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P11940

- PABP1_HUMAN

UniProt

P11940 - PABP1_HUMAN

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Protein

Polyadenylate-binding protein 1

Gene

PABPC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.4 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. poly(U) RNA binding Source: MGI
  5. protein C-terminus binding Source: UniProtKB
  6. translation activator activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. gene silencing by RNA Source: UniProtKB
  4. mRNA metabolic process Source: Reactome
  5. mRNA polyadenylation Source: UniProtKB
  6. mRNA splicing, via spliceosome Source: UniProtKB
  7. mRNA stabilization Source: UniProtKB
  8. negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  9. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  10. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  11. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  12. positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  13. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  14. positive regulation of translation Source: GOC
  15. RNA metabolic process Source: Reactome
  16. translation Source: Reactome
  17. translational initiation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 1
Short name:
PABP-1
Short name:
Poly(A)-binding protein 1
Gene namesi
Name:PABPC1
Synonyms:PAB1, PABP1, PABPC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:8554. PABPC1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  4. cytoplasmic stress granule Source: UniProtKB
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProtKB
  7. focal adhesion Source: UniProtKB
  8. membrane Source: UniProtKB
  9. nucleus Source: MGI
  10. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi455 – 4551R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-460. 1 Publication
Mutagenesisi460 – 4601R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455. 1 Publication

Organism-specific databases

PharmGKBiPA32880.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Polyadenylate-binding protein 1PRO_0000081698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei299 – 2991N6-methyllysine1 Publication
Modified residuei315 – 3151Phosphoserine2 Publications
Modified residuei455 – 4551Omega-N-methylated arginine; by CARM1; partial1 Publication
Modified residuei460 – 4601Omega-N-methylated arginine; by CARM1; partial1 Publication
Modified residuei493 – 4931Dimethylated arginine; alternate2 Publications
Modified residuei493 – 4931Omega-N-methylarginine; alternate2 Publications
Modified residuei512 – 5121N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by MAPKAPK2.3 Publications
Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine.3 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP11940.
PaxDbiP11940.
PRIDEiP11940.

PTM databases

PhosphoSiteiP11940.

Miscellaneous databases

PMAP-CutDBP11940.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP11940.
CleanExiHS_PABPC1.
ExpressionAtlasiP11940. baseline and differential.
GenevestigatoriP11940.

Organism-specific databases

HPAiCAB011536.
HPA045423.

Interactioni

Subunit structurei

May form homodimers. Component of a multisubunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Directly interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. The interaction with CSDE1 is direct and RNA-independent. Found in a mRNP complex with YBX2. Interacts with PAPD4/GLD2. Identified in the spliceosome C complex. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with NFX1. Interacts with PIWIL1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with LARP1 and LARP4B.21 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN2Q997006EBI-81531,EBI-697691
DDX3XO0057110EBI-81531,EBI-353779
EIF4G1Q046372EBI-81531,EBI-73711
GSPT1P15170-22EBI-81531,EBI-9094806
GSPT2Q8IYD17EBI-81531,EBI-3869637
HNRNPDQ14103-42EBI-81531,EBI-432545
IRS1P355682EBI-81531,EBI-517592
PAIP1Q9H07410EBI-81531,EBI-81519
PAIP2Q9BPZ35EBI-81531,EBI-2957445
PAN3Q58A454EBI-81531,EBI-2513054
SMG1Q96Q152EBI-81531,EBI-1049832
TNRC6BQ9UPQ93EBI-81531,EBI-947158
TNRC6CQ9HCJ017EBI-81531,EBI-6507625
TOB1P506164EBI-81531,EBI-723281
TOB2Q141064EBI-81531,EBI-2562000

Protein-protein interaction databases

BioGridi117939. 160 interactions.
DIPiDIP-31613N.
IntActiP11940. 86 interactions.
MINTiMINT-96210.
STRINGi9606.ENSP00000313007.

Structurei

Secondary structure

1
636
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176Combined sources
Helixi24 – 318Combined sources
Helixi32 – 343Combined sources
Beta strandi37 – 448Combined sources
Turni46 – 483Combined sources
Beta strandi51 – 6111Combined sources
Helixi62 – 7211Combined sources
Beta strandi83 – 864Combined sources
Helixi92 – 965Combined sources
Beta strandi100 – 1056Combined sources
Helixi112 – 1198Combined sources
Helixi120 – 1223Combined sources
Beta strandi125 – 1339Combined sources
Beta strandi136 – 14611Combined sources
Helixi148 – 15811Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi169 – 1746Combined sources
Helixi176 – 1838Combined sources
Helixi547 – 5515Combined sources
Helixi555 – 5573Combined sources
Helixi558 – 57316Combined sources
Turni575 – 5773Combined sources
Helixi578 – 5858Combined sources
Helixi590 – 5989Combined sources
Helixi600 – 61920Combined sources
Turni623 – 6253Combined sources
Beta strandi628 – 6303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVJX-ray2.60A/B/C/D/E/F/G/H1-190[»]
1G9LNMR-A498-636[»]
1JGNNMR-A544-636[»]
1JH4NMR-A544-636[»]
2K8GNMR-A90-182[»]
2RQGNMR-B541-623[»]
2RQHNMR-B541-623[»]
2X04X-ray1.49A/B545-619[»]
3KTPX-ray1.50A544-626[»]
3KTRX-ray1.70A544-626[»]
3KUIX-ray2.30A544-626[»]
3KUJX-ray1.40A544-626[»]
3KURX-ray2.50A/B/C/D/E/F/G/H544-617[»]
3KUSX-ray1.40A/B544-626[»]
3KUTX-ray1.50A/B544-626[»]
3PKNX-ray1.80A544-626[»]
3PTHX-ray1.70A543-621[»]
4F02X-ray2.00A/D1-190[»]
4F25X-ray1.90A99-199[»]
4F26X-ray2.00A99-199[»]
ProteinModelPortaliP11940.
SMRiP11940. Positions 10-435, 494-636.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11940.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 8979RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini99 – 17577RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 26878RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini294 – 37077RRM 4PROSITE-ProRule annotationAdd
BLAST
Domaini542 – 61978PABCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 289124CSDE1-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi495 – 5017Poly-Ala

Domaini

The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
The RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.

Sequence similaritiesi

Contains 1 PABC domain.PROSITE-ProRule annotation
Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
HOVERGENiHBG002295.
InParanoidiP11940.
KOiK13126.
OMAiXAVDEMN.
OrthoDBiEOG7RV9FP.
PhylomeDBiP11940.
TreeFamiTF300458.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P11940-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR
60 70 80 90 100
SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN
110 120 130 140 150
IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA
160 170 180 190 200
AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE
210 220 230 240 250
DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE
260 270 280 290 300
MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
310 320 330 340 350
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV
360 370 380 390 400
TEMNGRIVAT KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY
410 420 430 440 450
QPAPPSGYFM AAIPQTQNRA AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM
460 470 480 490 500
PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ RVANTSTQTM GPRPAAAAAA
510 520 530 540 550
ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ GQEPLTASML
560 570 580 590 600
ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP
610 620 630
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
Length:636
Mass (Da):70,671
Last modified:July 15, 1998 - v2
Checksum:i2EB1B02A346132EE
GO
Isoform 2 (identifier: P11940-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     447-535: Missing.

Note: No experimental confirmation available.

Show »
Length:547
Mass (Da):61,181
Checksum:i8088B4F7DFABAFB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2133Missing in CAA68428. (PubMed:2885805)Curated
Sequence conflicti410 – 4101M → I in CAA88401. 1 PublicationCurated
Sequence conflicti428 – 4281I → V in CAA68428. (PubMed:2885805)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei447 – 53589Missing in isoform 2. 1 PublicationVSP_009846Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00345 mRNA. Translation: CAA68428.1.
U68104
, U68093, U68094, U68095, U68097, U68098, U68099, U68100, U68101, U68102, U68103 Genomic DNA. Translation: AAD08718.1.
AP001205 Genomic DNA. No translation available.
BC015958 mRNA. Translation: AAH15958.1.
BC023520 mRNA. Translation: AAH23520.1.
Z48501 mRNA. Translation: CAA88401.1.
CCDSiCCDS6289.1. [P11940-1]
PIRiA93668. DNHUPA.
S52491.
RefSeqiNP_002559.2. NM_002568.3. [P11940-1]
XP_005250918.1. XM_005250861.1. [P11940-1]
UniGeneiHs.387804.

Genome annotation databases

EnsembliENST00000318607; ENSP00000313007; ENSG00000070756. [P11940-1]
GeneIDi26986.
KEGGihsa:26986.
UCSCiuc003yjs.1. human. [P11940-1]

Polymorphism databases

DMDMi3183544.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00345 mRNA. Translation: CAA68428.1 .
U68104
, U68093 , U68094 , U68095 , U68097 , U68098 , U68099 , U68100 , U68101 , U68102 , U68103 Genomic DNA. Translation: AAD08718.1 .
AP001205 Genomic DNA. No translation available.
BC015958 mRNA. Translation: AAH15958.1 .
BC023520 mRNA. Translation: AAH23520.1 .
Z48501 mRNA. Translation: CAA88401.1 .
CCDSi CCDS6289.1. [P11940-1 ]
PIRi A93668. DNHUPA.
S52491.
RefSeqi NP_002559.2. NM_002568.3. [P11940-1 ]
XP_005250918.1. XM_005250861.1. [P11940-1 ]
UniGenei Hs.387804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CVJ X-ray 2.60 A/B/C/D/E/F/G/H 1-190 [» ]
1G9L NMR - A 498-636 [» ]
1JGN NMR - A 544-636 [» ]
1JH4 NMR - A 544-636 [» ]
2K8G NMR - A 90-182 [» ]
2RQG NMR - B 541-623 [» ]
2RQH NMR - B 541-623 [» ]
2X04 X-ray 1.49 A/B 545-619 [» ]
3KTP X-ray 1.50 A 544-626 [» ]
3KTR X-ray 1.70 A 544-626 [» ]
3KUI X-ray 2.30 A 544-626 [» ]
3KUJ X-ray 1.40 A 544-626 [» ]
3KUR X-ray 2.50 A/B/C/D/E/F/G/H 544-617 [» ]
3KUS X-ray 1.40 A/B 544-626 [» ]
3KUT X-ray 1.50 A/B 544-626 [» ]
3PKN X-ray 1.80 A 544-626 [» ]
3PTH X-ray 1.70 A 543-621 [» ]
4F02 X-ray 2.00 A/D 1-190 [» ]
4F25 X-ray 1.90 A 99-199 [» ]
4F26 X-ray 2.00 A 99-199 [» ]
ProteinModelPortali P11940.
SMRi P11940. Positions 10-435, 494-636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117939. 160 interactions.
DIPi DIP-31613N.
IntActi P11940. 86 interactions.
MINTi MINT-96210.
STRINGi 9606.ENSP00000313007.

Chemistry

BindingDBi P11940.
ChEMBLi CHEMBL1293286.

PTM databases

PhosphoSitei P11940.

Polymorphism databases

DMDMi 3183544.

Proteomic databases

MaxQBi P11940.
PaxDbi P11940.
PRIDEi P11940.

Protocols and materials databases

DNASUi 26986.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318607 ; ENSP00000313007 ; ENSG00000070756 . [P11940-1 ]
GeneIDi 26986.
KEGGi hsa:26986.
UCSCi uc003yjs.1. human. [P11940-1 ]

Organism-specific databases

CTDi 26986.
GeneCardsi GC08M101715.
HGNCi HGNC:8554. PABPC1.
HPAi CAB011536.
HPA045423.
MIMi 604679. gene.
neXtProti NX_P11940.
PharmGKBi PA32880.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00760000118913.
HOGENOMi HOG000217922.
HOVERGENi HBG002295.
InParanoidi P11940.
KOi K13126.
OMAi XAVDEMN.
OrthoDBi EOG7RV9FP.
PhylomeDBi P11940.
TreeFami TF300458.

Enzyme and pathway databases

Reactomei REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSi PABPC1. human.
EvolutionaryTracei P11940.
GeneWikii PABPC1.
GenomeRNAii 26986.
NextBioi 49454.
PMAP-CutDB P11940.
PROi P11940.
SOURCEi Search...

Gene expression databases

Bgeei P11940.
CleanExi HS_PABPC1.
ExpressionAtlasi P11940. baseline and differential.
Genevestigatori P11940.

Family and domain databases

Gene3Di 1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view ]
SMARTi SM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view ]
SUPFAMi SSF63570. SSF63570. 1 hit.
TIGRFAMsi TIGR01628. PABP-1234. 1 hit.
PROSITEi PS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif."
    Grange T., de Sa C.M., Oddos J., Pictet R.
    Nucleic Acids Res. 15:4771-4787(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The human poly(A)-binding protein (PABP) gene: structural and functional analysis."
    Hornstein E., Abramzon-Talianker A., Wiesel I., Meyuhas O.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lung.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    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 1).
    Tissue: Lung and Muscle.
  5. "Nucleotide sequence of a partial cDNA encoding a novel human polyadenylate-binding protein."
    Murphy E.P., McKenna N.J., Headon D.R.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-636 (ISOFORM 2).
  6. Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 158-166; 189-196; 214-221; 232-240; 291-309; 312-324; 357-370; 375-385; 482-506; 566-580 AND 605-620, METHYLATION AT ARG-493, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Ovarian carcinoma.
  7. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166; 187-208; 214-221; 232-240; 291-324; 334-348; 357-370; 375-385; 482-506; 519-559; 566-620 AND 626-636, METHYLATION AT LYS-299 AND ARG-493, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  8. "The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity."
    Goerlach M., Burd C.G., Dreyfuss G.
    Exp. Cell Res. 211:400-407(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  9. "The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm."
    Afonina E., Stauber R., Pavlakis G.N.
    J. Biol. Chem. 273:13015-13021(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation."
    Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.
    Nature 392:520-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAIP1.
  11. "A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
    Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
    Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; SYNCRIP; PAIP1 AND CSDE1.
  12. "Translational repression by a novel partner of human poly(A) binding protein, Paip2."
    Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C., Burley S.K., Sonenberg N.
    Mol. Cell 7:205-216(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAIP2.
  13. "Dual interactions of the translational repressor Paip2 with poly(A) binding protein."
    Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N.
    Mol. Cell. Biol. 21:5200-5213(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAIP2.
  14. "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays."
    Lee J., Bedford M.T.
    EMBO Rep. 3:268-273(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-455 AND ARG-460, MUTAGENESIS OF ARG-455 AND ARG-460.
  15. "Paip1 interacts with poly(A) binding protein through two independent binding motifs."
    Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N.
    Mol. Cell. Biol. 22:3769-3782(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAIP1.
  16. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  17. "Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization."
    Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.
    Biochem. Biophys. Res. Commun. 301:665-670(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPKAPK2.
  18. "UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant."
    Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.
    Genes Dev. 18:2010-2023(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSDE1.
  19. "The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex."
    Patel G.P., Ma S., Bag J.
    Nucleic Acids Res. 33:7074-7089(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND CSDE1.
  20. "IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain."
    Patel G.P., Bag J.
    FEBS J. 273:5678-5690(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH IGF2BP1, RNA-BINDING.
  21. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
    Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
    EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGO1 AND AGO2.
  22. "NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells."
    Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.
    J. Virol. 81:3786-3796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFX1.
  23. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
  24. "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
    Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
    J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay."
    Singh G., Rebbapragada I., Lykke-Andersen J.
    PLoS Biol. 6:E111-E111(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH GSPT2.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
    Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
    RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Poly(A)-binding protein (PABP): a common viral target."
    Smith R.W., Gray N.K.
    Biochem. J. 426:1-12(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  31. Cited for: INTERACTION WITH LARP1.
  32. "Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1."
    Aoyagi M., Gaspar M., Shenk T.E.
    Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
  33. "A stimulatory role for the La-related protein 4B in translation."
    Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.
    RNA 16:1488-1499(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PABPC1 AND GNB2L1.
  34. "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 SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation."
    Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P., Roux P.P.
    Genes Dev. 28:357-371(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LARP1.
  37. "Recognition of polyadenylate RNA by the poly(A)-binding protein."
    Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K.
    Cell 98:835-845(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-190.
  38. "Structure and function of the C-terminal PABC domain of human poly(A)-binding protein."
    Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.
    Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 498-636, INTERACTION WITH GSPT1; PAIP1 AND PAIP2.
  39. "Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp with chemical exchange using two overlapping motifs."
    Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I., Shimada I.
    Submitted (MAY-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 541-623 IN COMPLEX WITH GSPT1.
  40. "Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein."
    Kozlov G., Menade M., Rosenauer A., Nguyen L., Gehring K.
    J. Mol. Biol. 397:397-407(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 544-626 IN COMPLEX WITH PAIP2.

Entry informationi

Entry nameiPABP1_HUMAN
AccessioniPrimary (citable) accession number: P11940
Secondary accession number(s): Q15097, Q93004
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Many viruses shutoff host mRNA translational machinery by inhibiting cellular PABPC1 activity using different mechanisms. Picornaviruses, caliciviruses or lentiviruses encode proteases that cleave PABPC1 at several defined sites in the proline-rich linker region between RRMs and the C-terminal domain. Rotaviruses, gammherpesviruses and bunyamwera virus relocalize PABPC1 from the cytoplasm to the nucleus thus altering its function. Many of these viruses translate their mRNA in a PABPC1-independent manner and are unaffected by host PABPC1 inhibition.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

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