PABPC4

PABPC4
Identifiers
Aliases	PABPC4 , APP-1, APP1, PABP4, iPABP, poly(A) binding protein cytoplasmic 4
External IDs	OMIM: 603407 MGI: 2385206 HomoloGene: 37855 GeneCards: PABPC4
Gene location (Human)
Chr.	Chromosome 1 (human)
End	39,576,790 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	123,192,718 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; gastrocnemius muscle; ; secondary oocyte; ; skeletal muscle tissue; ; vastus lateralis muscle; ; body of tongue; ; triceps brachii muscle; ; tibialis anterior muscle; ; body of stomach; ; sural nerve;
	Top expressed in
	bone marrow; ; skeletal muscle tissue; ; quadriceps femoris muscle; ; morula; ; yolk sac; ; islet of Langerhans; ; spleen; ; secondary oocyte; ; heart; ; esophagus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	poly(C) RNA binding ; protein binding ; poly(A) binding ; nucleic acid binding ; poly(U) RNA binding ; RNA binding ; mRNA binding ; mRNA 3'-UTR binding ;
Cellular component	cytoplasmic stress granule ; nucleus ; cytoplasm ; cytosol ; ribonucleoprotein complex ;
Biological process	RNA processing ; RNA catabolic process ; blood coagulation ; protein biosynthesis ; regulation of mRNA stability ; myeloid cell development ;
	Sources:Amigo / QuickGO
Orthologs
	8761
	230721
	ENSG00000090621
	ENSMUSG00000011257
	Q13310
	n/a
	NM_003819 ; NM_001135653 ; NM_001135654
	NM_130881 ; NM_148917 ; NM_001356377
	NP_001129125 ; NP_001129126 ; NP_003810
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 02, 2023

Polyadenylate-binding protein 4 (PABPC4) is a protein that in humans is encoded by the PABPC4 gene.^[5]^[6]

Function

Poly(A)-binding proteins (PABPs) bind to the poly(A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules.^[6]

Model organisms

*Pabpc4* knockout mouse phenotype
Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Abnormal^[7]
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
All tests and analysis from^[8]^[9]

Model organisms have been used in the study of PABPC4 function. A conditional knockout mouse line, called Pabpc4^{tm1a(KOMP)Wtsi}^[10]^[11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.^[12]^[13]^[14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[8]^[15] Twenty tests were carried out on mutant mice and one significant abnormality was observed: female homozygous mutants displayed impaired glucose tolerance.^[8]

Interactions

PABPC4 has been shown to interact with PHLDA1.^[16]

Related Research Articles

Polyadenylation is the addition of a poly(A) tail to an RNA transcript, typically a messenger RNA (mRNA). The poly(A) tail consists of multiple adenosine monophosphates; in other words, it is a stretch of RNA that has only adenine bases. In eukaryotes, polyadenylation is part of the process that produces mature mRNA for translation. In many bacteria, the poly(A) tail promotes degradation of the mRNA. It, therefore, forms part of the larger process of gene expression.

Zinc finger protein GLI1 also known as glioma-associated oncogene is a protein that in humans is encoded by the GLI1 gene. It was originally isolated from human glioblastoma cells.

Nuclear factor NF-kappa-B p105 subunit is a protein that in humans is encoded by the NFKB1 gene.

Polyadenylate-binding protein 1 is a protein that in humans is encoded by the PABPC1 gene. The protein PABP1 binds mRNA and facilitates a variety of functions such as transport into and out of the nucleus, degradation, translation, and stability. There are two separate PABP1 proteins, one which is located in the nucleus (PABPN1) and the other which is found in the cytoplasm (PABPC1). The location of PABP1 affects the role of that protein and its function with RNA.

ELAV-like protein 1 or HuR is a protein that in humans is encoded by the ELAVL1 gene.

5'-AMP-activated protein kinase subunit beta-1 is an enzyme that in humans is encoded by the PRKAB1 gene.

Heterogeneous nuclear ribonucleoprotein F is a protein that in humans is encoded by the HNRNPF gene.

Polyadenylate-binding protein 2 (PABP-2) also known as polyadenylate-binding nuclear protein 1 (PABPN1) is a protein that in humans is encoded by the PABPN1 gene. PABN1 is a member of a larger family of poly(A)-binding proteins in the human genome.

Ras GTPase-activating protein-binding protein 1 is an enzyme that in humans is encoded by the G3BP1 gene.

Microtubule-associated serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the MAST2 gene. The protein encoded by this gene controls TRAF6 and NF-kappaB activity.

Platelet-derived growth factor C, also known as PDGF-C, is a 345-amino acid protein that in humans is encoded by the PDGFC gene. Platelet-derived growth factors are important in connective tissue growth, survival and function, and consist of disulphide-linked dimers involving two polypeptide chains, PDGF-A and PDGF-B. PDGF-C is a member of the PDGF/VEGF family of growth factors with a unique two-domain structure and expression pattern. PDGF-C was not previously identified with PDGF-A and PDGF-B, possibly because it may be that it is synthesized and secreted as a latent growth factor, requiring proteolytic removal of the N-terminal CUB domain for receptor binding and activation.

DNA-binding protein A is a protein that in humans is encoded by the CSDA gene.

Poly(A) polymerase alpha is an enzyme that in humans is encoded by the PAPOLA gene.

Protein kinase C-binding protein 1 is an enzyme that in humans is encoded by the ZMYND8 gene.

Polyadenylate-binding protein-interacting protein 2 is a protein that in humans is encoded by the PAIP2 gene.

Cleavage and polyadenylation specificity factor subunit 3 is a protein that in humans is encoded by the CPSF3 gene.

Poly(rC)-binding protein 4 is a protein that in humans is encoded by the PCBP4 gene.

CD2 antigen cytoplasmic tail-binding protein 2 is a protein that in humans is encoded by the CD2BP2 gene.

Polyadenylate-binding protein-interacting protein 1 is a protein that in humans is encoded by the PAIP1 gene.

<span class="mw-page-title-main">PABPC3</span> Protein-coding gene in the species Homo sapiens

Polyadenylate-binding protein 3 is a protein that in humans is encoded by the PABPC3 gene. PABPC3 is a member of a larger family of poly(A)-binding proteins in the human genome.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000090621 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000011257 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Féral C, Mattéi MG, Pawlak A, Guellaën G (Nov 1999). "Chromosomal localization of three human poly(A)-binding protein genes and four related pseudogenes". Hum Genet. 105 (4): 347–53. doi:10.1007/s004390051113. PMC 1865476 . PMID 10543404.
1 2 "Entrez Gene: PABPC4 poly(A) binding protein, cytoplasmic 4 (inducible form)".
↑ "Glucose tolerance test data for Pabpc4". Wellcome Trust Sanger Institute.
1 2 3 Gerdin, AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
↑ "International Knockout Mouse Consortium".
↑ "Mouse Genome Informatics".
↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410 . PMID 21677750.
↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi: 10.1038/474262a . PMID 21677718.
↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi: 10.1016/j.cell.2006.12.018 . PMID 17218247. S2CID 18872015.
↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi: 10.1186/gb-2011-12-6-224 . PMC 3218837 . PMID 21722353.
↑ Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (May 2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Yang H, Duckett CS, Lindsten T (1996). "iPABP, an inducible poly(A)-binding protein detected in activated human T cells". Mol. Cell. Biol. 15 (12): 6770–6. doi:10.1128/mcb.15.12.6770. PMC 230930 . PMID 8524242.
Houng AK, Maggini L, Clement CY, Reed GL (1997). "Identification and structure of activated-platelet protein-1, a protein with RNA-binding domain motifs that is expressed by activated platelets". Eur. J. Biochem. 243 (1–2): 209–18. doi: 10.1111/j.1432-1033.1997.0209a.x . PMID 9030741.
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Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.
Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (2003). "Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins". Mol. Cell. Biol. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616 . PMID 14559993.
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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000090621 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000011257 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10543404-5] Féral C, Mattéi MG, Pawlak A, Guellaën G (Nov 1999). "Chromosomal localization of three human poly(A)-binding protein genes and four related pseudogenes". Hum Genet. 105 (4): 347–53. doi:10.1007/s004390051113. PMC 1865476 . PMID 10543404.

[entrez-6] 1 2 "Entrez Gene: PABPC4 poly(A) binding protein, cytoplasmic 4 (inducible form)".

[Glucose_tolerance_test-7] "Glucose tolerance test data for Pabpc4". Wellcome Trust Sanger Institute.

[mgp_reference-8] 1 2 3 Gerdin, AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.

[9] Mouse Resources Portal, Wellcome Trust Sanger Institute.

[allele_ref-10] "International Knockout Mouse Consortium".

[mgi_allele_ref-11] "Mouse Genome Informatics".

[pmid21677750-12] Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410 . PMID 21677750.

[mouse_library-13] Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi: 10.1038/474262a . PMID 21677718.

[mouse_for_all_reasons-14] Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi: 10.1016/j.cell.2006.12.018 . PMID 17218247. S2CID 18872015.

[pmid21722353-15] van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi: 10.1186/gb-2011-12-6-224 . PMC 3218837 . PMID 21722353.

[pmid11369516-16] Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (May 2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.

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