HNRNPC

HNRNPC
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHNRNPC, C1, C2, HNRNP, HNRPC, SNRPC, heterogeneous nuclear ribonucleoprotein C (C1/C2)
External IDsMGI: 107795 HomoloGene: 74524 GeneCards: HNRNPC
Gene location (Human)
Chr.Chromosome 14 (human)[1]
BandNo data availableStart21,209,136 bp[1]
End21,269,494 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

3183

15381

Ensembl

ENSG00000092199

ENSMUSG00000060373

UniProt

P07910

Q9Z204

RefSeq (mRNA)

NM_001077442
NM_001077443
NM_004500
NM_031314

NM_001170981
NM_001170982
NM_001170983
NM_001170984
NM_016884

RefSeq (protein)

NP_001070910
NP_001070911
NP_004491
NP_112604

NP_001164452
NP_001164453
NP_001164454
NP_001164455
NP_058580

Location (UCSC)Chr 14: 21.21 – 21.27 MbChr 14: 52.07 – 52.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Heterogeneous nuclear ribonucleoproteins C1/C2 is a protein that in humans is encoded by the HNRNPC gene.[5][6]

It is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increase risk of birth defects in these ART.[7]

Function

This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing(reference: Koenig J. nature structural and Molecular Biology 2010: iCLIP) and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. Transcriptional regulation by hormonal 1,25-dihydroxyvitamin D(3) (calcitriol) involves occupancy of vitamin D response elements (VDREs) by HNRNPC or 1,25(OH)(2)D(3)-bound vitamin D receptor (VDR).[8][9][10] This relationship is disrupted by elevated HNRNPC, causing a form of hereditary vitamin D-resistant rickets (HVDRR) in both humans[8] and non-human primates.[11] The protein encoded by this gene can act as a tetramer and is involved in the assembly of 40S hnRNP particles. Species-specific tetramerization of HNRNPC subunits is important to its nucleic acid binding, whereby over-expression of major human HNRNPC subunits in mouse osteoblastic cells confers vitamin D resistance.[12] Multiple transcript variants encoding at least two different isoforms have been described for this gene.[6]

Interactions

HNRNPC has been shown to interact with Grb2.[13]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000092199 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060373 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Nakagawa TY, Swanson MS, Wold BJ, Dreyfuss G (May 1986). "Molecular cloning of cDNA for the nuclear ribonucleoprotein particle C proteins: a conserved gene family". Proc Natl Acad Sci U S A. 83 (7): 2007–11. PMC 323219 Freely accessible. PMID 3457372. doi:10.1073/pnas.83.7.2007.
  6. 1 2 "Entrez Gene: HNRPC heterogeneous nuclear ribonucleoprotein C (C1/C2)".
  7. ↑ Zhang Y, Zhang YL, Feng C, Wu YT, Liu AX, Sheng JZ, Cai J, Huang HF (September 2008). "Comparative proteomic analysis of human placenta derived from assisted reproductive technology". Proteomics. 8 (20): 4344–56. PMID 18792929. doi:10.1002/pmic.200800294.
  8. 1 2 Lisse TS, Liu T, Irmler M, Beckers J, Chen H, Adams JS, Hewison M (March 2011). "Gene targeting by the vitamin D response element binding protein reveals a role for vitamin D in osteoblast mTOR signaling.". FASEB J. 25 (3): 937–47. PMID 21123297. doi:10.1096/fj.10-172577.
  9. ↑ Chen H, Hewison M, Adams JS (December 2006). "Functional characterization of heterogeneous nuclear ribonuclear protein C1/C2 in vitamin D resistance: a novel response element-binding protein.". J Biol Chem. 281 (51): 39114–20. PMID 17071612. doi:10.1074/jbc.m608006200.
  10. ↑ Lisse TS, Hewison M, Adams JS (March 2011). "Hormone response element binding proteins: novel regulators of vitamin D and estrogen signaling.". Steroids. 76 (4): 331–9. PMC 3042887 Freely accessible. PMID 21236284. doi:10.1016/j.steroids.2011.01.002.
  11. ↑ Adams JS, Chen H, Chun RF, Nguyen L, Wu S, Ren SY, Barsony J, Gacad MA (Feb 2003). "Novel regulators of vitamin D action and metabolism: Lessons learned at the Los Angeles zoo.". J Cell Biochem. 88 (2): 308–14. PMID 12520531. doi:10.1002/jcb.10333.
  12. ↑ Lisse TS, Vadivel K, Bajaj SP, Chun RF, Hewison M, Adams JS (July 2014). "The heterodimeric structure of heterogeneous nuclear ribonucleoprotein C1/C2 dictates 1,25-dihydroxyvitamin D-directed transcriptional events in osteoblasts.". Bone Research. 2: 14011. PMID 25506471. doi:10.1038/boneres.2014.11.
  13. ↑ Romero F, Ramos-Morales F, Domínguez A, Rios RM, Schweighoffer F, Tocqué B, Pintor-Toro JA, Fischer S, Tortolero M (Mar 1998). "Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by poly(U) RNA". J. Biol. Chem. 273 (13): 7776–81. PMID 9516488. doi:10.1074/jbc.273.13.7776.

Further reading

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