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Q9BZI7 (REN3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence 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 independent 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 adaptive 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 processmRNA transport
Nonsense-mediated mRNA decay
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Mental retardation
   LigandRNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA metabolic process

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

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Non-traceable author statement Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

exon-exon junction complex

Inferred from direct assay Ref.10. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionmRNA 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

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20930030. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Regulator of nonsense transcripts 3B
PRO_0000215297

Regions

Region30 – 255226Necessary for interaction with UPF2
Region52 – 576Binds to UPF2
Region94 – 483390Sufficient for association with EJC core
Region430 – 44718Necessary for interaction with RBM8A and for activating NMD

Amino acid modifications

Modified residue1691Phosphothreonine Ref.12 Ref.13 Ref.16
Modified residue1981Phosphothreonine Ref.14
Modified residue3101Phosphoserine Ref.16

Natural variations

Alternative sequence270 – 28213Missing in isoform 2.
VSP_012963
Natural variant1601Y → D in MRXS14. Ref.19
VAR_037666

Experimental info

Mutagenesis521K → E: Abolishes interaction with UPF2. Ref.17
Mutagenesis53 – 586VVIRRL → AVARRA: Abolishes interaction with UPF2. Ref.2
Mutagenesis561R → E: Does not abolish interaction with UPF2. Ref.17
Mutagenesis117 – 1193YVF → DVD: Abolishes interaction with UPF2. Ref.2
Mutagenesis4301R → A: Reduces NMD. Ref.7
Mutagenesis4321R → A: Reduces NMD. Ref.7 Ref.10
Mutagenesis434 – 44714Missing: Abolishes NMD. Ref.7 Ref.18
Mutagenesis4341K → A: Reduces NMD. Ref.7
Mutagenesis4351D → A: Reduces NMD. Ref.7
Mutagenesis4361R → A: Impairs association with EJC. Ref.7 Ref.18
Mutagenesis4361R → A: Reduces NMD. Ref.7 Ref.18
Mutagenesis4411L → F: Reduces NMD. Ref.7
Mutagenesis4421Y → A: Impairs association with EJC. Ref.18
Mutagenesis4471R → E: Abolishes NMD; when associated with E-449 and E-451. Ref.18
Mutagenesis4491R → E: Abolishes NMD; when associated with E-447 and E-451. Ref.18
Mutagenesis4511R → E: Abolishes NMD; when associated with E-447 and E-449. Ref.18
Sequence conflict3581R → H in AAI21018. Ref.4

Secondary structure

.................. 483
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: F5A8A395783D1A69

FASTA48357,762
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C012044D45D9957F
Show »

FASTA47056,213

References

« Hide '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. expand/collapse author list , 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, 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, 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , 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.
CCDSCCDS14587.1. [Q9BZI7-2]
CCDS14588.1. [Q9BZI7-1]
RefSeqNP_075386.1. NM_023010.3. [Q9BZI7-2]
NP_542199.1. NM_080632.2. [Q9BZI7-1]
UniGeneHs.103832.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UW4X-ray1.95A/C50-140[»]
2XB2X-ray3.40G/U424-483[»]
ProteinModelPortalQ9BZI7.
SMRQ9BZI7. Positions 50-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122396. 23 interactions.
DIPDIP-31143N.
IntActQ9BZI7. 19 interactions.
MINTMINT-265168.
STRING9606.ENSP00000276201.

PTM databases

PhosphoSiteQ9BZI7.

Polymorphism databases

DMDM60390643.

Proteomic databases

MaxQBQ9BZI7.
PaxDbQ9BZI7.
PRIDEQ9BZI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276201; ENSP00000276201; ENSG00000125351. [Q9BZI7-1]
ENST00000345865; ENSP00000245418; ENSG00000125351. [Q9BZI7-2]
GeneID65109.
KEGGhsa:65109.
UCSCuc004erz.2. human. [Q9BZI7-1]
uc004esa.2. human. [Q9BZI7-2]

Organism-specific databases

CTD65109.
GeneCardsGC0XM118967.
HGNCHGNC:20439. UPF3B.
HPAHPA001800.
HPA001882.
MIM300298. gene.
300676. phenotype.
neXtProtNX_Q9BZI7.
Orphanet323. FG syndrome.
776. X-linked intellectual disability with marfanoid habitus.
777. X-linked non-syndromic intellectual disability.
PharmGKBPA128394708.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251520.
HOGENOMHOG000230909.
HOVERGENHBG059714.
InParanoidQ9BZI7.
KOK14328.
OMAYFEFFAN.
OrthoDBEOG7M6D9K.
PhylomeDBQ9BZI7.
TreeFamTF316034.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ9BZI7.
BgeeQ9BZI7.
CleanExHS_UPF3B.
GenevestigatorQ9BZI7.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR005120. Nonsense_mediated_decay_UPF3.
IPR012677. Nucleotide-bd_a/b_plait.
[Graphical view]
PfamPF03467. Smg4_UPF3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUPF3B. human.
EvolutionaryTraceQ9BZI7.
GeneWikiUPF3B.
GenomeRNAi65109.
NextBio67302.
PROQ9BZI7.
SOURCESearch...

Entry information

Entry nameREN3B_HUMAN
AccessionPrimary (citable) accession number: Q9BZI7
Secondary accession number(s): D3DWI3 expand/collapse secondary AC list , D3DWI4, Q0VAK8, Q9H1J0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 117 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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