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Q9UK59 (DBR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lariat debranching enzyme

EC=3.1.-.-
Gene names
Name:DBR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Catalytic activity

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

Cofactor

Divalent metal cations. Ref.4

Subcellular location

Nucleus Probable.

Miscellaneous

Cells lacking DBR1 show an inhibition of HIV-1 replication.

Sequence similarities

Belongs to the lariat debranching enzyme family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.4

Sequence caution

The sequence AAD53327.2 differs from that shown. Reason: Frameshift at positions 450 and 463.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UK59-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UK59-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.
     233-237: ALMQH → MIHIV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 544544Lariat debranching enzyme
PRO_0000250358

Amino acid modifications

Modified residue1281N6-acetyllysine Ref.8
Modified residue4741Phosphoserine Ref.7
Modified residue4781Phosphoserine Ref.7
Modified residue4791Phosphoserine Ref.7
Modified residue4991Phosphoserine By similarity
Modified residue5141Phosphoserine Ref.6 Ref.9 Ref.11

Natural variations

Alternative sequence1 – 232232Missing in isoform 2.
VSP_020631
Alternative sequence233 – 2375ALMQH → MIHIV in isoform 2.
VSP_020632

Experimental info

Sequence conflict3081N → S in BAA90954. Ref.2
Sequence conflict4961T → L in AAD53327. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 19, 2006. Version 2.
Checksum: DDA5F4FADA194BAA

FASTA54461,555
        10         20         30         40         50         60 
MRVAVAGCCH GELDKIYETL ALAERRGPGP VDLLLCCGDF QAVRNEADLR CMAVPPKYRH 

        70         80         90        100        110        120 
MQTFYRYYSG EKKAPVLTLF IGGNHEASNH LQELPYGGWV APNIYYLGLA GVVKYRGVRI 

       130        140        150        160        170        180 
GGISGIFKSH DYRKGHFECP PYNSSTIRSI YHVRNIEVYK LKQLKQPIDI FLSHDWPRSI 

       190        200        210        220        230        240 
YHYGNKKQLL KTKSFFRQEV ENNTLGSPAA SELLEHLKPT YWFSAHLHVK FAALMQHQAK 

       250        260        270        280        290        300 
DKGQTARATK FLALDKCLPH RDFLQILEIE HDPSAPDYLE YDIEWLTILR ATDDLINVTG 

       310        320        330        340        350        360 
RLWNMPENNG LHARWDYSAT EEGMKEVLEK LNHDLKVPCN FSVTAACYDP SKPQTQMQLI 

       370        380        390        400        410        420 
HRINPQTTEF CAQLGIIDIN VRLQKSKEEH HVCGEYEEQD DVESNDSGED QSEYNTDTSA 

       430        440        450        460        470        480 
LSSINPDEIM LDEEEDEDSI VSAHSGMNTP SVEPSDQASE FSASFSDVRI LPGSMIVSSD 

       490        500        510        520        530        540 
DTVDSTIDRE GKPGGTVESG NGEDLTKVPL KRLSDEHEPE QRKKIKRRNQ AIYAAVDDDD 


DDAA 

« Hide

Isoform 2 [UniParc].

Checksum: 4E874B871647E9F5
Show »

FASTA31235,022

References

« Hide 'large scale' references
[1]"Human RNA lariat debranching enzyme cDNA complements the phenotypes of Saccharomyces cerevisiae dbr1 and Schizosaccharomyces pombe dbr1 mutants."
Kim J.-W., Kim H.-C., Kim G.-M., Yang J.-M., Boeke J.D., Nam K.
Nucleic Acids Res. 28:3666-3673(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Colon.
[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] (ISOFORM 1).
Tissue: Brain.
[4]"Purification of a RNA debranching activity from HeLa cells."
Arenas J., Hurwitz J.
J. Biol. Chem. 262:4274-4279(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"DBR1 siRNA inhibition of HIV-1 replication."
Ye Y., De Leon J., Yokoyama N., Naidu Y., Camerini D.
Retrovirology 2:63-63(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-478 AND SER-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF180919 mRNA. Translation: AAD53327.2. Frameshift.
AK000116 mRNA. Translation: BAA90954.1.
BC009472 mRNA. Translation: AAH09472.1.
CCDSCCDS33863.1. [Q9UK59-1]
RefSeqNP_057300.2. NM_016216.3. [Q9UK59-1]
UniGeneHs.477700.

3D structure databases

ProteinModelPortalQ9UK59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119344. 4 interactions.
IntActQ9UK59. 3 interactions.
STRING9606.ENSP00000260803.

PTM databases

PhosphoSiteQ9UK59.

Polymorphism databases

DMDM115311701.

Proteomic databases

MaxQBQ9UK59.
PaxDbQ9UK59.
PeptideAtlasQ9UK59.
PRIDEQ9UK59.

Protocols and materials databases

DNASU51163.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260803; ENSP00000260803; ENSG00000138231. [Q9UK59-1]
GeneID51163.
KEGGhsa:51163.
UCSCuc003ert.3. human. [Q9UK59-2]
uc003eru.3. human. [Q9UK59-1]

Organism-specific databases

CTD51163.
GeneCardsGC03M137879.
HGNCHGNC:15594. DBR1.
HPAHPA035365.
MIM607024. gene.
neXtProtNX_Q9UK59.
PharmGKBPA27166.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG133819.
HOGENOMHOG000216468.
HOVERGENHBG079917.
InParanoidQ9UK59.
OMAKVPCNFS.
OrthoDBEOG7BW0J7.
PhylomeDBQ9UK59.
TreeFamTF313221.

Gene expression databases

ArrayExpressQ9UK59.
BgeeQ9UK59.
CleanExHS_DBR1.
GenevestigatorQ9UK59.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR007708. DBR1_C.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF05011. DBR1. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Other

GeneWikiDBR1.
GenomeRNAi51163.
NextBio54089.
PROQ9UK59.
SOURCESearch...

Entry information

Entry nameDBR1_HUMAN
AccessionPrimary (citable) accession number: Q9UK59
Secondary accession number(s): Q96GH0, Q9NXQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM