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Protein

Embryonic polyadenylate-binding protein 2-B

Gene

Pabpn1l-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds the poly(A) tail of mRNA. Unable to interact with the cap-binding complex and is therefore unlikely to be involved in translation initiation.By similarity1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Embryonic polyadenylate-binding protein 2-B
Short name:
Embryonic poly(A)-binding protein 2-B
Short name:
XePABP2-B
Short name:
ePABP-2B
Short name:
ePABP2-B
Alternative name(s):
Embryonic poly(A)-binding protein type II-B
Gene namesi
Name:Pabpn1l-b
Synonyms:epabp2-b, pabpnl1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1000606. pabpn1l.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Embryonic polyadenylate-binding protein 2-BPRO_0000239464Add
BLAST

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Restricted to oogenesis, early embryogenesis and the adult ovary. Levels decrease after the onset of zygotic transcription (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer; Upon poly(A) binding, undergoes a dimer-monomer transition that removes the polyproline motif from the RNA recognition site and allows it to be replaced by the adenosine nucleotides of poly(A).1 Publication

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi84 – 929Combined sources
Beta strandi94 – 1007Combined sources
Helixi106 – 1149Combined sources
Beta strandi119 – 1279Combined sources
Beta strandi134 – 14310Combined sources
Helixi144 – 1518Combined sources
Turni152 – 1554Combined sources
Beta strandi164 – 1696Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JWNNMR-A/B60-180[»]
ProteinModelPortaliQ6TY21.
SMRiQ6TY21. Positions 60-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6TY21.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 17078RRMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG107480.
KOiK14396.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6TY21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSERVSEEPG LDKGDRAEEC ELDDPELKAI RMRVREMEEE AERLKGLSGQ
60 70 80 90 100
DKSIGVSTRP CMQTTHSKMT AGAYTEGPPQ PLSAEEKKEI DKRSVYVGNV
110 120 130 140 150
DYGSTAQDLE AHFSSCGSIN RITILCDKFS GHPKGYAYIE FAERNSVDAA
160 170 180 190 200
VAMDETVFRG RTIKVLPKRT NMPGISSTDR GGFRGRPRGN RGNYQRGQRP
210
RGRPFRGRGR PGPLNNPY
Length:218
Mass (Da):24,270
Last modified:July 5, 2004 - v1
Checksum:i3571AC009E95EDBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY382837 mRNA. Translation: AAR26263.1.
RefSeqiNP_001084418.1. NM_001090949.1.
UniGeneiXl.86989.

Genome annotation databases

GeneIDi403372.
KEGGixla:403372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY382837 mRNA. Translation: AAR26263.1.
RefSeqiNP_001084418.1. NM_001090949.1.
UniGeneiXl.86989.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JWNNMR-A/B60-180[»]
ProteinModelPortaliQ6TY21.
SMRiQ6TY21. Positions 60-180.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403372.
KEGGixla:403372.

Organism-specific databases

CTDi403372.
XenbaseiXB-GENE-1000606. pabpn1l.

Phylogenomic databases

HOVERGENiHBG107480.
KOiK14396.

Miscellaneous databases

EvolutionaryTraceiQ6TY21.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Xenopus embryonic poly(A) binding protein 2 (ePABP2) defines a new family of cytoplasmic poly(A) binding proteins expressed during the early stages of vertebrate development."
    Good P.J., Abler L., Herring D., Sheets M.D.
    Genesis 38:166-175(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Tissue: Oocyte1 Publication.
  2. "Structural basis for RNA recognition by a type II poly(A)-binding protein."
    Song J., McGivern J.V., Nichols K.W., Markley J.L., Sheets M.D.
    Proc. Natl. Acad. Sci. U.S.A. 105:15317-15322(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 60-180, SUBUNIT.

Entry informationi

Entry nameiEPA2B_XENLA
AccessioniPrimary (citable) accession number: Q6TY21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: July 5, 2004
Last modified: January 20, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.