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Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3)

 ZO3_HUMAN               Reviewed;         919 AA.
O95049; A6NFP3; B3KR73; B3KXZ0; B4E2W6; F5H2X0; F5H4S9; K7EK22;
Q32N01;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
19-MAR-2014, sequence version 3.
10-OCT-2018, entry version 163.
RecName: Full=Tight junction protein ZO-3;
AltName: Full=Tight junction protein 3;
AltName: Full=Zona occludens protein 3;
AltName: Full=Zonula occludens protein 3;
Name=TJP3; Synonyms=ZO3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
TISSUE=Stomach, Testis, and Tongue;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
THR-898.
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).
[5]
FUNCTION.
PubMed=16129888; DOI=10.1242/jcs.02528;
Michel D., Arsanto J.P., Massey-Harroche D., Beclin C., Wijnholds J.,
Le Bivic A.;
"PATJ connects and stabilizes apical and lateral components of tight
junctions in human intestinal cells.";
J. Cell Sci. 118:4049-4057(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-905 AND
SER-906, 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).
[7]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[8]
INTERACTION WITH UBN1.
PubMed=18823282; DOI=10.1042/BC20080072;
Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P.,
Sergeant A., Manet E., Boyer V., Gruffat H.;
"Characterization of the ubinuclein protein as a new member of the
nuclear and adhesion complex components (NACos).";
Biol. Cell 101:319-334(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, 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).
[10]
INDUCTION.
PubMed=20434232; DOI=10.1016/j.ejcb.2010.03.002;
Vikstroem E., Bui L., Konradsson P., Magnusson K.E.;
"Role of calcium signalling and phosphorylations in disruption of the
epithelial junctions by Pseudomonas aeruginosa quorum sensing
molecule.";
Eur. J. Cell Biol. 89:584-597(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-905 AND
SER-906, 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).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCND1.
PubMed=21411630; DOI=10.1091/mbc.E10-08-0677;
Capaldo C.T., Koch S., Kwon M., Laur O., Parkos C.A., Nusrat A.;
"Tight function zonula occludens-3 regulates cyclin D1-dependent cell
proliferation.";
Mol. Biol. Cell 22:1677-1685(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND 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).
[14]
INDUCTION.
PubMed=22354024; DOI=10.1128/IAI.00001-12;
Kwak Y.K., Vikstroem E., Magnusson K.E., Vecsey-Semjen B.,
Colque-Navarro P., Moellby R.;
"The Staphylococcus aureus alpha-toxin perturbs the barrier function
in Caco-2 epithelial cell monolayers by altering junctional
integrity.";
Infect. Immun. 80:1670-1680(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-164; SER-203;
SER-591 AND SER-856, 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).
[16]
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=23608536; DOI=10.1128/MCB.01435-12;
Aschauer L., Gruber L.N., Pfaller W., Limonciel A., Athersuch T.J.,
Cavill R., Khan A., Gstraunthaler G., Grillari J., Grillari R.,
Hewitt P., Leonard M.O., Wilmes A., Jennings P.;
"Delineation of the key aspects in the regulation of epithelial
monolayer formation.";
Mol. Cell. Biol. 33:2535-2550(2013).
[17]
INDUCTION.
PubMed=24314862; DOI=10.1016/j.jnutbio.2013.08.011;
Kim C.Y., Kim K.H.;
"Curcumin prevents leptin-induced tight junction dysfunction in
intestinal Caco-2 BBe cells.";
J. Nutr. Biochem. 25:26-35(2014).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-319; THR-325;
SER-327; SER-371; SER-591 AND SER-906, 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).
[19]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 475-775.
Structural genomics consortium (SGC);
"Crystal structure of the SH3-kinase fragment of tight junction
protein 3 (TJP3) in apo-form.";
Submitted (NOV-2009) to the PDB data bank.
-!- FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding
proteins that link tight junction (TJ) transmembrane proteins such
as claudins, junctional adhesion molecules, and occludin to the
actin cytoskeleton (PubMed:16129888). The tight junction acts to
limit movement of substances through the paracellular space and as
a boundary between the compositionally distinct apical and
basolateral plasma membrane domains of epithelial and endothelial
cells. Binds and recruits PATJ to tight junctions where it
connects and stabilizes apical and lateral components of tight
junctions (PubMed:16129888). Promotes cell-cycle progression
through the sequestration of cyclin D1 (CCND1) at tight junctions
during mitosis which prevents CCND1 degradation during M-phase and
enables S-phase transition (PubMed:21411630). With TJP1 and TJP2,
participates to the junctional retention and stability of the
transcription factor DBPA, but is not involved in its shuttling to
the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable
for individual viability, embryonic development, epithelial
differentiation, and the establishment of TJs, at least in the
laboratory environment (By similarity).
{ECO:0000250|UniProtKB:O62683, ECO:0000250|UniProtKB:Q9QXY1,
ECO:0000269|PubMed:16129888, ECO:0000269|PubMed:21411630}.
-!- SUBUNIT: Interacts with occludin OCLN, claudins and TPJ1 (By
similarity). Interacts with PATJ (By similarity). Interacts with
UBN1 (PubMed:20434232). Interacts with FASLG (PubMed:19807924).
Interacts with CCND1 (PubMed:21411630).
{ECO:0000250|UniProtKB:O62683, ECO:0000269|PubMed:18823282,
ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:21411630}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21411630};
Peripheral membrane protein {ECO:0000269|PubMed:21411630};
Cytoplasmic side {ECO:0000269|PubMed:21411630}. Cell junction,
tight junction {ECO:0000269|PubMed:21411630,
ECO:0000269|PubMed:23608536}. Nucleus
{ECO:0000269|PubMed:23608536}. Note=Exhibits predominant nuclear
expression in proliferating cells but is exclusively junctionally
expressed after confluence is reached (PubMed:23608536). Shows an
epithelial-specific tight junction localization in a TJP1/TJP2-
dependent fashion (By similarity). {ECO:0000250|UniProtKB:Q9QXY1,
ECO:0000269|PubMed:23608536}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=5;
IsoId=O95049-1; Sequence=Displayed;
Name=3;
IsoId=O95049-3; Sequence=VSP_040238;
Note=No experimental confirmation available.;
Name=4;
IsoId=O95049-4; Sequence=VSP_047022;
Name=6;
IsoId=O95049-5; Sequence=VSP_053844;
-!- INDUCTION: Exhibits enhanced expression in matured epithelial
layers (PubMed:23608536). Apical leptin, Staphylococcus aureus
alpha-toxin and Pseudomonas aeruginosa acyl-homoserine lactone 3O-
C12-HSl lower expression levels, altering junctional integrity in
intestinal cells (PubMed:20434232, PubMed:22354024,
PubMed:24314862). {ECO:0000269|PubMed:20434232,
ECO:0000269|PubMed:22354024, ECO:0000269|PubMed:23608536,
ECO:0000269|PubMed:24314862}.
-!- PTM: Phosphorylated (By similarity).
{ECO:0000250|UniProtKB:O62683}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC72274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW69293.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AK091118; BAG52285.1; -; mRNA.
EMBL; AK128237; BAG54652.1; -; mRNA.
EMBL; AK304462; BAG65278.1; -; mRNA.
EMBL; AC005954; AAC72274.1; ALT_SEQ; Genomic_DNA.
EMBL; AC006125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69293.1; ALT_SEQ; Genomic_DNA.
EMBL; BC108906; AAI08907.1; -; mRNA.
CCDS; CCDS32873.2; -. [O95049-1]
CCDS; CCDS59332.1; -. [O95049-4]
RefSeq; NP_001254489.1; NM_001267560.1. [O95049-1]
RefSeq; NP_001254490.1; NM_001267561.1. [O95049-4]
UniGene; Hs.25527; -.
PDB; 3KFV; X-ray; 2.80 A; A=475-775.
PDBsum; 3KFV; -.
ProteinModelPortal; O95049; -.
SMR; O95049; -.
BioGrid; 118025; 7.
IntAct; O95049; 5.
MINT; O95049; -.
STRING; 9606.ENSP00000262968; -.
GlyConnect; 1809; -.
iPTMnet; O95049; -.
PhosphoSitePlus; O95049; -.
BioMuta; TJP3; -.
EPD; O95049; -.
MaxQB; O95049; -.
PaxDb; O95049; -.
PeptideAtlas; O95049; -.
PRIDE; O95049; -.
ProteomicsDB; 50630; -.
ProteomicsDB; 50632; -. [O95049-3]
Ensembl; ENST00000539908; ENSP00000439991; ENSG00000105289. [O95049-5]
Ensembl; ENST00000541714; ENSP00000439278; ENSG00000105289. [O95049-1]
Ensembl; ENST00000587686; ENSP00000467864; ENSG00000105289. [O95049-3]
Ensembl; ENST00000589378; ENSP00000465419; ENSG00000105289. [O95049-4]
GeneID; 27134; -.
KEGG; hsa:27134; -.
UCSC; uc010xhs.4; human. [O95049-1]
CTD; 27134; -.
DisGeNET; 27134; -.
EuPathDB; HostDB:ENSG00000105289.14; -.
GeneCards; TJP3; -.
H-InvDB; HIX0014645; -.
HGNC; HGNC:11829; TJP3.
HPA; CAB013244; -.
HPA; HPA046863; -.
HPA; HPA053337; -.
MIM; 612689; gene.
neXtProt; NX_O95049; -.
OpenTargets; ENSG00000105289; -.
PharmGKB; PA36534; -.
eggNOG; ENOG410IQ5J; Eukaryota.
eggNOG; ENOG410XS08; LUCA.
GeneTree; ENSGT00760000118866; -.
HOGENOM; HOG000230923; -.
HOVERGEN; HBG017627; -.
InParanoid; O95049; -.
KO; K06097; -.
OMA; EDGYDWG; -.
OrthoDB; EOG091G0AJZ; -.
TreeFam; TF315606; -.
ChiTaRS; TJP3; human.
EvolutionaryTrace; O95049; -.
GeneWiki; TJP3; -.
GenomeRNAi; 27134; -.
PRO; PR:O95049; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105289; Expressed in 123 organ(s), highest expression level in mucosa of transverse colon.
CleanEx; HS_TJP3; -.
ExpressionAtlas; O95049; baseline and differential.
Genevisible; O95049; HS.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR005417; ZO.
InterPro; IPR005420; ZO-3.
PANTHER; PTHR13865:SF11; PTHR13865:SF11; 1.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF00595; PDZ; 3.
Pfam; PF07653; SH3_2; 1.
PRINTS; PR01597; ZONOCCLUDNS.
PRINTS; PR01600; ZONOCCLUDNS3.
SMART; SM00072; GuKc; 1.
SMART; SM00228; PDZ; 3.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS50106; PDZ; 3.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3 domain; Tight junction.
CHAIN 1 919 Tight junction protein ZO-3.
/FTId=PRO_0000094546.
DOMAIN 11 93 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 195 272 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 380 446 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 475 549 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 580 761 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXY1}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 325 325 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 856 856 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 906 906 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 36 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053844.
VAR_SEQ 1 1 M -> MNLCGLMPIFPAPLDQVADM (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040238.
VAR_SEQ 1 1 M -> MAVRFQVADM (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047022.
VARIANT 898 898 M -> T (in dbSNP:rs1046268).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_056114.
CONFLICT 19 19 R -> H (in Ref. 4; AAI08907).
{ECO:0000305}.
CONFLICT 96 96 H -> L (in Ref. 1; BAG52285).
{ECO:0000305}.
CONFLICT 449 449 L -> P (in Ref. 1; BAG54652).
{ECO:0000305}.
CONFLICT 802 802 R -> H (in Ref. 1; BAG52285).
{ECO:0000305}.
CONFLICT 901 901 H -> R (in Ref. 1; BAG52285).
{ECO:0000305}.
CONFLICT 917 917 T -> M (in Ref. 1; BAG65278).
{ECO:0000305}.
STRAND 478 482 {ECO:0000244|PDB:3KFV}.
STRAND 490 493 {ECO:0000244|PDB:3KFV}.
STRAND 501 506 {ECO:0000244|PDB:3KFV}.
STRAND 522 527 {ECO:0000244|PDB:3KFV}.
STRAND 533 539 {ECO:0000244|PDB:3KFV}.
HELIX 542 555 {ECO:0000244|PDB:3KFV}.
HELIX 596 602 {ECO:0000244|PDB:3KFV}.
STRAND 606 614 {ECO:0000244|PDB:3KFV}.
STRAND 621 625 {ECO:0000244|PDB:3KFV}.
HELIX 628 638 {ECO:0000244|PDB:3KFV}.
TURN 640 642 {ECO:0000244|PDB:3KFV}.
STRAND 643 645 {ECO:0000244|PDB:3KFV}.
HELIX 661 669 {ECO:0000244|PDB:3KFV}.
STRAND 673 676 {ECO:0000244|PDB:3KFV}.
HELIX 680 688 {ECO:0000244|PDB:3KFV}.
STRAND 694 701 {ECO:0000244|PDB:3KFV}.
HELIX 703 713 {ECO:0000244|PDB:3KFV}.
HELIX 721 735 {ECO:0000244|PDB:3KFV}.
HELIX 736 738 {ECO:0000244|PDB:3KFV}.
STRAND 740 745 {ECO:0000244|PDB:3KFV}.
STRAND 747 749 {ECO:0000244|PDB:3KFV}.
HELIX 751 763 {ECO:0000244|PDB:3KFV}.
STRAND 766 771 {ECO:0000244|PDB:3KFV}.
SEQUENCE 919 AA; 101397 MW; D36EB684E7E4A6C8 CRC64;
MEELTIWEQH TATLSKDPRR GFGIAISGGR DRPGGSMVVS DVVPGGPAEG RLQTGDHIVM
VNGVSMENAT SAFAIQILKT CTKMANITVK RPRRIHLPAT KASPSSPGRQ DSDEDDGPQR
VEEVDQGRGY DGDSSSGSGR SWDERSRRPR PGRRGRAGSH GRRSPGGGSE ANGLALVSGF
KRLPRQDVQM KPVKSVLVKR RDSEEFGVKL GSQIFIKHIT DSGLAARHRG LQEGDLILQI
NGVSSQNLSL NDTRRLIEKS EGKLSLLVLR DRGQFLVNIP PAVSDSDSSP LEDISDLASE
LSQAPPSHIP PPPRHAQRSP EASQTDSPVE SPRLRRESSV DSRTISEPDE QRSELPRESS
YDIYRVPSSQ SMEDRGYSPD TRVVRFLKGK SIGLRLAGGN DVGIFVSGVQ AGSPADGQGI
QEGDQILQVN DVPFQNLTRE EAVQFLLGLP PGEEMELVTQ RKQDIFWKMV QSRVGDSFYI
RTHFELEPSP PSGLGFTRGD VFHVLDTLHP GPGQSHARGG HWLAVRMGRD LREQERGIIP
NQSRAEQLAS LEAAQRAVGV GPGSSAGSNA RAEFWRLRGL RRGAKKTTQR SREDLSALTR
QGRYPPYERV VLREASFKRP VVILGPVADI AMQKLTAEMP DQFEIAETVS RTDSPSKIIK
LDTVRVIAEK DKHALLDVTP SAIERLNYVQ YYPIVVFFIP ESRPALKALR QWLAPASRRS
TRRLYAQAQK LRKHSSHLFT ATIPLNGTSD TWYQELKAII REQQTRPIWT AEDQLDGSLE
DNLDLPHHGL ADSSADLSCD SRVNSDYETD GEGGAYTDGE GYTDGEGGPY TDVDDEPPAP
ALARSSEPVQ ADESQSPRDR GRISAHQGAQ VDSRHPQGQW RQDSMRTYER EALKKKFMRV
HDAESSDEDG YDWGPATDL


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