combined sources
Beta strandi149 – 1568Combined sources
Helixi157 – 1648Combined sources
Helixi174 – 1829Combined sources
Beta strandi183 – 1919Combined sources
Helixi193 – 1953Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi204 – 2118Combined sources
Helixi220 – 23112Combined sources
Turni232 – 2354Combined sources
Helixi238 – 2414Combined sources
Helixi245 – 26218Combined sources
Helixi272 – 28211Combined sources
Helixi290 – 2923Combined sources
Helixi295 – 30612Combined sources
Turni307 – 3093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZQ9X-ray1.90A/B31-313[»]
ProteinModelPortaliQ9UNQ2.
SMRiQ9UNQ2. Positions 36-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNQ2.

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0820. Eukaryota.
COG0030. LUCA.
GeneTreeiENSGT00530000063389.
HOGENOMiHOG000227963.
HOVERGENiHBG031507.
InParanoidiQ9UNQ2.
KOiK14191.
OMAiPRFDICV.
OrthoDBiEOG091G0CD4.
PhylomeDBiQ9UNQ2.
TreeFamiTF354255.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00755. ksgA. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UNQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKVKSGAIG RRRGRQEQRR ELKSAGGLMF NTGIGQHILK NPLIINSIID
60 70 80 90 100
KAALRPTDVV LEVGPGTGNM TVKLLEKAKK VVACELDPRL VAELHKRVQG
110 120 130 140 150
TPVASKLQVL VGDVLKTDLP FFDTCVANLP YQISSPFVFK LLLHRPFFRC
160 170 180 190 200
AILMFQREFA LRLVAKPGDK LYCRLSINTQ LLARVDHLMK VGKNNFRPPP
210 220 230 240 250
KVESSVVRIE PKNPPPPINF QEWDGLVRIT FVRKNKTLSA AFKSSAVQQL
260 270 280 290 300
LEKNYRIHCS VHNIIIPEDF SIADKIQQIL TSTGFSDKRA RSMDIDDFIR
310
LLHGFNAEGI HFS
Length:313
Mass (Da):35,236
Last modified:May 1, 2000 - v1
Checksum:i306B9D4A4F9494A6
GO

Sequence cautioni

The sequence AAC72947 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1582RE → EN in CAA08815 (PubMed:11124703).Curated
Sequence conflicti265 – 27511IIPEDFSIADK → VSAAVYPVKQI in AAH02841 (PubMed:15489334).CuratedAdd
BLAST
Sequence conflicti276 – 31338Missing in AAH02841 (PubMed:15489334).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3981.1.
RefSeqiNP_055288.1. NM_014473.2.
UniGeneiHs.731665.

Genome annotation databases

EnsembliENST00000199320; ENSP00000199320; ENSG00000086189.
GeneIDi27292.
KEGGihsa:27292.
UCSCiuc003jta.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3981.1.
RefSeqiNP_055288.1. NM_014473.2.
UniGeneiHs.731665.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZQ9X-ray1.90A/B31-313[»]
ProteinModelPortaliQ9UNQ2.
SMRiQ9UNQ2. Positions 36-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118116. 45 interactions.
IntActiQ9UNQ2. 13 interactions.
MINTiMINT-3082856.
STRINGi9606.ENSP00000199320.

PTM databases

iPTMnetiQ9UNQ2.
PhosphoSiteiQ9UNQ2.

Polymorphism and mutation databases

BioMutaiDIMT1.
DMDMi27151492.

2D gel databases

SWISS-2DPAGEQ9UNQ2.

Proteomic databases

EPDiQ9UNQ2.
MaxQBiQ9UNQ2.
PaxDbiQ9UNQ2.
PeptideAtlasiQ9UNQ2.
PRIDEiQ9UNQ2.

Protocols and materials databases

DNASUi27292.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000199320; ENSP00000199320; ENSG00000086189.
GeneIDi27292.
KEGGihsa:27292.
UCSCiuc003jta.4. human.

Organism-specific databases

CTDi27292.
GeneCardsiDIMT1.
HGNCiHGNC:30217. DIMT1.
HPAiHPA042944.
MIMi612499. gene.
neXtProtiNX_Q9UNQ2.
PharmGKBiPA162383599.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0820. Eukaryota.
COG0030. LUCA.
GeneTreeiENSGT00530000063389.
HOGENOMiHOG000227963.
HOVERGENiHBG031507.
InParanoidiQ9UNQ2.
KOiK14191.
OMAiPRFDICV.
OrthoDBiEOG091G0CD4.
PhylomeDBiQ9UNQ2.
TreeFamiTF354255.

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.

Miscellaneous databases

ChiTaRSiDIMT1. human.
EvolutionaryTraceiQ9UNQ2.
GenomeRNAii27292.
PROiQ9UNQ2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000086189.
CleanExiHS_DIMT1L.
ExpressionAtlasiQ9UNQ2. baseline and differential.
GenevisibleiQ9UNQ2. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00755. ksgA. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDIM1_HUMAN
AccessioniPrimary (citable) accession number: Q9UNQ2
Secondary accession number(s): O76025, Q9BU77, Q9UES1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 156 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.