ERBIN_HUMAN
ID ERBIN_HUMAN Reviewed; 1412 AA.
AC Q96RT1; A0AVR1; B4E3F1; B7ZLV9; E7EQW9; E9PCR8; Q1RMD0; Q86W38; Q9NR18;
AC Q9NW48; Q9ULJ5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Erbin {ECO:0000303|PubMed:10878805};
DE AltName: Full=Densin-180-like protein;
DE AltName: Full=Erbb2-interacting protein {ECO:0000303|PubMed:10878805};
DE AltName: Full=Protein LAP2;
GN Name=ERBIN {ECO:0000303|PubMed:10878805};
GN Synonyms=ERBB2IP {ECO:0000303|PubMed:10878805},
GN KIAA1225 {ECO:0000312|EMBL:BAA86539.2}, LAP2;
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 2), INTERACTION WITH ERBB2, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=B-cell;
RX PubMed=10878805; DOI=10.1038/35017038;
RA Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V., Jaulin-Bastard F.,
RA Saito H., Fournier E., Adelaide J., Margolis B., Birnbaum D.;
RT "ERBIN: a basolateral PDZ protein that interacts with the mammalian
RT ERBB2/HER2 receptor.";
RL Nat. Cell Biol. 2:407-414(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), INTERACTION
RP WITH BPAG1; DST AND ITGB4, SUBCELLULAR LOCATION, AND VARIANT GLU-1207.
RX PubMed=11375975; DOI=10.1074/jbc.m011005200;
RA Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H.,
RA Sonnenberg A., Borradori L.;
RT "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin
RT beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative
RT splice variants of ERBIN and analysis of their tissue expression.";
RL J. Biol. Chem. 276:32427-32436(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 601-1206 (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 8 AND 9), AND VARIANTS
RP LEU-274 AND VAL-313.
RC TISSUE=Cerebellum, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH DELTA CATENIN AND ARVCF.
RX PubMed=11821434; DOI=10.1074/jbc.m200818200;
RA Laura R.P., Witt A.S., Held H.A., Gerstner R., Deshayes K., Koehler M.F.T.,
RA Kosik K.S., Sidhu S.S., Lasky L.A.;
RT "The Erbin PDZ domain binds with high affinity and specificity to the
RT carboxyl termini of delta-catenin and ARVCF.";
RL J. Biol. Chem. 277:12906-12914(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-920, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP FUNCTION, INTERACTION WITH NOD2, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=16203728; DOI=10.1074/jbc.m508538200;
RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S., Lecine P.,
RA Borg J.P., Nunez G.;
RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT signaling.";
RL J. Biol. Chem. 280:40301-40309(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-972, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-857; THR-917 AND
RP SER-1286, AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; THR-917; SER-931 AND
RP SER-1158, AND IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-602 AND SER-603, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485; SER-620; SER-872;
RP SER-1158 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485 AND SER-852, 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1321-1412 IN COMPLEX WITH ERBB2
RP C-TERMINUS.
RX PubMed=12444095; DOI=10.1074/jbc.c200571200;
RA Birrane G., Chung J., Ladias J.A.;
RT "Novel mode of ligand recognition by the Erbin PDZ domain.";
RL J. Biol. Chem. 278:1399-1402(2003).
RN [22]
RP STRUCTURE BY NMR OF 1314-1412 IN COMPLEX WITH PHAGE-DERIVED PEPTIDE.
RX PubMed=12446668; DOI=10.1074/jbc.m209751200;
RA Skelton N.J., Koehler M.F.T., Zobel K., Wong W.L., Yeh S., Pisabarro M.T.,
RA Yin J.P., Lasky L.A., Sidhu S.S.;
RT "Origins of PDZ domain ligand specificity. Structure determination and
RT mutagenesis of the Erbin PDZ domain.";
RL J. Biol. Chem. 278:7645-7654(2003).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1314-1412.
RX PubMed=16737969; DOI=10.1074/jbc.m602901200;
RA Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J.,
RA Sidhu S.S., Wiesmann C.;
RT "Comparative structural analysis of the erbin PDZ domain and the first PDZ
RT domain of ZO-1. Insights into determinants of PDZ domain specificity.";
RL J. Biol. Chem. 281:22312-22320(2006).
CC -!- FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia. By
CC binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may
CC contribute to stabilize this unphosphorylated state (PubMed:16203728).
CC Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory
CC cytokine secretion (PubMed:16203728). {ECO:0000269|PubMed:10878805,
CC ECO:0000269|PubMed:16203728}.
CC -!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4 (PubMed:10878805,
CC PubMed:11375975, PubMed:12444095). May favor the localization of ERBB2,
CC by restricting its presence to the basolateral membrane of epithelial
CC cells. Also found to interact with ARVCF and delta catenin
CC (PubMed:11821434). Interacts (via C-terminus) with DST Isoform 3 (via
CC N-terminus) (PubMed:11375975). Interacts with NOD2 (via CARD domain)
CC (PubMed:16203728). {ECO:0000269|PubMed:10878805,
CC ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:11821434,
CC ECO:0000269|PubMed:12444095, ECO:0000269|PubMed:12446668,
CC ECO:0000269|PubMed:16203728}.
CC -!- INTERACTION:
CC Q96RT1; Q9HC29: NOD2; NbExp=5; IntAct=EBI-993903, EBI-7445625;
CC Q96RT1; Q99569: PKP4; NbExp=4; IntAct=EBI-993903, EBI-726447;
CC Q96RT1-2; Q9HC29: NOD2; NbExp=5; IntAct=EBI-8449250, EBI-7445625;
CC Q96RT1-2; Q99569: PKP4; NbExp=4; IntAct=EBI-8449250, EBI-726447;
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}. Nucleus
CC membrane {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are
CC cell-substrate adhesion complexes in stratified epithelia. In
CC transfected cells, either diffusely distributed over the cytoplasm or
CC concentrated at the basolateral membrane. Colocalizes with the
CC adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of
CC cardiac myocytes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q96RT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RT1-2; Sequence=VSP_010802;
CC Name=3;
CC IsoId=Q96RT1-3; Sequence=VSP_010802, VSP_010804;
CC Name=4;
CC IsoId=Q96RT1-4; Sequence=VSP_010802, VSP_010807;
CC Name=5;
CC IsoId=Q96RT1-5; Sequence=VSP_010802, VSP_010803;
CC Name=6;
CC IsoId=Q96RT1-6; Sequence=VSP_010802, VSP_010806;
CC Name=7;
CC IsoId=Q96RT1-7; Sequence=VSP_010802, VSP_010803, VSP_010804,
CC VSP_010805;
CC Name=8;
CC IsoId=Q96RT1-8; Sequence=VSP_044536;
CC Name=9;
CC IsoId=Q96RT1-9; Sequence=VSP_047389, VSP_010802;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, muscle
CC and stomach, followed by liver, spleen and intestine.
CC {ECO:0000269|PubMed:10878805}.
CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50692.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91538.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF263744; AAF77048.1; -; mRNA.
DR EMBL; AF276423; AAK69431.1; -; mRNA.
DR EMBL; AB033051; BAA86539.2; -; mRNA.
DR EMBL; AK001180; BAA91538.1; ALT_INIT; mRNA.
DR EMBL; AK304693; BAG65463.1; -; mRNA.
DR EMBL; AC010359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050692; AAH50692.1; ALT_SEQ; mRNA.
DR EMBL; BC115012; AAI15013.1; -; mRNA.
DR EMBL; BC126464; AAI26465.1; -; mRNA.
DR EMBL; BC144075; AAI44076.1; -; mRNA.
DR CCDS; CCDS34172.1; -. [Q96RT1-7]
DR CCDS; CCDS3990.1; -. [Q96RT1-2]
DR CCDS; CCDS58951.1; -. [Q96RT1-9]
DR CCDS; CCDS58952.1; -. [Q96RT1-8]
DR CCDS; CCDS58953.1; -. [Q96RT1-1]
DR CCDS; CCDS58954.1; -. [Q96RT1-4]
DR RefSeq; NP_001006600.1; NM_001006600.2. [Q96RT1-7]
DR RefSeq; NP_001240626.1; NM_001253697.1. [Q96RT1-1]
DR RefSeq; NP_001240627.1; NM_001253698.1. [Q96RT1-4]
DR RefSeq; NP_001240628.1; NM_001253699.1. [Q96RT1-8]
DR RefSeq; NP_001240630.1; NM_001253701.1. [Q96RT1-9]
DR RefSeq; NP_061165.1; NM_018695.3. [Q96RT1-2]
DR PDB; 1MFG; X-ray; 1.25 A; A=1321-1412.
DR PDB; 1MFL; X-ray; 1.88 A; A=1321-1412.
DR PDB; 1N7T; NMR; -; A=1314-1412.
DR PDB; 2H3L; X-ray; 1.00 A; A/B=1314-1412.
DR PDB; 2QBW; X-ray; 1.80 A; A=1330-1410.
DR PDB; 3CH8; X-ray; 1.90 A; A=1330-1410.
DR PDB; 6Q0M; X-ray; 1.20 A; A/B=1321-1410.
DR PDB; 6Q0N; X-ray; 1.18 A; A/B=1321-1410.
DR PDB; 6Q0U; X-ray; 1.89 A; A/B=1321-1410.
DR PDB; 6UBH; X-ray; 1.80 A; A/B/C/D=1321-1412.
DR PDB; 7LUL; X-ray; 1.65 A; A=1321-1412.
DR PDBsum; 1MFG; -.
DR PDBsum; 1MFL; -.
DR PDBsum; 1N7T; -.
DR PDBsum; 2H3L; -.
DR PDBsum; 2QBW; -.
DR PDBsum; 3CH8; -.
DR PDBsum; 6Q0M; -.
DR PDBsum; 6Q0N; -.
DR PDBsum; 6Q0U; -.
DR PDBsum; 6UBH; -.
DR PDBsum; 7LUL; -.
DR AlphaFoldDB; Q96RT1; -.
DR BMRB; Q96RT1; -.
DR SMR; Q96RT1; -.
DR BioGRID; 120997; 218.
DR ELM; Q96RT1; -.
DR IntAct; Q96RT1; 152.
DR MINT; Q96RT1; -.
DR STRING; 9606.ENSP00000426632; -.
DR iPTMnet; Q96RT1; -.
DR MetOSite; Q96RT1; -.
DR PhosphoSitePlus; Q96RT1; -.
DR SwissPalm; Q96RT1; -.
DR BioMuta; ERBIN; -.
DR DMDM; 116242614; -.
DR EPD; Q96RT1; -.
DR jPOST; Q96RT1; -.
DR MassIVE; Q96RT1; -.
DR MaxQB; Q96RT1; -.
DR PaxDb; Q96RT1; -.
DR PeptideAtlas; Q96RT1; -.
DR PRIDE; Q96RT1; -.
DR ProteomicsDB; 17666; -.
DR ProteomicsDB; 19501; -.
DR ProteomicsDB; 78021; -. [Q96RT1-1]
DR ProteomicsDB; 78022; -. [Q96RT1-2]
DR ProteomicsDB; 78023; -. [Q96RT1-3]
DR ProteomicsDB; 78024; -. [Q96RT1-4]
DR ProteomicsDB; 78025; -. [Q96RT1-5]
DR ProteomicsDB; 78026; -. [Q96RT1-6]
DR ProteomicsDB; 78027; -. [Q96RT1-7]
DR Antibodypedia; 23812; 201 antibodies from 32 providers.
DR DNASU; 55914; -.
DR Ensembl; ENST00000284037.10; ENSP00000284037.4; ENSG00000112851.15. [Q96RT1-1]
DR Ensembl; ENST00000380935.5; ENSP00000370322.1; ENSG00000112851.15. [Q96RT1-7]
DR Ensembl; ENST00000380938.6; ENSP00000370325.2; ENSG00000112851.15. [Q96RT1-4]
DR Ensembl; ENST00000380943.6; ENSP00000370330.2; ENSG00000112851.15. [Q96RT1-2]
DR Ensembl; ENST00000506030.5; ENSP00000426632.1; ENSG00000112851.15. [Q96RT1-8]
DR Ensembl; ENST00000508515.1; ENSP00000422015.1; ENSG00000112851.15. [Q96RT1-7]
DR Ensembl; ENST00000511297.5; ENSP00000422766.1; ENSG00000112851.15. [Q96RT1-9]
DR GeneID; 55914; -.
DR KEGG; hsa:55914; -.
DR MANE-Select; ENST00000284037.10; ENSP00000284037.4; NM_001253697.2; NP_001240626.1.
DR UCSC; uc003jui.3; human. [Q96RT1-1]
DR CTD; 55914; -.
DR DisGeNET; 55914; -.
DR GeneCards; ERBIN; -.
DR HGNC; HGNC:15842; ERBIN.
DR HPA; ENSG00000112851; Tissue enhanced (brain).
DR MIM; 606944; gene.
DR neXtProt; NX_Q96RT1; -.
DR OpenTargets; ENSG00000112851; -.
DR PharmGKB; PA27845; -.
DR VEuPathDB; HostDB:ENSG00000112851; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159526; -.
DR HOGENOM; CLU_004220_1_0_1; -.
DR InParanoid; Q96RT1; -.
DR OMA; QLPETIX; -.
DR PhylomeDB; Q96RT1; -.
DR TreeFam; TF351429; -.
DR PathwayCommons; Q96RT1; -.
DR Reactome; R-HSA-1227986; Signaling by ERBB2.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2.
DR Reactome; R-HSA-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665233; Resistance of ERBB2 KD mutants to trastuzumab.
DR Reactome; R-HSA-9665244; Resistance of ERBB2 KD mutants to sapitinib.
DR Reactome; R-HSA-9665245; Resistance of ERBB2 KD mutants to tesevatinib.
DR Reactome; R-HSA-9665246; Resistance of ERBB2 KD mutants to neratinib.
DR Reactome; R-HSA-9665247; Resistance of ERBB2 KD mutants to osimertinib.
DR Reactome; R-HSA-9665249; Resistance of ERBB2 KD mutants to afatinib.
DR Reactome; R-HSA-9665250; Resistance of ERBB2 KD mutants to AEE788.
DR Reactome; R-HSA-9665251; Resistance of ERBB2 KD mutants to lapatinib.
DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR Reactome; R-HSA-9665737; Drug resistance in ERBB2 TMD/JMD mutants.
DR SignaLink; Q96RT1; -.
DR SIGNOR; Q96RT1; -.
DR BioGRID-ORCS; 55914; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; ERBIN; human.
DR EvolutionaryTrace; Q96RT1; -.
DR GeneWiki; Erbin_(protein); -.
DR GenomeRNAi; 55914; -.
DR Pharos; Q96RT1; Tbio.
DR PRO; PR:Q96RT1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96RT1; protein.
DR Bgee; ENSG00000112851; Expressed in corpus callosum and 208 other tissues.
DR ExpressionAtlas; Q96RT1; baseline and differential.
DR Genevisible; Q96RT1; HS.
DR GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
DR GO; GO:0005604; C:basement membrane; TAS:ProtInc.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0005176; F:ErbB-2 class receptor binding; TAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0045175; P:basal protein localization; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0032495; P:response to muramyl dipeptide; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR IDEAL; IID00494; -.
DR InterPro; IPR032927; Erbin.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR23119:SF46; PTHR23119:SF46; 2.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51450; LRR; 15.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Leucine-rich repeat; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1412
FT /note="Erbin"
FT /id="PRO_0000188301"
FT REPEAT 23..44
FT /note="LRR 1"
FT REPEAT 47..68
FT /note="LRR 2"
FT REPEAT 70..91
FT /note="LRR 3"
FT REPEAT 93..114
FT /note="LRR 4"
FT REPEAT 116..137
FT /note="LRR 5"
FT REPEAT 139..161
FT /note="LRR 6"
FT REPEAT 162..183
FT /note="LRR 7"
FT REPEAT 185..206
FT /note="LRR 8"
FT REPEAT 208..229
FT /note="LRR 9"
FT REPEAT 231..252
FT /note="LRR 10"
FT REPEAT 254..275
FT /note="LRR 11"
FT REPEAT 277..298
FT /note="LRR 12"
FT REPEAT 300..321
FT /note="LRR 13"
FT REPEAT 323..344
FT /note="LRR 14"
FT REPEAT 346..367
FT /note="LRR 15"
FT REPEAT 369..391
FT /note="LRR 16"
FT REPEAT 392..413
FT /note="LRR 17"
FT DOMAIN 1321..1410
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 464..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TH2"
FT MOD_RES 483
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80TH2"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TH2"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TH2"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 917
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 920
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 972
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 1104
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80TH2"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 531..534
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047389"
FT VAR_SEQ 1212..1252
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6, isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:10878805, ECO:0000303|PubMed:11375975,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_010802"
FT VAR_SEQ 1212..1252
FT /note="KHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMK -> SMLSRSF
FT NSNFTTVSSFHCGSSRDLHGSQGSLALSVADRRGSGGHIFR (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044536"
FT VAR_SEQ 1253..1267
FT /note="Missing (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11375975"
FT /id="VSP_010803"
FT VAR_SEQ 1268..1278
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11375975"
FT /id="VSP_010804"
FT VAR_SEQ 1279..1321
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11375975"
FT /id="VSP_010805"
FT VAR_SEQ 1322..1352
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11375975"
FT /id="VSP_010806"
FT VAR_SEQ 1353..1377
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11375975,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_010807"
FT VARIANT 274
FT /note="S -> L (in dbSNP:rs3213837)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019346"
FT VARIANT 313
FT /note="A -> V (in dbSNP:rs191137999)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_068905"
FT VARIANT 746
FT /note="K -> E (in dbSNP:rs16894812)"
FT /id="VAR_028304"
FT VARIANT 914
FT /note="K -> R (in dbSNP:rs34521887)"
FT /id="VAR_046673"
FT VARIANT 1089
FT /note="G -> V (in dbSNP:rs35601230)"
FT /id="VAR_046674"
FT VARIANT 1112
FT /note="S -> L (in dbSNP:rs3805466)"
FT /id="VAR_019347"
FT VARIANT 1207
FT /note="K -> E"
FT /evidence="ECO:0000269|PubMed:11375975"
FT /id="VAR_019348"
FT CONFLICT 271
FT /note="T -> P (in Ref. 7; AAI15013)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="D -> G (in Ref. 7; AAI15013)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="E -> G (in Ref. 5; BAA91538)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="Y -> C (in Ref. 2; AAK69431)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="G -> C (in Ref. 5; BAG65463)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="R -> S (in Ref. 5; BAG65463)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205
FT /note="E -> G (in Ref. 7; AAI15013)"
FT /evidence="ECO:0000305"
FT CONFLICT 1267
FT /note="Q -> P (in Ref. 7; AAI15013)"
FT /evidence="ECO:0000305"
FT CONFLICT 1328
FT /note="K -> R (in Ref. 7; AAI15013)"
FT /evidence="ECO:0000305"
FT STRAND 1318..1327
FT /evidence="ECO:0007829|PDB:2H3L"
FT STRAND 1329..1331
FT /evidence="ECO:0007829|PDB:2H3L"
FT STRAND 1333..1338
FT /evidence="ECO:0007829|PDB:2H3L"
FT TURN 1339..1342
FT /evidence="ECO:0007829|PDB:2H3L"
FT STRAND 1346..1348
FT /evidence="ECO:0007829|PDB:2H3L"
FT STRAND 1353..1359
FT /evidence="ECO:0007829|PDB:2H3L"
FT TURN 1364..1368
FT /evidence="ECO:0007829|PDB:2H3L"
FT STRAND 1374..1378
FT /evidence="ECO:0007829|PDB:2H3L"
FT HELIX 1388..1397
FT /evidence="ECO:0007829|PDB:2H3L"
FT STRAND 1400..1410
FT /evidence="ECO:0007829|PDB:2H3L"
SQ SEQUENCE 1412 AA; 158298 MW; 304DFC81578CF671 CRC64;
MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE
LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV
EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM
NRLTQLERLD LGSNEFTEVP EVLEQLSGLK EFWMDANRLT FIPGFIGSLK QLTYLDVSKN
NIEMVEEGIS TCENLQDLLL SSNSLQQLPE TIGSLKNITT LKIDENQLMY LPDSIGGLIS
VEELDCSFNE VEALPSSIGQ LTNLRTFAAD HNYLQQLPPE IGSWKNITVL FLHSNKLETL
PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDSETQKM
VLTNYMFPQQ PRTEDVMFIS DNESFNPSLW EEQRKQRAQV AFECDEDKDE REAPPREGNL
KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEDSGRDLKP HEDQQDINKD VGVKTSESTT
TVKSKVDERE KYMIGNSVQK ISEPEAEISP GSLPVTANMK ASENLKHIVN HDDVFEESEE
LSSDEEMKMA EMRPPLIETS INQPKVVALS NNKKDDTKET DSLSDEVTHN SNQNNSNCSS
PSRMSDSVSL NTDSSQDTSL CSPVKQTHID INSKIRQEDE NFNSLLQNGD ILNSSTEEKF
KAHDKKDFNL PEYDLNVEER LVLIEKSVDS TATADDTHKL DHINMNLNKL ITNDTFQPEI
MERSKTQDIV LGTSFLSINS KEETEHLENG NKYPNLESVN KVNGHSEETS QSPNRTEPHD
SDCSVDLGIS KSTEDLSPQK SGPVGSVVKS HSITNMEIGG LKIYDILSDN GPQQPSTTVK
ITSAVDGKNI VRSKSATLLY DQPLQVFTGS SSSSDLISGT KAIFKFDSNH NPEEPNIIRG
PTSGPQSAPQ IYGPPQYNIQ YSSSAAVKDT LWHSKQNPQI DHASFPPQLL PRSESTENQS
YAKHSANMNF SNHNNVRANT AYHLHQRLGP ARHGEMWAIS PNDRLIPAVT RSTIQRQSSV
SSTASVNLGD PGSTRRAQIP EGDYLSYREF HSAGRTPPMM PGSQRPLSAR TYSIDGPNAS
RPQSARPSIN EIPERTMSVS DFNYSRTSPS KRPNARVGSE HSLLDPPGKS KVPRDWREQV
LRHIEAKKLE KKHPQTSSSG DPCQDGIFIS GQQNYSSATL SHKDVPPDSL MKMPLSNGQM
GQPLRPQANY SQIHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTQPHCS PRQGHELAKQ
EIRVRVEKDP ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG
YSFINIEHGQ AVSLLKTFQN TVELIIVREV SS
