Protein 4.2

Protein 4.2

Erythrocyte membrane protein band 4.2, also known as EPB42, is a human gene.cite web | title = Entrez Gene: EPB42 erythrocyte membrane protein band 4.2| url =| accessdate = ]

Protein 4.2 is a cytoskeleton protein found in red blood cells.

section_title =
summary_text = Erythrocyte membrane protein band 4.2 is an ATP-binding protein which may regulate the association of protein 3 with ankyrin. It probably has a role in erythrocyte shape and mechanical property regulation. Mutations in the EPB42 gene are associated with recessive spherocytic elliptocytosis and recessively transmitted hereditary hemolytic anemia.cite web | title = Entrez Gene: EPB42 erythrocyte membrane protein band 4.2| url =| accessdate = ]


Further reading

citations =
*cite journal | author=Falcón-Pérez JM, Dell'Angelica EC |title=The pallidin (Pldn) gene and the role of SNARE proteins in melanosome biogenesis. |journal=Pigment Cell Res. |volume=15 |issue= 2 |pages= 82–6 |year= 2002 |pmid= 11936273 |doi=
*cite journal | author=White RA, Peters LL, Adkison LR, "et al." |title=The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene. |journal=Nat. Genet. |volume=2 |issue= 1 |pages= 80–3 |year= 1993 |pmid= 1284644 |doi= 10.1038/ng0992-80
*cite journal | author=Sung LA, Chien S, Fan YS, "et al." |title=Human erythrocyte protein 4.2: isoform expression, differential splicing, and chromosomal assignment. |journal=Blood |volume=79 |issue= 10 |pages= 2763–70 |year= 1992 |pmid= 1350227 |doi=
*cite journal | author=Risinger MA, Dotimas EM, Cohen CM |title=Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5680–5 |year= 1992 |pmid= 1544941 |doi=
*cite journal | author=Bouhassira EE, Schwartz RS, Yawata Y, "et al." |title=An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON). |journal=Blood |volume=79 |issue= 7 |pages= 1846–54 |year= 1992 |pmid= 1558976 |doi=
*cite journal | author=Sung LA, Chien S, Chang LS, "et al." |title=Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 955–9 |year= 1990 |pmid= 1689063 |doi=
*cite journal | author=Najfeld V, Ballard SG, Menninger J, "et al." |title=The gene for human erythrocyte protein 4.2 maps to chromosome 15q15. |journal=Am. J. Hum. Genet. |volume=50 |issue= 1 |pages= 71–5 |year= 1992 |pmid= 1729896 |doi=
*cite journal | author=Low PS, Willardson BM, Mohandas N, "et al." |title=Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability. |journal=Blood |volume=77 |issue= 7 |pages= 1581–6 |year= 1991 |pmid= 1826225 |doi=
*cite journal | author=Korsgren C, Cohen CM |title=Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4840–4 |year= 1991 |pmid= 2052563 |doi=
*cite journal | author=Korsgren C, Lawler J, Lambert S, "et al." |title=Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 613–7 |year= 1990 |pmid= 2300550 |doi=
*cite journal | author=Korsgren C, Cohen CM |title=Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. |journal=J. Biol. Chem. |volume=263 |issue= 21 |pages= 10212–8 |year= 1988 |pmid= 2968981 |doi=
*cite journal | author=Tanimoto T, Hoshijima M, Kawata M, "et al." |title=Binding of ras p21 to bands 4.2 and 6 of human erythrocyte membranes. |journal=FEBS Lett. |volume=226 |issue= 2 |pages= 291–6 |year= 1988 |pmid= 3276554 |doi=
*cite journal | author=Rybicki AC, Musto S, Schwartz RS |title=Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2. |journal=Biochem. J. |volume=309 ( Pt 2) |issue= |pages= 677–81 |year= 1995 |pmid= 7626035 |doi=
*cite journal | author=Hayette S, Morle L, Bozon M, "et al." |title=A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. |journal=Br. J. Haematol. |volume=89 |issue= 4 |pages= 762–70 |year= 1995 |pmid= 7772513 |doi=
*cite journal | author=Hayette S, Dhermy D, dos Santos ME, "et al." |title=A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia. |journal=Blood |volume=85 |issue= 1 |pages= 250–6 |year= 1995 |pmid= 7803799 |doi=
*cite journal | author=Takaoka Y, Ideguchi H, Matsuda M, "et al." |title=A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka). |journal=Br. J. Haematol. |volume=88 |issue= 3 |pages= 527–33 |year= 1995 |pmid= 7819064 |doi=
*cite journal | author=Das AK, Bhattacharya R, Kundu M, "et al." |title=Human erythrocyte membrane protein 4.2 is palmitoylated. |journal=Eur. J. Biochem. |volume=224 |issue= 2 |pages= 575–80 |year= 1994 |pmid= 7925374 |doi=
*cite journal | author=Dotimas E, Speicher DW, GuptaRoy B, Cohen CM |title=Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2). |journal=Biochim. Biophys. Acta |volume=1148 |issue= 1 |pages= 19–29 |year= 1993 |pmid= 8499466 |doi=
*cite journal | author=Azim AC, Marfatia SM, Korsgren C, "et al." |title=Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins. |journal=Biochemistry |volume=35 |issue= 9 |pages= 3001–6 |year= 1996 |pmid= 8608138 |doi= 10.1021/bi951745y
*cite journal | author=Bhattacharyya R, Das AK, Moitra PK, "et al." |title=Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2. |journal=Biochem. J. |volume=340 ( Pt 2) |issue= |pages= 505–12 |year= 1999 |pmid= 10333496 |doi=

ee also

* Hereditary elliptocytosis

External links


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

Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Protein S — is a vitamin K dependent plasma glycoprotein synthesized in the liver. In the circulation, Protein S exists in two forms: a free form and a complex form bound to complement protein C4b. FunctionThe best characterized function of Protein S is its… …   Wikipedia

  • Protein A — is a 40 60 kDa MSCRAMM surface protein originally found in the cell wall of the bacteria Staphylococcus aureus . It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two component system… …   Wikipedia

  • Protein A/G — is a recombinant fusion protein that combines IgG binding domains of both Protein A and Protein G. Protein A/G contains four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50,460 daltons. The binding of Protein …   Wikipedia

  • Protein L — is a 36,000 dalton immunoglobulin binding protein isolated from the bacteria Peptostreptococcus magnus . Unlike Protein A and Protein G, which bind to the Fc region of immunoglobilins (antibodies), Protein L binds antibodies through light chain… …   Wikipedia

  • Protein C — Vorhandene Strukturdaten …   Deutsch Wikipedia

  • Protein-C — Vorhandene Strukturdaten: 1aut …   Deutsch Wikipedia

  • Protein Z — protein Name = protein Z caption = width = HGNCid = 9460 Symbol = PROZ AltSymbols = EntrezGene = 8858 OMIM = 176895 RefSeq = NM 003891 UniProt = P22891 PDB = ECnumber = Chromosome = 13 Arm = q Band = 34 LocusSupplementaryData = Protein Z is a… …   Wikipedia

  • Protein G — is an immunoglobulin binding protein expressed in group C and G Streptococcal bacteria much like Protein A but with differing specificities. It is a 65 kDa (G148 protein G) and a 58 kDa (C40 protein G) [1] cell surface protein that has found… …   Wikipedia

  • Protein — Pro te*in, n. [Gr. prw^tos first: cf. prwtei^on the first place.] (Physiol. Chem.) any polymer of an amino acid joined by peptide (amide) bonds. Most natural proteins have alpha amino acids as the monomeric constituents. All classical enzymes are …   The Collaborative International Dictionary of English

  • Protein-S — Vorhandene Strukturdaten: 1z6c Gr …   Deutsch Wikipedia

  • Protein S — Vorhandene Strukturdaten …   Deutsch Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”

We are using cookies for the best presentation of our site. Continuing to use this site, you agree with this.