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Protein

Lariat debranching enzyme

Gene

Dbr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis (By similarity).By similarity1 Publication

Catalytic activityi

RNA processing activity that hydrolyzes the 2'-5' phosphodiester linkage at the branchpoint of excised intron lariats.

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lariat debranching enzyme (EC:3.1.-.-)
Gene namesi
Name:Dbr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1931520. Dbr1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550Lariat debranching enzymePRO_0000250359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineCombined sources
Modified residuei128 – 1281N6-acetyllysineBy similarity
Modified residuei470 – 4701PhosphoserineBy similarity
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei485 – 4851PhosphoserineBy similarity
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei491 – 4911PhosphoserineCombined sources
Modified residuei494 – 4941PhosphoserineCombined sources
Modified residuei505 – 5051PhosphoserineCombined sources
Modified residuei520 – 5201PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ923B1.
MaxQBiQ923B1.
PaxDbiQ923B1.
PeptideAtlasiQ923B1.
PRIDEiQ923B1.

PTM databases

iPTMnetiQ923B1.
PhosphoSiteiQ923B1.

Expressioni

Gene expression databases

BgeeiQ923B1.
CleanExiMM_DBR1.
ExpressionAtlasiQ923B1. baseline and differential.
GenevisibleiQ923B1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070991.

Structurei

3D structure databases

ProteinModelPortaliQ923B1.
SMRiQ923B1. Positions 3-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the lariat debranching enzyme family.Curated

Phylogenomic databases

eggNOGiKOG2863. Eukaryota.
ENOG410XP0F. LUCA.
GeneTreeiENSGT00510000047481.
HOGENOMiHOG000216468.
HOVERGENiHBG079917.
InParanoidiQ923B1.
KOiK18328.
OMAiLMQHQAK.
OrthoDBiEOG7BW0J7.
PhylomeDBiQ923B1.
TreeFamiTF313221.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR007708. DBR1_C.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF05011. DBR1. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
SMARTiSM01124. DBR1. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.

Sequencei

Sequence statusi: Complete.

Q923B1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVAVAGCCH GELDKIYETL ALAERRGSGP VDLLLCCGDF QAVRNEADLR
60 70 80 90 100
CMAVPPKYRH MQTFYRYYSG EKKAPVLTIF IGGNHEASNH LQELPYGGWV
110 120 130 140 150
APNIYYLGLA GVVKYRGVRI GGISGIFKSH DYRKGHFECP PYNSSTIRSI
160 170 180 190 200
YHVRNIEVYK LKQLKQPVHI FLSHDWPRNI YHYGNKKQLL KTKSFFRQEV
210 220 230 240 250
ENSTLGSPAA SELLEHLQPA YWFSAHLHVK FAALMQHQAT DKDQAGKETK
260 270 280 290 300
FLALDKCLPH RDFLQVLEIE HDPSAPEYLE YDVEWLTVLR ATDDLINVTG
310 320 330 340 350
GLWNMPEDNG LHTRWDYSAT EETMKEVMEK LNHDPKVPCN FTMTAACYDP
360 370 380 390 400
SKPQTQVKLV HRINPQTTEF CAQLGITDIN VMIQKAREEE HHQCGEYEQQ
410 420 430 440 450
GDPGTEESEE DRSEYNTDTS ALSSINPDEI MLDEEEEEEE EEEEAVSAHS
460 470 480 490 500
DMNTPSVEPA SDQASDLSTS FSDIRNLPSS MFVSSDDASR SPASGEGKCG
510 520 530 540 550
ETVESGDEKD LAKFPLKRLS DEHEPEQRKK IKRRNQAIYA AVDDGDASAE
Length:550
Mass (Da):62,289
Last modified:September 19, 2006 - v2
Checksum:i3496D481AB876545
GO

Sequence cautioni

The sequence AAK18789.1 differs from that shown. Reason: Frameshift at position 502. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 492DL → EV in AAK18789 (PubMed:11355701).Curated
Sequence conflicti243 – 2442DQ → GR in AAH06661 (PubMed:15489334).Curated
Sequence conflicti270 – 2701E → G in BAC41182 (PubMed:16141072).Curated
Sequence conflicti434 – 4363Missing in AAH06661 (PubMed:15489334).Curated
Sequence conflicti474 – 4741I → V in BAC34064 (PubMed:16141072).Curated
Sequence conflicti517 – 5171K → N in AAK18789 (PubMed:11355701).Curated
Sequence conflicti523 – 5231H → P in AAK18789 (PubMed:11355701).Curated
Sequence conflicti525 – 5251P → R in BAC41182 (PubMed:16141072).Curated
Sequence conflicti536 – 5361Q → P in AAK18789 (PubMed:11355701).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300293 mRNA. Translation: AAK18789.1. Frameshift.
AK050090 mRNA. Translation: BAC34064.1.
AK090351 mRNA. Translation: BAC41182.1.
BC006661 mRNA. Translation: AAH06661.1.
CCDSiCCDS23435.1.
RefSeqiNP_113580.2. NM_031403.3.
UniGeneiMm.31324.

Genome annotation databases

EnsembliENSMUST00000066650; ENSMUSP00000070991; ENSMUSG00000032469.
GeneIDi83703.
KEGGimmu:83703.
UCSCiuc009rei.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300293 mRNA. Translation: AAK18789.1. Frameshift.
AK050090 mRNA. Translation: BAC34064.1.
AK090351 mRNA. Translation: BAC41182.1.
BC006661 mRNA. Translation: AAH06661.1.
CCDSiCCDS23435.1.
RefSeqiNP_113580.2. NM_031403.3.
UniGeneiMm.31324.

3D structure databases

ProteinModelPortaliQ923B1.
SMRiQ923B1. Positions 3-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070991.

PTM databases

iPTMnetiQ923B1.
PhosphoSiteiQ923B1.

Proteomic databases

EPDiQ923B1.
MaxQBiQ923B1.
PaxDbiQ923B1.
PeptideAtlasiQ923B1.
PRIDEiQ923B1.

Protocols and materials databases

DNASUi83703.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066650; ENSMUSP00000070991; ENSMUSG00000032469.
GeneIDi83703.
KEGGimmu:83703.
UCSCiuc009rei.1. mouse.

Organism-specific databases

CTDi51163.
MGIiMGI:1931520. Dbr1.

Phylogenomic databases

eggNOGiKOG2863. Eukaryota.
ENOG410XP0F. LUCA.
GeneTreeiENSGT00510000047481.
HOGENOMiHOG000216468.
HOVERGENiHBG079917.
InParanoidiQ923B1.
KOiK18328.
OMAiLMQHQAK.
OrthoDBiEOG7BW0J7.
PhylomeDBiQ923B1.
TreeFamiTF313221.

Miscellaneous databases

PROiQ923B1.
SOURCEiSearch...

Gene expression databases

BgeeiQ923B1.
CleanExiMM_DBR1.
ExpressionAtlasiQ923B1. baseline and differential.
GenevisibleiQ923B1. MM.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR007708. DBR1_C.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF05011. DBR1. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
SMARTiSM01124. DBR1. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and complementation test of the RNA lariat debranching enzyme cDNA from mouse."
    Kim H.-C., Kim G.-M., Yang J.-M., Ki J.W.
    Mol. Cells 11:198-203(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Liver.
  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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-489; SER-491; SER-494 AND SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Lung and Spleen.

Entry informationi

Entry nameiDBR1_MOUSE
AccessioniPrimary (citable) accession number: Q923B1
Secondary accession number(s): Q8C1T9, Q8C7J7, Q99MT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: July 6, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.