Full text data of EPB41L1
EPB41L1
(KIAA0338)
[Confidence: low (only semi-automatic identification from reviews)]
Band 4.1-like protein 1 (Neuronal protein 4.1; 4.1N)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Band 4.1-like protein 1 (Neuronal protein 4.1; 4.1N)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H4G0
ID E41L1_HUMAN Reviewed; 881 AA.
AC Q9H4G0; O15046; Q4VXM6; Q4VXM7; Q4VXM8; Q4VXN4; Q6ZT61; Q8IUU7;
read moreAC Q96CV5; Q96L65;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Band 4.1-like protein 1;
DE AltName: Full=Neuronal protein 4.1;
DE Short=4.1N;
GN Name=EPB41L1; Synonyms=KIAA0338;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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
RT project: 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
RT regulated 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-79; THR-475;
RP SER-540; SER-541; SER-544; SER-546; SER-578; SER-648; SER-650 AND
RP SER-784, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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.,
RA Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A.,
RA Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O.,
RA Shekarabi M., Marineau C., Shevell M., Maranda B., Mitchell G.,
RA Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G.,
RA Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K.,
RA 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
CC neuronal membrane via multiple interactions, including the
CC spectrin-actin-based cytoskeleton, integral membrane channels and
CC membrane-associated guanylate kinases.
CC -!- SUBUNIT: Interacts with AGAP2.
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 Note=No experimental confirmation available;
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: Mental retardation, autosomal dominant 11 (MRD11)
CC [MIM:614257]: A disorder characterized by significantly below
CC average general intellectual functioning associated with
CC impairments in adaptive behavior and manifested during the
CC developmental period. Note=The disease is caused by mutations
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20796.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB002336; BAA20796.1; ALT_INIT; mRNA.
DR EMBL; AK126875; BAC86733.1; -; mRNA.
DR EMBL; AL121895; CAI95018.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95019.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95023.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95024.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95025.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95027.1; -; Genomic_DNA.
DR EMBL; BC013885; AAH13885.1; -; mRNA.
DR EMBL; BC040259; AAH40259.1; -; mRNA.
DR EMBL; AY049789; AAL15446.1; -; mRNA.
DR RefSeq; NP_001245258.1; NM_001258329.1.
DR RefSeq; NP_001245259.1; NM_001258330.1.
DR RefSeq; NP_001245260.1; NM_001258331.1.
DR RefSeq; NP_036288.2; NM_012156.2.
DR RefSeq; NP_818932.1; NM_177996.2.
DR RefSeq; XP_005260376.1; XM_005260319.1.
DR UniGene; Hs.437422; -.
DR ProteinModelPortal; Q9H4G0; -.
DR SMR; Q9H4G0; 95-377.
DR IntAct; Q9H4G0; 3.
DR MINT; MINT-5005633; -.
DR PhosphoSite; Q9H4G0; -.
DR DMDM; 14916561; -.
DR PaxDb; Q9H4G0; -.
DR PRIDE; Q9H4G0; -.
DR DNASU; 2036; -.
DR Ensembl; ENST00000202028; ENSP00000202028; ENSG00000088367.
DR Ensembl; ENST00000338074; ENSP00000337168; ENSG00000088367.
DR Ensembl; ENST00000373941; ENSP00000363052; ENSG00000088367.
DR Ensembl; ENST00000373946; ENSP00000363057; ENSG00000088367.
DR Ensembl; ENST00000373950; ENSP00000363061; ENSG00000088367.
DR Ensembl; ENST00000441639; ENSP00000399214; ENSG00000088367.
DR GeneID; 2036; -.
DR KEGG; hsa:2036; -.
DR UCSC; uc002xev.3; human.
DR CTD; 2036; -.
DR GeneCards; GC20P034679; -.
DR HGNC; HGNC:3378; EPB41L1.
DR MIM; 602879; gene.
DR MIM; 614257; phenotype.
DR neXtProt; NX_Q9H4G0; -.
DR Orphanet; 178469; Autosomal dominant nonsyndromic intellectual deficit.
DR PharmGKB; PA27811; -.
DR eggNOG; NOG242913; -.
DR HOVERGEN; HBG007777; -.
DR KO; K06107; -.
DR OMA; SNEKHPS; -.
DR OrthoDB; EOG7Z69BP; -.
DR PhylomeDB; Q9H4G0; -.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; EPB41L1; human.
DR GeneWiki; EPB41L1; -.
DR GenomeRNAi; 2036; -.
DR NextBio; 8267; -.
DR PRO; PR:Q9H4G0; -.
DR ArrayExpress; Q9H4G0; -.
DR Bgee; Q9H4G0; -.
DR Genevestigator; Q9H4G0; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
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; IPR019750; Band_41_fam.
DR InterPro; IPR021187; Band_41_protein.
DR InterPro; IPR000798; Ez/rad/moesin_like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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.
DR InterPro; IPR007477; SAB_dom.
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 PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SUPFAM; SSF47031; SSF47031; 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 Actin-binding; Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoskeleton; Disease mutation; Mental retardation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 881 Band 4.1-like protein 1.
FT /FTId=PRO_0000219395.
FT DOMAIN 97 378 FERM.
FT REGION 483 541 Spectrin--actin-binding.
FT REGION 746 881 C-terminal (CTD).
FT MOD_RES 75 75 Phosphoserine.
FT MOD_RES 79 79 Phosphothreonine.
FT MOD_RES 343 343 Phosphotyrosine (By similarity).
FT MOD_RES 430 430 Phosphoserine.
FT MOD_RES 475 475 Phosphothreonine.
FT MOD_RES 510 510 Phosphoserine.
FT MOD_RES 540 540 Phosphoserine.
FT MOD_RES 541 541 Phosphoserine.
FT MOD_RES 544 544 Phosphoserine.
FT MOD_RES 546 546 Phosphoserine.
FT MOD_RES 550 550 Phosphothreonine (By similarity).
FT MOD_RES 564 564 Phosphoserine.
FT MOD_RES 578 578 Phosphoserine.
FT MOD_RES 648 648 Phosphoserine.
FT MOD_RES 650 650 Phosphoserine.
FT MOD_RES 784 784 Phosphoserine.
FT VAR_SEQ 1 62 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_023958.
FT VAR_SEQ 1 59 MTTETGPDSEVKKAQEEAPQQPEAAAAVTTPVTPAGHGHPE
FT ANSNEKHPSQQDTRPAEQ -> MVFLGRINEVEPAKGLAES
FT LAPTERSVK (in isoform 4).
FT /FTId=VSP_023959.
FT VAR_SEQ 115 149 Missing (in isoform 3).
FT /FTId=VSP_023960.
FT VAR_SEQ 484 495 Missing (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_023961.
FT VAR_SEQ 556 692 Missing (in isoform 4).
FT /FTId=VSP_023962.
FT VAR_SEQ 729 756 Missing (in isoform 2).
FT /FTId=VSP_023963.
FT VARIANT 854 854 P -> S (in MRD11; results in a 50%
FT reduction of interaction of 4.1N protein
FT to GRIA1 compared to wild-type).
FT /FTId=VAR_066600.
FT CONFLICT 728 728 Missing (in Ref. 3; CAI95019/CAI95025, 4;
FT AAH40259 and 5; AAL15446).
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
//
ID E41L1_HUMAN Reviewed; 881 AA.
AC Q9H4G0; O15046; Q4VXM6; Q4VXM7; Q4VXM8; Q4VXN4; Q6ZT61; Q8IUU7;
read moreAC Q96CV5; Q96L65;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Band 4.1-like protein 1;
DE AltName: Full=Neuronal protein 4.1;
DE Short=4.1N;
GN Name=EPB41L1; Synonyms=KIAA0338;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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
RT project: 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
RT regulated 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-79; THR-475;
RP SER-540; SER-541; SER-544; SER-546; SER-578; SER-648; SER-650 AND
RP SER-784, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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.,
RA Higashi K., Park A.R., Spiegelman D., Dobrzeniecka S., Piton A.,
RA Tomitori H., Daoud H., Massicotte C., Henrion E., Diallo O.,
RA Shekarabi M., Marineau C., Shevell M., Maranda B., Mitchell G.,
RA Nadeau A., D'Anjou G., Vanasse M., Srour M., Lafreniere R.G.,
RA Drapeau P., Lacaille J.C., Kim E., Lee J.R., Igarashi K.,
RA 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
CC neuronal membrane via multiple interactions, including the
CC spectrin-actin-based cytoskeleton, integral membrane channels and
CC membrane-associated guanylate kinases.
CC -!- SUBUNIT: Interacts with AGAP2.
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 Note=No experimental confirmation available;
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: Mental retardation, autosomal dominant 11 (MRD11)
CC [MIM:614257]: A disorder characterized by significantly below
CC average general intellectual functioning associated with
CC impairments in adaptive behavior and manifested during the
CC developmental period. Note=The disease is caused by mutations
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20796.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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DR EMBL; AB002336; BAA20796.1; ALT_INIT; mRNA.
DR EMBL; AK126875; BAC86733.1; -; mRNA.
DR EMBL; AL121895; CAI95018.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95019.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95023.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95024.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95025.1; -; Genomic_DNA.
DR EMBL; AL121895; CAI95027.1; -; Genomic_DNA.
DR EMBL; BC013885; AAH13885.1; -; mRNA.
DR EMBL; BC040259; AAH40259.1; -; mRNA.
DR EMBL; AY049789; AAL15446.1; -; mRNA.
DR RefSeq; NP_001245258.1; NM_001258329.1.
DR RefSeq; NP_001245259.1; NM_001258330.1.
DR RefSeq; NP_001245260.1; NM_001258331.1.
DR RefSeq; NP_036288.2; NM_012156.2.
DR RefSeq; NP_818932.1; NM_177996.2.
DR RefSeq; XP_005260376.1; XM_005260319.1.
DR UniGene; Hs.437422; -.
DR ProteinModelPortal; Q9H4G0; -.
DR SMR; Q9H4G0; 95-377.
DR IntAct; Q9H4G0; 3.
DR MINT; MINT-5005633; -.
DR PhosphoSite; Q9H4G0; -.
DR DMDM; 14916561; -.
DR PaxDb; Q9H4G0; -.
DR PRIDE; Q9H4G0; -.
DR DNASU; 2036; -.
DR Ensembl; ENST00000202028; ENSP00000202028; ENSG00000088367.
DR Ensembl; ENST00000338074; ENSP00000337168; ENSG00000088367.
DR Ensembl; ENST00000373941; ENSP00000363052; ENSG00000088367.
DR Ensembl; ENST00000373946; ENSP00000363057; ENSG00000088367.
DR Ensembl; ENST00000373950; ENSP00000363061; ENSG00000088367.
DR Ensembl; ENST00000441639; ENSP00000399214; ENSG00000088367.
DR GeneID; 2036; -.
DR KEGG; hsa:2036; -.
DR UCSC; uc002xev.3; human.
DR CTD; 2036; -.
DR GeneCards; GC20P034679; -.
DR HGNC; HGNC:3378; EPB41L1.
DR MIM; 602879; gene.
DR MIM; 614257; phenotype.
DR neXtProt; NX_Q9H4G0; -.
DR Orphanet; 178469; Autosomal dominant nonsyndromic intellectual deficit.
DR PharmGKB; PA27811; -.
DR eggNOG; NOG242913; -.
DR HOVERGEN; HBG007777; -.
DR KO; K06107; -.
DR OMA; SNEKHPS; -.
DR OrthoDB; EOG7Z69BP; -.
DR PhylomeDB; Q9H4G0; -.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; EPB41L1; human.
DR GeneWiki; EPB41L1; -.
DR GenomeRNAi; 2036; -.
DR NextBio; 8267; -.
DR PRO; PR:Q9H4G0; -.
DR ArrayExpress; Q9H4G0; -.
DR Bgee; Q9H4G0; -.
DR Genevestigator; Q9H4G0; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
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; IPR019750; Band_41_fam.
DR InterPro; IPR021187; Band_41_protein.
DR InterPro; IPR000798; Ez/rad/moesin_like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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.
DR InterPro; IPR007477; SAB_dom.
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 PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SUPFAM; SSF47031; SSF47031; 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 Actin-binding; Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoskeleton; Disease mutation; Mental retardation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 881 Band 4.1-like protein 1.
FT /FTId=PRO_0000219395.
FT DOMAIN 97 378 FERM.
FT REGION 483 541 Spectrin--actin-binding.
FT REGION 746 881 C-terminal (CTD).
FT MOD_RES 75 75 Phosphoserine.
FT MOD_RES 79 79 Phosphothreonine.
FT MOD_RES 343 343 Phosphotyrosine (By similarity).
FT MOD_RES 430 430 Phosphoserine.
FT MOD_RES 475 475 Phosphothreonine.
FT MOD_RES 510 510 Phosphoserine.
FT MOD_RES 540 540 Phosphoserine.
FT MOD_RES 541 541 Phosphoserine.
FT MOD_RES 544 544 Phosphoserine.
FT MOD_RES 546 546 Phosphoserine.
FT MOD_RES 550 550 Phosphothreonine (By similarity).
FT MOD_RES 564 564 Phosphoserine.
FT MOD_RES 578 578 Phosphoserine.
FT MOD_RES 648 648 Phosphoserine.
FT MOD_RES 650 650 Phosphoserine.
FT MOD_RES 784 784 Phosphoserine.
FT VAR_SEQ 1 62 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_023958.
FT VAR_SEQ 1 59 MTTETGPDSEVKKAQEEAPQQPEAAAAVTTPVTPAGHGHPE
FT ANSNEKHPSQQDTRPAEQ -> MVFLGRINEVEPAKGLAES
FT LAPTERSVK (in isoform 4).
FT /FTId=VSP_023959.
FT VAR_SEQ 115 149 Missing (in isoform 3).
FT /FTId=VSP_023960.
FT VAR_SEQ 484 495 Missing (in isoform 2, isoform 3 and
FT isoform 4).
FT /FTId=VSP_023961.
FT VAR_SEQ 556 692 Missing (in isoform 4).
FT /FTId=VSP_023962.
FT VAR_SEQ 729 756 Missing (in isoform 2).
FT /FTId=VSP_023963.
FT VARIANT 854 854 P -> S (in MRD11; results in a 50%
FT reduction of interaction of 4.1N protein
FT to GRIA1 compared to wild-type).
FT /FTId=VAR_066600.
FT CONFLICT 728 728 Missing (in Ref. 3; CAI95019/CAI95025, 4;
FT AAH40259 and 5; AAL15446).
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
//
MIM
602879
*RECORD*
*FIELD* NO
602879
*FIELD* TI
*602879 ERYTHROCYTE MEMBRANE PROTEIN BAND 4.1-LIKE 1; EPB41L1
;;NONERYTHROID PROTEIN 4.1, NEURON TYPE; 4.1N
read more*FIELD* TX
CLONING
Erythrocyte membrane protein band 4.1 (EPB41; 130500) is a
multifunctional protein that mediates interactions between the
erythrocyte cytoskeleton and the overlying plasma membrane. By screening
human brain cDNAs for the potential to encode proteins larger than 100
kD, Nagase et al. (1997) identified a partial EPB41L1 cDNA. The 6,263-bp
cDNA contains an open reading frame encoding 934 amino acids; it may
lack 5-prime coding sequence. The predicted polypeptide is 46% identical
to EPB41 across 670 amino acids. By SDS-PAGE, the in vitro
transcribed/translated product of the cDNA had a molecular mass of
greater than 100 kD. RT-PCR detected EPB41L1 expression in several human
tissues.
MAPPING
By radiation hybrid mapping and somatic cell hybrid analysis, Kim et al.
(1998) localized the EPB41L1 gene to 20q11.2-q12.
MOLECULAR GENETICS
Hamdan et al. (2011) identified a heterozygous missense mutation in the
EPB41L1 gene causing nonsyndromic intellectual disability (MRD11;
614257). This mutation replaces a highly conserved proline at position
854 in the C-terminal domain of the 4.1N protein encoded by EPB41L1.
*FIELD* AV
.0001
MENTAL RETARDATION, AUTOSOMAL DOMINANT 11
EPB41L1, PRO854SER
In a patient with nonsyndromic severe intellectual disability (MRD11;
614257), Hamdan et al. (2011) identified a heterozygous C-to-T
transition in the EPB41L1 gene that resulted in a pro-to-ser
substitution at codon 854 (P854S). The patient had hypotonia, no
evidence of epilepsy, and normal brain imaging by MRI. 4.1N is a
neuronal cytoskeletal protein, which binds to AMPA receptor subunits
through its C-terminal domain and regulates their expression at the
synaptic membrane (Lin et al., 2009, Shen et al., 2000). Hamdan et al.
(2011) showed that substitution of proline for serine at position 854
results in a 50% reduction of binding of 4.1N to GLUR1 (138248) compared
to wildtype.
*FIELD* RF
1. Hamdan, F. F.; Gauthier, J.; Araki, Y.; Lin, D.-T.; Yoshizawa,
Y.; Higashi, K.; Park, A.-R.; Spiegelman, D.; Dobrzeniecka, S.; Piton,
A.; Tomitori, H.; Daoud, H.; and 22 others: Excess of de novo deleterious
mutations in genes associated with glutamatergic systems in nonsyndromic
intellectual disability. Am. J. Hum. Genet. 88: 306-316, 2011. Note:
Erratum: Am. J. Hum. Genet. 88: 516 only, 2011.
2. Kim, A. C.; Van Huffel, C.; Lutchman, M.; Chishti, A. H.: Radiation
hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human
chromosome 20q11.2-q12. Genomics 49: 165-166, 1998.
3. Lin, D.-T.; Makino, Y.; Sharma, K.; Hayashi, T.; Neve, R.; Takamiya,
K.; Huganir, R. L.: Regulation of AMPA receptor extrasynaptic insertion
by 4.1N, phosphorylation and palmitoylation. Nature Neurosci. 12:
879-887, 2009.
4. Nagase, T.; Ishikawa, K.; Nakajima, D.; Ohira, M.; Seki, N.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VII. The complete
sequences of 100 new cDNA clones from brain which can code for large
proteins in vitro. DNA Res. 4: 141-150, 1997.
5. Shen, L.; Liang, F.; Walensky, L. D.; Huganir, R. L.: Regulation
of AMPA receptor GluR1 subunit surface expression by 4.1N-linked actin
cytoskeletal association. J. Neurosci. 20: 7932-7940, 2000.
*FIELD* CN
Ada Hamosh - updated: 9/23/2011
*FIELD* CD
Patti M. Sherman: 7/23/1998
*FIELD* ED
terry: 07/06/2012
terry: 10/10/2011
alopez: 10/3/2011
terry: 9/23/2011
carol: 1/16/2008
mgross: 3/10/2003
alopez: 7/28/1998
*RECORD*
*FIELD* NO
602879
*FIELD* TI
*602879 ERYTHROCYTE MEMBRANE PROTEIN BAND 4.1-LIKE 1; EPB41L1
;;NONERYTHROID PROTEIN 4.1, NEURON TYPE; 4.1N
read more*FIELD* TX
CLONING
Erythrocyte membrane protein band 4.1 (EPB41; 130500) is a
multifunctional protein that mediates interactions between the
erythrocyte cytoskeleton and the overlying plasma membrane. By screening
human brain cDNAs for the potential to encode proteins larger than 100
kD, Nagase et al. (1997) identified a partial EPB41L1 cDNA. The 6,263-bp
cDNA contains an open reading frame encoding 934 amino acids; it may
lack 5-prime coding sequence. The predicted polypeptide is 46% identical
to EPB41 across 670 amino acids. By SDS-PAGE, the in vitro
transcribed/translated product of the cDNA had a molecular mass of
greater than 100 kD. RT-PCR detected EPB41L1 expression in several human
tissues.
MAPPING
By radiation hybrid mapping and somatic cell hybrid analysis, Kim et al.
(1998) localized the EPB41L1 gene to 20q11.2-q12.
MOLECULAR GENETICS
Hamdan et al. (2011) identified a heterozygous missense mutation in the
EPB41L1 gene causing nonsyndromic intellectual disability (MRD11;
614257). This mutation replaces a highly conserved proline at position
854 in the C-terminal domain of the 4.1N protein encoded by EPB41L1.
*FIELD* AV
.0001
MENTAL RETARDATION, AUTOSOMAL DOMINANT 11
EPB41L1, PRO854SER
In a patient with nonsyndromic severe intellectual disability (MRD11;
614257), Hamdan et al. (2011) identified a heterozygous C-to-T
transition in the EPB41L1 gene that resulted in a pro-to-ser
substitution at codon 854 (P854S). The patient had hypotonia, no
evidence of epilepsy, and normal brain imaging by MRI. 4.1N is a
neuronal cytoskeletal protein, which binds to AMPA receptor subunits
through its C-terminal domain and regulates their expression at the
synaptic membrane (Lin et al., 2009, Shen et al., 2000). Hamdan et al.
(2011) showed that substitution of proline for serine at position 854
results in a 50% reduction of binding of 4.1N to GLUR1 (138248) compared
to wildtype.
*FIELD* RF
1. Hamdan, F. F.; Gauthier, J.; Araki, Y.; Lin, D.-T.; Yoshizawa,
Y.; Higashi, K.; Park, A.-R.; Spiegelman, D.; Dobrzeniecka, S.; Piton,
A.; Tomitori, H.; Daoud, H.; and 22 others: Excess of de novo deleterious
mutations in genes associated with glutamatergic systems in nonsyndromic
intellectual disability. Am. J. Hum. Genet. 88: 306-316, 2011. Note:
Erratum: Am. J. Hum. Genet. 88: 516 only, 2011.
2. Kim, A. C.; Van Huffel, C.; Lutchman, M.; Chishti, A. H.: Radiation
hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human
chromosome 20q11.2-q12. Genomics 49: 165-166, 1998.
3. Lin, D.-T.; Makino, Y.; Sharma, K.; Hayashi, T.; Neve, R.; Takamiya,
K.; Huganir, R. L.: Regulation of AMPA receptor extrasynaptic insertion
by 4.1N, phosphorylation and palmitoylation. Nature Neurosci. 12:
879-887, 2009.
4. Nagase, T.; Ishikawa, K.; Nakajima, D.; Ohira, M.; Seki, N.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VII. The complete
sequences of 100 new cDNA clones from brain which can code for large
proteins in vitro. DNA Res. 4: 141-150, 1997.
5. Shen, L.; Liang, F.; Walensky, L. D.; Huganir, R. L.: Regulation
of AMPA receptor GluR1 subunit surface expression by 4.1N-linked actin
cytoskeletal association. J. Neurosci. 20: 7932-7940, 2000.
*FIELD* CN
Ada Hamosh - updated: 9/23/2011
*FIELD* CD
Patti M. Sherman: 7/23/1998
*FIELD* ED
terry: 07/06/2012
terry: 10/10/2011
alopez: 10/3/2011
terry: 9/23/2011
carol: 1/16/2008
mgross: 3/10/2003
alopez: 7/28/1998
MIM
614257
*RECORD*
*FIELD* NO
614257
*FIELD* TI
#614257 MENTAL RETARDATION, AUTOSOMAL DOMINANT 11; MRD11
*FIELD* TX
A number sign (#) is used with this entry because this form of mental
read moreretardation is caused by heterozygous mutation in the EPB41L1 gene
(602879) on chromosome 20q11.2-q12.
CLINICAL FEATURES
Hamdan et al. (2011) hypothesized that de novo mutations in synaptic
genes explain an important fraction of sporadic nonsyndromic
intellectual disability (NSID) cases. To investigate the possibility,
they sequenced 197 genes encoding glutamate receptors and a large subset
of their known interacting proteins in 95 sporadic cases of NSID. They
identified a single patient with a missense mutation in the EPB41L1
gene. The male patient, 6 years old at the time of the report, had
severe intellectual disability, no evidence of epilepsy, hypotonia, and
normal brain imaging by MRI.
MOLECULAR GENETICS
In a patient with nonsyndromic intellectual disability, Hamdan et al.
(2011) identified a heterozygous missense mutation in the EPB41L1 gene
(P854S; 602879.0001). This mutation affects a highly conserved proline
in the C-terminal domain of the 4.1N protein, which binds AMPA receptor
subunits. Coimmunoprecipitation studies showed that the
proline-to-serine substitution at codon 854 reduces the binding of 4.1N
to GLUR1 (138248) by 50% in HEK293 cells. Moreover, insertion of GLUR1
at the synaptic membrane was significantly decreased in transfected
hippocampal neurons producing mutant 4.1N when compared to cells
producing wildtype 4.1N.
*FIELD* RF
1. Hamdan, F. F.; Gauthier, J.; Araki, Y.; Lin, D.-T.; Yoshizawa,
Y.; Higashi, K.; Park, A.-R.; Spiegelman, D.; Dobrzeniecka, S.; Piton,
A.; Tomitori, H.; Daoud, H.; and 22 others: Excess of de novo deleterious
mutations in genes associated with glutamatergic systems in nonsyndromic
intellectual disability. Am. J. Hum. Genet. 88: 306-316, 2011. Note;
Erratum: Am. J. Hum. Genet. 88: 516 only, 2011.
*FIELD* CD
Ada Hamosh: 9/28/2011
*FIELD* ED
terry: 07/06/2012
alopez: 10/3/2011
*RECORD*
*FIELD* NO
614257
*FIELD* TI
#614257 MENTAL RETARDATION, AUTOSOMAL DOMINANT 11; MRD11
*FIELD* TX
A number sign (#) is used with this entry because this form of mental
read moreretardation is caused by heterozygous mutation in the EPB41L1 gene
(602879) on chromosome 20q11.2-q12.
CLINICAL FEATURES
Hamdan et al. (2011) hypothesized that de novo mutations in synaptic
genes explain an important fraction of sporadic nonsyndromic
intellectual disability (NSID) cases. To investigate the possibility,
they sequenced 197 genes encoding glutamate receptors and a large subset
of their known interacting proteins in 95 sporadic cases of NSID. They
identified a single patient with a missense mutation in the EPB41L1
gene. The male patient, 6 years old at the time of the report, had
severe intellectual disability, no evidence of epilepsy, hypotonia, and
normal brain imaging by MRI.
MOLECULAR GENETICS
In a patient with nonsyndromic intellectual disability, Hamdan et al.
(2011) identified a heterozygous missense mutation in the EPB41L1 gene
(P854S; 602879.0001). This mutation affects a highly conserved proline
in the C-terminal domain of the 4.1N protein, which binds AMPA receptor
subunits. Coimmunoprecipitation studies showed that the
proline-to-serine substitution at codon 854 reduces the binding of 4.1N
to GLUR1 (138248) by 50% in HEK293 cells. Moreover, insertion of GLUR1
at the synaptic membrane was significantly decreased in transfected
hippocampal neurons producing mutant 4.1N when compared to cells
producing wildtype 4.1N.
*FIELD* RF
1. Hamdan, F. F.; Gauthier, J.; Araki, Y.; Lin, D.-T.; Yoshizawa,
Y.; Higashi, K.; Park, A.-R.; Spiegelman, D.; Dobrzeniecka, S.; Piton,
A.; Tomitori, H.; Daoud, H.; and 22 others: Excess of de novo deleterious
mutations in genes associated with glutamatergic systems in nonsyndromic
intellectual disability. Am. J. Hum. Genet. 88: 306-316, 2011. Note;
Erratum: Am. J. Hum. Genet. 88: 516 only, 2011.
*FIELD* CD
Ada Hamosh: 9/28/2011
*FIELD* ED
terry: 07/06/2012
alopez: 10/3/2011