ZO1_RAT
ID ZO1_RAT Reviewed; 1765 AA.
AC A0A0G2K2P5;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Tight junction protein ZO-1 {ECO:0000250|UniProtKB:Q07157};
DE AltName: Full=Tight junction protein 1 {ECO:0000250|UniProtKB:Q07157};
DE AltName: Full=Zona occludens protein 1 {ECO:0000303|PubMed:3528172};
DE AltName: Full=Zonula occludens protein 1 {ECO:0000250|UniProtKB:Q07157};
GN Name=Tjp1 {ECO:0000303|PubMed:3528172};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=3528172; DOI=10.1083/jcb.103.3.755;
RA Stevenson B.R., Siliciano J.D., Mooseker M.S., Goodenough D.A.;
RT "Identification of ZO-1: a high molecular weight polypeptide associated
RT with the tight junction (zonula occludens) in a variety of epithelia.";
RL J. Cell Biol. 103:755-766(1986).
RN [3]
RP FUNCTION, INTERACTION WITH GJA1, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=9707407; DOI=10.1016/s0960-9822(07)00375-2;
RA Giepmans B.N., Moolenaar W.H.;
RT "The gap junction protein connexin43 interacts with the second PDZ domain
RT of the zona occludens-1 protein.";
RL Curr. Biol. 8:931-934(1998).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; TYR-132 AND SER-617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-178;
RP SER-212; SER-275; SER-277; SER-280; SER-290; SER-294; SER-297; SER-300;
RP SER-617; SER-810; SER-828; THR-846; THR-868 AND SER-1614, AND
RP 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).
CC -!- FUNCTION: TjpP1, Tjp2, and Tjp3 are closely related scaffolding
CC proteins that link tight junction (TJ) transmembrane proteins such as
CC claudins, junctional adhesion molecules, and occludin to the actin
CC cytoskeleton (PubMed:9707407). The tight junction acts to limit
CC movement of substances through the paracellular space and as a boundary
CC between the compositionally distinct apical and basolateral plasma
CC membrane domains of epithelial and endothelial cells. Necessary for
CC lumenogenesis, and particularly efficient epithelial polarization and
CC barrier formation (By similarity). Plays a role in the regulation of
CC cell migration by targeting Cdc42bpb to the leading edge of migrating
CC cells (By similarity). Plays an important role in podosome formation
CC and associated function, thus regulating cell adhesion and matrix
CC remodeling (By similarity). With Tjp2 and Tjp3, participates in the
CC junctional retention and stability of the transcription factor Dbpa,
CC but is not involved in its shuttling to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O97758, ECO:0000250|UniProtKB:Q07157,
CC ECO:0000269|PubMed:9707407}.
CC -!- SUBUNIT: Homodimer, and heterodimer with TJP2 and TJP3 (By similarity).
CC Interacts with OCLN (By similarity). Interacts with CALM, claudins,
CC CGN/cingulin, CXADR, GJA12, GJD3 and UBN1 (By similarity). Interacts
CC (via ZU5 domain) with CDC42BPB and MYZAP (By similarity). Interacts
CC (via PDZ domain) with GJA1 (PubMed:9707407). Interacts (via PDZ
CC domains) with ANKRD2 (By similarity). Interacts with BVES (via the C-
CC terminus cytoplasmic tail) (By similarity). Interacts with HSPA4 (By
CC similarity). Interacts with KIRREL1 (By similarity). Interacts with
CC DLL1 (By similarity). Interacts with USP53 (via the C-terminal region)
CC (By similarity). Interacts with DNMBP (via C-terminal domain); required
CC for the apical cell-cell junction localization of DNMBP (By
CC similarity). Interacts with SPEF1 (By similarity).
CC {ECO:0000250|UniProtKB:P39447, ECO:0000250|UniProtKB:Q07157,
CC ECO:0000269|PubMed:9707407}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07157};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q07157}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q07157}. Cell junction, tight junction
CC {ECO:0000269|PubMed:3528172, ECO:0000269|PubMed:9707407}. Cell junction
CC {ECO:0000250|UniProtKB:P12830}. Cell junction, gap junction
CC {ECO:0000250|UniProtKB:Q07157}. Note=Moves from the cytoplasm to the
CC cell membrane concurrently with cell-cell contact (By similarity).
CC Distributed over the entire lateral surface of the plasma membrane and
CC other actin-rich structures (By similarity). Detected at the leading
CC edge of migrating and wounded cells (By similarity). Colocalizes with
CC SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By
CC similarity). {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:3528172,
CC ECO:0000269|PubMed:9707407}.
CC -!- DOMAIN: The 244-aa domain between residues 633 and 876 is the primary
CC occludin (Ocln)-binding site and is required for stable association
CC with the tight junction (By similarity).
CC {ECO:0000250|UniProtKB:Q07157}.
CC -!- DOMAIN: The C-terminal region (residues 1151-1372) is an actin-binding
CC region (ABR) that interacts directly with F-actin and plays an
CC important role in the localization of Tjp1 at junctions (By
CC similarity). The ABR is also required for the localization to puncta at
CC the free edge of cells before initiation of cell-cell contact (By
CC similarity). The ABR is also necessary for Tjp1 recruitment to
CC podosomes (By similarity). {ECO:0000250|UniProtKB:Q07157}.
CC -!- DOMAIN: The second PDZ domain (PDZ2) mediates homodimerization and
CC heterodimerization with Tjp2 and Tjp3 (By similarity). PDZ2 domain also
CC mediates interaction with Gja1 (PubMed:9707407).
CC {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:9707407}.
CC -!- PTM: Phosphorylated at tyrosine redidues in response to epidermal
CC growth factor (EGF) (By similarity). This response is dependent on an
CC intact actin microfilament system (By similarity). Dephosphorylated by
CC Ptprj (By similarity). {ECO:0000250|UniProtKB:Q07157}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AABR07004128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07004129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0G2K2P5; -.
DR SMR; A0A0G2K2P5; -.
DR CORUM; A0A0G2K2P5; -.
DR IntAct; A0A0G2K2P5; 2.
DR STRING; 10116.ENSRNOP00000014988; -.
DR iPTMnet; A0A0G2K2P5; -.
DR PhosphoSitePlus; A0A0G2K2P5; -.
DR jPOST; A0A0G2K2P5; -.
DR Ensembl; ENSRNOT00000112594; ENSRNOP00000078542; ENSRNOG00000011077.
DR RGD; 1306305; Tjp1.
DR GeneTree; ENSGT00940000155164; -.
DR OMA; DQILRXY; -.
DR Reactome; R-RNO-191650; Regulation of gap junction activity.
DR Reactome; R-RNO-2028269; Signaling by Hippo.
DR Reactome; R-RNO-351906; Apoptotic cleavage of cell adhesion proteins.
DR PRO; PR:A0A0G2K2P5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000011077; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; A0A0G2K2P5; baseline and differential.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0046581; C:intercellular canaliculus; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008013; F:beta-catenin binding; IPI:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0071253; F:connexin binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0034334; P:adherens junction maintenance; ISO:RGD.
DR GO; GO:0001825; P:blastocyst formation; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:RGD.
DR GO; GO:2000250; P:negative regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEP:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:RGD.
DR GO; GO:0071896; P:protein localization to adherens junction; ISO:RGD.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:RGD.
DR GO; GO:0150105; P:protein localization to cell-cell junction; ISO:RGD.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:1901888; P:regulation of cell junction assembly; ISO:RGD.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071000; P:response to magnetism; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR CDD; cd12026; SH3_ZO-1; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR005417; ZO.
DR InterPro; IPR005418; ZO-1.
DR InterPro; IPR035597; ZO-1_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR13865:SF25; PTHR13865:SF25; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01598; ZONOCCLUDNS1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Gap junction; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Tight junction; Transferase.
FT CHAIN 1..1765
FT /note="Tight junction protein ZO-1"
FT /id="PRO_0000443108"
FT DOMAIN 23..110
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 186..264
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 421..502
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 516..584
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 690..791
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 1631..1765
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT REGION 102..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..876
FT /note="Occludin (OCLN)-binding region"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT REGION 825..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1370
FT /note="Actin-binding region (ABR)"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT COMPBIAS 134..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 809
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 848
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 854
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 868
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1164
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1765 AA; 197148 MW; 185CBB4C3B3ECC52 CRC64;
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD
PDPVSDNEDD SYDEDVHDPR SGRGALANRR GEKSWARDRS ASRDRSLSPR SDRRSVASSQ
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
VRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AVSTPVKHVD
DHTPKAVEEV TVEKHEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIVPNKNRA EQLASVQYTL PKTAGGDRAD
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK
LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP
QAQPQAIHRI DSPGLKTASQ QKAEASSPVP YLSPETNPAS SASAVKHNVN LTNVNLEEPT
PAPPTSHVSQ ADCLGAPSPE APHTMLRDEG VSLPSHVDPA KVYRKEPYPE EMMRQNHILK
QPALGHPGQR LDKEPNPAYD PQLPYVEKQA SRDLEQPPYR YESSSYTDQF SRNYDHRLRF
EDRVPTYEDQ WSYYDDKQPY PTRPFDTQHP RDLDSRQHPE EASERGYFQR FEEPAPLPYD
SRPRYEQLPR TSTLRHEEQP TSGYEVHNRY RPEAQPYAPA GPKSSEPKQY FDQYPRSYEQ
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ HKPEVLPSAT KPQPPPPALT EEEEDPAMKP
QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP SASLVGPKPV SQTQFSEHDK
TLYRLPEPQK PQAKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFESKP PAHIPAGHHS
EPAKPVHSQS QPNFSSYSSK GKPETDAMDR SFSEKRYDPT QAMPPPPPLP SQYSQPVPPL
SNSSLHIHSK AAQSEGNSVS LDFQNSYISK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS
FPDKASVNGA EQTQKTITPA YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL
SSKPPPSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ INNISTMPKA VPVSPSAVEE
DEDEDGHTVV ATARGIFNSN GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP
PLDKEKGETL LSPLVMCGPH GLKFLKPVEL RLPHCASMTP DGWSFALKSS DSSSGDPKTW
QNKCLPGDPN YLVGANCVSV LIDHF
