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Erbin (Densin-180-like protein) (Erbb2-interacting protein) (Protein LAP2)

 ERBIN_HUMAN             Reviewed;        1412 AA.
Q96RT1; A0AVR1; B4E3F1; B7ZLV9; E7EQW9; E9PCR8; Q1RMD0; Q86W38;
Q9NR18; Q9NW48; Q9ULJ5;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
31-JUL-2019, entry version 185.
RecName: Full=Erbin {ECO:0000303|PubMed:10878805};
AltName: Full=Densin-180-like protein;
AltName: Full=Erbb2-interacting protein {ECO:0000303|PubMed:10878805};
AltName: Full=Protein LAP2;
Name=ERBIN {ECO:0000303|PubMed:10878805};
Synonyms=ERBB2IP {ECO:0000303|PubMed:10878805},
KIAA1225 {ECO:0000312|EMBL:BAA86539.2}, LAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB2, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=B-cell;
PubMed=10878805; DOI=10.1038/35017038;
Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V.,
Jaulin-Bastard F., Saito H., Fournier E., Adelaide J., Margolis B.,
Birnbaum D.;
"ERBIN: a basolateral PDZ protein that interacts with the mammalian
ERBB2/HER2 receptor.";
Nat. Cell Biol. 2:407-414(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7),
INTERACTION WITH BPAG1; DST AND ITGB4, SUBCELLULAR LOCATION, AND
VARIANT GLU-1207.
PubMed=11375975; DOI=10.1074/jbc.M011005200;
Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F.,
Saurat J.-H., Sonnenberg A., Borradori L.;
"The hemidesmosomal protein bullous pemphigoid antigen 1 and the
integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple
alternative splice variants of ERBIN and analysis of their tissue
expression.";
J. Biol. Chem. 276:32427-32436(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 601-1206 (ISOFORM 1).
TISSUE=Teratocarcinoma, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 8 AND 9), AND
VARIANTS LEU-274 AND VAL-313.
TISSUE=Cerebellum, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH DELTA CATENIN AND ARVCF.
PubMed=11821434; DOI=10.1074/jbc.M200818200;
Laura R.P., Witt A.S., Held H.A., Gerstner R., Deshayes K.,
Koehler M.F.T., Kosik K.S., Sidhu S.S., Lasky L.A.;
"The Erbin PDZ domain binds with high affinity and specificity to the
carboxyl termini of delta-catenin and ARVCF.";
J. Biol. Chem. 277:12906-12914(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-920, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
FUNCTION, INTERACTION WITH NOD2, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16203728; DOI=10.1074/jbc.M508538200;
McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S.,
Lecine P., Borg J.P., Nunez G.;
"A role for Erbin in the regulation of Nod2-dependent NF-kappaB
signaling.";
J. Biol. Chem. 280:40301-40309(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-972, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-857; THR-917
AND SER-1286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; THR-917; SER-931
AND SER-1158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-602 AND
SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485; SER-620; SER-872;
SER-1158 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485 AND SER-852, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1321-1412 IN COMPLEX WITH
ERBB2 C-TERMINUS.
PubMed=12444095; DOI=10.1074/jbc.C200571200;
Birrane G., Chung J., Ladias J.A.;
"Novel mode of ligand recognition by the Erbin PDZ domain.";
J. Biol. Chem. 278:1399-1402(2003).
[22]
STRUCTURE BY NMR OF 1314-1412 IN COMPLEX WITH PHAGE-DERIVED PEPTIDE.
PubMed=12446668; DOI=10.1074/jbc.M209751200;
Skelton N.J., Koehler M.F.T., Zobel K., Wong W.L., Yeh S.,
Pisabarro M.T., Yin J.P., Lasky L.A., Sidhu S.S.;
"Origins of PDZ domain ligand specificity. Structure determination and
mutagenesis of the Erbin PDZ domain.";
J. Biol. Chem. 278:7645-7654(2003).
[23]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1314-1412.
PubMed=16737969; DOI=10.1074/jbc.M602901200;
Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J.,
Sidhu S.S., Wiesmann C.;
"Comparative structural analysis of the erbin PDZ domain and the first
PDZ domain of ZO-1. Insights into determinants of PDZ domain
specificity.";
J. Biol. Chem. 281:22312-22320(2006).
-!- FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia.
By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it
may contribute to stabilize this unphosphorylated state
(PubMed:16203728). Inhibits NOD2-dependent NF-kappa-B signaling
and proinflammatory cytokine secretion (PubMed:16203728).
{ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:16203728}.
-!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4 (PubMed:10878805,
PubMed:11375975, PubMed:12444095). May favor the localization of
ERBB2, by restricting its presence to the basolateral membrane of
epithelial cells. Also found to interact with ARVCF and delta
catenin (PubMed:11821434). Interacts (via C-terminus) with DST
Isoform 3 (via N-terminus) (PubMed:11375975). Interacts with NOD2
(via CARD domain) (PubMed:16203728). {ECO:0000269|PubMed:10878805,
ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:11821434,
ECO:0000269|PubMed:12444095, ECO:0000269|PubMed:12446668,
ECO:0000269|PubMed:16203728}.
-!- INTERACTION:
Q9HC29:NOD2; NbExp=5; IntAct=EBI-8449250, EBI-7445625;
Q99569:PKP4; NbExp=4; IntAct=EBI-993903, EBI-726447;
-!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
{ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}.
Nucleus membrane {ECO:0000250}. Basolateral cell membrane
{ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which
are cell-substrate adhesion complexes in stratified epithelia. In
transfected cells, either diffusely distributed over the cytoplasm
or concentrated at the basolateral membrane. Colocalizes with the
adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane
of cardiac myocytes (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1;
IsoId=Q96RT1-1; Sequence=Displayed;
Name=2;
IsoId=Q96RT1-2; Sequence=VSP_010802;
Name=3;
IsoId=Q96RT1-3; Sequence=VSP_010802, VSP_010804;
Name=4;
IsoId=Q96RT1-4; Sequence=VSP_010802, VSP_010807;
Name=5;
IsoId=Q96RT1-5; Sequence=VSP_010802, VSP_010803;
Name=6;
IsoId=Q96RT1-6; Sequence=VSP_010802, VSP_010806;
Name=7;
IsoId=Q96RT1-7; Sequence=VSP_010802, VSP_010803, VSP_010804,
VSP_010805;
Name=8;
IsoId=Q96RT1-8; Sequence=VSP_044536;
Note=No experimental confirmation available.;
Name=9;
IsoId=Q96RT1-9; Sequence=VSP_047389, VSP_010802;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
muscle and stomach, followed by liver, spleen and intestine.
{ECO:0000269|PubMed:10878805}.
-!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH50692.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA91538.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF263744; AAF77048.1; -; mRNA.
EMBL; AF276423; AAK69431.1; -; mRNA.
EMBL; AB033051; BAA86539.2; -; mRNA.
EMBL; AK001180; BAA91538.1; ALT_INIT; mRNA.
EMBL; AK304693; BAG65463.1; -; mRNA.
EMBL; AC010359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050692; AAH50692.1; ALT_SEQ; mRNA.
EMBL; BC115012; AAI15013.1; -; mRNA.
EMBL; BC126464; AAI26465.1; -; mRNA.
EMBL; BC144075; AAI44076.1; -; mRNA.
CCDS; CCDS34172.1; -. [Q96RT1-7]
CCDS; CCDS3990.1; -. [Q96RT1-2]
CCDS; CCDS58951.1; -. [Q96RT1-9]
CCDS; CCDS58952.1; -. [Q96RT1-8]
CCDS; CCDS58953.1; -. [Q96RT1-1]
CCDS; CCDS58954.1; -. [Q96RT1-4]
RefSeq; NP_001006600.1; NM_001006600.2. [Q96RT1-7]
RefSeq; NP_001240626.1; NM_001253697.1. [Q96RT1-1]
RefSeq; NP_001240627.1; NM_001253698.1. [Q96RT1-4]
RefSeq; NP_001240628.1; NM_001253699.1. [Q96RT1-8]
RefSeq; NP_001240630.1; NM_001253701.1. [Q96RT1-9]
RefSeq; NP_061165.1; NM_018695.3. [Q96RT1-2]
PDB; 1MFG; X-ray; 1.25 A; A=1321-1412.
PDB; 1MFL; X-ray; 1.88 A; A=1321-1412.
PDB; 1N7T; NMR; -; A=1314-1412.
PDB; 2H3L; X-ray; 1.00 A; A/B=1314-1412.
PDB; 2QBW; X-ray; 1.80 A; A=1330-1410.
PDB; 3CH8; X-ray; 1.90 A; A=1330-1410.
PDBsum; 1MFG; -.
PDBsum; 1MFL; -.
PDBsum; 1N7T; -.
PDBsum; 2H3L; -.
PDBsum; 2QBW; -.
PDBsum; 3CH8; -.
SMR; Q96RT1; -.
BioGrid; 120997; 121.
ELM; Q96RT1; -.
IntAct; Q96RT1; 57.
MINT; Q96RT1; -.
STRING; 9606.ENSP00000426632; -.
iPTMnet; Q96RT1; -.
PhosphoSitePlus; Q96RT1; -.
SwissPalm; Q96RT1; -.
BioMuta; ERBIN; -.
DMDM; 116242614; -.
EPD; Q96RT1; -.
jPOST; Q96RT1; -.
MaxQB; Q96RT1; -.
PaxDb; Q96RT1; -.
PeptideAtlas; Q96RT1; -.
PRIDE; Q96RT1; -.
ProteomicsDB; 17666; -.
ProteomicsDB; 19501; -.
ProteomicsDB; 78021; -. [Q96RT1-1]
ProteomicsDB; 78022; -. [Q96RT1-2]
ProteomicsDB; 78023; -. [Q96RT1-3]
ProteomicsDB; 78024; -. [Q96RT1-4]
ProteomicsDB; 78025; -. [Q96RT1-5]
ProteomicsDB; 78026; -. [Q96RT1-6]
ProteomicsDB; 78027; -. [Q96RT1-7]
Ensembl; ENST00000284037; ENSP00000284037; ENSG00000112851. [Q96RT1-1]
Ensembl; ENST00000380935; ENSP00000370322; ENSG00000112851. [Q96RT1-7]
Ensembl; ENST00000380938; ENSP00000370325; ENSG00000112851. [Q96RT1-4]
Ensembl; ENST00000380943; ENSP00000370330; ENSG00000112851. [Q96RT1-2]
Ensembl; ENST00000506030; ENSP00000426632; ENSG00000112851. [Q96RT1-8]
Ensembl; ENST00000508515; ENSP00000422015; ENSG00000112851. [Q96RT1-7]
Ensembl; ENST00000511297; ENSP00000422766; ENSG00000112851. [Q96RT1-9]
GeneID; 55914; -.
KEGG; hsa:55914; -.
UCSC; uc003jui.3; human. [Q96RT1-1]
CTD; 55914; -.
DisGeNET; 55914; -.
GeneCards; ERBIN; -.
HGNC; HGNC:15842; ERBIN.
HPA; HPA048606; -.
HPA; HPA059863; -.
MIM; 606944; gene.
neXtProt; NX_Q96RT1; -.
OpenTargets; ENSG00000112851; -.
PharmGKB; PA27845; -.
eggNOG; ENOG410KCZ0; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000159526; -.
HOGENOM; HOG000060229; -.
InParanoid; Q96RT1; -.
KO; K12796; -.
OMA; FHYGSSR; -.
PhylomeDB; Q96RT1; -.
TreeFam; TF351429; -.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
SignaLink; Q96RT1; -.
SIGNOR; Q96RT1; -.
ChiTaRS; ERBIN; human.
EvolutionaryTrace; Q96RT1; -.
GeneWiki; Erbin_(protein); -.
GenomeRNAi; 55914; -.
PRO; PR:Q96RT1; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000112851; Expressed in 238 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; Q96RT1; baseline and differential.
Genevisible; Q96RT1; HS.
GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
GO; GO:0005604; C:basement membrane; TAS:ProtInc.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0098794; C:postsynapse; IEA:Ensembl.
GO; GO:0005176; F:ErbB-2 class receptor binding; TAS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
GO; GO:0045175; P:basal protein localization; NAS:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; NAS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; NAS:UniProtKB.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0032495; P:response to muramyl dipeptide; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR032927; Erbin.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR23119:SF46; PTHR23119:SF46; 2.
Pfam; PF13855; LRR_8; 4.
Pfam; PF00595; PDZ; 1.
SMART; SM00369; LRR_TYP; 12.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS51450; LRR; 15.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Leucine-rich repeat; Membrane; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 1412 Erbin.
/FTId=PRO_0000188301.
REPEAT 23 44 LRR 1.
REPEAT 47 68 LRR 2.
REPEAT 70 91 LRR 3.
REPEAT 93 114 LRR 4.
REPEAT 116 137 LRR 5.
REPEAT 139 161 LRR 6.
REPEAT 162 183 LRR 7.
REPEAT 185 206 LRR 8.
REPEAT 208 229 LRR 9.
REPEAT 231 252 LRR 10.
REPEAT 254 275 LRR 11.
REPEAT 277 298 LRR 12.
REPEAT 300 321 LRR 13.
REPEAT 323 344 LRR 14.
REPEAT 346 367 LRR 15.
REPEAT 369 391 LRR 16.
REPEAT 392 413 LRR 17.
DOMAIN 1321 1410 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COMPBIAS 930 934 Poly-Ser.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TH2}.
MOD_RES 483 483 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q80TH2}.
MOD_RES 485 485 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TH2}.
MOD_RES 602 602 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 603 603 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TH2}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 872 872 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 917 917 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 920 920 Phosphotyrosine.
{ECO:0000244|PubMed:15144186}.
MOD_RES 931 931 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 972 972 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 1104 1104 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q80TH2}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1179 1179 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1286 1286 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 531 534 Missing (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047389.
VAR_SEQ 1212 1252 Missing (in isoform 2, isoform 3, isoform
4, isoform 5, isoform 6, isoform 7 and
isoform 9). {ECO:0000303|PubMed:10574462,
ECO:0000303|PubMed:10878805,
ECO:0000303|PubMed:11375975,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010802.
VAR_SEQ 1212 1252 KHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMK
-> SMLSRSFNSNFTTVSSFHCGSSRDLHGSQGSLALSVAD
RRGSGGHIFR (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044536.
VAR_SEQ 1253 1267 Missing (in isoform 5 and isoform 7).
{ECO:0000303|PubMed:11375975}.
/FTId=VSP_010803.
VAR_SEQ 1268 1278 Missing (in isoform 3 and isoform 7).
{ECO:0000303|PubMed:11375975}.
/FTId=VSP_010804.
VAR_SEQ 1279 1321 Missing (in isoform 7).
{ECO:0000303|PubMed:11375975}.
/FTId=VSP_010805.
VAR_SEQ 1322 1352 Missing (in isoform 6).
{ECO:0000303|PubMed:11375975}.
/FTId=VSP_010806.
VAR_SEQ 1353 1377 Missing (in isoform 4).
{ECO:0000303|PubMed:11375975,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_010807.
VARIANT 274 274 S -> L (in dbSNP:rs3213837).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_019346.
VARIANT 313 313 A -> V (in dbSNP:rs191137999).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_068905.
VARIANT 746 746 K -> E (in dbSNP:rs16894812).
/FTId=VAR_028304.
VARIANT 914 914 K -> R (in dbSNP:rs34521887).
/FTId=VAR_046673.
VARIANT 1089 1089 G -> V (in dbSNP:rs35601230).
/FTId=VAR_046674.
VARIANT 1112 1112 S -> L (in dbSNP:rs3805466).
/FTId=VAR_019347.
VARIANT 1207 1207 K -> E. {ECO:0000269|PubMed:11375975}.
/FTId=VAR_019348.
CONFLICT 271 271 T -> P (in Ref. 7; AAI15013).
{ECO:0000305}.
CONFLICT 547 547 D -> G (in Ref. 7; AAI15013).
{ECO:0000305}.
CONFLICT 805 805 E -> G (in Ref. 5; BAA91538).
{ECO:0000305}.
CONFLICT 813 813 Y -> C (in Ref. 2; AAK69431).
{ECO:0000305}.
CONFLICT 848 848 G -> C (in Ref. 5; BAG65463).
{ECO:0000305}.
CONFLICT 1047 1047 R -> S (in Ref. 5; BAG65463).
{ECO:0000305}.
CONFLICT 1205 1205 E -> G (in Ref. 7; AAI15013).
{ECO:0000305}.
CONFLICT 1267 1267 Q -> P (in Ref. 7; AAI15013).
{ECO:0000305}.
CONFLICT 1328 1328 K -> R (in Ref. 7; AAI15013).
{ECO:0000305}.
STRAND 1318 1327 {ECO:0000244|PDB:2H3L}.
STRAND 1329 1331 {ECO:0000244|PDB:2H3L}.
STRAND 1333 1338 {ECO:0000244|PDB:2H3L}.
TURN 1339 1342 {ECO:0000244|PDB:2H3L}.
STRAND 1346 1348 {ECO:0000244|PDB:2H3L}.
STRAND 1353 1359 {ECO:0000244|PDB:2H3L}.
TURN 1364 1368 {ECO:0000244|PDB:2H3L}.
STRAND 1374 1378 {ECO:0000244|PDB:2H3L}.
HELIX 1388 1397 {ECO:0000244|PDB:2H3L}.
STRAND 1400 1410 {ECO:0000244|PDB:2H3L}.
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


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Bibliography :