[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND PROTEIN SEQUENCE OF 378-393.
TISSUE=Reticulocyte;
PubMed=3467321 [NCBI, ExPASy, EBI, Israel, Japan]
Conboy J.G.,
Kan Y.W.,
Shohet S.B.,
Mohandas N.;
"Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton.";
Proc. Natl. Acad. Sci. U.S.A. 83:9512-9516(1986).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
PubMed=3223413 [NCBI, ExPASy, EBI, Israel, Japan]
Tang T.K.,
Leto T.L.,
Marchesi V.T.,
Benz E.J. Jr.;
"Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues.";
Adv. Exp. Med. Biol. 241:81-95(1988).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
PubMed=3375238 [NCBI, ExPASy, EBI, Israel, Japan]
Tang T.K.,
Leto T.L.,
Correas I.,
Alonso M.A.,
Marchesi V.T.,
Benz E.J. Jr.;
"Selective expression of an erythroid-specific isoform of protein 4.1.";
Proc. Natl. Acad. Sci. U.S.A. 85:3713-3717(1988).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=2022644 [NCBI, ExPASy, EBI, Israel, Japan]
Conboy J.G.,
Chan J.Y.C.,
Chasis J.A.,
Kan Y.W.,
Mohandas N.;
"Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1.";
J. Biol. Chem. 266:8273-8280(1991).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Huang S.C.,
Wang C.,
Lichtenauer U.,
Vortmeyer A.,
Zhuang Z.;
"Sequence of protein 4.1 from a human neuroblastoma cell line: LAN5.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G.,
Barlow K.F.,
McLay K.E.,
Kaul R.,
Swarbreck D.,
Dunham A.,
Scott C.E.,
Howe K.L.,
Woodfine K.,
Spencer C.C.A.,
Jones M.C.,
Gillson C.,
Searle S.,
Zhou Y.,
Kokocinski F.,
McDonald L.,
Evans R.,
Phillips K.,
Atkinson A., ![]()
Cooper R.,
Jones C.,
Hall R.E.,
Andrews T.D.,
Lloyd C.,
Ainscough R.,
Almeida J.P.,
Ambrose K.D.,
Anderson F.,
Andrew R.W.,
Ashwell R.I.S.,
Aubin K.,
Babbage A.K.,
Bagguley C.L.,
Bailey J.,
Beasley H.,
Bethel G.,
Bird C.P.,
Bray-Allen S.,
Brown J.Y.,
Brown A.J.,
Buckley D.,
Burton J.,
Bye J.,
Carder C.,
Chapman J.C.,
Clark S.Y.,
Clarke G.,
Clee C.,
Cobley V.,
Collier R.E.,
Corby N.,
Coville G.J.,
Davies J.,
Deadman R.,
Dunn M.,
Earthrowl M.,
Ellington A.G.,
Errington H.,
Frankish A.,
Frankland J.,
French L.,
Garner P.,
Garnett J.,
Gay L.,
Ghori M.R.J.,
Gibson R.,
Gilby L.M.,
Gillett W.,
Glithero R.J.,
Grafham D.V.,
Griffiths C.,
Griffiths-Jones S.,
Grocock R.,
Hammond S.,
Harrison E.S.I.,
Hart E.,
Haugen E.,
Heath P.D.,
Holmes S.,
Holt K.,
Howden P.J.,
Hunt A.R.,
Hunt S.E.,
Hunter G.,
Isherwood J.,
James R.,
Johnson C.,
Johnson D.,
Joy A.,
Kay M.,
Kershaw J.K.,
Kibukawa M.,
Kimberley A.M.,
King A.,
Knights A.J.,
Lad H.,
Laird G.,
Lawlor S.,
Leongamornlert D.A.,
Lloyd D.M.,
Loveland J.,
Lovell J.,
Lush M.J.,
Lyne R.,
Martin S.,
Mashreghi-Mohammadi M.,
Matthews L.,
Matthews N.S.W.,
McLaren S.,
Milne S.,
Mistry S.,
Moore M.J.F.,
Nickerson T.,
O'Dell C.N.,
Oliver K.,
Palmeiri A.,
Palmer S.A.,
Parker A.,
Patel D.,
Pearce A.V.,
Peck A.I.,
Pelan S.,
Phelps K.,
Phillimore B.J.,
Plumb R.,
Rajan J.,
Raymond C.,
Rouse G.,
Saenphimmachak C.,
Sehra H.K.,
Sheridan E.,
Shownkeen R.,
Sims S.,
Skuce C.D.,
Smith M.,
Steward C.,
Subramanian S.,
Sycamore N.,
Tracey A.,
Tromans A.,
Van Helmond Z.,
Wall M.,
Wallis J.M.,
White S.,
Whitehead S.L.,
Wilkinson J.E.,
Willey D.L.,
Williams H.,
Wilming L.,
Wray P.W.,
Wu Z.,
Coulson A.,
Vaudin M.,
Sulston J.E.,
Durbin R.M.,
Hubbard T.,
Wooster R.,
Dunham I.,
Carter N.P.,
McVean G.,
Ross M.T.,
Harrow J.,
Olson M.V.,
Beck S.,
Rogers J.,
Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
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[7]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[8]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-227, AND VARIANT ILE-214.
Lichtenauer U.,
Huang S.C.,
Vortmeyer A.,
Zhuang Z.;
"Valine to isoleucine polymorphism in exon 4 of human protein 4.1.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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[9]
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NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), AND ALTERNATIVE SPLICING.
PubMed=3194408 [NCBI, ExPASy, EBI, Israel, Japan]
Conboy J.G.,
Chan J.,
Mohandas N.,
Kan Y.W.;
"Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:9062-9065(1988).
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[10]
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PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, AND PHOSPHORYLATION AT SERINE RESIDUES.
DOI=10.1016/0167-4889(90)90095-U; PubMed=2171679 [NCBI, ExPASy, EBI, Israel, Japan]
Horne W.C.,
Prinz W.C.,
Tang E.K.;
"Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1.";
Biochim. Biophys. Acta 1055:87-92(1990).
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[11]
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PROTEIN SEQUENCE OF 648-714.
PubMed=3531202 [NCBI, ExPASy, EBI, Israel, Japan]
Correas I.,
Speicher D.W.,
Marchesi V.T.;
"Structure of the spectrin-actin binding site of erythrocyte protein 4.1.";
J. Biol. Chem. 261:13362-13366(1986).
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[12]
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STRUCTURE OF CARBOHYDRATES.
PubMed=2808371 [NCBI, ExPASy, EBI, Israel, Japan]
Inaba M.,
Maede Y.;
"O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.";
J. Biol. Chem. 264:18149-18155(1989).
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[13]
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PHOSPHORYLATION AT TYR-660.
PubMed=1647028 [NCBI, ExPASy, EBI, Israel, Japan]
Subrahmanyan G.,
Bertics P.J.,
Anderson R.A.;
"Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro.";
Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991).
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[14]
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INTERACTION WITH DLG1.
PubMed=7937897 [NCBI, ExPASy, EBI, Israel, Japan]
Lue R.A.,
Marfatia S.M.,
Branton D.,
Chishti A.H.;
"Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1.";
Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994).
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[15]
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INTERACTION WITH CALMODULIN.
DOI=10.1074/jbc.275.9.6360; PubMed=10692436 [NCBI, ExPASy, EBI, Israel, Japan]
Nunomura W.,
Takakuwa Y.,
Parra M.,
Conboy J.G.,
Mohandas N.;
"Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins.";
J. Biol. Chem. 275:6360-6367(2000).
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[16]
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INTERACTION WITH CENPJ.
DOI=10.1128/MCB.20.20.7813-7825.2000; PubMed=11003675 [NCBI, ExPASy, EBI, Israel, Japan]
Hung L.-Y.,
Tang C.J.,
Tang T.K.;
"Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex.";
Mol. Cell. Biol. 20:7813-7825(2000).
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[17]
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CHARACTERIZATION OF C-TERMINAL DOMAIN.
DOI=10.1046/j.1432-1327.2001.02276.x; PubMed=11432737 [NCBI, ExPASy, EBI, Israel, Japan]
Scott C.,
Phillips G.W.,
Baines A.J.;
"Properties of the C-terminal domain of 4.1 proteins.";
Eur. J. Biochem. 268:3709-3717(2001).
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[18]
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SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
DOI=10.1074/jbc.M201521200; PubMed=12427749 [NCBI, ExPASy, EBI, Israel, Japan]
Luque C.M.,
Perez-Ferreiro C.M.,
Perez-Gonzalez A.,
Englmeier L.,
Koffa M.D.,
Correas I.;
"An alternative domain containing a leucine-rich sequence regulates nuclear cytoplasmic localization of protein 4.1R.";
J. Biol. Chem. 278:2686-2691(2003).
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[19]
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MUTAGENESIS OF THR-60 AND SER-712, AND PHOSPHORYLATION AT THR-60 AND SER-712.
DOI=10.1091/mbc.E04-05-0426; PubMed=15525677 [NCBI, ExPASy, EBI, Israel, Japan]
Huang S.-C.,
Liu E.S.,
Chan S.-H.,
Munagala I.D.,
Cho H.T.,
Jagadeeswaran R.,
Benz E.J. Jr.;
"Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase.";
Mol. Biol. Cell 16:117-127(2005).
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[20]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H.,
Horn D.M.,
Tang N.,
Mathivanan S.,
Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
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[21]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T.,
Yi W.,
Lu B.,
Park S.K.,
Xu T.,
Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
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[22]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-555 AND SER-712, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N.,
Zhou C.,
Villen J.,
Beausoleil S.A.,
Bakalarski C.E.,
Elledge S.J.,
Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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[23]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488.
DOI=10.1038/82819; PubMed=11017195 [NCBI, ExPASy, EBI, Israel, Japan]
Han B.-G.,
Nunomura W.,
Takakuwa Y.,
Mohandas N.,
Jap B.K.;
"Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization.";
Nat. Struct. Biol. 7:871-875(2000).
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