Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P16452

- EPB42_HUMAN

UniProt

P16452 - EPB42_HUMAN

Protein

Erythrocyte membrane protein band 4.2

Gene

EPB42

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.

    GO - Molecular functioni

    1. ATP binding Source: ProtInc
    2. protein binding Source: IntAct
    3. protein-glutamine gamma-glutamyltransferase activity Source: InterPro
    4. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. cell morphogenesis Source: Ensembl
    2. erythrocyte maturation Source: UniProtKB-KW
    3. hemoglobin metabolic process Source: Ensembl
    4. iron ion homeostasis Source: Ensembl
    5. peptide cross-linking Source: InterPro
    6. regulation of cell shape Source: UniProtKB-KW
    7. spleen development Source: Ensembl

    Keywords - Biological processi

    Cell shape, Erythrocyte maturation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythrocyte membrane protein band 4.2
    Short name:
    Erythrocyte protein 4.2
    Short name:
    P4.2
    Gene namesi
    Name:EPB42
    Synonyms:E42P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:3381. EPB42.

    Subcellular locationi

    Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton
    Note: Cytoplasmic surface of erythrocyte membranes.

    GO - Cellular componenti

    1. cortical cytoskeleton Source: Ensembl
    2. cytoskeleton Source: ProtInc
    3. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Spherocytosis 5 (SPH5) [MIM:612690]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Absence of band 4.2 associated with spur or target erythrocytes has also been reported.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121A → T in SPH5; Nippon/Fukuoka. 4 Publications
    Corresponds to variant rs28933988 [ dbSNP | Ensembl ].
    VAR_007482
    Natural varianti145 – 1451D → Y in SPH5; Komatsu. 1 Publication
    VAR_058099
    Natural varianti280 – 2801R → Q in SPH5; Tozeur. 1 Publication
    VAR_012268
    Natural varianti287 – 2871R → C in SPH5; Shiga. 1 Publication
    VAR_058100

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi612690. phenotype.
    Orphaneti822. Hereditary spherocytosis.
    PharmGKBiPA27814.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 691690Erythrocyte membrane protein band 4.2PRO_0000213720Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei248 – 2481Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Both cAMP-dependent kinase (CAPK) and another kinase present in the red-blood cells seem to be able to phosphorylate EPB42.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    PaxDbiP16452.
    PRIDEiP16452.

    PTM databases

    PhosphoSiteiP16452.

    Expressioni

    Gene expression databases

    ArrayExpressiP16452.
    BgeeiP16452.
    CleanExiHS_EPB42.
    GenevestigatoriP16452.

    Organism-specific databases

    HPAiHPA040261.

    Interactioni

    Subunit structurei

    Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SPINK7P580623EBI-1182496,EBI-1182445

    Protein-protein interaction databases

    BioGridi108352. 6 interactions.
    IntActiP16452. 3 interactions.
    STRINGi9606.ENSP00000300215.

    Structurei

    3D structure databases

    ProteinModelPortaliP16452.
    SMRiP16452. Positions 5-689.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni31 – 399Band 3 bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG87163.
    HOGENOMiHOG000231695.
    HOVERGENiHBG106048.
    InParanoidiP16452.
    OMAiSCFAQED.
    OrthoDBiEOG7Z0JVS.
    PhylomeDBiP16452.
    TreeFamiTF324278.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view]
    PANTHERiPTHR11590. PTHR11590. 1 hit.
    PfamiPF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
    SMARTiSM00460. TGc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Short (identifier: P16452-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR    50
    AFLPALKKVA LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ 100
    SWTISVTTPA DAVIGHYSLL LQVSGRKQLL LGQFTLLFNP WNREDAVFLK 150
    NEAQRMEYLL NQNGLIYLGT ADCIQAESWD FGQFEGDVID LSLRLLSKDK 200
    QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA LLNKRRGSVP 250
    ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG 300
    RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH 350
    PSAPNGGGVL GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE 400
    DGTLELTDSN TKYVGNNIST KGVGSDRCED ITQNYKYPEG SLQEKEVLER 450
    VEKEKMEREK DNGIRPPSLE TASPLYLLLK APSSLPLRGD AQISVTLVNH 500
    SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE KIITIGLFFS 550
    NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ 600
    YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA 650
    KFQFTPTHVG LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A 691

    Note: Major isoform.

    Length:691
    Mass (Da):77,009
    Last modified:November 25, 2008 - v3
    Checksum:i38225C311E478580
    GO
    Isoform Long (identifier: P16452-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3-3: Q → QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD

    Show »
    Length:721
    Mass (Da):79,927
    Checksum:iA1C85B41298A93C0
    GO
    Isoform 3 (identifier: P16452-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         324-395: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:619
    Mass (Da):69,455
    Checksum:i640A1E12CC4ED420
    GO

    Sequence cautioni

    The sequence AAA36401.1 differs from that shown. Reason: Frameshift at positions 335 and 340.
    The sequence AAA36402.1 differs from that shown. Reason: Frameshift at positions 335 and 340.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti350 – 3501H → D in AAA74589. (PubMed:2052563)Curated
    Sequence conflicti350 – 3501H → D in AAA52385. (PubMed:2052563)Curated
    Sequence conflicti350 – 3501H → D in AAA35798. (PubMed:2300550)Curated
    Sequence conflicti376 – 3761L → V in AAA74589. (PubMed:2052563)Curated
    Sequence conflicti376 – 3761L → V in AAA52385. (PubMed:2052563)Curated
    Sequence conflicti376 – 3761L → V in AAA35798. (PubMed:2300550)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121A → T in SPH5; Nippon/Fukuoka. 4 Publications
    Corresponds to variant rs28933988 [ dbSNP | Ensembl ].
    VAR_007482
    Natural varianti145 – 1451D → Y in SPH5; Komatsu. 1 Publication
    VAR_058099
    Natural varianti280 – 2801R → Q in SPH5; Tozeur. 1 Publication
    VAR_012268
    Natural varianti287 – 2871R → C in SPH5; Shiga. 1 Publication
    VAR_058100

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei3 – 31Q → QGEPSQRSTGLAGLYAAPAA SPVFIKGSGMD in isoform Long. 2 PublicationsVSP_006416
    Alternative sequencei324 – 39572Missing in isoform 3. 1 PublicationVSP_055340Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60298 mRNA. Translation: AAA74589.1.
    L06519
    , L06447, L06448, L06449, L06450, L06511, L06512, L06513, L06515, L06516, L06517, L06518 Genomic DNA. Translation: AAA52385.1.
    M29399 mRNA. Translation: AAA35798.1.
    M30647 mRNA. Translation: AAA36401.1. Frameshift.
    M30646 mRNA. Translation: AAA36402.1. Frameshift.
    AC068724 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92591.1.
    BC096093 mRNA. Translation: AAH96093.1.
    BC096094 mRNA. Translation: AAH96094.1.
    BC099627 mRNA. Translation: AAH99627.1.
    CCDSiCCDS10093.1. [P16452-2]
    CCDS45249.1. [P16452-1]
    PIRiA39707.
    RefSeqiNP_000110.2. NM_000119.2. [P16452-2]
    NP_001107606.1. NM_001114134.1. [P16452-1]
    UniGeneiHs.368642.

    Genome annotation databases

    EnsembliENST00000300215; ENSP00000300215; ENSG00000166947. [P16452-2]
    ENST00000441366; ENSP00000396616; ENSG00000166947. [P16452-1]
    GeneIDi2038.
    KEGGihsa:2038.
    UCSCiuc001zqz.4. human. [P16452-1]
    uc001zrb.4. human. [P16452-2]

    Polymorphism databases

    DMDMi215274164.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60298 mRNA. Translation: AAA74589.1 .
    L06519
    , L06447 , L06448 , L06449 , L06450 , L06511 , L06512 , L06513 , L06515 , L06516 , L06517 , L06518 Genomic DNA. Translation: AAA52385.1 .
    M29399 mRNA. Translation: AAA35798.1 .
    M30647 mRNA. Translation: AAA36401.1 . Frameshift.
    M30646 mRNA. Translation: AAA36402.1 . Frameshift.
    AC068724 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92591.1 .
    BC096093 mRNA. Translation: AAH96093.1 .
    BC096094 mRNA. Translation: AAH96094.1 .
    BC099627 mRNA. Translation: AAH99627.1 .
    CCDSi CCDS10093.1. [P16452-2 ]
    CCDS45249.1. [P16452-1 ]
    PIRi A39707.
    RefSeqi NP_000110.2. NM_000119.2. [P16452-2 ]
    NP_001107606.1. NM_001114134.1. [P16452-1 ]
    UniGenei Hs.368642.

    3D structure databases

    ProteinModelPortali P16452.
    SMRi P16452. Positions 5-689.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108352. 6 interactions.
    IntActi P16452. 3 interactions.
    STRINGi 9606.ENSP00000300215.

    PTM databases

    PhosphoSitei P16452.

    Polymorphism databases

    DMDMi 215274164.

    Proteomic databases

    PaxDbi P16452.
    PRIDEi P16452.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300215 ; ENSP00000300215 ; ENSG00000166947 . [P16452-2 ]
    ENST00000441366 ; ENSP00000396616 ; ENSG00000166947 . [P16452-1 ]
    GeneIDi 2038.
    KEGGi hsa:2038.
    UCSCi uc001zqz.4. human. [P16452-1 ]
    uc001zrb.4. human. [P16452-2 ]

    Organism-specific databases

    CTDi 2038.
    GeneCardsi GC15M043398.
    HGNCi HGNC:3381. EPB42.
    HPAi HPA040261.
    MIMi 177070. gene.
    612690. phenotype.
    neXtProti NX_P16452.
    Orphaneti 822. Hereditary spherocytosis.
    PharmGKBi PA27814.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87163.
    HOGENOMi HOG000231695.
    HOVERGENi HBG106048.
    InParanoidi P16452.
    OMAi SCFAQED.
    OrthoDBi EOG7Z0JVS.
    PhylomeDBi P16452.
    TreeFami TF324278.

    Miscellaneous databases

    GeneWikii Protein_4.2.
    GenomeRNAii 2038.
    NextBioi 8277.
    PROi P16452.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16452.
    Bgeei P16452.
    CleanExi HS_EPB42.
    Genevestigatori P16452.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view ]
    PANTHERi PTHR11590. PTHR11590. 1 hit.
    Pfami PF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
    SMARTi SM00460. TGc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Reticulocyte.
    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]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE (ISOFORM SHORT).
      Tissue: Reticulocyte.
    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]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
      Tissue: Reticulocyte.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT AND 3).
    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]
      Cited for: MYRISTOYLATION AT GLY-2.
    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. Acta 1148:19-29(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-248.
    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.
      Blood 79:1846-1854(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH5 THR-112.
    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]
      Cited for: VARIANT SPH5 THR-112.
    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]
      Cited for: VARIANT SPH5 GLN-280.
    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]
      Cited for: VARIANTS SPH5 THR-112 AND CYS-287.
    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]
      Cited for: VARIANT SPH5 TYR-145.
    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.
      Haematologica 84:660-662(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPH5 THR-112.

    Entry informationi

    Entry nameiEPB42_HUMAN
    AccessioniPrimary (citable) accession number: P16452
    Secondary accession number(s): Q4KKX0, Q4VB97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The substitution of an Ala for a Cys in the active site may be responsible for the lack of transglutaminase activity of band 4.2.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3