HNRPH1

Heterogeneous nuclear ribonucleoprotein H1 (H), also known as HNRPH1, is a human gene.cite web | title = Entrez Gene: HNRPH1 heterogeneous nuclear ribonucleoprotein H1 (H)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3187| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 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. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNAs. It is very similar to the family member HNRPF. This gene is thought to be potentially involved in hereditary lymphedema type I phenotype.cite web | title = Entrez Gene: HNRPH1 heterogeneous nuclear ribonucleoprotein H1 (H)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3187| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Rasmussen HH, van Damme J, Puype M, "et al." |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=
*cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=
*cite journal | author=Honoré B, Rasmussen HH, Vorum H, "et al." |title=Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 28780–9 |year= 1996 |pmid= 7499401 |doi=
*cite journal | author=Matunis MJ, Xing J, Dreyfuss G |title=The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization. |journal=Nucleic Acids Res. |volume=22 |issue= 6 |pages= 1059–67 |year= 1994 |pmid= 7512260 |doi=
*cite journal | author=Gamberi C, Izaurralde E, Beisel C, Mattaj IW |title=Interaction between the human nuclear cap-binding protein complex and hnRNP F. |journal=Mol. Cell. Biol. |volume=17 |issue= 5 |pages= 2587–97 |year= 1997 |pmid= 9111328 |doi=
*cite journal | author=Chou MY, Rooke N, Turck CW, Black DL |title=hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 69–77 |year= 1999 |pmid= 9858532 |doi=
*cite journal | author=Evans AL, Brice G, Sotirova V, "et al." |title=Mapping of primary congenital lymphedema to the 5q35.3 region. |journal=Am. J. Hum. Genet. |volume=64 |issue= 2 |pages= 547–55 |year= 1999 |pmid= 9973292 |doi=
*cite journal | author=Honoré B, Vorum H, Baandrup U |title=hnRNPs H, H' and F behave differently with respect to posttranslational cleavage and subcellular localization. |journal=FEBS Lett. |volume=456 |issue= 2 |pages= 274–80 |year= 1999 |pmid= 10456323 |doi=
*cite journal | author=Markovtsov V, Nikolic JM, Goldman JA, "et al." |title=Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. |journal=Mol. Cell. Biol. |volume=20 |issue= 20 |pages= 7463–79 |year= 2000 |pmid= 11003644 |doi=
*cite journal | author=Andersen JS, Lyon CE, Fox AH, "et al." |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1–11 |year= 2002 |pmid= 11790298 |doi=
*cite journal | author=Jurica MS, Licklider LJ, Gygi SR, "et al." |title=Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. |journal=RNA |volume=8 |issue= 4 |pages= 426–39 |year= 2002 |pmid= 11991638 |doi=
*cite journal | author=Angenstein F, Evans AM, Settlage RE, "et al." |title=A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons. |journal=J. Neurosci. |volume=22 |issue= 20 |pages= 8827–37 |year= 2002 |pmid= 12388589 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Li J, Hawkins IC, Harvey CD, "et al." |title=Regulation of alternative splicing by SRrp86 and its interacting proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437–47 |year= 2003 |pmid= 14559993 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Honoré B, Baandrup U, Vorum H |title=Heterogeneous nuclear ribonucleoproteins F and H/H' show differential expression in normal and selected cancer tissues. |journal=Exp. Cell Res. |volume=294 |issue= 1 |pages= 199–209 |year= 2004 |pmid= 14980514 |doi= 10.1016/j.yexcr.2003.11.011
*cite journal | author=Brill LM, Salomon AR, Ficarro SB, "et al." |title=Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. |journal=Anal. Chem. |volume=76 |issue= 10 |pages= 2763–72 |year= 2004 |pmid= 15144186 |doi= 10.1021/ac035352d
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Lin KT, Lu RM, Tarn WY |title=The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo. |journal=Mol. Cell. Biol. |volume=24 |issue= 20 |pages= 9176–85 |year= 2004 |pmid= 15456888 |doi= 10.1128/MCB.24.20.9176-9185.2004

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes