E41L2_HUMAN
ID E41L2_HUMAN Reviewed; 1005 AA.
AC O43491; B4DHI8; E9PPD9; Q5T4F0; Q68DV2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Band 4.1-like protein 2;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 2 {ECO:0000312|HGNC:HGNC:3379};
DE AltName: Full=Generally expressed protein 4.1;
DE Short=4.1G;
GN Name=EPB41L2 {ECO:0000312|HGNC:HGNC:3379};
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 [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., 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., 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 [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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 IDENTIFICATION BY MASS
RP 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 requires
RT 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 IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT 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 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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; SER-550;
RP SER-715 AND SER-718, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT 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., Uhlen M.,
RA 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).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP FUNCTION, INTERACTION WITH NUMA1, AND SUBCELLULAR LOCATION.
RX PubMed=23870127; DOI=10.1016/j.cell.2013.06.010;
RA Kiyomitsu T., Cheeseman I.M.;
RT "Cortical dynein and asymmetric membrane elongation coordinately position
RT the spindle in anaphase.";
RL Cell 154:391-402(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-39; SER-58; SER-87;
RP SER-170; SER-386; SER-499; SER-550; SER-562; SER-598; SER-614; SER-647;
RP SER-715; SER-718 AND SER-828, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-550 AND SER-715, 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 [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-140 AND LYS-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at
CC the mitotic cell cortex during anaphase (PubMed:23870127).
CC {ECO:0000269|PubMed:23870127}.
CC -!- SUBUNIT: Interacts with FCGR1A (PubMed:18023480). Interacts with TRPC4
CC (PubMed:16254212). Interacts (via CTD domain) with FKBP2 (By
CC similarity). Interacts with NUMA1; this interaction is negatively
CC regulated by CDK1 during metaphase and promotes anaphase-specific
CC localization of NUMA1 in symmetrically dividing cells
CC (PubMed:23870127). {ECO:0000250|UniProtKB:O70318,
CC ECO:0000269|PubMed:16254212, ECO:0000269|PubMed:18023480,
CC ECO:0000269|PubMed:23870127}.
CC -!- INTERACTION:
CC O43491; P12314: FCGR1A; NbExp=3; IntAct=EBI-1052044, EBI-2869867;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:23870127}. Cell membrane
CC {ECO:0000269|PubMed:22361696}.
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 Name=3;
CC IsoId=O43491-3; Sequence=VSP_045090;
CC Name=4;
CC IsoId=O43491-4; Sequence=VSP_047181, VSP_047182;
CC -!- TISSUE SPECIFICITY: Widely expressed.
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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; AL355360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48062.1; -; Genomic_DNA.
DR CCDS; CCDS47474.1; -. [O43491-2]
DR CCDS; CCDS5141.1; -. [O43491-1]
DR CCDS; CCDS56450.1; -. [O43491-4]
DR CCDS; CCDS59037.1; -. [O43491-3]
DR RefSeq; NP_001129026.1; NM_001135554.1. [O43491-2]
DR RefSeq; NP_001129027.1; NM_001135555.3. [O43491-2]
DR RefSeq; NP_001239589.1; NM_001252660.1. [O43491-3]
DR RefSeq; NP_001422.1; NM_001431.3. [O43491-1]
DR RefSeq; XP_011533832.1; XM_011535530.1.
DR RefSeq; XP_011533836.1; XM_011535534.1.
DR RefSeq; XP_016865844.1; XM_017010355.1.
DR RefSeq; XP_016865848.1; XM_017010359.1.
DR RefSeq; XP_016865849.1; XM_017010360.1.
DR RefSeq; XP_016865850.1; XM_017010361.1.
DR RefSeq; XP_016865851.1; XM_017010362.1.
DR AlphaFoldDB; O43491; -.
DR SMR; O43491; -.
DR BioGRID; 108351; 160.
DR DIP; DIP-17034N; -.
DR IntAct; O43491; 78.
DR MINT; O43491; -.
DR STRING; 9606.ENSP00000338481; -.
DR GlyGen; O43491; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O43491; -.
DR MetOSite; O43491; -.
DR PhosphoSitePlus; O43491; -.
DR SwissPalm; O43491; -.
DR BioMuta; EPB41L2; -.
DR EPD; O43491; -.
DR jPOST; O43491; -.
DR MassIVE; O43491; -.
DR MaxQB; O43491; -.
DR PaxDb; O43491; -.
DR PeptideAtlas; O43491; -.
DR PRIDE; O43491; -.
DR ProteomicsDB; 22689; -.
DR ProteomicsDB; 48974; -. [O43491-1]
DR ProteomicsDB; 48975; -. [O43491-2]
DR ProteomicsDB; 66104; -.
DR TopDownProteomics; O43491-3; -. [O43491-3]
DR Antibodypedia; 1358; 246 antibodies from 34 providers.
DR DNASU; 2037; -.
DR Ensembl; ENST00000337057.8; ENSP00000338481.3; ENSG00000079819.19. [O43491-1]
DR Ensembl; ENST00000368128.6; ENSP00000357110.2; ENSG00000079819.19. [O43491-1]
DR Ensembl; ENST00000392427.7; ENSP00000376222.3; ENSG00000079819.19. [O43491-2]
DR Ensembl; ENST00000445890.6; ENSP00000402041.2; ENSG00000079819.19. [O43491-3]
DR Ensembl; ENST00000525271.5; ENSP00000432803.1; ENSG00000079819.19. [O43491-2]
DR Ensembl; ENST00000528282.5; ENSP00000434308.1; ENSG00000079819.19. [O43491-3]
DR Ensembl; ENST00000530481.5; ENSP00000434576.1; ENSG00000079819.19. [O43491-4]
DR GeneID; 2037; -.
DR KEGG; hsa:2037; -.
DR MANE-Select; ENST00000337057.8; ENSP00000338481.3; NM_001431.4; NP_001422.1.
DR UCSC; uc003qcg.2; human. [O43491-1]
DR CTD; 2037; -.
DR DisGeNET; 2037; -.
DR GeneCards; EPB41L2; -.
DR HGNC; HGNC:3379; EPB41L2.
DR HPA; ENSG00000079819; Tissue enhanced (retina).
DR MIM; 603237; gene.
DR neXtProt; NX_O43491; -.
DR OpenTargets; ENSG00000079819; -.
DR PharmGKB; PA27812; -.
DR VEuPathDB; HostDB:ENSG00000079819; -.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000155617; -.
DR HOGENOM; CLU_003623_0_1_1; -.
DR InParanoid; O43491; -.
DR OMA; DSVCEHL; -.
DR OrthoDB; 262540at2759; -.
DR PhylomeDB; O43491; -.
DR TreeFam; TF351626; -.
DR PathwayCommons; O43491; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; O43491; -.
DR BioGRID-ORCS; 2037; 13 hits in 1086 CRISPR screens.
DR ChiTaRS; EPB41L2; human.
DR GeneWiki; EPB41L2; -.
DR GenomeRNAi; 2037; -.
DR Pharos; O43491; Tbio.
DR PRO; PR:O43491; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O43491; protein.
DR Bgee; ENSG00000079819; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; O43491; baseline and differential.
DR Genevisible; O43491; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008091; C:spectrin; TAS:ProtInc.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042731; F:PH domain binding; IEA:Ensembl.
DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
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; IPR030546; E41L2.
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 PANTHER; PTHR23280:SF17; PTHR23280:SF17; 1.
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; Cell cycle;
KW Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Membrane; Mitosis;
KW Phosphoprotein; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..1005
FT /note="Band 4.1-like protein 2"
FT /id="PRO_0000219397"
FT DOMAIN 218..499
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..610
FT /note="Hydrophilic"
FT REGION 611..676
FT /note="Spectrin--actin-binding"
FT REGION 652..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..1005
FT /note="C-terminal (CTD)"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70318"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70318"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70318"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 623
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O70318"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70318"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 763
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70318"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 612..943
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042910"
FT VAR_SEQ 612..869
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045090"
FT VAR_SEQ 612..681
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047181"
FT VAR_SEQ 787..869
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047182"
FT VARIANT 17
FT /note="Q -> H (in dbSNP:rs2297852)"
FT /id="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
