Q9BZI7 (REN3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of nonsense transcripts 3B

Alternative name(s):
Nonsense mRNA reducing factor 3B
Up-frameshift suppressor 3 homolog B
Short name=hUpf3B
Up-frameshift suppressor 3 homolog on chromosome X
Short name=hUpf3p-X

Gene names

Name:	UPF3B
Synonyms:	RENT3B, UPF3X

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is indepenedent of association with UPF2 and components of the EJC core. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11
Subunit structure	Found in a post-splicing messenger ribonucleoprotein (mRNP) complex. Associates with the exon junction complex (EJC); the EJC core components EIF4A3 and the MAGOH-RBM8A dimer form a composite binding site for UPF3B which overlaps with the EJC binding site for WIBG. Interacts with EST1A, UPF2 and RBM8A. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Nucleus. Cytoplasm. Note: Shuttling between the nucleus and the cytoplasm. Ref.1 Ref.2
Tissue specificity	Expressed in testis, uterus, prostate, heart, muscle, brain, spinal cord and placenta. Ref.2
Involvement in disease	Mental retardation, X-linked, syndromic, 14 (MRXS14) [MIM:300676]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRXS14 patients manifest mental retardation associated with other variable signs such as autistic features, slender build, poor musculature, long, thin face, high-arched palate, high nasal bridge, and pectus deformities. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19
Sequence similarities	Belongs to the RENT3 family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Transport mRNA transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Mental retardation
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of translation Inferred from direct assay Ref.10. Source: UniProtKB termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome exon-exon junction complex Inferred from direct assay Ref.10. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	mRNA binding Inferred from direct assay Ref.5. Source: UniProtKB nucleocytoplasmic transporter activity Non-traceable author statement Ref.1. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4A3	P38919	4	EBI-372780,EBI-299104
RBM8A	Q9Y5S9	8	EBI-372780,EBI-447231
UPF1	Q92900	8	EBI-372780,EBI-373471
UPF2	Q9HAU5	6	EBI-372780,EBI-372073

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BZI7-1)

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: Q9BZI7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     270-282: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 483

483

Regulator of nonsense transcripts 3B

PRO_0000215297

Regions

Region

30 – 255

226

Necessary for interaction with UPF2

Region

52 – 57

6

Binds to UPF2

Region

94 – 483

390

Sufficient for association with EJC core

Region

430 – 447

18

Necessary for interaction with RBM8A and for activating NMD

Amino acid modifications

Modified residue

169

1

Phosphothreonine Ref.12 Ref.13 Ref.16

Modified residue

198

1

Phosphothreonine Ref.14

Modified residue

310

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

270 – 282

13

Missing in isoform 2.

VSP_012963

Natural variant

160

1

Y → D in MRXS14. Ref.19

VAR_037666

Experimental info

Mutagenesis

52

1

K → E: Abolishes interaction with UPF2. Ref.17

Mutagenesis

53 – 58

6

VVIRRL → AVARRA: Abolishes interaction with UPF2. Ref.2

Mutagenesis

56

1

R → E: Does not abolish interaction with UPF2. Ref.17

Mutagenesis

117 – 119

3

YVF → DVD: Abolishes interaction with UPF2. Ref.2

Mutagenesis

430

1

R → A: Reduces NMD. Ref.7

Mutagenesis

432

1

R → A: Reduces NMD. Ref.7 Ref.10

Mutagenesis

434 – 447

14

Missing: Abolishes NMD. Ref.7 Ref.18

Mutagenesis

434

1

K → A: Reduces NMD. Ref.7

Mutagenesis

435

1

D → A: Reduces NMD. Ref.7

Mutagenesis

436

1

R → A: Impairs association with EJC. Ref.7 Ref.18

Mutagenesis

436

1

R → A: Reduces NMD. Ref.7 Ref.18

Mutagenesis

441

1

L → F: Reduces NMD. Ref.7

Mutagenesis

442

1

Y → A: Impairs association with EJC. Ref.18

Mutagenesis

447

1

R → E: Abolishes NMD; when associated with E-449 and E-451. Ref.18

Mutagenesis

449

1

R → E: Abolishes NMD; when associated with E-447 and E-451. Ref.18

Mutagenesis

451

1

R → E: Abolishes NMD; when associated with E-447 and E-449. Ref.18

Sequence conflict

358

1

R → H in AAI21018. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

483

Helix Strand Turn

Details...

Beta strand

52 – 58

7

Helix

64 – 71

8

Beta strand

77 – 85

9

Beta strand

95 – 104

10

Helix

105 – 114

10

Beta strand

118 – 120

3

Beta strand

126 – 128

3

Beta strand

130 – 133

4

Turn

433 – 435

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: F5A8A395783D1A69	FASTA	483	57,762
	10 20 30 40 50 60 MKEEKEHRPK EKRVTLLTPA GATGSGGGTS GDSSKGEDKQ DRNKEKKEAL SKVVIRRLPP 70 80 90 100 110 120 TLTKEQLQEH LQPMPEHDYF EFFSNDTSLY PHMYARAYIN FKNQEDIILF RDRFDGYVFL 130 140 150 160 170 180 DNKGQEYPAI VEFAPFQKAA KKKTKKRDTK VGTIDDDPEY RKFLESYATD NEKMTSTPET 190 200 210 220 230 240 LLEEIEAKNR ELIAKKTTPL LSFLKNKQRM REEKREERRR REIERKRQRE EERRKWKEEE 250 260 270 280 290 300 KRKRKDIEKL KKIDRIPERD KLKDEPKIKV HRFLLQAVNQ KNLLKKPEKG DEKELDKREK 310 320 330 340 350 360 AKKLDKENLS DERASGQSCT LPKRSDSELK DEKPKRPEDE SGRDYRERER EYERDQERIL 370 380 390 400 410 420 RERERLKRQE EERRRQKERY EKEKTFKRKE EEMKKEKDTL RDKGKKAEST ESIGSSEKTE 430 440 450 460 470 480 KKEEVVKRDR IRNKDRPAMQ LYQPGARSRN RLCPPDDSTK SGDSAAERKQ ESGISHRKEG GEE
	Isoform 2 [UniParc]. Checksum: C012044D45D9957F	FASTA	470	56,213
	10 20 30 40 50 60 MKEEKEHRPK EKRVTLLTPA GATGSGGGTS GDSSKGEDKQ DRNKEKKEAL SKVVIRRLPP 70 80 90 100 110 120 TLTKEQLQEH LQPMPEHDYF EFFSNDTSLY PHMYARAYIN FKNQEDIILF RDRFDGYVFL 130 140 150 160 170 180 DNKGQEYPAI VEFAPFQKAA KKKTKKRDTK VGTIDDDPEY RKFLESYATD NEKMTSTPET 190 200 210 220 230 240 LLEEIEAKNR ELIAKKTTPL LSFLKNKQRM REEKREERRR REIERKRQRE EERRKWKEEE 250 260 270 280 290 300 KRKRKDIEKL KKIDRIPERD KLKDEPKIKL LKKPEKGDEK ELDKREKAKK LDKENLSDER 310 320 330 340 350 360 ASGQSCTLPK RSDSELKDEK PKRPEDESGR DYREREREYE RDQERILRER ERLKRQEEER 370 380 390 400 410 420 RRQKERYEKE KTFKRKEEEM KKEKDTLRDK GKKAESTESI GSSEKTEKKE EVVKRDRIRN 430 440 450 460 470 KDRPAMQLYQ PGARSRNRLC PPDDSTKSGD SAAERKQESG ISHRKEGGEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon." Lykke-Andersen J., Shu M.-D., Steitz J.A. Cell 103:1121-1131(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH UPF1 AND UPF2, SUBCELLULAR LOCATION.
[2]	"Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4)." Serin G., Gersappe A., Black J.D., Aronoff R., Maquat L.E. Mol. Cell. Biol. 21:209-223(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UPF2, MUTAGENESIS OF 53-VAL--LEU-58 AND 117-TYR--PHE-119, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 2).
[5]	"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex." Kim V.N., Kataoka N., Dreyfuss G. Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBM8A, IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, ASSOCIATION WITH THE EJC COMPLEX, RNA-BINDING.
[6]	"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1." Lykke-Andersen J., Shu M.-D., Steitz J.A. Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, ASSOCIATION WITH THE EJC COMPLEX.
[7]	"Y14 and hUpf3b form an NMD-activating complex." Gehring N.H., Neu-Yilik G., Schell T., Hentze M.W., Kulozik A.E. Mol. Cell 11:939-949(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH RBM8A, MUTAGENESIS OF ARG-430; ARG-432; 434-LYS--ARG-447; LYS-434; ASP-435; ARG-436 AND LEU-441.
[8]	"Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1." Chiu S.-Y., Serin G., Ohara O., Maquat L.E. RNA 9:77-87(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EST1A.
[9]	"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements." Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E. Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD), ASSOCIATION WITH THE EJC COMPLEX, IDENTIFICATION IN A COMPLEX WITH UPF2 AND RNPS1.
[10]	"Functions of hUpf3a and hUpf3b in nonsense-mediated mRNA decay and translation." Kunz J.B., Neu-Yilik G., Hentze M.W., Kulozik A.E., Gehring N.H. RNA 12:1015-1022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD), FUNCTION IN TRANSLATION STIMULATION, ASSOCIATION WITH THE EJC COMPLEX, MUTAGENESIS OF ARG-432.
[11]	"NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity." Chamieh H., Ballut L., Bonneau F., Le Hir H. Nat. Struct. Mol. Biol. 15:85-93(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, RECONSTITUTION OF THE EJC CORE-UPF COMPLEX.
[12]	"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 THR-169, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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 THR-198, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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 THR-169 AND SER-310, MASS SPECTROMETRY.
[17]	"The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3." Kadlec J., Izaurralde E., Cusack S. Nat. Struct. Mol. Biol. 11:330-337(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 50-140 IN COMPLEX WITH UPF2, RNA-BINDING, MUTAGENESIS OF LYS-52 AND ARG-56.
[18]	"Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex." Buchwald G., Ebert J., Basquin C., Sauliere J., Jayachandran U., Bono F., Le Hir H., Conti E. Proc. Natl. Acad. Sci. U.S.A. 107:10050-10055(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 424-483 IN COMPLEX WITH EIF4A3; MAGOH; RBM8A AND CASC3, MUTAGENESIS OF ARG-436; TYR-442; ARG-447; ARG-449 AND ARG-451.
[19]	"Mutations in UPF3B, a member of the nonsense-mediated mRNA decay complex, cause syndromic and nonsyndromic mental retardation." Tarpey P.S., Raymond F.L., Nguyen L.S., Rodriguez J., Hackett A., Vandeleur L., Smith R., Shoubridge C., Edkins S., Stevens C., O'Meara S., Tofts C., Barthorpe S., Buck G., Cole J., Halliday K., Hills K., Jones D. , Mironenko T., Perry J., Varian J., West S., Widaa S., Teague J., Dicks E., Butler A., Menzies A., Richardson D., Jenkinson A., Shepherd R., Raine K., Moon J., Luo Y., Parnau J., Bhat S.S., Gardner A., Corbett M., Brooks D., Thomas P., Parkinson-Lawrence E., Porteous M.E., Warner J.P., Sanderson T., Pearson P., Simensen R.J., Skinner C., Hoganson G., Superneau D., Wooster R., Bobrow M., Turner G., Stevenson R.E., Schwartz C.E., Futreal P.A., Srivastava A.K., Stratton M.R., Gecz J. Nat. Genet. 39:1127-1133(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRXS14 ASP-160.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY013251 mRNA. Translation: AAG48511.1.
AF318576 mRNA. Translation: AAG60691.1.
CH471161 Genomic DNA. Translation: EAW89842.1.
CH471161 Genomic DNA. Translation: EAW89844.1.
CH471161 Genomic DNA. Translation: EAW89845.1.
CH471161 Genomic DNA. Translation: EAW89846.1.
BC121017 mRNA. Translation: AAI21018.1.

IPI

IPI00023409.
IPI00074183.

RefSeq

NP_075386.1. NM_023010.3.
NP_542199.1. NM_080632.2.

UniGene

Hs.103832.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UW4	X-ray	1.95	A/C	50-140	[»]
2XB2	X-ray	3.40	G/U	424-483	[»]

ProteinModelPortal

Q9BZI7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31143N.

IntAct

Q9BZI7. 19 interactions.

MINT

MINT-265168.

STRING

9606.ENSP00000276201.

PTM databases

PhosphoSite

Q9BZI7.

Polymorphism databases

DMDM

60390643.

Proteomic databases

PaxDb

Q9BZI7.

PRIDE

Q9BZI7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276201; ENSP00000276201; ENSG00000125351.
ENST00000345865; ENSP00000245418; ENSG00000125351.

GeneID

65109.

KEGG

hsa:65109.

UCSC

uc004erz.2. human.
uc004esa.2. human.

Organism-specific databases

CTD

65109.

GeneCards

GC0XM118967.

HGNC

HGNC:20439. UPF3B.

HPA

HPA001800.
HPA001882.

MIM

300298. gene.
300676. phenotype.

neXtProt

NX_Q9BZI7.

Orphanet

323. FG syndrome.
776. X-linked intellectual deficit with marfanoid habitus.
777. X-linked nonsyndromic intellectual deficit.

PharmGKB

PA128394708.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG251520.

HOGENOM

HOG000230909.

HOVERGEN

HBG059714.

InParanoid

Q9BZI7.

KO

K14328.

OMA

HLFARAY.

OrthoDB

EOG4001K9.

PhylomeDB

Q9BZI7.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

Bgee

Q9BZI7.

CleanEx

HS_UPF3B.

Genevestigator

Q9BZI7.

GermOnline

ENSG00000125351. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR005120. Nonsense_mediated_decay_UPF3.
IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]

Pfam

PF03467. Smg4_UPF3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UPF3B. human.

EvolutionaryTrace

Q9BZI7.

GenomeRNAi

65109.

NextBio

67302.

SOURCE

Search...

Entry information

Entry name

REN3B_HUMAN

Accession

Primary (citable) accession number: Q9BZI7
Secondary accession number(s): D3DWI3 , D3DWI4, Q0VAK8, Q9H1J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 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.