Reviewed, UniProtKB/Swiss-Prot P11940 (PABP1_HUMAN)

Names and origin

Protein names

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

Gene names

Name:	PABPC1
Synonyms:	PAB1, PABP1, PABPC2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. May be 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. Ref.13
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, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. 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.
Subcellular location	Cytoplasm. Nucleus. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus. Relocalizes to the nucleus upon rotavirus A infection. Ref.7 Ref.8 Ref.19 Ref.26
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	Methylated by CARM1. Ref.5 Ref.6 Ref.15 Ref.25 Arg-493 is dimethylated, probably to asymmetric dimethylarginine. Ref.5 Ref.6 Ref.15 Ref.25
Sequence similarities	Belongs to the polyadenylate-binding protein type-1 family. Contains 1 PABC domain. Contains 4 RRM (RNA recognition motif) domains.
Caution	Was originally (Ref.4) termed polyadenylate binding protein II.

Ontologies

Keywords
Biological process	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
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA polyadenylation Ref.1 Traceable author statement. Source: UniProtKB mRNA stabilization Ref.12 Traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Ref.1 Traceable author statement. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB translation activator activity Ref.12 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN2	Q99700	1	EBI-81531,EBI-697691
BCAR3	O75815	1	EBI-81531,EBI-702336
DYNLL1	P63167	1	EBI-81531,EBI-349105
EIF4A2	Q14240	1	EBI-81531,EBI-73473
EIF4G1	Q04637	1	EBI-81531,EBI-73711
HNRNPD	Q14103-4	1	EBI-81531,EBI-432545
IKBKE	Q14164	1	EBI-81531,EBI-307369
NDRG1	Q92597	1	EBI-81531,EBI-716486
PAIP1	Q9H074	3	EBI-81531,EBI-81519
PINX1	Q96BK5	1	EBI-81531,EBI-721782
PUF60	Q9UHX1	1	EBI-81531,EBI-1053259

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

96

1

Phosphoserine Ref.20

Modified residue

116

1

Phosphotyrosine By similarity

Modified residue

299

1

N6-methyllysine Ref.6

Modified residue

315

1

Phosphoserine Ref.20

Modified residue

342

1

Phosphoserine Ref.20

Modified residue

364

1

Phosphotyrosine Ref.16

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.5 Ref.6 Ref.15

Modified residue

493

1

Omega-N-methylarginine; alternate Ref.5 Ref.6 Ref.15

Modified residue

512

1

N6-acetyllysine Ref.22

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.25

Mutagenesis

460

1

R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455. Ref.25

Sequence conflict

211 – 213

3

Missing Ref.1

Sequence conflict

410

1

M → I in CAA88401. Ref.4

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 – 69

8

Beta strand

83 – 86

4

Helix

92 – 95

4

Turn

96 – 99

4

Beta strand

100 – 105

6

Helix

112 – 120

9

Beta strand

125 – 130

6

Beta strand

141 – 146

6

Helix

148 – 154

7

Beta strand

157 – 163

7

Beta strand

166 – 172

7

Turn

176 – 178

3

Helix

547 – 550

4

Beta strand

558 – 560

3

Helix

566 – 573

8

Helix

578 – 585

8

Helix

590 – 597

8

Helix

600 – 616

17

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. 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: 2885805] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung, Muscle and Testis.
[4]	"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).
[5]	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.
[6]	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.
[7]	"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: 7908267] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[8]	"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: 9582337] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"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: 9548260] [Abstract] Cited for: INTERACTION WITH PAIP1.
[10]	"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: 11172725] [Abstract] Cited for: INTERACTION WITH PAIP2.
[11]	"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: 11438674] [Abstract] Cited for: INTERACTION WITH PAIP2.
[12]	"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: 11997512] [Abstract] Cited for: INTERACTION WITH PAIP1.
[13]	"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: 11051545] [Abstract] Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; SYNCRIP; PAIP1 AND CSDE1.
[14]	"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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[15]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-493, MASS SPECTROMETRY.
[16]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, MASS SPECTROMETRY.
[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: 16356927] [Abstract] Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND CSDE1.
[18]	"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: 17267499] [Abstract] Cited for: INTERACTION WITH NFX1.
[19]	"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: 18799579] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-315 AND SER-342, MASS SPECTROMETRY.
[21]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, MASS SPECTROMETRY.
[23]	"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: 10499800] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-190.
[24]	"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: 15314026] [Abstract] Cited for: INTERACTION WITH CSDE1.
[25]	"PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays." Lee J., Bedford M.T. EMBO Rep. 3:268-273(2002) [PubMed: 11850402] [Abstract] Cited for: METHYLATION AT ARG-455 AND ARG-460, MUTAGENESIS OF ARG-455 AND ARG-460.
[26]	"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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
[27]	"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: 19029303] [Abstract] Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00345 mRNA. Translation: CAA68428.1.
U68104 , U68093, U68094, U68095, U68097, U68098, U68099, U68100, U68101, U68102, U68103 Genomic DNA. Translation: AAD08718.1.
BC015958 mRNA. Translation: AAH15958.1.
BC023520 mRNA. Translation: AAH23520.1.
BC041863 mRNA. Translation: AAH41863.1.
Z48501 mRNA. Translation: CAA88401.1.

IPI

IPI00008524.
IPI00410017.

PIR

DNHUPA. A93668.
S52491.

RefSeq

NP_002559.2.

UniGene

Hs.387804

3D structure databases

PDBPDBe

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	[»]

SMR

P11940. Positions 286-376.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11940. 25 interactions.

STRING

P11940.

PTM databases

PhosphoSite

P11940.

2-D gel databases

Aarhus/Ghent-2DPAGE

612. NEPHGE.

Proteomic databases

PRIDE

P11940.

Genome annotation databases

Ensembl

ENST00000318607; ENSP00000313007; ENSG00000070756; Homo sapiens. [Genome view]
ENST00000347137; ENSP00000174661; ENSG00000070756; Homo sapiens. [Genome view]

GeneID

26986.

KEGG

hsa:26986.

UCSC

uc003yjs.1. human.

Organism-specific databases

CTD

26986.

GeneCards

GC08M101784.

H-InvDB

HIX0007688.
HIX0056425.
HIX0077138.

HGNC

HGNC:8554. PABPC1.

HPA

CAB011536.

MIM

604679. gene.

PharmGKB

PA32880.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P11940.

HOVERGEN

P11940.

OMA

TITSAKX.

Enzyme and pathway databases

Reactome

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

Gene expression databases

Bgee

P11940.

CleanEx

HS_PABPC1.

Genevestigator

P11940.

GermOnline

ENSG00000070756. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 4 hits.
G3DSA:1.10.1900.10. PABP_HYD. 1 hit.

Pfam

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

SMART

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

TIGRFAMs

TIGR01628. PABP-1234. 1 hit.

PROSITE

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

ProtoNet

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Other Resources

NextBio

49454.

PMAP-CutDB

P11940.

SOURCE

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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:	November 3, 2009
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.