Probable dimethyladenosine transferase

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Q9UNQ2 (DIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	DIMT1
Synonyms:	DIMT1L
ORF Names:	HUSSY-05

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Catalytic activity	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.
Subcellular location	Nucleus › nucleolus Ref.5.
Sequence similarities	Belongs to the methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.
Sequence caution	The sequence AAC72947.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW rRNA (adenine-N6,N6-)-dimethyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

Probable dimethyladenosine transferase

PRO_0000101465

Sites

Binding site

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

S-adenosyl-L-methionine; via amide nitrogen

Binding site

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

S-adenosyl-L-methionine

Binding site

113

S-adenosyl-L-methionine

Binding site

128

S-adenosyl-L-methionine

Experimental info

Sequence conflict

157 – 158

RE → EN in CAA08815. Ref.3

Sequence conflict

265 – 275

IIPEDFSIADK → VSAAVYPVKQI in AAH02841. Ref.2

Sequence conflict

276 – 313

Missing in AAH02841. Ref.2

Secondary structure

313

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9UNQ2 [UniParc].

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

FASTA

313

35,236

        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

References

	« Hide 'large scale' referencesShow '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. Tissue: Cervix carcinoma.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00004459.

RefSeq

NP_055288.1. NM_014473.2.

UniGene

Hs.726092.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZQ9	X-ray	1.90	A/B	31-313	[»]

ProteinModelPortal

Q9UNQ2.

SMR

Q9UNQ2. Positions 36-313.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UNQ2. 4 interactions.

STRING

Q9UNQ2.

Polymorphism databases

DMDM

27151492.

2D gel databases

SWISS-2DPAGE

Q9UNQ2.

Proteomic databases

PeptideAtlas

Q9UNQ2.

PRIDE

Q9UNQ2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000199320; ENSP00000199320; ENSG00000086189.

GeneID

27292.

KEGG

hsa:27292.

UCSC

uc003jta.1. human.

Organism-specific databases

CTD

27292.

GeneCards

GC05M061683.

HGNC

HGNC:30217. DIMT1.

MIM

612499. gene.

neXtProt

NX_Q9UNQ2.

PharmGKB

PA162383599.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05571.

GeneTree

ENSGT00530000063389.

HOGENOM

HBG319664.

HOVERGEN

HBG031507.

InParanoid

Q9UNQ2.

OMA

VCVANLP.

OrthoDB

EOG49GKH2.

PhylomeDB

Q9UNQ2.

Gene expression databases

ArrayExpress

Q9UNQ2.

Bgee

Q9UNQ2.

CleanEx

HS_DIMT1L.

Genevestigator

Q9UNQ2.

GermOnline

ENSG00000086189. Homo sapiens.

Family and domain databases

InterPro

IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR001737. rRNA_Ade_methylase_transferase.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR011530. rRNA_adenine_dimethylase.
[Graphical view]

K14191.

PANTHER

PTHR11727. RRNA_meth_trans. 1 hit.

Pfam

PF00398. RrnaAD. 1 hit.
[Graphical view]

SMART

SM00650. rADc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00755. KsgA. 1 hit.

PROSITE

PS01131. RRNA_A_DIMETH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

50248.

SOURCE

Search...

Entry information

Entry name

DIM1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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 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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents