Q9UK59 (DBR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lariat debranching enzyme
EC=3.1.-.-

Gene names

Name:

DBR1

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	544 AA.
Sequence status	Complete.
Protein existence	Evidence 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 a 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.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	RNA lariat debranching enzyme activity Inferred from mutant phenotype Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 544	544	Lariat debranching enzyme		PRO_0000250358
Amino acid modifications
	Modified residue	128	1	N6-acetyllysine Ref.9
	Modified residue	474	1	Phosphoserine Ref.7 Ref.8
	Modified residue	478	1	Phosphoserine Ref.7
	Modified residue	479	1	Phosphoserine Ref.7
	Modified residue	499	1	Phosphoserine By similarity
	Modified residue	514	1	Phosphoserine Ref.6 Ref.7
Natural variations
	Alternative sequence	1 – 232	232	Missing in isoform 2.		VSP_020631
	Alternative sequence	233 – 237	5	ALMQH → MIHIV in isoform 2.		VSP_020632
Experimental info
	Sequence conflict	308	1	N → S in BAA90954. Ref.2
	Sequence conflict	496	1	T → L in AAD53327. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2006. Version 2. Checksum: DDA5F4FADA194BAA	FASTA	544	61,555
	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
	Isoform 2 [UniParc]. Checksum: 4E874B871647E9F5	FASTA	312	35,022
	10 20 30 40 50 60 MIHIVQAKDK GQTARATKFL ALDKCLPHRD FLQILEIEHD PSAPDYLEYD IEWLTILRAT 70 80 90 100 110 120 DDLINVTGRL WNMPENNGLH ARWDYSATEE GMKEVLEKLN HDLKVPCNFS VTAACYDPSK 130 140 150 160 170 180 PQTQMQLIHR INPQTTEFCA QLGIIDINVR LQKSKEEHHV CGEYEEQDDV ESNDSGEDQS 190 200 210 220 230 240 EYNTDTSALS SINPDEIMLD EEEDEDSIVS AHSGMNTPSV EPSDQASEFS ASFSDVRILP 250 260 270 280 290 300 GSMIVSSDDT VDSTIDREGK PGGTVESGNG EDLTKVPLKR LSDEHEPEQR KKIKRRNQAI 310 YAAVDDDDDD AA

References

	« Hide 'large scale' referencesShow '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: 10982890] [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: 14702039] [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: 15489334] [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: 2435736] [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: 16232320] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, MASS SPECTROMETRY. 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-478; SER-479 AND SER-514, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00305545. IPI00787976.
RefSeq	NP_057300.2. NM_016216.3.
UniGene	Hs.477700.
3D structure databases
ProteinModelPortal	Q9UK59.
SMR	Q9UK59. Positions 1-42.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UK59. 1 interaction.
STRING	Q9UK59.
PTM databases
PhosphoSite	Q9UK59.
Polymorphism databases
DMDM	115311701.
Proteomic databases
PeptideAtlas	Q9UK59.
PRIDE	Q9UK59.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260803; ENSP00000260803; ENSG00000138231.
GeneID	51163.
KEGG	hsa:51163.
UCSC	uc003ert.1. human. uc003erv.1. human.
Organism-specific databases
CTD	51163.
GeneCards	GC03M137879.
H-InvDB	HIX0018421.
HGNC	HGNC:15594. DBR1.
HPA	HPA035365.
MIM	607024. gene.
neXtProt	NX_Q9UK59.
PharmGKB	PA27166.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16494.
GeneTree	ENSGT00510000047481.
HOGENOM	HBG605012.
HOVERGEN	HBG079917.
InParanoid	Q9UK59.
OMA	LMQHQAK.
OrthoDB	EOG4QNMVW.
PhylomeDB	Q9UK59.
Gene expression databases
ArrayExpress	Q9UK59.
Bgee	Q9UK59.
CleanEx	HS_DBR1.
Genevestigator	Q9UK59.
GermOnline	ENSG00000138231. Homo sapiens.
Family and domain databases
InterPro	IPR007708. DBR1_C. IPR004843. Metallo_PEstase_dom. [Graphical view]
Pfam	PF05011. DBR1. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	54089.
SOURCE	Search...

Entry information

Entry name

DBR1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 71 of the entry and version 2 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.