P11940 (PABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyadenylate-binding protein 1
Short name=PABP-1
Short name=Poly(A)-binding protein 1

Gene names

Name:	PABPC1
Synonyms:	PAB1, PABP1, PABPC2

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	636 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds the poly(A) tail of mRNA. 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. Ref.14 Ref.21 Ref.30
Subunit structure	Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with IGF2BP1 and NFX1. Interacts with PIWIL1 By similarity. Interacts with EIF2C1, EIF2C2, GSPT1 and GSPT2. Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with LARP4B. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.26 Ref.29 Ref.30 Ref.34
Subcellular location	Cytoplasm. Nucleus. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus. Ref.8 Ref.9 Ref.20 Ref.24 Ref.30
Tissue specificity	Ubiquitous.
Domain	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.
Post-translational modification	Phosphorylated by MAPKAPK2. Ref.16 Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine. Ref.6 Ref.7 Ref.23
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.
Sequence similarities	Belongs to the polyadenylate-binding protein type-1 family. Contains 1 PABC domain. Contains 4 RRM (RNA recognition motif) domains.
Caution	Was termed (Ref.5) polyadenylate binding protein II.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA polyadenylation Traceable author statement Ref.1. Source: UniProtKB mRNA splicing, via spliceosome Inferred by curator Ref.15. Source: UniProtKB mRNA stabilization Traceable author statement Ref.13. Source: UniProtKB negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from direct assay Ref.21. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome nuclear-transcribed mRNA poly(A) tail shortening Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.15. Source: UniProtKB cytoplasmic stress granule Inferred from direct assay PubMed 21883093. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Traceable author statement Ref.1. Source: UniProtKB translation activator activity Traceable author statement Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN2	Q99700	3	EBI-81531,EBI-697691
DDX3X	O00571	9	EBI-81531,EBI-353779
EIF4G1	Q04637	2	EBI-81531,EBI-73711
GSPT2	Q8IYD1	3	EBI-81531,EBI-3869637
HNRNPD	Q14103-4	2	EBI-81531,EBI-432545
PAIP1	Q9H074	6	EBI-81531,EBI-81519
SMG1	Q96Q15	2	EBI-81531,EBI-1049832
TNRC6C	Q9HCJ0	5	EBI-81531,EBI-6507625

Alternative products

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

Isoform 1 (identifier: P11940-1)

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: P11940-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 636

636

Polyadenylate-binding protein 1

PRO_0000081698

Regions

Domain

11 – 89

79

RRM 1

Domain

99 – 175

77

RRM 2

Domain

191 – 268

78

RRM 3

Domain

294 – 370

77

RRM 4

Domain

542 – 619

78

PABC

Region

166 – 289

124

CSDE1-binding

Compositional bias

495 – 501

7

Poly-Ala

Amino acid modifications

Modified residue

116

1

Phosphotyrosine By similarity

Modified residue

299

1

N6-methyllysine Ref.7

Modified residue

315

1

Phosphoserine Ref.25 Ref.31

Modified residue

455

1

Omega-N-methylated arginine; by CARM1; partial Probable

Modified residue

460

1

Omega-N-methylated arginine; by CARM1; partial Probable

Modified residue

493

1

Dimethylated arginine; alternate Ref.6 Ref.7

Modified residue

493

1

Omega-N-methylarginine; alternate Ref.6 Ref.7

Modified residue

512

1

N6-acetyllysine Ref.27

Natural variations

Alternative sequence

447 – 535

89

Missing in isoform 2.

VSP_009846

Experimental info

Mutagenesis

455

1

R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-460. Ref.23

Mutagenesis

460

1

R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455. Ref.23

Sequence conflict

211 – 213

3

Missing in CAA68428. Ref.1

Sequence conflict

410

1

M → I in CAA88401. Ref.5

Sequence conflict

428

1

I → V in CAA68428. Ref.1

Secondary structure

1

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636

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Helix

24 – 31

8

Helix

32 – 34

3

Beta strand

37 – 44

8

Turn

46 – 48

3

Beta strand

51 – 61

11

Helix

62 – 72

11

Beta strand

83 – 86

4

Helix

92 – 96

5

Beta strand

100 – 105

6

Helix

112 – 119

8

Helix

120 – 122

3

Beta strand

125 – 133

9

Beta strand

136 – 146

11

Helix

148 – 158

11

Beta strand

161 – 163

3

Beta strand

169 – 174

6

Helix

176 – 183

8

Helix

547 – 551

5

Helix

555 – 557

3

Helix

558 – 573

16

Turn

575 – 577

3

Helix

578 – 585

8

Helix

590 – 598

9

Helix

600 – 619

20

Turn

623 – 625

3

Beta strand

628 – 630

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 2EB1B02A346132EE	FASTA	636	70,671
	10 20 30 40 50 60 MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ 70 80 90 100 110 120 QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS 130 140 150 160 170 180 AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE 190 200 210 220 230 240 AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER 250 260 270 280 290 300 HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN 310 320 330 340 350 360 LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT 370 380 390 400 410 420 KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA 430 440 450 460 470 480 AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ 490 500 510 520 530 540 RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ 550 560 570 580 590 600 GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP 610 620 630 ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
	Isoform 2 [UniParc]. Checksum: 8088B4F7DFABAFB8	FASTA	547	61,181
	10 20 30 40 50 60 MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ 70 80 90 100 110 120 QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS 130 140 150 160 170 180 AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE 190 200 210 220 230 240 AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER 250 260 270 280 290 300 HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN 310 320 330 340 350 360 LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT 370 380 390 400 410 420 KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA 430 440 450 460 470 480 AYYPPSQIAQ LRPSPRWTAQ GARPHPAVHV QGQEPLTASM LASAPPQEQK QMLGERLFPL 490 500 510 520 530 540 IQAMHPTLAG KITGMLLEID NSELLHMLES PESLRSKVDE AVAVLQAHQA KEAAQKAVNS ATGVPTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB 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, 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, 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]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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 EIF2C1 AND EIF2C2.
[19]	"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.
[20]	"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.
[21]	"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 NMD, INTERACTION WITH GSPT2.
[22]	"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.
[23]	"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.
[24]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
[25]	"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 SER-315, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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.
[27]	"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, MASS SPECTROMETRY.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"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].
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00008524.
IPI00410017.

PIR

DNHUPA. A93668.
S52491.

RefSeq

NP_002559.2. NM_002568.3.

UniGene

Hs.387804.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P11940.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31613N.

IntAct

P11940. 61 interactions.

MINT

MINT-96210.

STRING

9606.ENSP00000313007.

PTM databases

PhosphoSite

P11940.

Polymorphism databases

DMDM

3183544.

Proteomic databases

PaxDb

P11940.

PRIDE

P11940.

Protocols and materials databases

DNASU

26986.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000318607; ENSP00000313007; ENSG00000070756.

GeneID

26986.

KEGG

hsa:26986.

UCSC

uc003yjs.1. human.

Organism-specific databases

CTD

26986.

GeneCards

GC08M101715.

HGNC

HGNC:8554. PABPC1.

HPA

CAB011536.
HPA045423.

MIM

604679. gene.

neXtProt

NX_P11940.

PharmGKB

PA32880.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000217922.

HOVERGEN

HBG002295.

InParanoid

P11940.

KO

K13126.

OMA

TITSAKX.

OrthoDB

EOG40ZQX5.

PhylomeDB

P11940.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P11940.

Bgee

P11940.

CleanEx

HS_PABPC1.

Genevestigator

P11940.

GermOnline

ENSG00000070756. Homo sapiens.

Family and domain databases

Gene3D

1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]

SMART

SM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]

SUPFAM

SSF63570. PABP_HYD. 1 hit.

TIGRFAMs

TIGR01628. PABP-1234. 1 hit.

PROSITE

PS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11940.

ChEMBL

CHEMBL1293286.

ChiTaRS

PABPC1. human.

EvolutionaryTrace

P11940.

GenomeRNAi

26986.

NextBio

49454.

PMAP-CutDB

P11940.

SOURCE

Search...

Entry information

Entry name

PABP1_HUMAN

Accession

Primary (citable) accession number: P11940
Secondary accession number(s): Q15097, Q93004

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	July 15, 1998
Last modified:	May 1, 2013
This is version 171 of the entry and version 2 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.