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Protein

Pre-miRNA 5'-monophosphate methyltransferase

Gene

BCDIN3D

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

Functioni

O-methyltransferase that specifically dimethylates the 5' monophosphate of pre-miRNAs, acting as a negative regulator of miRNA processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1 and is required for pre-miRNAs processing: methylation at this position reduces the processing of pre-miRNAs by DICER1. Able to mediate methylation of pre-miR-145, as well as other pre-miRNAs.1 Publication

GO - Molecular functioni

  • O-methyltransferase activity Source: UniProtKB
  • RNA methyltransferase activity Source: UniProtKB

GO - Biological processi

  • miRNA metabolic process Source: UniProtKB
  • negative regulation of pre-miRNA processing Source: UniProtKB
  • RNA methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-miRNA 5'-monophosphate methyltransferase (EC:2.1.1.-)
Alternative name(s):
BCDIN3 domain-containing protein
Gene namesi
Name:BCDIN3D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:27050. BCDIN3D.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 743DVG → AVA: Abolishes methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA162377410.

Polymorphism and mutation databases

BioMutaiBCDIN3D.
DMDMi74738762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Pre-miRNA 5'-monophosphate methyltransferasePRO_0000289265Add
BLAST

Proteomic databases

MaxQBiQ7Z5W3.
PaxDbiQ7Z5W3.
PRIDEiQ7Z5W3.

PTM databases

PhosphoSiteiQ7Z5W3.

Expressioni

Gene expression databases

BgeeiQ7Z5W3.
CleanExiHS_BCDIN3D.
GenevisibleiQ7Z5W3. HS.

Organism-specific databases

HPAiHPA039911.

Interactioni

Subunit structurei

Interacts with DICER1; the interaction may be mediated by RNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ZFP2Q6ZN573EBI-10257921,EBI-7236323

Protein-protein interaction databases

BioGridi126839. 5 interactions.
IntActiQ7Z5W3. 1 interaction.
STRINGi9606.ENSP00000335201.

Structurei

3D structure databases

ProteinModelPortaliQ7Z5W3.
SMRiQ7Z5W3. Positions 46-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 274222Bin3-type SAMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the methyltransferase superfamily.Curated
Contains 1 Bin3-type SAM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG255867.
GeneTreeiENSGT00390000014918.
HOGENOMiHOG000013152.
HOVERGENiHBG057674.
OMAiFNPPENR.
OrthoDBiEOG715Q5R.
PhylomeDBiQ7Z5W3.
TreeFamiTF324061.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR010675. Bin3.
IPR024160. BIN3_SAM-bd_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7Z5W3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPTELDGG SVKETAAEEE SRVLAPGAAP FGNFPHYSRF HPPEQRLRLL
60 70 80 90 100
PPELLRQLFP ESPENGPILG LDVGCNSGDL SVALYKHFLS LPDGETCSDA
110 120 130 140 150
SREFRLLCCD IDPVLVKRAE KECPFPDALT FITLDFMNQR TRKVLLSSFL
160 170 180 190 200
SQFGRSVFDI GFCMSITMWI HLNHGDHGLW EFLAHLSSLC HYLLVEPQPW
210 220 230 240 250
KCYRAAARRL RKLGLHDFDH FHSLAIRGDM PNQIVQILTQ DHGMELICCF
260 270 280 290
GNTSWDRSLL LFRAKQTIET HPIPESLIEK GKEKNRLSFQ KQ
Length:292
Mass (Da):33,200
Last modified:October 1, 2003 - v1
Checksum:i361EF0BBAAC0CCAF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti288 – 2881S → R.
Corresponds to variant rs11169172 [ dbSNP | Ensembl ].
VAR_032614

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK292194 mRNA. Translation: BAF84883.1.
CH471111 Genomic DNA. Translation: EAW58101.1.
BC053560 mRNA. Translation: AAH53560.1.
CCDSiCCDS8790.1.
RefSeqiNP_859059.1. NM_181708.2.
UniGeneiHs.142736.

Genome annotation databases

EnsembliENST00000333924; ENSP00000335201; ENSG00000186666.
GeneIDi144233.
KEGGihsa:144233.
UCSCiuc001rvh.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK292194 mRNA. Translation: BAF84883.1.
CH471111 Genomic DNA. Translation: EAW58101.1.
BC053560 mRNA. Translation: AAH53560.1.
CCDSiCCDS8790.1.
RefSeqiNP_859059.1. NM_181708.2.
UniGeneiHs.142736.

3D structure databases

ProteinModelPortaliQ7Z5W3.
SMRiQ7Z5W3. Positions 46-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126839. 5 interactions.
IntActiQ7Z5W3. 1 interaction.
STRINGi9606.ENSP00000335201.

PTM databases

PhosphoSiteiQ7Z5W3.

Polymorphism and mutation databases

BioMutaiBCDIN3D.
DMDMi74738762.

Proteomic databases

MaxQBiQ7Z5W3.
PaxDbiQ7Z5W3.
PRIDEiQ7Z5W3.

Protocols and materials databases

DNASUi144233.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333924; ENSP00000335201; ENSG00000186666.
GeneIDi144233.
KEGGihsa:144233.
UCSCiuc001rvh.3. human.

Organism-specific databases

CTDi144233.
GeneCardsiGC12M050231.
HGNCiHGNC:27050. BCDIN3D.
HPAiHPA039911.
neXtProtiNX_Q7Z5W3.
PharmGKBiPA162377410.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255867.
GeneTreeiENSGT00390000014918.
HOGENOMiHOG000013152.
HOVERGENiHBG057674.
OMAiFNPPENR.
OrthoDBiEOG715Q5R.
PhylomeDBiQ7Z5W3.
TreeFamiTF324061.

Miscellaneous databases

GenomeRNAii144233.
NextBioi84869.
PROiQ7Z5W3.

Gene expression databases

BgeeiQ7Z5W3.
CleanExiHS_BCDIN3D.
GenevisibleiQ7Z5W3. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR010675. Bin3.
IPR024160. BIN3_SAM-bd_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  4. "Human RNA methyltransferase BCDIN3D regulates microRNA processing."
    Xhemalce B., Robson S.C., Kouzarides T.
    Cell 151:278-288(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DICER1, MUTAGENESIS OF 72-ASP--GLU-74, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiBN3D2_HUMAN
AccessioniPrimary (citable) accession number: Q7Z5W3
Secondary accession number(s): A8K829
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2003
Last modified: June 24, 2015
This is version 85 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.