DAB2_RAT
ID DAB2_RAT Reviewed; 768 AA.
AC O88797; O55048; O55049; O55050; O55051; O88798; Q4QRA2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Disabled homolog 2;
DE AltName: Full=Adaptor molecule disabled-2;
DE AltName: Full=C9;
DE AltName: Full=Differentially expressed in ovarian carcinoma 2;
DE Short=DOC-2;
DE AltName: Full=Mitogen-responsive phosphoprotein;
GN Name=Dab2; Synonyms=Doc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P59 AND P82), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=9681506; DOI=10.1210/endo.139.8.6159;
RA Tseng C.-P., Ely B.D., Li Y., Pong R.-C., Hsieh J.-T.;
RT "Regulation of rat DOC-2 gene during castration-induced rat ventral
RT prostate degeneration and its growth inhibitory function in human prostatic
RT carcinoma cells.";
RL Endocrinology 139:3542-3553(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P82).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-47; 117-189; 634-687 AND 753-768.
RC TISSUE=Kidney, and Prostate;
RA Lau K.M., Mok S.C., Ho S.M.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH DAB2IP.
RX PubMed=11812785; DOI=10.1074/jbc.m110568200;
RA Wang Z., Tseng C.-P., Pong R.-C., Chen H., McConnell J.D., Navone N.,
RA Hsieh J.-T.;
RT "The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
RT cancer. Characterization of a novel GTPase-activating protein associated
RT with N-terminal domain of DOC-2/DAB2.";
RL J. Biol. Chem. 277:12622-12631(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH GRB2 AND SRC.
RX PubMed=12473651; DOI=10.1074/jbc.m210628200;
RA Zhou J., Scholes J., Hsieh J.T.;
RT "Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src in
RT normal prostatic epithelium and cancer.";
RL J. Biol. Chem. 278:6936-6941(2003).
RN [6]
RP FUNCTION.
RX PubMed=19000037; DOI=10.1042/bj20081288;
RA Chetrit D., Ziv N., Ehrlich M.;
RT "Dab2 regulates clathrin assembly and cell spreading.";
RL Biochem. J. 418:701-715(2009).
RN [7]
RP PHOSPHORYLATION AT SER-326; SER-328 AND SER-401, AND MUTAGENESIS OF
RP SER-393; SER-394 AND SER-401.
RX PubMed=21097498; DOI=10.1074/jbc.m110.161851;
RA Chetrit D., Barzilay L., Horn G., Bielik T., Smorodinsky N.I., Ehrlich M.;
RT "Negative regulation of the endocytic adaptor disabled-2 (Dab2) in
RT mitosis.";
RL J. Biol. Chem. 286:5392-5403(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-193; SER-401 AND
RP SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 675-713 IN COMPLEX WITH MYO6.
RX PubMed=19665975; DOI=10.1016/j.cell.2009.05.030;
RA Yu C., Feng W., Wei Z., Miyanoiri Y., Wen W., Zhao Y., Zhang M.;
RT "Myosin VI undergoes cargo-mediated dimerization.";
RL Cell 138:537-548(2009).
CC -!- FUNCTION: Adapter protein that functions as clathrin-associated sorting
CC protein (CLASP) required for clathrin-mediated endocytosis of selected
CC cargo proteins. Can bind and assemble clathrin, and binds
CC simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)
CC and cargos containing non-phosphorylated NPXY internalization motifs,
CC such as the LDL receptor, to recruit them to clathrin-coated pits. Can
CC function in clathrin-mediated endocytosis independently of the AP-2
CC complex. Involved in endocytosis of integrin beta-1; this function
CC seems to redundant with the AP-2 complex and seems to require DAB2
CC binding to endocytosis accessory EH domain-containing proteins such as
CC EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis
CC transmembrane conductance regulator/CFTR. Involved in endocytosis of
CC megalin/LRP2 lipoprotein receptor during embryonal development.
CC Required for recycling of the TGF-beta receptor. Involved in CFTR
CC trafficking to the late endosome. Involved in several receptor-mediated
CC signaling pathways. Involved in TGF-beta receptor signaling and
CC facilitates phosphorylation of the signal transducer SMAD2. Mediates
CC TFG-beta-stimulated JNK activation. May inhibit the canoniocal
CC Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin
CC destruction complex through a competing association with axin
CC preventing its dephosphorylation through protein phosphatase 1 (PP1).
CC Sequesters LRP6 towards clathrin-mediated endocytosis, leading to
CC inhibition of Wnt/beta-catenin signaling. May activate non-canonical
CC Wnt signaling. In cell surface growth factor/Ras signaling pathways
CC proposed to inhibit ERK activation by interrupting the binding of GRB2
CC to SOS1 and to inhibit SRC by preventing its activating phosphorylation
CC at 'Tyr-419'. Proposed to be involved in modulation of androgen
CC receptor (AR) signaling mediated by SRC activation; seems to compete
CC with AR for interaction with SRC. Plays a role in the CSF-1 signal
CC transduction pathway. Plays a role in cellular differentiation.
CC Involved in cell positioning and formation of visceral endoderm (VE)
CC during embryogenesis and proposed to be required in the VE to respond
CC to Nodal signaling coming from the epiblast. Required for the
CC epithelial to mesenchymal transition, a process necessary for proper
CC embryonic development. May be involved in myeloid cell differentiation
CC and can induce macrophage adhesion and spreading. May act as a tumor
CC suppressor. {ECO:0000269|PubMed:12473651, ECO:0000269|PubMed:19000037}.
CC -!- SUBUNIT: Can interact (via PID domain) with LDLR, APP, APLP1 and APLP2,
CC and weakly with INPP5D (via NPXY motifs); the interaction is impaired
CC by tyrosine phosphorylation of the respective NPXY motifs. Can weakly
CC interact (via PID domain) with LRP1 (via NPXY motif); the interaction
CC is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts
CC with LRP2 (via NPXY motif); the interaction is not affected by tyrosine
CC phosphorylation of the NPXY motif. Interacts with clathrin; in vitro
CC can assemble clathrin triskelia into polyhedral coats. Interacts with
CC AP2A2, ITGB1, ITGB3, ITGB5, PIAS2, DAB2IP, NOSTRIN, FCHO1, DVL3, EPS15,
CC ITSN1 and EPS15L1. Interacts with SH3KBP1 (via SH3 domains). Interacts
CC with GRB2; competes with SOS1 for binding to GRB2 and the interaction
CC is enhanced by EGF and NT-3 stimulation. Interacts with MAP3K7; the
CC interaction is induced by TGF-beta stimulation and may mediate TGF-beta
CC stimulated JNK activation. Interacts with AXIN1 and PPP1CA; the
CC interactions are mutually exclusive. Interacts with the globular tail
CC of MYO6. Interacts (via DPF motifs) with FCHO2; the interaction is
CC direct and required for DAB2-mediated LDLR endocytosis. Interacts with
CC LRP6; the interaction involves LRP6 phosphorylation by CK2 and
CC sequesters LRP6 towards clathrin-mediated endocytosis. Associates with
CC the TGF-beta receptor complex (Probable). Interacts with SMAD2 and
CC SMAD3; the interactions are enhanced upon TGF-beta stimulation.
CC Interacts with GRB2; the interaction is enhanced by EGF and NT-3
CC stimulation. Interacts with SRC; the interaction is enhanced by EGF
CC stimulation. Interacts with GRB2; the interaction is enhanced by EGF
CC and NT-3 stimulation. Interacts (via NPXY motif) with DAB2 (via PID
CC domain). {ECO:0000269|PubMed:11812785, ECO:0000269|PubMed:12473651,
CC ECO:0000269|PubMed:19665975, ECO:0000305}.
CC -!- INTERACTION:
CC O88797; P98158: Lrp2; NbExp=2; IntAct=EBI-6109302, EBI-6306650;
CC O88797; P52800: Efnb2; Xeno; NbExp=2; IntAct=EBI-6109302, EBI-1032676;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane. Membrane, clathrin-coated pit.
CC Note=Colocalizes with large insert-containing isoforms of MYO6 at
CC clathrin-coated pits/vesicles. During mitosis is progressively
CC displaced from the membrane and translocated to the cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=p82;
CC IsoId=O88797-1; Sequence=Displayed;
CC Name=p59;
CC IsoId=O88797-2; Sequence=VSP_004184;
CC -!- TISSUE SPECIFICITY: Prostate. {ECO:0000269|PubMed:9681506}.
CC -!- DOMAIN: The PID domain binds to predominantly non-phosphorylated NPXY
CC internalization motifs present in members of the LDLR and APP family;
CC it also mediates simultaneous binding to phosphatidylinositol 4,5-
CC bisphosphate. {ECO:0000250}.
CC -!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
CC involved in the endocytic pathway, mediate the interaction with the EH
CC domain of EPS15, EPS15R and ITSN1. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation during mitosis is leading to
CC membrane displacement. There is some ambiguity for the mitotic
CC phosphosite Ser-326/328. {ECO:0000269|PubMed:21097498}.
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DR EMBL; U95177; AAC33405.1; -; mRNA.
DR EMBL; U95178; AAC33406.1; -; mRNA.
DR EMBL; BC097314; AAH97314.1; -; mRNA.
DR EMBL; AF045657; AAC03360.1; -; mRNA.
DR EMBL; AF045658; AAC03361.1; -; mRNA.
DR EMBL; AF045659; AAC03362.1; -; mRNA.
DR EMBL; AF045660; AAC03363.1; -; mRNA.
DR RefSeq; NP_077073.1; NM_024159.1. [O88797-1]
DR PDB; 3H8D; X-ray; 2.20 A; E/F/G/H=675-713.
DR PDBsum; 3H8D; -.
DR AlphaFoldDB; O88797; -.
DR BMRB; O88797; -.
DR SMR; O88797; -.
DR BioGRID; 249412; 1.
DR DIP; DIP-60713N; -.
DR IntAct; O88797; 5.
DR MINT; O88797; -.
DR STRING; 10116.ENSRNOP00000043878; -.
DR iPTMnet; O88797; -.
DR PhosphoSitePlus; O88797; -.
DR PaxDb; O88797; -.
DR PRIDE; O88797; -.
DR Ensembl; ENSRNOT00000050655; ENSRNOP00000043878; ENSRNOG00000028930. [O88797-1]
DR Ensembl; ENSRNOT00000107345; ENSRNOP00000085574; ENSRNOG00000028930. [O88797-2]
DR GeneID; 79128; -.
DR KEGG; rno:79128; -.
DR UCSC; RGD:621007; rat. [O88797-1]
DR CTD; 1601; -.
DR RGD; 621007; Dab2.
DR eggNOG; KOG3535; Eukaryota.
DR GeneTree; ENSGT00940000155567; -.
DR InParanoid; O88797; -.
DR OrthoDB; 279276at2759; -.
DR PhylomeDB; O88797; -.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; O88797; -.
DR PRO; PR:O88797; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0030132; C:clathrin coat of coated pit; ISO:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISO:RGD.
DR GO; GO:0038024; F:cargo receptor activity; ISO:RGD.
DR GO; GO:0035615; F:clathrin adaptor activity; ISO:RGD.
DR GO; GO:0030276; F:clathrin binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:RGD.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0035026; P:leading edge cell differentiation; ISO:RGD.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:RGD.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032349; P:positive regulation of aldosterone biosynthetic process; IDA:RGD.
DR GO; GO:2000860; P:positive regulation of aldosterone secretion; IDA:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; ISO:RGD.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:RGD.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:RGD.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:RGD.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0097017; P:renal protein absorption; ISO:RGD.
DR GO; GO:1902074; P:response to salt; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IMP:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Coated pit;
KW Cytoplasm; Cytoplasmic vesicle; Developmental protein; Differentiation;
KW Endocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P98082"
FT CHAIN 2..768
FT /note="Disabled homolog 2"
FT /id="PRO_0000079772"
FT DOMAIN 45..196
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..447
FT /note="Required for localization to clathrin-coated pits"
FT /evidence="ECO:0000250"
FT REGION 285..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..731
FT /note="Sufficient for interaction with GRB2"
FT /evidence="ECO:0000250"
FT REGION 619..627
FT /note="Required for interaction with CSK"
FT REGION 649..768
FT /note="Required for interaction with MYO6"
FT /evidence="ECO:0000250"
FT REGION 660..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..671
FT /note="Required for interaction with GRB2 and CSK"
FT /evidence="ECO:0000269|PubMed:12473651"
FT REGION 708..724
FT /note="Sufficient for interaction with SH3KBP1 SH3 domain"
FT /evidence="ECO:0000250"
FT REGION 709..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..295
FT /note="DPF 1"
FT MOTIF 298..300
FT /note="DPF 2"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P98082"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 170
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P98078"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 326
FT /note="Phosphoserine; in mitosis"
FT /evidence="ECO:0000305|PubMed:21097498"
FT MOD_RES 328
FT /note="Phosphoserine; in mitosis"
FT /evidence="ECO:0000305|PubMed:21097498"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 673
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P98078"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98082"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98078"
FT VAR_SEQ 230..447
FT /note="Missing (in isoform p59)"
FT /evidence="ECO:0000303|PubMed:9681506"
FT /id="VSP_004184"
FT MUTAGEN 393
FT /note="S->A: Reduces phosphorylation, reduces mitotic
FT membrane displacement; when associated with A-394 and A-
FT 401."
FT /evidence="ECO:0000269|PubMed:21097498"
FT MUTAGEN 394
FT /note="S->A: Reduces phosphorylation, reduces mitotic
FT membrane displacement; when associated with A-393 and A-
FT 401."
FT /evidence="ECO:0000269|PubMed:21097498"
FT MUTAGEN 401
FT /note="S->A: Reduces phosphorylation, reduces mitotic
FT membrane displacement; when associated with A-393 and A-
FT 394."
FT /evidence="ECO:0000269|PubMed:21097498"
FT CONFLICT 3..4
FT /note="NE -> TN (in Ref. 3; AAC03360)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> K (in Ref. 3; AAC03361)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="S -> P (in Ref. 3; AAC03362)"
FT /evidence="ECO:0000305"
FT CONFLICT 764..768
FT /note="GNPFA -> WKSFC (in Ref. 3; AAC03363)"
FT /evidence="ECO:0000305"
FT HELIX 680..689
FT /evidence="ECO:0007829|PDB:3H8D"
FT HELIX 699..711
FT /evidence="ECO:0007829|PDB:3H8D"
SQ SEQUENCE 768 AA; 82377 MW; 930FB25248ADAC6E CRC64;
MSNEVETSTT NGQPDQQAAP KAPSKKEKKK GSEKTDEYLL ARFKGDGVKY KAKLIGIDDV
PDARGDKMSQ DSMMKLKGMA AAGRSQGQHK QRIWVNISLS GIKIIDEKTG VIEHEHPVNK
ISFIARDVTD NRAFGYVCGG EGQHQFFAIK TGQQAEPLVV DLKDLFQVIY NVKKKEEEKK
KVEEANKAEE NGSEALMTLD DQANKLKLGV DQMDLFGDMS TPPDLNNPTE SRDILLVDLN
SEIDTNQNSL RENPFLTNGV TSCSLPRPKP QASFLPESAF SANLNFFPTP NPDPFRDDPF
AQPDQSAPSS FHSLTSADQK KANPGSLSTP QSKGPLNGDT DYFGQQFDQI SNRTGKQEAQ
GGPWPYPSSQ TQQAVRTQNG VSEKEQNGFH IKSSPNPFVG SPPKGLSVPN GVKQDLESSV
QSSAHDSIAI IPPPQSTKPG RGRRTAKSSA NDLLASDIFA SEPPGQMSPT GQPAVPQANF
MDLFKTSAPA PMGSGPLVGL GTVPVTPPQA GPWTPVVFTP STTVVPGAII SGQPSGFGQP
LVFGTTPAVQ VWNQPSSFAT AASPPPPAVW CPTTSVAPNT WSSTSPLGNP FQSSNIFPPS
TISTQSFPQP MMSSVLVTPP QPPPRNGPLK DTLSDAFTGL DPLGDKEVKE VKEMFKDFQL
RQPPLVPSRK GETPSSGTSS AFSSYFNNKV GIPQEHVDHD DFDANQLLNK INEPPKPAPR
QGVLSGTKSA DNSLENPFSK GFSSTNPSVV SQPASSDAHR SPFGNPFA
