EDE1_YEAST
ID EDE1_YEAST Reviewed; 1381 AA.
AC P34216; D6VPV1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=EH domain-containing and endocytosis protein 1;
DE AltName: Full=Bud site selection protein 15;
GN Name=EDE1; Synonyms=BUD15; OrderedLocusNames=YBL047C;
GN ORFNames=YBL0501, YBL0520;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-961.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871888; DOI=10.1002/yea.320101113;
RA de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA Goffeau A.;
RT "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT chromosome II reveals homologues to bacterial proline synthetase and murine
RT alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL Yeast 10:1489-1496(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 579-1381.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10954428; DOI=10.1242/jcs.113.18.3309;
RA Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H.,
RA Haguenauer-Tsapis R.;
RT "A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in
RT endocytosis.";
RL J. Cell Sci. 113:3309-3319(2000).
RN [6]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(2001).
RN [7]
RP FUNCTION, INTERACTION WITH UBIQUITIN AND ENT1, AND REGION.
RX PubMed=12529323; DOI=10.1074/jbc.m211622200;
RA Aguilar R.C., Watson H.A., Wendland B.;
RT "The yeast Epsin Ent1 is recruited to membranes through multiple
RT independent interactions.";
RL J. Biol. Chem. 278:10737-10743(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION, AND DISRUPTION MUTANT.
RX PubMed=16239147; DOI=10.1016/j.cell.2005.09.024;
RA Kaksonen M., Toret C.P., Drubin D.G.;
RT "A modular design for the clathrin- and actin-mediated endocytosis
RT machinery.";
RL Cell 123:305-320(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238; SER-241; SER-244;
RP THR-245; SER-248; SER-249; THR-487; SER-1093; SER-1096; SER-1100 AND
RP THR-1307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1093 AND SER-1100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-56; TRP-176 AND
RP TRP-319.
RX PubMed=18448668; DOI=10.1091/mbc.e07-10-1019;
RA Maldonado-Baez L., Dores M.R., Perkins E.M., Drivas T.G., Hicke L.,
RA Wendland B.;
RT "Interaction between Epsin/Yap180 adaptors and the scaffolds Ede1/Pan1 is
RT required for endocytosis.";
RL Mol. Biol. Cell 19:2936-2948(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-265; SER-419;
RP SER-495; SER-848; SER-931; SER-950; SER-1069; SER-1087; SER-1093; SER-1100;
RP THR-1111 AND THR-1307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-244; THR-245;
RP SER-248; THR-251; THR-450; THR-477; SER-495; SER-931; SER-964; SER-1008;
RP SER-1012; SER-1020; THR-1046; SER-1087; SER-1093; SER-1095; SER-1096;
RP SER-1100; SER-1181; SER-1187 AND SER-1343, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAL1.
RX PubMed=22190733; DOI=10.1091/mbc.e11-02-0108;
RA Carroll S.Y., Stimpson H.E., Weinberg J., Toret C.P., Sun Y., Drubin D.G.;
RT "Analysis of yeast endocytic site formation and maturation through a
RT regulatory transition point.";
RL Mol. Biol. Cell 23:657-668(2012).
RN [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-674 AND LYS-1329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [19]
RP STRUCTURE BY NMR OF 1339-1381 IN COMPLEX WITH MONOUBIQUITIN, IDENTIFICATION
RP BY MASS SPECTROMETRY, INTERACTION WITH MONOUBIQUITIN, UBA DOMAIN, AND
RP MUTAGENESIS OF MET-1352; LEU-1370; THR-1374 AND LEU-1378.
RX PubMed=16563434; DOI=10.1016/j.jmb.2006.02.059;
RA Swanson K.A., Hicke L., Radhakrishnan I.;
RT "Structural basis for monoubiquitin recognition by the Ede1 UBA domain.";
RL J. Mol. Biol. 358:713-724(2006).
RN [20]
RP INTERACTION WITH SYP1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19713939; DOI=10.1038/emboj.2009.248;
RA Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Baez L.,
RA Hurley J.H., Traub L.M., Wendland B.;
RT "Syp1 is a conserved endocytic adaptor that contains domains involved in
RT cargo selection and membrane tubulation.";
RL EMBO J. 28:3103-3116(2009).
RN [21]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19776351; DOI=10.1091/mbc.e09-05-0429;
RA Stimpson H.E., Toret C.P., Cheng A.T., Pauly B.S., Drubin D.G.;
RT "Early-arriving Syp1p and Ede1p function in endocytic site placement and
RT formation in budding yeast.";
RL Mol. Biol. Cell 20:4640-4651(2009).
CC -!- FUNCTION: Functions at the internalization step of the clathrin-
CC mediated endocytosis (CME) as an early-acting scaffold protein.
CC Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal
CC spatiotemporal dynamics and viability. Binds to biological membranes in
CC a ubiquitin-dependent manner. {ECO:0000269|PubMed:10954428,
CC ECO:0000269|PubMed:12529323, ECO:0000269|PubMed:16239147,
CC ECO:0000269|PubMed:18448668, ECO:0000269|PubMed:19713939,
CC ECO:0000269|PubMed:19776351, ECO:0000269|PubMed:22190733}.
CC -!- SUBUNIT: Interacts (via UBA domain) with monoubiquitin and ENT1 (via
CC asparagine-proline-phenylalanine tripeptide motif called NPF).
CC Interacts with PAL1 and SYP1. {ECO:0000269|PubMed:12529323,
CC ECO:0000269|PubMed:16563434, ECO:0000269|PubMed:19713939,
CC ECO:0000269|PubMed:22190733}.
CC -!- INTERACTION:
CC P34216; P25623: SYP1; NbExp=6; IntAct=EBI-21243, EBI-21900;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10954428,
CC ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18448668, ECO:0000269|PubMed:19713939,
CC ECO:0000269|PubMed:19776351, ECO:0000269|PubMed:22190733}.
CC Note=Localized to actin cortical patches concentrated in the developing
CC bud tip in cells with small buds and at the mother-daughter neck in
CC cells undergoing cytokinesis. Localization can be maintained in the
CC absence of polymerized actin filaments.
CC -!- DISRUPTION PHENOTYPE: Random budding pattern and morphological defects.
CC Defects in fluid-phase endocytosis and defective internalization of the
CC pheromone alpha-factor and uracil permease. Deletion has only a small
CC impact on actin cytoskeleton organization. Deletion shows synthetic
CC growth defects with thermosensitive mutants of PAN1, END3 and RSP5.
CC {ECO:0000269|PubMed:10954428, ECO:0000269|PubMed:11452010}.
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}.
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DR EMBL; Z35808; CAA84867.1; -; Genomic_DNA.
DR EMBL; X78214; CAA55048.1; -; Genomic_DNA.
DR EMBL; Z23261; CAA80797.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07071.1; -; Genomic_DNA.
DR PIR; S45781; S45781.
DR RefSeq; NP_009506.1; NM_001178287.1.
DR PDB; 2G3Q; NMR; -; A=1339-1381.
DR PDB; 6WY6; X-ray; 1.77 A; C/D=1220-1247.
DR PDBsum; 2G3Q; -.
DR PDBsum; 6WY6; -.
DR AlphaFoldDB; P34216; -.
DR BMRB; P34216; -.
DR SMR; P34216; -.
DR BioGRID; 32650; 365.
DR DIP; DIP-5817N; -.
DR IntAct; P34216; 28.
DR MINT; P34216; -.
DR STRING; 4932.YBL047C; -.
DR iPTMnet; P34216; -.
DR MaxQB; P34216; -.
DR PaxDb; P34216; -.
DR PRIDE; P34216; -.
DR EnsemblFungi; YBL047C_mRNA; YBL047C; YBL047C.
DR GeneID; 852233; -.
DR KEGG; sce:YBL047C; -.
DR SGD; S000000143; EDE1.
DR VEuPathDB; FungiDB:YBL047C; -.
DR eggNOG; KOG0998; Eukaryota.
DR GeneTree; ENSGT00940000170943; -.
DR HOGENOM; CLU_002993_0_0_1; -.
DR InParanoid; P34216; -.
DR OMA; WDEIFAG; -.
DR BioCyc; YEAST:G3O-28947-MON; -.
DR Reactome; R-SCE-416482; G alpha (12/13) signalling events.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR EvolutionaryTrace; P34216; -.
DR PRO; PR:P34216; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P34216; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0044396; P:actin cortical patch organization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IGI:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR CDD; cd00052; EH; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF12763; EF-hand_4; 3.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF47473; SSF47473; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Coiled coil; Cytoplasm; Endocytosis;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1381
FT /note="EH domain-containing and endocytosis protein 1"
FT /id="PRO_0000202457"
FT DOMAIN 14..113
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 47..82
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 135..227
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 167..202
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 276..311
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 277..366
FT /note="EH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 1338..1380
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 389..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1381
FT /note="Able to bind biological membranes"
FT REGION 1298..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..882
FT /evidence="ECO:0000255"
FT COMPBIAS 389..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 245
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1046
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1307
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 674
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 1329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 56
FT /note="W->A: Abnormal spatiotemporal behavior."
FT /evidence="ECO:0000269|PubMed:18448668"
FT MUTAGEN 176
FT /note="W->A: Abnormal spatiotemporal behavior."
FT /evidence="ECO:0000269|PubMed:18448668"
FT MUTAGEN 319
FT /note="W->A: Abnormal spatiotemporal behavior."
FT /evidence="ECO:0000269|PubMed:18448668"
FT MUTAGEN 1352
FT /note="M->A: Reduced ubiquitin-binding."
FT /evidence="ECO:0000269|PubMed:16563434"
FT MUTAGEN 1370
FT /note="L->A: Reduced ubiquitin-binding."
FT /evidence="ECO:0000269|PubMed:16563434"
FT MUTAGEN 1374
FT /note="T->A: Enhanced ubiquitin-binding."
FT /evidence="ECO:0000269|PubMed:16563434"
FT MUTAGEN 1378
FT /note="L->A: Reduced ubiquitin-binding."
FT /evidence="ECO:0000269|PubMed:16563434"
FT HELIX 1221..1223
FT /evidence="ECO:0007829|PDB:6WY6"
FT HELIX 1229..1234
FT /evidence="ECO:0007829|PDB:6WY6"
FT HELIX 1243..1246
FT /evidence="ECO:0007829|PDB:6WY6"
FT HELIX 1341..1350
FT /evidence="ECO:0007829|PDB:2G3Q"
FT TURN 1351..1353
FT /evidence="ECO:0007829|PDB:2G3Q"
FT HELIX 1356..1365
FT /evidence="ECO:0007829|PDB:2G3Q"
FT HELIX 1370..1378
FT /evidence="ECO:0007829|PDB:2G3Q"
SQ SEQUENCE 1381 AA; 150783 MW; 626FD261DCBA7D99 CRC64;
MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ LLSQVWATVD
IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT QLASFSINQN PAPMQSGSAT
GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA QTVAGDKAKD IFLKARLPNQ TLGEIWALCD
RDASGVLDKS EFIMAMYLIQ LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL
SANSTGVSSL TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV
LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE LPDVIPNELL
QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV SAPAVNTQPT VPQVLPQNSN
NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT NNSFSYDNNN GQATLQQQQP QQPPPLTHSS
SGLKKFTPTS NFGQSIIKEE PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV
PNFSVFSMPA GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS
NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN LRSTHDQNVK
QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL TTDLQESQTK NAELKEQITN
LNSMTASLQS QLNEKQQQVK QERSMVDVNS KQLELNQVTV ANLQKEIDGL GEKISVYLTK
QKELNDYQKT VEEQHAQLQA KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL
QEMFDDLSQR KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS
NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES DVFDRDVPTL
GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE YGIPRSQSLT SSVANNAPQS
VRDDVELPET LEERDTINNT ANRDNTGNLS HIPGEWEATP ATASTDVLSN ETTEVIEDGS
TTKRANSNED GESVSSIQES PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT
REIPSATVKT LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD
EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL QMNAFTGTLT
SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA EPTKVATPSI PQQPIPLKND
PIVDASLSKG PIVNRGVATT PKSLAVEELS GMGFTEEEAH NALEKCNWDL EAATNFLLDS
A
