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2025-05-09 18:53:59, GGRNA : RefSeq release 60 (20130726)
LOCUS NM_001114134 2464 bp mRNA linear PRI 17-APR-2013
DEFINITION Homo sapiens erythrocyte membrane protein band 4.2 (EPB42),
transcript variant 2, mRNA.
ACCESSION NM_001114134
VERSION NM_001114134.1 GI:166362736
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (bases 1 to 2464)
AUTHORS Bustos,S.P. and Reithmeier,R.A.
TITLE Protein 4.2 interaction with hereditary spherocytosis mutants of
the cytoplasmic domain of human anion exchanger 1
JOURNAL Biochem. J. 433 (2), 313-322 (2011)
PUBMED 21039340
REMARK GeneRIF: study shows that cytoplasmic hereditary spherocytosis
mutants cause impaired binding of protein 4.2 to AE1, leaving
protein 4.2 susceptible to loss during erythrocyte development
REFERENCE 2 (bases 1 to 2464)
AUTHORS Korsgren,C., Peters,L.L. and Lux,S.E.
TITLE Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid
alpha-spectrin in a calcium- and calmodulin-dependent manner
JOURNAL J. Biol. Chem. 285 (7), 4757-4770 (2010)
PUBMED 20007969
REMARK GeneRIF: Data suggest that one or both of proteins 4.1 and 4.2
cause a portion of band 3 to localize near the spectrin-actin
junctions and provide another point of attachment between the
membrane skeleton and the lipid bilayer.
REFERENCE 3 (bases 1 to 2464)
AUTHORS Satchwell,T.J., Shoemark,D.K., Sessions,R.B. and Toye,A.M.
TITLE Protein 4.2: a complex linker
JOURNAL Blood Cells Mol. Dis. 42 (3), 201-210 (2009)
PUBMED 19269200
REMARK GeneRIF: Current understanding of protein 4.2, its known
interactions & implications of protein 4.2 deficiency are reviewed.
A new speculative 'open' homology structure for the the active,
membrane associated form is proposed. Review.
Review article
REFERENCE 4 (bases 1 to 2464)
AUTHORS Su,Y., Ding,Y., Jiang,M., Jiang,W., Hu,X. and Zhang,Z.
TITLE Associations of protein 4.2 with band 3 and ankyrin
JOURNAL Mol. Cell. Biochem. 289 (1-2), 159-166 (2006)
PUBMED 16718373
REMARK GeneRIF: The interactions of three protein 4.2-derived recombinant
proteins with CDB3 and ankyrin were investigated by using
Far-Western blot and pull-down assay.
REFERENCE 5 (bases 1 to 2464)
AUTHORS Dahl,K.N., Parthasarathy,R., Westhoff,C.M., Layton,D.M. and
Discher,D.E.
TITLE Protein 4.2 is critical to CD47-membrane skeleton attachment in
human red cells
JOURNAL Blood 103 (3), 1131-1136 (2004)
PUBMED 14551146
REMARK GeneRIF: protein 4.2 strongly influences CD47 levels as well as the
extent of membrane skeleton attachment in erythrocytes
REFERENCE 6 (bases 1 to 2464)
AUTHORS White,R.A., Peters,L.L., Adkison,L.R., Korsgren,C., Cohen,C.M. and
Lux,S.E.
TITLE The murine pallid mutation is a platelet storage pool disease
associated with the protein 4.2 (pallidin) gene
JOURNAL Nat. Genet. 2 (1), 80-83 (1992)
PUBMED 1284644
REFERENCE 7 (bases 1 to 2464)
AUTHORS Sung,L.A., Chien,S., Fan,Y.S., Lin,C.C., Lambert,K., Zhu,L.,
Lam,J.S. and Chang,L.S.
TITLE Human erythrocyte protein 4.2: isoform expression, differential
splicing, and chromosomal assignment
JOURNAL Blood 79 (10), 2763-2770 (1992)
PUBMED 1350227
REFERENCE 8 (bases 1 to 2464)
AUTHORS Bouhassira,E.E., Schwartz,R.S., Yawata,Y., Ata,K., Kanzaki,A.,
Qiu,J.J., Nagel,R.L. and Rybicki,A.C.
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 79 (7), 1846-1854 (1992)
PUBMED 1558976
REFERENCE 9 (bases 1 to 2464)
AUTHORS Risinger,M.A., Dotimas,E.M. and Cohen,C.M.
TITLE Human erythrocyte protein 4.2, a high copy number membrane protein,
is N-myristylated
JOURNAL J. Biol. Chem. 267 (8), 5680-5685 (1992)
PUBMED 1544941
REFERENCE 10 (bases 1 to 2464)
AUTHORS Sung,L.A., Chien,S., Chang,L.S., Lambert,K., Bliss,S.A.,
Bouhassira,E.E., Nagel,R.L., Schwartz,R.S. and Rybicki,A.C.
TITLE Molecular cloning of human protein 4.2: a major component of the
erythrocyte membrane
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 87 (3), 955-959 (1990)
PUBMED 1689063
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from DW451374.1, BC096094.2 and
BU741892.1.
Summary: 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. Alternatively spliced
transcript variants encoding different isoforms have been found for
this gene. [provided by RefSeq, Jul 2008].
Transcript Variant: This variant (2) has an alternate splice site
in the 5' region, as compared to variant 1. The resulting isoform 2
lacks an internal segment in the N-terminal region, as compared to
isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: M30646.1, M29399.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
ERS025081, ERS025084 [ECO:0000348]
##Evidence-Data-END##
COMPLETENESS: complete on the 3' end.
PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP
1-221 DW451374.1 158-378 c
222-2413 BC096094.2 1-2192
2414-2464 BU741892.1 1-51 c
FEATURES Location/Qualifiers
source 1..2464
/organism="Homo sapiens"
/mol_type="mRNA"
/db_xref="taxon:9606"
/chromosome="15"
/map="15q15-q21"
gene 1..2464
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="erythrocyte membrane protein band 4.2"
/db_xref="GeneID:2038"
/db_xref="HGNC:3381"
/db_xref="MIM:177070"
exon 1..310
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
misc_feature 280..282
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="upstream in-frame stop codon"
CDS 301..2376
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="isoform 2 is encoded by transcript variant 2;
erythrocyte surface protein band 4.2; P4.2; erythrocyte
protein 4.2"
/codon_start=1
/product="erythrocyte membrane protein band 4.2 isoform 2"
/protein_id="NP_001107606.1"
/db_xref="GI:166362737"
/db_xref="CCDS:CCDS45249.1"
/db_xref="GeneID:2038"
/db_xref="HGNC:3381"
/db_xref="MIM:177070"
/translation="
MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVALTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWDFGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVLGSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNISTKGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLKAPSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVGLQRLTVEVDCNMFQNLTNYKSVTVVAPELSA
"
misc_feature 313..678
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="Transglutaminase family; Region: Transglut_N;
pfam00868"
/db_xref="CDD:201479"
misc_feature 391..417
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="non-experimental evidence, no additional
details recorded"
/note="propagated from UniProtKB/Swiss-Prot (P16452.3);
Region: Band 3 binding (By similarity)"
misc_feature 1081..1356
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="Transglutaminase/protease-like homologues; Region:
TGc; smart00460"
/db_xref="CDD:128736"
misc_feature 1729..2037
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="Transglutaminase family, C-terminal ig like domain;
Region: Transglut_C; pfam00927"
/db_xref="CDD:201509"
misc_feature 2068..2352
/gene="EPB42"
/gene_synonym="PA; SPH5"
/note="Transglutaminase family, C-terminal ig like domain;
Region: Transglut_C; pfam00927"
/db_xref="CDD:201509"
exon 311..496
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 497..730
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
variation 630
/gene="EPB42"
/gene_synonym="PA; SPH5"
/replace="a"
/replace="g"
/db_xref="dbSNP:1042168"
exon 731..849
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
variation 741
/gene="EPB42"
/gene_synonym="PA; SPH5"
/replace="g"
/replace="t"
/db_xref="dbSNP:1126529"
exon 850..954
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 955..1132
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 1133..1271
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 1272..1375
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 1376..1618
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 1619..1918
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 1919..2079
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
exon 2080..2213
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
variation 2126
/gene="EPB42"
/gene_synonym="PA; SPH5"
/replace="g"
/replace="t"
/db_xref="dbSNP:11555770"
STS 2207..2370
/gene="EPB42"
/gene_synonym="PA; SPH5"
/standard_name="RH17526"
/db_xref="UniSTS:70727"
exon 2214..2451
/gene="EPB42"
/gene_synonym="PA; SPH5"
/inference="alignment:Splign:1.39.8"
polyA_site 2451
/gene="EPB42"
/gene_synonym="PA; SPH5"
ORIGIN
ccccagggctgccaggcgtattcctgcctgggcctcctggcacaagagataaaatgaacagggttactcccagtaactggtccaggagataccagcagagagggagtaggagagaagaaacatgtcagggtgctcacaggagtagtggggggaggttttgctatttccagattcttaagccaacaaaagtgccttcatattttctgtctggaagacagaaagcccagaaggagcccagaagcaacagtttgagagaggcgctttctgcggccaagtggataagaggagcggcctgcaaccatgggacaggccctgggtatcaagagctgtgactttcaggcagcaagaaacaatgaggagcaccacaccaaggccctcagctcccggcgcctctttgtgaggagggggcagcccttcaccatcatcctgtacttccgcgctccagtccgtgcatttctgcctgccctgaagaaggtggccctcactgcacaaactggagagcagccttccaagatcaacaggacccaagccacattcccaatttccagtctgggggaccgaaagtggtggagtgcagtggtggaggagagagatgcccagtcctggaccatctctgtgaccacacctgcggacgctgtcattggccactactcgcttctgctgcaggtctcaggcaggaagcaactcctcttgggtcagttcacactgctttttaacccctggaatagagaggatgctgtgttcctgaagaatgaggctcagcgcatggagtacttgttgaaccagaatggtctcatctacctgggtacagctgactgcatccaggcagagtcctgggactttggccagttcgagggggatgtcattgacctcagcctgcgcttgctgagcaaggacaagcaggtagagaagtggagccagccggtgcacgtggcccgtgtgttgggtgccttgctgcattttctcaaggagcagagggtcctgcccaccccgcagacccaggccacccaggaaggggccttgctgaacaagcgccggggcagcgtgcccatcctgcggcagtggctcaccggccgaggccgacctgtgtatgatggccaggcctgggtgttggctgctgttgcttgcacagtgctgcgatgcctgggaatccctgcccgcgtggtgaccacgtttgcctcagcacagggcaccggtgggcgtcttctcatagatgaatactataatgaggagggacttcagaacggagaaggccagagaggcagaatctggatcttccagacttccacagagtgctggatgacgcggcctgccttgccccagggttatgatggatggcagattctgcacccaagtgctcctaatggaggtggagtcctggggtcctgtgatctggtgccggtcagagcagtcaaggaggggacgctggggctgaccccagcagtgtcagacctttttgctgccataaatgcctcatgtgtggtctggaagtgctgtgaggatgggacactggagttgactgactccaacacaaagtatgttggcaacaacatcagcaccaagggtgtgggcagtgaccgctgcgaggacatcactcagaactacaagtatcctgaagggtctcttcaggaaaaagaggtgctggagagagtcgagaaagagaaaatggaacgtgagaaagacaacggcatccgtcctcccagtctcgagactgccagtcctctgtacctgctcttgaaagcacccagctccctacccctgagaggggatgcccagatctcagtgacgctggttaatcacagtgagcaggagaaggcagtgcagctggcaattggggtccaggctgtacactacaacggtgtccttgctgccaagctctggaggaagaagctgcacctcacgctcagtgccaacctggaaaagataataaccatcggcctgttcttctccaattttgagcgaaacccacccgagaacaccttccttagactcaccgccatggcaacacactctgaatccaaccttagctgctttgctcaggaagacattgccatttgtagaccacaccttgccatcaagatgccagagaaagcagagcagtatcaacccctcacagcctcagtcagcctccagaactccctagatgcccccatggaggactgtgtgatctccatcctgggaagggggctcattcacagagagaggagctacagattccgttcagtgtggcctgaaaacaccatgtgtgccaagttccagttcacgccaacacatgtggggctccagagactcactgtggaagtggactgcaacatgttccagaacctaaccaactataaaagcgtcaccgtggtagcccctgaactatcagcttaaacttccagctctatcaccactctcctgccaacccttgttctacaatctaaaccaaacatgtgctaggaagagaaaaaaaaaaaaaaaa
//
ANNOTATIONS from NCBI Entrez Gene (20130726):
GeneID:2038 -> Molecular function: GO:0003810 [protein-glutamine gamma-glutamyltransferase activity] evidence: IEA
GeneID:2038 -> Molecular function: GO:0005200 [structural constituent of cytoskeleton] evidence: TAS
GeneID:2038 -> Molecular function: GO:0005515 [protein binding] evidence: IPI
GeneID:2038 -> Molecular function: GO:0005524 [ATP binding] evidence: TAS
GeneID:2038 -> Biological process: GO:0000902 [cell morphogenesis] evidence: IEA
GeneID:2038 -> Biological process: GO:0008360 [regulation of cell shape] evidence: IEA
GeneID:2038 -> Biological process: GO:0018149 [peptide cross-linking] evidence: IEA
GeneID:2038 -> Biological process: GO:0020027 [hemoglobin metabolic process] evidence: IEA
GeneID:2038 -> Biological process: GO:0043249 [erythrocyte maturation] evidence: IEA
GeneID:2038 -> Biological process: GO:0048536 [spleen development] evidence: IEA
GeneID:2038 -> Biological process: GO:0055072 [iron ion homeostasis] evidence: IEA
GeneID:2038 -> Cellular component: GO:0005856 [cytoskeleton] evidence: TAS
GeneID:2038 -> Cellular component: GO:0005886 [plasma membrane] evidence: IEA
GeneID:2038 -> Cellular component: GO:0030863 [cortical cytoskeleton] evidence: IEA
by
@meso_cacase at
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