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Q5B630 (PABP_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polyadenylate-binding protein, cytoplasmic and nuclear
Short name=PABP
Short name=Poly(A)-binding protein
Alternative name(s):
Polyadenylate tail-binding protein
Gene names
Name:pab1
Synonyms:fabM
ORF Names:AN4000
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Induction

Constitutively expressed throughout the vegetative cell cycle. Ref.1

Sequence similarities

Belongs to the polyadenylate-binding protein type-1 family.

Contains 1 PABC domain.

Contains 4 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processTranslation regulation
Transport
mRNA processing
mRNA transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandRNA-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 732732Polyadenylate-binding protein, cytoplasmic and nuclear
PRO_0000295390

Regions

Domain42 – 12079RRM 1
Domain130 – 20778RRM 2
Domain223 – 30078RRM 3
Domain326 – 454129RRM 4
Domain630 – 70778PABC
Compositional bias477 – 4815Poly-Ala
Compositional bias495 – 625131Gly-rich

Experimental info

Sequence conflict4011K → E in AAB16848. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5B630 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 69D3FD71EA49668E

FASTA73279,321
        10         20         30         40         50         60 
MSAETSTTPA PAENTNGTPD NAPAPEVTAV EAPATTSQPH SASLYVGELD PSVTEAMLYE 

        70         80         90        100        110        120 
LFSSIGQVAS IRVCRDAVTR RSLGYAYVNY NDTAHGERAL DELNYTLIKG KPCRIMWSQR 

       130        140        150        160        170        180 
DPALRKTGQG NVFIKNLDSA IDNKALHDTF AAFGNILSCK VAQDEFGVSK GYGFVHYETA 

       190        200        210        220        230        240 
EAANNAIKHV NGMLLNDKKV FVGHHISKKD RQSKFEEMKA NFTNIYIKNI DPEVEDEEFR 

       250        260        270        280        290        300 
KLFEKFGEIT SATLSRDSEG KSRGFGFVNF STHESAQAAV EEMNDKEVRS QKLYVGRAQK 

       310        320        330        340        350        360 
KHEREEELRK QYEAARMEKA SKYQGVNLYV KNLTDDVDDD KLRELFGPYG TITSAKVMRD 

       370        380        390        400        410        420 
TAPVETATPE SETKESANKE NEKAAEGEKE PAAEEKEKEE KKEAEQKPEK KPLGKSKGFG 

       430        440        450        460        470        480 
FVCFSSPDEA SKAVTEMNQR MVNGKPLYVA LAQRKDVRRS QLEASIQARN NIRQQQAAAA 

       490        500        510        520        530        540 
AGMGQAYMAP AVFYGPGQQG FIPGAQRGGM FPPQPGMMMG MPGRPGQYPG PFPGQQGGRG 

       550        560        570        580        590        600 
VGPNQQIPPN FQGLPMGAMQ GPGIPNGMGY PMVQGQFGGG RGRGQVPGMG GPMRGGYGGG 

       610        620        630        640        650        660 
RGGVPLGGQM RPGQGGRGQA VGQPGPETPV GVLTAQALSA APPQQQKQML GEALYPKIQA 

       670        680        690        700        710        720 
TQPELAGKIT GMLLEMDNTE LLGLLEDDEA LRAKVDEALS VYDEYMKNKS DEPAAEKPKE 

       730 
AAQEAPAEEN KA

« Hide

References

« Hide 'large scale' references
[1]"Aspergillus fabM encodes an essential product that is related to poly(A)-binding proteins and activates development when overexpressed."
Marhoul J.F., Adams T.H.
Genetics 144:1463-1470(1996) [PubMed: 8978035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U70731 Genomic DNA. Translation: AAB16848.1.
AACD01000065 Genomic DNA. Translation: EAA59471.1.
BN001302 Genomic DNA. Translation: CBF74916.1.
RefSeqXP_661604.1. XM_656512.1.

3D structure databases

HSSPHSSP built from PDB template 1CVJ based on UniProtKB P11940.
ProteinModelPortalQ5B630.
SMRQ5B630. Positions 42-211, 633-712.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5B630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004687; CADANIAP00004687; CADANIAG00004687.
GeneID2873424.
KEGGani:AN4000.2.

Phylogenomic databases

OMADNKTLHE.
OrthoDBEOG4QJVWJ.
PhylomeDBQ5B630.

Family and domain databases

InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 5 hits.
G3DSA:1.10.1900.10. PABP_HYD. 1 hit.
KOK13126.
PfamPF00658. PABP. 1 hit.
PF00076. RRM_1. 5 hits.
[Graphical view]
SMARTSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMSSF63570. PABP_HYD. 1 hit.
TIGRFAMsTIGR01628. PABP-1234. 1 hit.
PROSITEPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePABP_EMENI
AccessionPrimary (citable) accession number: Q5B630
Secondary accession number(s): C8V5R9, Q92227
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: January 25, 2012
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents