E41L1_HUMAN
ID E41L1_HUMAN Reviewed; 881 AA.
AC Q9H4G0; O15046; Q4VXM6; Q4VXM7; Q4VXM8; Q4VXN4; Q6ZT61; Q8IUU7; Q96CV5;
AC Q96L65;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Band 4.1-like protein 1;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 1 {ECO:0000312|HGNC:HGNC:3378};
DE AltName: Full=Neuronal protein 4.1;
DE Short=4.1N;
GN Name=EPB41L1 {ECO:0000312|HGNC:HGNC:3378};
GN Synonyms=KIAA0338 {ECO:0000312|HGNC:HGNC:3378};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-873 (ISOFORM 1).
RA Liu J., Zhou Y., Zhang B., Peng X., Yuan J., Qiang B.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH AGAP2.
RX PubMed=11136977; DOI=10.1016/s0092-8674(00)00195-1;
RA Ye K., Hurt K.J., Wu F.Y., Fang M., Luo H.R., Hong J.J., Blackshaw S.,
RA Ferris C.D., Snyder S.H.;
RT "PIKE: a nuclear GTPase that enhances PI3kinase activity and is regulated
RT by protein 4.1N.";
RL Cell 103:919-930(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-79; THR-475; SER-540;
RP SER-541; SER-544; SER-546; SER-578; SER-648; SER-650 AND SER-784, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-430; SER-510;
RP SER-544; SER-546; SER-564 AND SER-650, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 2 AND 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-79; SER-378; SER-430;
RP SER-437; THR-475; SER-510; SER-544; SER-546; THR-550; SER-648; SER-650;
RP SER-678 AND SER-784, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP VARIANT MRD11 SER-854, AND CHARACTERIZATION OF VARIANT MRD11 SER-854.
RX PubMed=21376300; DOI=10.1016/j.ajhg.2011.02.001;
RA Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y., Higashi K.,
RA Park A.R., Spiegelman D., Dobrzeniecka S., Piton A., Tomitori H., Daoud H.,
RA Massicotte C., Henrion E., Diallo O., Shekarabi M., Marineau C.,
RA Shevell M., Maranda B., Mitchell G., Nadeau A., D'Anjou G., Vanasse M.,
RA Srour M., Lafreniere R.G., Drapeau P., Lacaille J.C., Kim E., Lee J.R.,
RA Igarashi K., Huganir R.L., Rouleau G.A., Michaud J.L.;
RT "Excess of de novo deleterious mutations in genes associated with
RT glutamatergic systems in nonsyndromic intellectual disability.";
RL Am. J. Hum. Genet. 88:306-316(2011).
CC -!- FUNCTION: May function to confer stability and plasticity to neuronal
CC membrane via multiple interactions, including the spectrin-actin-based
CC cytoskeleton, integral membrane channels and membrane-associated
CC guanylate kinases.
CC -!- SUBUNIT: Interacts with AGAP2. {ECO:0000269|PubMed:11136977}.
CC -!- INTERACTION:
CC Q9H4G0; P54274: TERF1; NbExp=2; IntAct=EBI-465536, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H4G0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4G0-2; Sequence=VSP_023958, VSP_023961, VSP_023963;
CC Name=3;
CC IsoId=Q9H4G0-3; Sequence=VSP_023958, VSP_023960, VSP_023961;
CC Name=4;
CC IsoId=Q9H4G0-4; Sequence=VSP_023959, VSP_023961, VSP_023962;
CC -!- TISSUE SPECIFICITY: Highest expression in brain, lower in heart,
CC kidney, pancreas, placenta, lung and skeletal muscle.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 11
CC (MRD11) [MIM:614257]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:21376300}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002336; BAA20796.1; ALT_INIT; mRNA.
DR EMBL; AK126875; BAC86733.1; -; mRNA.
DR EMBL; AL121895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013885; AAH13885.1; -; mRNA.
DR EMBL; BC040259; AAH40259.1; -; mRNA.
DR EMBL; AY049789; AAL15446.1; -; mRNA.
DR CCDS; CCDS13271.1; -. [Q9H4G0-1]
DR CCDS; CCDS13272.1; -. [Q9H4G0-2]
DR CCDS; CCDS58770.1; -. [Q9H4G0-4]
DR RefSeq; NP_001245258.1; NM_001258329.1.
DR RefSeq; NP_001245259.1; NM_001258330.1. [Q9H4G0-4]
DR RefSeq; NP_001245260.1; NM_001258331.1. [Q9H4G0-2]
DR RefSeq; NP_036288.2; NM_012156.2. [Q9H4G0-1]
DR RefSeq; NP_818932.1; NM_177996.2. [Q9H4G0-2]
DR RefSeq; XP_016883205.1; XM_017027716.1.
DR RefSeq; XP_016883206.1; XM_017027717.1.
DR RefSeq; XP_016883208.1; XM_017027719.1. [Q9H4G0-4]
DR AlphaFoldDB; Q9H4G0; -.
DR SMR; Q9H4G0; -.
DR BioGRID; 108350; 170.
DR IntAct; Q9H4G0; 38.
DR MINT; Q9H4G0; -.
DR STRING; 9606.ENSP00000337168; -.
DR GlyGen; Q9H4G0; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q9H4G0; -.
DR PhosphoSitePlus; Q9H4G0; -.
DR BioMuta; EPB41L1; -.
DR DMDM; 14916561; -.
DR EPD; Q9H4G0; -.
DR jPOST; Q9H4G0; -.
DR MassIVE; Q9H4G0; -.
DR MaxQB; Q9H4G0; -.
DR PaxDb; Q9H4G0; -.
DR PeptideAtlas; Q9H4G0; -.
DR PRIDE; Q9H4G0; -.
DR ProteomicsDB; 80831; -. [Q9H4G0-1]
DR ProteomicsDB; 80832; -. [Q9H4G0-2]
DR ProteomicsDB; 80833; -. [Q9H4G0-3]
DR ProteomicsDB; 80834; -. [Q9H4G0-4]
DR Antibodypedia; 26438; 101 antibodies from 19 providers.
DR DNASU; 2036; -.
DR Ensembl; ENST00000202028.9; ENSP00000202028.5; ENSG00000088367.23. [Q9H4G0-2]
DR Ensembl; ENST00000338074.7; ENSP00000337168.2; ENSG00000088367.23. [Q9H4G0-1]
DR Ensembl; ENST00000373950.6; ENSP00000363061.2; ENSG00000088367.23. [Q9H4G0-3]
DR Ensembl; ENST00000441639.5; ENSP00000399214.1; ENSG00000088367.23. [Q9H4G0-2]
DR Ensembl; ENST00000628415.2; ENSP00000487049.2; ENSG00000088367.23. [Q9H4G0-4]
DR GeneID; 2036; -.
DR KEGG; hsa:2036; -.
DR MANE-Select; ENST00000338074.7; ENSP00000337168.2; NM_012156.2; NP_036288.2.
DR UCSC; uc002xeu.4; human. [Q9H4G0-1]
DR CTD; 2036; -.
DR DisGeNET; 2036; -.
DR GeneCards; EPB41L1; -.
DR HGNC; HGNC:3378; EPB41L1.
DR HPA; ENSG00000088367; Low tissue specificity.
DR MalaCards; EPB41L1; -.
DR MIM; 602879; gene.
DR MIM; 614257; phenotype.
DR neXtProt; NX_Q9H4G0; -.
DR OpenTargets; ENSG00000088367; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA27811; -.
DR VEuPathDB; HostDB:ENSG00000088367; -.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000158442; -.
DR InParanoid; Q9H4G0; -.
DR OrthoDB; 193911at2759; -.
DR PhylomeDB; Q9H4G0; -.
DR TreeFam; TF351626; -.
DR PathwayCommons; Q9H4G0; -.
DR Reactome; R-HSA-399719; Trafficking of AMPA receptors.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q9H4G0; -.
DR BioGRID-ORCS; 2036; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; EPB41L1; human.
DR GeneWiki; EPB41L1; -.
DR GenomeRNAi; 2036; -.
DR Pharos; Q9H4G0; Tbio.
DR PRO; PR:Q9H4G0; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H4G0; protein.
DR Bgee; ENSG00000088367; Expressed in superior vestibular nucleus and 191 other tissues.
DR ExpressionAtlas; Q9H4G0; baseline and differential.
DR Genevisible; Q9H4G0; HS.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR007477; SAB_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF04382; SAB; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Intellectual disability; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..881
FT /note="Band 4.1-like protein 1"
FT /id="PRO_0000219395"
FT DOMAIN 97..378
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..541
FT /note="Spectrin--actin-binding"
FT REGION 514..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..881
FT /note="C-terminal (CTD)"
FT COMPBIAS 41..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP0"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP0"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 686
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP0"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023958"
FT VAR_SEQ 1..59
FT /note="MTTETGPDSEVKKAQEEAPQQPEAAAAVTTPVTPAGHGHPEANSNEKHPSQQ
FT DTRPAEQ -> MVFLGRINEVEPAKGLAESLAPTERSVK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023959"
FT VAR_SEQ 115..149
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_023960"
FT VAR_SEQ 484..495
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023961"
FT VAR_SEQ 556..692
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023962"
FT VAR_SEQ 729..756
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023963"
FT VARIANT 854
FT /note="P -> S (in MRD11; results in a 50% reduction of
FT interaction of 4.1N protein to GRIA1 compared to wild-type;
FT dbSNP:rs1569376434)"
FT /evidence="ECO:0000269|PubMed:21376300"
FT /id="VAR_066600"
FT CONFLICT 728
FT /note="Missing (in Ref. 4; AAH40259 and 5; AAL15446)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9H4G0-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9H4G0-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 881 AA; 98503 MW; D923CF554EDB41D3 CRC64;
MTTETGPDSE VKKAQEEAPQ QPEAAAAVTT PVTPAGHGHP EANSNEKHPS QQDTRPAEQS
LDMEEKDYSE ADGLSERTTP SKAQKSPQKI AKKYKSAICR VTLLDASEYE CEVEKHGRGQ
VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL
RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
SSKRYTMSRS LDGAEFSRPA SVSENHDAGP DGDKRDEDGE SGGQRSEAEE GEVRTPTKIK
ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWERERRLPS
SPASPSPKGT PEKANERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD TVFLKDNHLA
IERKCSSITV SSTSSLEAEV DFTVIGDYHG SAFEDFSRSL PELDRDKSDS DTEGLLFSRD
LNKGAPSQDD ESGGIEDSPD RGACSTPDMP QFEPVKTETM TVSSLAIRKK IEPEAVLQTR
VSAMDNTQQV DGSASVGREF IATTPSITTE TISTTMENSL KSGKGAAAMI PGPQTVATEI
RSLSPIIGKD VLTSTYGATA ETLSTSTTTH VTKTVKGGFS ETRIEKRIII TGDEDVDQDQ
ALALAIKEAK LQHPDMLVTK AVVYRETDPS PEERDKKPQE S
