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Index > Protein center > EPB42(Gene name) > Human
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  • EPB42 (Gene name),
  • Erythrocyte membrane protein band 4.2 (Protein name ),  EPB42_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • 3D
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  • Predicted Eptitope
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  • Vaild Sequence
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  • Gene name:
    EPB42(E42P);
    Protein name:
    Erythrocyte membrane protein band 4.2(Erythrocyte protein 4.2;P4.2);
    Alternative:

    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein.
    Function:
    Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.
    Subcellular Location:
    Cell membrane Lipid-anchor Cytoplasmic side Cytoplasm cytoskeleton Cytoplasmic surface of erythrocyte membranes.
    Protein Attributes:
    Sequence length:
    691
    Sequence:
    50:
    MGQALGIKSC | DFQAARNNEE | HHTKALSSRR | LFVRRGQPFT | IILYFRAPVR | 
    100:
    AFLPALKKVA | LTAQTGEQPS | KINRTQATFP | ISSLGDRKWW | SAVVEERDAQ | 
    150:
    SWTISVTTPA | DAVIGHYSLL | LQVSGRKQLL | LGQFTLLFNP | WNREDAVFLK | 
    200:
    NEAQRMEYLL | NQNGLIYLGT | ADCIQAESWD | FGQFEGDVID | LSLRLLSKDK | 
    250:
    QVEKWSQPVH | VARVLGALLH | FLKEQRVLPT | PQTQATQEGA | LLNKRRGSVP | 
    300:
    ILRQWLTGRG | RPVYDGQAWV | LAAVACTVLR | CLGIPARVVT | TFASAQGTGG | 
    350:
    RLLIDEYYNE | EGLQNGEGQR | GRIWIFQTST | ECWMTRPALP | QGYDGWQILH | 
    400:
    PSAPNGGGVL | GSCDLVPVRA | VKEGTLGLTP | AVSDLFAAIN | ASCVVWKCCE | 
    450:
    DGTLELTDSN | TKYVGNNIST | KGVGSDRCED | ITQNYKYPEG | SLQEKEVLER | 
    500:
    VEKEKMEREK | DNGIRPPSLE | TASPLYLLLK | APSSLPLRGD | AQISVTLVNH | 
    550:
    SEQEKAVQLA | IGVQAVHYNG | VLAAKLWRKK | LHLTLSANLE | KIITIGLFFS | 
    600:
    NFERNPPENT | FLRLTAMATH | SESNLSCFAQ | EDIAICRPHL | AIKMPEKAEQ | 
    650:
    YQPLTASVSL | QNSLDAPMED | CVISILGRGL | IHRERSYRFR | SVWPENTMCA | 
    691:
    KFQFTPTHVG | LQRLTVEVDC | NMFQNLTNYK | SVTVVAPELS | A
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    UniGene:
    MIM:
    SMR:
    String:
    KEGG:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Human Erythrocyte protein 4.2
    Cat.:
    E0298h
    Price:
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    MSDS:
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    Packing:
    96T
    Range:
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    ELISA Kit for Human Erythrocyte protein 4.2
    Cat.:
    E0298m
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    ELISA Kit for Human Erythrocyte protein 4.2
    Cat.:
    E0298b
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Erythrocyte protein 4.2
    Cat.:
    U0298b
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Erythrocyte protein 4.2
    Cat.:
    U0298m
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Erythrocyte protein 4.2
    Cat.:
    U0298h
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Polyclonal Antibody for Human Erythrocyte protein 4.2
    Cat.:
    P0298Rb-h
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Erythrocyte protein 4.2
    Polyclonal Antibody for Human Erythrocyte protein 4.2
    Cat.:
    P0298Rb-m
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Monoclonal Antibody for Human Erythrocyte protein 4.2
    Monoclonal Antibody for Human Erythrocyte protein 4.2
    Monoclonal Antibody for Human Erythrocyte protein 4.2
    Protein for Human Erythrocyte protein 4.2
    Protein for Human Erythrocyte protein 4.2
    Protein for Human Erythrocyte protein 4.2

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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII."
      Korsgren C. , Cohen C.M.
      Proc. Natl. Acad. Sci. U.S.A.88:4840-4844(1991) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG)
      tissue: Reticulocyte.
    2. 2.
      "Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2."
      Korsgren C. , Lawler J. , Lambert S. , Speicher D. , Cohen C.M.
      Proc. Natl. Acad. Sci. U.S.A.87:613-617(1990) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE (ISOFORM SHORT)
      tissue: Reticulocyte.
    3. 3.
      "Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane."
      Sung L.A. , Chien S. , Chang L.-S. , Lambert K. , Bliss S.A. , Bouhassira E.E. , Nagel R.L. , Schwartz R.S. , Rybicki A.C.
      Proc. Natl. Acad. Sci. U.S.A.87:955-959(1990) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT)
      tissue: Reticulocyte.
    4. 5.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
    5. 6.
      "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] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT AND 3)
    6. 7.
      "Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated."
      Risinger M.A. , Dotimas E.M. , Cohen C.M.
      J. Biol. Chem.267:5680-5685(1992) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: MYRISTOYLATION AT GLY-2
    7. 8.
      "Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2)."
      Dotimas E. , Speicher D.W. , Guptaroy B. , Cohen C.M.
      Biochim. Biophys. Acta1148:19-29(1993) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT SER-248
    8. 9.
      "An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2 Nippon)."
      Bouhassira E.E. , Schwartz R.S. , Yawata Y. , Ata K. , Kanzaki A. , Qiu J.J.-H. , Nagel R.L. , Rybicki A.C.
      Blood79:1846-1854(1992) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT SPH5 THR-112
    9. 10.
      "A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka)."
      Takaoka Y. , Ideguchi H. , Matsuda M. , Sakamoto N. , Takeuchi T. , Fukumaki Y.
      Br. J. Haematol.88:527-533(1994) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT SPH5 THR-112
    10. 11.
      "A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia."
      Hayette S. , Morle L. , Bozon M. , Ghanem A. , Risinger M. , Korsgren C. , Tanner M.J.A. , Fattoum S. , Cohen C.M. , Delaunay J.
      Br. J. Haematol.89:762-770(1995) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT SPH5 GLN-280
    11. 12.
      "Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT results in band 4.2 deficiency and microspherocytosis."
      Kanzaki A. , Yasunaga M. , Okamoto N. , Inoue T. , Yawata A. , Wada H. , Andoh A. , Hodohara K. , Fujiyama Y. , Bamba T. , Harano T. , Harano K. , Yawata Y.
      Br. J. Haematol.91:333-340(1995) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANTS SPH5 THR-112 AND CYS-287
    12. 13.
      "Band 4.2 Komatsu: 523 GAT-->TAT (175 Asp-->Tyr) in exon 4 of the band 4.2 gene associated with total deficiency of band 4.2, hemolytic anemia with ovalostomatocytosis and marked disruption of the cytoskeletal network."
      Kanzaki A. , Yawata Y. , Yawata A. , Inoue T. , Okamoto N. , Wada H. , Harano T. , Harano K. , Wilmotte R. , Hayette S. , Nakamura Y. , Niki T. , Kawamura Y. , Nakamura S. , Matsuda T.
      Int. J. Hematol.61:165-178(1995) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT SPH5 TYR-145
    13. 14.
      "4.2 Nippon mutation in a non-Japanese patient with hereditary spherocytosis."
      Perrotta S. , Iolascon A. , Polito R. , d'Urzo G. , Conte M.L. , Miraglia del Giudice E.
      Haematologica84:660-662(1999) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT SPH5 THR-112
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