Full text data of EPB41L2
EPB41L2
[Confidence: high (present in two of the MS resources)]
Band 4.1-like protein 2 (Generally expressed protein 4.1; 4.1G)
Band 4.1-like protein 2 (Generally expressed protein 4.1; 4.1G)
UniProt
O43491
ID E41L2_HUMAN Reviewed; 1005 AA.
AC O43491; B4DHI8; E9PPD9; Q5T4F0; Q68DV2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Band 4.1-like protein 2;
DE AltName: Full=Generally expressed protein 4.1;
DE Short=4.1G;
GN Name=EPB41L2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Heart;
RX PubMed=9598318; DOI=10.1006/geno.1998.5265;
RA Parra M., Gascard P., Walensky L.D., Snyder S.H., Mohandas N.,
RA Conboy J.G.;
RT "Cloning and characterization of 4.1G (EPB41L2), a new member of the
RT skeletal protein 4.1 (EPB41) gene family.";
RL Genomics 49:298-306(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-13; 161-171; 508-514 AND 875-886, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma, and Pre-B cell;
RA Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W., Dozynkiewicz M.,
RA Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP INTERACTION WITH TRPC4.
RX PubMed=16254212; DOI=10.1161/01.RES.0000193597.65217.00;
RA Cioffi D.L., Wu S., Alexeyev M., Goodman S.R., Zhu M.X., Stevens T.;
RT "Activation of the endothelial store-operated ISOC Ca2+ channel
RT requires interaction of protein 4.1 with TRPC4.";
RL Circ. Res. 97:1164-1172(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND MASS
RP SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP INTERACTION WITH FCGR1A.
RX PubMed=18023480; DOI=10.1016/j.molimm.2007.10.024;
RA Beekman J.M., Bakema J.E., van der Poel C.E., van der Linden J.A.,
RA van de Winkel J.G.J., Leusen J.H.W.;
RT "Protein 4.1G binds to a unique motif within the FcgammaRI cytoplasmic
RT tail.";
RL Mol. Immunol. 45:2069-2075(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550 AND SER-614, AND
RP 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; THR-89; SER-499;
RP SER-550; SER-715 AND SER-718, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-87; THR-89 AND
RP SER-715, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=22361696; DOI=10.1016/j.jprot.2012.01.030;
RA Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R.,
RA Uhlen M., Lundberg E.;
RT "Systematic validation of antibody binding and protein subcellular
RT localization using siRNA and confocal microscopy.";
RL J. Proteomics 75:2236-2251(2012).
CC -!- SUBUNIT: Interacts with FCGR1A. Interacts with TRPC4. The CTD
CC domain interacts with FKBP2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43491-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43491-2; Sequence=VSP_042910;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O43491-3; Sequence=VSP_045090;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O43491-4; Sequence=VSP_047181, VSP_047182;
CC Note=No experimental confirmation available. Gene prediction
CC based on cDNA data;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Contains 1 FERM domain.
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DR EMBL; AF027299; AAC16923.1; -; mRNA.
DR EMBL; AY047584; AAK95850.1; -; mRNA.
DR EMBL; AK295124; BAG58150.1; -; mRNA.
DR EMBL; CR749262; CAH18118.1; -; mRNA.
DR EMBL; AL109938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358943; CAI20310.1; -; Genomic_DNA.
DR EMBL; AL355360; CAI20310.1; JOINED; Genomic_DNA.
DR EMBL; AL590014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48062.1; -; Genomic_DNA.
DR RefSeq; NP_001129026.1; NM_001135554.1.
DR RefSeq; NP_001129027.1; NM_001135555.3.
DR RefSeq; NP_001239589.1; NM_001252660.1.
DR RefSeq; NP_001422.1; NM_001431.3.
DR RefSeq; XP_005266904.1; XM_005266847.1.
DR RefSeq; XP_005266905.1; XM_005266848.1.
DR UniGene; Hs.486470; -.
DR UniGene; Hs.708219; -.
DR ProteinModelPortal; O43491; -.
DR SMR; O43491; 216-498.
DR DIP; DIP-17034N; -.
DR IntAct; O43491; 17.
DR MINT; MINT-5003841; -.
DR STRING; 9606.ENSP00000338481; -.
DR PhosphoSite; O43491; -.
DR PaxDb; O43491; -.
DR PRIDE; O43491; -.
DR Ensembl; ENST00000337057; ENSP00000338481; ENSG00000079819.
DR Ensembl; ENST00000368128; ENSP00000357110; ENSG00000079819.
DR Ensembl; ENST00000392427; ENSP00000376222; ENSG00000079819.
DR Ensembl; ENST00000445890; ENSP00000402041; ENSG00000079819.
DR Ensembl; ENST00000525271; ENSP00000432803; ENSG00000079819.
DR Ensembl; ENST00000528282; ENSP00000434308; ENSG00000079819.
DR Ensembl; ENST00000530481; ENSP00000434576; ENSG00000079819.
DR GeneID; 2037; -.
DR KEGG; hsa:2037; -.
DR UCSC; uc003qch.2; human.
DR CTD; 2037; -.
DR GeneCards; GC06M131202; -.
DR HGNC; HGNC:3379; EPB41L2.
DR HPA; HPA005730; -.
DR HPA; HPA006642; -.
DR MIM; 603237; gene.
DR neXtProt; NX_O43491; -.
DR PharmGKB; PA27812; -.
DR eggNOG; NOG242913; -.
DR HOGENOM; HOG000228841; -.
DR HOVERGEN; HBG007777; -.
DR InParanoid; O43491; -.
DR KO; K06107; -.
DR OMA; VGEYQPH; -.
DR OrthoDB; EOG7Z69BP; -.
DR PhylomeDB; O43491; -.
DR ChiTaRS; EPB41L2; human.
DR GeneWiki; EPB41L2; -.
DR GenomeRNAi; 2037; -.
DR NextBio; 8273; -.
DR PRO; PR:O43491; -.
DR ArrayExpress; O43491; -.
DR Bgee; O43491; -.
DR CleanEx; HS_EPB41L2; -.
DR Genevestigator; O43491; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008091; C:spectrin; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
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 Acetylation; Actin-binding; Alternative splicing; Cell membrane;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1005 Band 4.1-like protein 2.
FT /FTId=PRO_0000219397.
FT DOMAIN 218 499 FERM.
FT REGION 502 610 Hydrophilic.
FT REGION 611 676 Spectrin--actin-binding.
FT REGION 855 1005 C-terminal (CTD).
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 39 39 Phosphoserine.
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 89 89 Phosphothreonine.
FT MOD_RES 208 208 Phosphoserine (By similarity).
FT MOD_RES 386 386 Phosphoserine.
FT MOD_RES 499 499 Phosphoserine.
FT MOD_RES 550 550 Phosphoserine.
FT MOD_RES 598 598 Phosphoserine (By similarity).
FT MOD_RES 614 614 Phosphoserine.
FT MOD_RES 623 623 Phosphotyrosine (By similarity).
FT MOD_RES 715 715 Phosphoserine.
FT MOD_RES 718 718 Phosphoserine.
FT VAR_SEQ 612 943 Missing (in isoform 2).
FT /FTId=VSP_042910.
FT VAR_SEQ 612 869 Missing (in isoform 3).
FT /FTId=VSP_045090.
FT VAR_SEQ 612 681 Missing (in isoform 4).
FT /FTId=VSP_047181.
FT VAR_SEQ 787 869 Missing (in isoform 4).
FT /FTId=VSP_047182.
FT VARIANT 17 17 Q -> H (in dbSNP:rs2297852).
FT /FTId=VAR_020145.
SQ SEQUENCE 1005 AA; 112588 MW; E86CB17488F6045F CRC64;
MTTEVGSVSE VKKDSSQLGT DATKEKPKEV AENQQNQSSD PEEEKGSQPP PAAESQSSLR
RQKREKETSE SRGISRFIPP WLKKQKSYTL VVAKDGGDKK EPTQAVVEEQ VLDKEEPLPE
EQRQAKGDAE EMAQKKQEIK VEVKEEKPSV SKEEKPSVSK VEMQPTELVS KEREEKVKET
QEDKLEGGAA KRETKEVQTN ELKAEKASQK VTKKTKTVQC KVTLLDGTEY SCDLEKHAKG
QVLFDKVCEH LNLLEKDYFG LLFQESPEQK NWLDPAKEIK RQLRNLPWLF TFNVKFYPPD
PSQLTEDITR YFLCLQLRQD IASGRLPCSF VTHALLGSYT LQAELGDYDP EEHGSIDLSE
FQFAPTQTKE LEEKVAELHK THRGLSPAQA DSQFLENAKR LSMYGVDLHH AKDSEGVDIK
LGVCANGLLI YKDRLRINRF AWPKILKISY KRSNFYIKVR PAELEQFEST IGFKLPNHRA
AKRLWKVCVE HHTFYRLVSP EQPPKAKFLT LGSKFRYSGR TQAQTRQAST LIDRPAPHFE
RTSSKRVSRS LDGAPIGVMD QSLMKDFPGA AGEISAYGPG LVSIAVVQDG DGRREVRSPT
KAPHLQLIEG KKNSLRVEGD NIYVRHSNLM LEELDKAQED ILKHQASISE LKRNFMESTP
EPRPNEWEKR RITPLSLQTQ GSSHETLNIV EEKKRAEVGK DERVITEEMN GKEISPGSGP
GEIRKVEPVT QKDSTSLSSE SSSSSSESEE EDVGEYRPHH RVTEGTIREE QEYEEEVEEE
PRPAAKVVER EEAVPEASPV TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE
EAEEEPQKVN GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE
TKTITYESPQ IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS ETRIEKRIVI
TGDGDIDHDQ ALAQAIREAR EQHPDMSVTR VVVHKETELA EEGED
//
ID E41L2_HUMAN Reviewed; 1005 AA.
AC O43491; B4DHI8; E9PPD9; Q5T4F0; Q68DV2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Band 4.1-like protein 2;
DE AltName: Full=Generally expressed protein 4.1;
DE Short=4.1G;
GN Name=EPB41L2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Heart;
RX PubMed=9598318; DOI=10.1006/geno.1998.5265;
RA Parra M., Gascard P., Walensky L.D., Snyder S.H., Mohandas N.,
RA Conboy J.G.;
RT "Cloning and characterization of 4.1G (EPB41L2), a new member of the
RT skeletal protein 4.1 (EPB41) gene family.";
RL Genomics 49:298-306(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-13; 161-171; 508-514 AND 875-886, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma, and Pre-B cell;
RA Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W., Dozynkiewicz M.,
RA Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP INTERACTION WITH TRPC4.
RX PubMed=16254212; DOI=10.1161/01.RES.0000193597.65217.00;
RA Cioffi D.L., Wu S., Alexeyev M., Goodman S.R., Zhu M.X., Stevens T.;
RT "Activation of the endothelial store-operated ISOC Ca2+ channel
RT requires interaction of protein 4.1 with TRPC4.";
RL Circ. Res. 97:1164-1172(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND MASS
RP SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP INTERACTION WITH FCGR1A.
RX PubMed=18023480; DOI=10.1016/j.molimm.2007.10.024;
RA Beekman J.M., Bakema J.E., van der Poel C.E., van der Linden J.A.,
RA van de Winkel J.G.J., Leusen J.H.W.;
RT "Protein 4.1G binds to a unique motif within the FcgammaRI cytoplasmic
RT tail.";
RL Mol. Immunol. 45:2069-2075(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550 AND SER-614, AND
RP 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; THR-89; SER-499;
RP SER-550; SER-715 AND SER-718, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-87; THR-89 AND
RP SER-715, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=22361696; DOI=10.1016/j.jprot.2012.01.030;
RA Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R.,
RA Uhlen M., Lundberg E.;
RT "Systematic validation of antibody binding and protein subcellular
RT localization using siRNA and confocal microscopy.";
RL J. Proteomics 75:2236-2251(2012).
CC -!- SUBUNIT: Interacts with FCGR1A. Interacts with TRPC4. The CTD
CC domain interacts with FKBP2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43491-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43491-2; Sequence=VSP_042910;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O43491-3; Sequence=VSP_045090;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O43491-4; Sequence=VSP_047181, VSP_047182;
CC Note=No experimental confirmation available. Gene prediction
CC based on cDNA data;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Contains 1 FERM domain.
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DR EMBL; AF027299; AAC16923.1; -; mRNA.
DR EMBL; AY047584; AAK95850.1; -; mRNA.
DR EMBL; AK295124; BAG58150.1; -; mRNA.
DR EMBL; CR749262; CAH18118.1; -; mRNA.
DR EMBL; AL109938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358943; CAI20310.1; -; Genomic_DNA.
DR EMBL; AL355360; CAI20310.1; JOINED; Genomic_DNA.
DR EMBL; AL590014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48062.1; -; Genomic_DNA.
DR RefSeq; NP_001129026.1; NM_001135554.1.
DR RefSeq; NP_001129027.1; NM_001135555.3.
DR RefSeq; NP_001239589.1; NM_001252660.1.
DR RefSeq; NP_001422.1; NM_001431.3.
DR RefSeq; XP_005266904.1; XM_005266847.1.
DR RefSeq; XP_005266905.1; XM_005266848.1.
DR UniGene; Hs.486470; -.
DR UniGene; Hs.708219; -.
DR ProteinModelPortal; O43491; -.
DR SMR; O43491; 216-498.
DR DIP; DIP-17034N; -.
DR IntAct; O43491; 17.
DR MINT; MINT-5003841; -.
DR STRING; 9606.ENSP00000338481; -.
DR PhosphoSite; O43491; -.
DR PaxDb; O43491; -.
DR PRIDE; O43491; -.
DR Ensembl; ENST00000337057; ENSP00000338481; ENSG00000079819.
DR Ensembl; ENST00000368128; ENSP00000357110; ENSG00000079819.
DR Ensembl; ENST00000392427; ENSP00000376222; ENSG00000079819.
DR Ensembl; ENST00000445890; ENSP00000402041; ENSG00000079819.
DR Ensembl; ENST00000525271; ENSP00000432803; ENSG00000079819.
DR Ensembl; ENST00000528282; ENSP00000434308; ENSG00000079819.
DR Ensembl; ENST00000530481; ENSP00000434576; ENSG00000079819.
DR GeneID; 2037; -.
DR KEGG; hsa:2037; -.
DR UCSC; uc003qch.2; human.
DR CTD; 2037; -.
DR GeneCards; GC06M131202; -.
DR HGNC; HGNC:3379; EPB41L2.
DR HPA; HPA005730; -.
DR HPA; HPA006642; -.
DR MIM; 603237; gene.
DR neXtProt; NX_O43491; -.
DR PharmGKB; PA27812; -.
DR eggNOG; NOG242913; -.
DR HOGENOM; HOG000228841; -.
DR HOVERGEN; HBG007777; -.
DR InParanoid; O43491; -.
DR KO; K06107; -.
DR OMA; VGEYQPH; -.
DR OrthoDB; EOG7Z69BP; -.
DR PhylomeDB; O43491; -.
DR ChiTaRS; EPB41L2; human.
DR GeneWiki; EPB41L2; -.
DR GenomeRNAi; 2037; -.
DR NextBio; 8273; -.
DR PRO; PR:O43491; -.
DR ArrayExpress; O43491; -.
DR Bgee; O43491; -.
DR CleanEx; HS_EPB41L2; -.
DR Genevestigator; O43491; -.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008091; C:spectrin; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
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 Acetylation; Actin-binding; Alternative splicing; Cell membrane;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1005 Band 4.1-like protein 2.
FT /FTId=PRO_0000219397.
FT DOMAIN 218 499 FERM.
FT REGION 502 610 Hydrophilic.
FT REGION 611 676 Spectrin--actin-binding.
FT REGION 855 1005 C-terminal (CTD).
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 39 39 Phosphoserine.
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 89 89 Phosphothreonine.
FT MOD_RES 208 208 Phosphoserine (By similarity).
FT MOD_RES 386 386 Phosphoserine.
FT MOD_RES 499 499 Phosphoserine.
FT MOD_RES 550 550 Phosphoserine.
FT MOD_RES 598 598 Phosphoserine (By similarity).
FT MOD_RES 614 614 Phosphoserine.
FT MOD_RES 623 623 Phosphotyrosine (By similarity).
FT MOD_RES 715 715 Phosphoserine.
FT MOD_RES 718 718 Phosphoserine.
FT VAR_SEQ 612 943 Missing (in isoform 2).
FT /FTId=VSP_042910.
FT VAR_SEQ 612 869 Missing (in isoform 3).
FT /FTId=VSP_045090.
FT VAR_SEQ 612 681 Missing (in isoform 4).
FT /FTId=VSP_047181.
FT VAR_SEQ 787 869 Missing (in isoform 4).
FT /FTId=VSP_047182.
FT VARIANT 17 17 Q -> H (in dbSNP:rs2297852).
FT /FTId=VAR_020145.
SQ SEQUENCE 1005 AA; 112588 MW; E86CB17488F6045F CRC64;
MTTEVGSVSE VKKDSSQLGT DATKEKPKEV AENQQNQSSD PEEEKGSQPP PAAESQSSLR
RQKREKETSE SRGISRFIPP WLKKQKSYTL VVAKDGGDKK EPTQAVVEEQ VLDKEEPLPE
EQRQAKGDAE EMAQKKQEIK VEVKEEKPSV SKEEKPSVSK VEMQPTELVS KEREEKVKET
QEDKLEGGAA KRETKEVQTN ELKAEKASQK VTKKTKTVQC KVTLLDGTEY SCDLEKHAKG
QVLFDKVCEH LNLLEKDYFG LLFQESPEQK NWLDPAKEIK RQLRNLPWLF TFNVKFYPPD
PSQLTEDITR YFLCLQLRQD IASGRLPCSF VTHALLGSYT LQAELGDYDP EEHGSIDLSE
FQFAPTQTKE LEEKVAELHK THRGLSPAQA DSQFLENAKR LSMYGVDLHH AKDSEGVDIK
LGVCANGLLI YKDRLRINRF AWPKILKISY KRSNFYIKVR PAELEQFEST IGFKLPNHRA
AKRLWKVCVE HHTFYRLVSP EQPPKAKFLT LGSKFRYSGR TQAQTRQAST LIDRPAPHFE
RTSSKRVSRS LDGAPIGVMD QSLMKDFPGA AGEISAYGPG LVSIAVVQDG DGRREVRSPT
KAPHLQLIEG KKNSLRVEGD NIYVRHSNLM LEELDKAQED ILKHQASISE LKRNFMESTP
EPRPNEWEKR RITPLSLQTQ GSSHETLNIV EEKKRAEVGK DERVITEEMN GKEISPGSGP
GEIRKVEPVT QKDSTSLSSE SSSSSSESEE EDVGEYRPHH RVTEGTIREE QEYEEEVEEE
PRPAAKVVER EEAVPEASPV TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE
EAEEEPQKVN GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE
TKTITYESPQ IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS ETRIEKRIVI
TGDGDIDHDQ ALAQAIREAR EQHPDMSVTR VVVHKETELA EEGED
//
MIM
603237
*RECORD*
*FIELD* NO
603237
*FIELD* TI
*603237 ERYTHROCYTE MEMBRANE PROTEIN 4.1-LIKE 2; EPB41L2
;;NONERYTHROID PROTEIN 4.1, GENERAL TYPE; 4.1G
read more*FIELD* TX
DESCRIPTION
EPB41L2 is a member of the protein 4.1 family (see 607619). Members of
this family function as adaptors linking transmembrane proteins to the
cytoskeleton (summary by Yang et al., 2011).
CLONING
Erythrocyte membrane protein 4.1 (EPB41; 130500) is a well-characterized
cytoskeletal protein. Several nonerythroid protein 4.1 homologs have
been identified, including ezrin (123900), radixin (179410), and moesin
(309845). Parra et al. (1998) used EST database searches and PCR to
identify and clone a novel protein 4.1 homolog, termed 4.1G. The longest
assembled cDNA sequence encoded a 1,005-amino acid polypeptide. 4.1G has
a high level of similarity to EPB41 in its membrane-binding domain,
spectrin/actin-binding domain, and C terminus. Northern blot analysis
detected wide 4.1G gene expression among human tissues, with most
tissues exhibiting a prominent mRNA of approximately 5 kb. Expression of
4.1G in COS cells revealed diffuse cytoplasmic and more intense
perinuclear localization, a staining pattern significantly different
from that of EPB41.
By RT-PCR of mouse testis, Yang et al. (2011) identified 3 splice
variants of 4.1G that differed from one another due to alternative
splicing involving exons 16 through 18. None of the variants contained
exons 14 and 15, and all downstream exons were spliced in-frame. Western
blot analysis detected 4.1G expression in brain, lung, and testis, but
not in liver, prostate, small intestine, kidney, or skeletal muscle.
Multiple 4.1G bands were detected in lung and brain. Electron microscopy
and immunofluorescence analysis of mouse testis revealed 4.1G expression
along the membranes of seminiferous epithelium, where it colocalized
with Necl4 (IGSF4C; 609744).
MAPPING
Parra et al. (1998) used fluorescence in situ hybridization to map the
EPB41L2 gene to chromosome 6q22-q23.
GENE FUNCTION
Using coimmunoprecipitation analysis, Yang et al. (2011) found that 4.1G
and Necl4 interacted directly in mouse testis. Mutation analysis
revealed that full-length 4.1G bound to the cytoplasmic domain of Necl4.
ANIMAL MODEL
Yang et al. (2011) found that 4.1G knockout had no effect on embryonic
development, health, or fertility of C57BL/6 mice. However, 4.1G
knockout caused male sterility in C57BL/6 and 129/Sv hybrid mice. 4.1G
-/- hybrid mice showed reduced testis weight, with abnormal seminiferous
epithelia, absence of Sertoli/germ cell contacts, and immature or
degenerated spermatogenic cells. 4.1G -/- hybrid testis showed normal
Necl4 mRNA content, but reduced Necl4 protein and lack of Necl4
expression at Sertoli cell membranes. Yang et al. (2011) concluded that
4.1G is required for Necl4 protein stability and formation of
Sertoli/germ cell contacts.
*FIELD* RF
1. Parra, M.; Gascard, P.; Walensky, L. D.; Snyder, S. H.; Mohandas,
N.; Conboy, J. G.: Cloning and characterization of 4.1G (EPB41L2),
a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49:
298-306, 1998.
2. Yang, S.; Weng, H.; Chen, L.; Guo, X.; Parra, M.; Conboy, J.; Debnath,
G.; Lambert, A. J.; Peters, L. L.; Baines, A. J.; Mohandas, N.; An,
X.: Lack of protein 4.1G causes altered expression and localization
of the cell adhesion molecule nectin-like 4 in testis and can cause
male infertility. Molec. Cell. Biol. 31: 2276-2286, 2011.
*FIELD* CN
Patricia A. Hartz - updated: 2/21/2012
*FIELD* CD
Jennifer P. Macke: 10/29/1998
*FIELD* ED
mgross: 03/06/2012
terry: 2/21/2012
carol: 1/16/2008
mgross: 3/10/2003
alopez: 10/29/1998
*RECORD*
*FIELD* NO
603237
*FIELD* TI
*603237 ERYTHROCYTE MEMBRANE PROTEIN 4.1-LIKE 2; EPB41L2
;;NONERYTHROID PROTEIN 4.1, GENERAL TYPE; 4.1G
read more*FIELD* TX
DESCRIPTION
EPB41L2 is a member of the protein 4.1 family (see 607619). Members of
this family function as adaptors linking transmembrane proteins to the
cytoskeleton (summary by Yang et al., 2011).
CLONING
Erythrocyte membrane protein 4.1 (EPB41; 130500) is a well-characterized
cytoskeletal protein. Several nonerythroid protein 4.1 homologs have
been identified, including ezrin (123900), radixin (179410), and moesin
(309845). Parra et al. (1998) used EST database searches and PCR to
identify and clone a novel protein 4.1 homolog, termed 4.1G. The longest
assembled cDNA sequence encoded a 1,005-amino acid polypeptide. 4.1G has
a high level of similarity to EPB41 in its membrane-binding domain,
spectrin/actin-binding domain, and C terminus. Northern blot analysis
detected wide 4.1G gene expression among human tissues, with most
tissues exhibiting a prominent mRNA of approximately 5 kb. Expression of
4.1G in COS cells revealed diffuse cytoplasmic and more intense
perinuclear localization, a staining pattern significantly different
from that of EPB41.
By RT-PCR of mouse testis, Yang et al. (2011) identified 3 splice
variants of 4.1G that differed from one another due to alternative
splicing involving exons 16 through 18. None of the variants contained
exons 14 and 15, and all downstream exons were spliced in-frame. Western
blot analysis detected 4.1G expression in brain, lung, and testis, but
not in liver, prostate, small intestine, kidney, or skeletal muscle.
Multiple 4.1G bands were detected in lung and brain. Electron microscopy
and immunofluorescence analysis of mouse testis revealed 4.1G expression
along the membranes of seminiferous epithelium, where it colocalized
with Necl4 (IGSF4C; 609744).
MAPPING
Parra et al. (1998) used fluorescence in situ hybridization to map the
EPB41L2 gene to chromosome 6q22-q23.
GENE FUNCTION
Using coimmunoprecipitation analysis, Yang et al. (2011) found that 4.1G
and Necl4 interacted directly in mouse testis. Mutation analysis
revealed that full-length 4.1G bound to the cytoplasmic domain of Necl4.
ANIMAL MODEL
Yang et al. (2011) found that 4.1G knockout had no effect on embryonic
development, health, or fertility of C57BL/6 mice. However, 4.1G
knockout caused male sterility in C57BL/6 and 129/Sv hybrid mice. 4.1G
-/- hybrid mice showed reduced testis weight, with abnormal seminiferous
epithelia, absence of Sertoli/germ cell contacts, and immature or
degenerated spermatogenic cells. 4.1G -/- hybrid testis showed normal
Necl4 mRNA content, but reduced Necl4 protein and lack of Necl4
expression at Sertoli cell membranes. Yang et al. (2011) concluded that
4.1G is required for Necl4 protein stability and formation of
Sertoli/germ cell contacts.
*FIELD* RF
1. Parra, M.; Gascard, P.; Walensky, L. D.; Snyder, S. H.; Mohandas,
N.; Conboy, J. G.: Cloning and characterization of 4.1G (EPB41L2),
a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49:
298-306, 1998.
2. Yang, S.; Weng, H.; Chen, L.; Guo, X.; Parra, M.; Conboy, J.; Debnath,
G.; Lambert, A. J.; Peters, L. L.; Baines, A. J.; Mohandas, N.; An,
X.: Lack of protein 4.1G causes altered expression and localization
of the cell adhesion molecule nectin-like 4 in testis and can cause
male infertility. Molec. Cell. Biol. 31: 2276-2286, 2011.
*FIELD* CN
Patricia A. Hartz - updated: 2/21/2012
*FIELD* CD
Jennifer P. Macke: 10/29/1998
*FIELD* ED
mgross: 03/06/2012
terry: 2/21/2012
carol: 1/16/2008
mgross: 3/10/2003
alopez: 10/29/1998