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Q9UK59

- DBR1_HUMAN

UniProt

Q9UK59 - DBR1_HUMAN

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Protein

Lariat debranching enzyme

Gene

DBR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.2 Publications

Catalytic activityi

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

Cofactori

a divalent metal cation1 PublicationNote: Divalent metal cations.1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA lariat debranching enzyme activity Source: UniProtKB

GO - Biological processi

  1. mRNA splicing, via spliceosome Source: Ensembl
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. RNA splicing, via transesterification reactions Source: UniProtKB
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:15594. DBR1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27166.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 544544Lariat debranching enzymePRO_0000250358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei474 – 4741Phosphoserine1 Publication
Modified residuei478 – 4781Phosphoserine1 Publication
Modified residuei479 – 4791Phosphoserine1 Publication
Modified residuei499 – 4991PhosphoserineBy similarity
Modified residuei514 – 5141Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UK59.
PaxDbiQ9UK59.
PeptideAtlasiQ9UK59.
PRIDEiQ9UK59.

PTM databases

PhosphoSiteiQ9UK59.

Expressioni

Gene expression databases

BgeeiQ9UK59.
CleanExiHS_DBR1.
ExpressionAtlasiQ9UK59. baseline and differential.
GenevestigatoriQ9UK59.

Organism-specific databases

HPAiHPA035365.

Interactioni

Protein-protein interaction databases

BioGridi119344. 5 interactions.
IntActiQ9UK59. 3 interactions.
STRINGi9606.ENSP00000260803.

Structurei

3D structure databases

ProteinModelPortaliQ9UK59.
SMRiQ9UK59. Positions 1-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the lariat debranching enzyme family.Curated

Phylogenomic databases

eggNOGiNOG133819.
GeneTreeiENSGT00510000047481.
HOGENOMiHOG000216468.
HOVERGENiHBG079917.
InParanoidiQ9UK59.
KOiK18328.
OMAiKVPCNFS.
OrthoDBiEOG7BW0J7.
PhylomeDBiQ9UK59.
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]
SUPFAMiSSF56300. SSF56300. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UK59-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRVAVAGCCH GELDKIYETL ALAERRGPGP VDLLLCCGDF QAVRNEADLR
60 70 80 90 100
CMAVPPKYRH MQTFYRYYSG EKKAPVLTLF IGGNHEASNH LQELPYGGWV
110 120 130 140 150
APNIYYLGLA GVVKYRGVRI GGISGIFKSH DYRKGHFECP PYNSSTIRSI
160 170 180 190 200
YHVRNIEVYK LKQLKQPIDI FLSHDWPRSI YHYGNKKQLL KTKSFFRQEV
210 220 230 240 250
ENNTLGSPAA SELLEHLKPT YWFSAHLHVK FAALMQHQAK DKGQTARATK
260 270 280 290 300
FLALDKCLPH RDFLQILEIE HDPSAPDYLE YDIEWLTILR ATDDLINVTG
310 320 330 340 350
RLWNMPENNG LHARWDYSAT EEGMKEVLEK LNHDLKVPCN FSVTAACYDP
360 370 380 390 400
SKPQTQMQLI HRINPQTTEF CAQLGIIDIN VRLQKSKEEH HVCGEYEEQD
410 420 430 440 450
DVESNDSGED QSEYNTDTSA LSSINPDEIM LDEEEDEDSI VSAHSGMNTP
460 470 480 490 500
SVEPSDQASE FSASFSDVRI LPGSMIVSSD DTVDSTIDRE GKPGGTVESG
510 520 530 540
NGEDLTKVPL KRLSDEHEPE QRKKIKRRNQ AIYAAVDDDD DDAA
Length:544
Mass (Da):61,555
Last modified:September 19, 2006 - v2
Checksum:iDDA5F4FADA194BAA
GO
Isoform 2 (identifier: Q9UK59-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.
     233-237: ALMQH → MIHIV

Note: No experimental confirmation available.

Show »
Length:312
Mass (Da):35,022
Checksum:i4E874B871647E9F5
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081N → S in BAA90954. (PubMed:14702039)Curated
Sequence conflicti496 – 4961T → L in AAD53327. (PubMed:10982890)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 232232Missing in isoform 2. 1 PublicationVSP_020631Add
BLAST
Alternative sequencei233 – 2375ALMQH → MIHIV in isoform 2. 1 PublicationVSP_020632

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180919 mRNA. Translation: AAD53327.2. Frameshift.
AK000116 mRNA. Translation: BAA90954.1.
BC009472 mRNA. Translation: AAH09472.1.
CCDSiCCDS33863.1. [Q9UK59-1]
RefSeqiNP_057300.2. NM_016216.3. [Q9UK59-1]
UniGeneiHs.477700.

Genome annotation databases

EnsembliENST00000260803; ENSP00000260803; ENSG00000138231. [Q9UK59-1]
GeneIDi51163.
KEGGihsa:51163.
UCSCiuc003ert.3. human. [Q9UK59-2]
uc003eru.3. human. [Q9UK59-1]

Polymorphism databases

DMDMi115311701.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF180919 mRNA. Translation: AAD53327.2 . Frameshift.
AK000116 mRNA. Translation: BAA90954.1 .
BC009472 mRNA. Translation: AAH09472.1 .
CCDSi CCDS33863.1. [Q9UK59-1 ]
RefSeqi NP_057300.2. NM_016216.3. [Q9UK59-1 ]
UniGenei Hs.477700.

3D structure databases

ProteinModelPortali Q9UK59.
SMRi Q9UK59. Positions 1-376.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119344. 5 interactions.
IntActi Q9UK59. 3 interactions.
STRINGi 9606.ENSP00000260803.

PTM databases

PhosphoSitei Q9UK59.

Polymorphism databases

DMDMi 115311701.

Proteomic databases

MaxQBi Q9UK59.
PaxDbi Q9UK59.
PeptideAtlasi Q9UK59.
PRIDEi Q9UK59.

Protocols and materials databases

DNASUi 51163.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260803 ; ENSP00000260803 ; ENSG00000138231 . [Q9UK59-1 ]
GeneIDi 51163.
KEGGi hsa:51163.
UCSCi uc003ert.3. human. [Q9UK59-2 ]
uc003eru.3. human. [Q9UK59-1 ]

Organism-specific databases

CTDi 51163.
GeneCardsi GC03M137879.
HGNCi HGNC:15594. DBR1.
HPAi HPA035365.
MIMi 607024. gene.
neXtProti NX_Q9UK59.
PharmGKBi PA27166.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG133819.
GeneTreei ENSGT00510000047481.
HOGENOMi HOG000216468.
HOVERGENi HBG079917.
InParanoidi Q9UK59.
KOi K18328.
OMAi KVPCNFS.
OrthoDBi EOG7BW0J7.
PhylomeDBi Q9UK59.
TreeFami TF313221.

Miscellaneous databases

GeneWikii DBR1.
GenomeRNAii 51163.
NextBioi 54089.
PROi Q9UK59.
SOURCEi Search...

Gene expression databases

Bgeei Q9UK59.
CleanExi HS_DBR1.
ExpressionAtlasi Q9UK59. baseline and differential.
Genevestigatori Q9UK59.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR007708. DBR1_C.
IPR029052. Metallo-depent_PP-like.
[Graphical view ]
Pfami PF05011. DBR1. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiDBR1_HUMAN
AccessioniPrimary (citable) accession number: Q9UK59
Secondary accession number(s): Q96GH0, Q9NXQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: November 26, 2014
This is version 99 of the entry and version 2 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

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3