ID CING_HUMAN Reviewed; 1203 AA.
AC Q9P2M7; A6H8L3; A7MD22; Q5T386; Q9NR25;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 24-JAN-2024, entry version 167.
DE RecName: Full=Cingulin {ECO:0000305};
GN Name=CGN {ECO:0000312|HGNC:HGNC:17429}; Synonyms=KIAA1319;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RC TISSUE=Neuroepithelium;
RX PubMed=11042084; DOI=10.1006/jsbi.2000.4284;
RA Citi S., D'Atri F., Parry D.A.D.;
RT "Human and Xenopus cingulin share a modular organization of the coiled-coil
RT rod domain: predictions for intra- and intermolecular assembly.";
RL J. Struct. Biol. 131:135-145(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP PROTEIN SEQUENCE OF 374-382.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP INTERACTION WITH TJP1.
RX PubMed=12023291; DOI=10.1074/jbc.m203717200;
RA D'Atri F., Nadalutti F., Citi S.;
RT "Evidence for a functional interaction between cingulin and ZO-1 in
RT cultured cells.";
RL J. Biol. Chem. 277:27757-27764(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-1182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-579, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-140; SER-155;
RP SER-165; SER-214; SER-217 AND THR-712, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-137; SER-140;
RP SER-258; SER-276; SER-1175 AND SER-1176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INTERACTION WITH SPEF1, AND SUBCELLULAR LOCATION.
RX PubMed=31473225; DOI=10.1053/j.gastro.2019.08.031;
RA Tapia R., Perez-Yepez E.A., Carlino M.J., Karandikar U.C., Kralicek S.E.,
RA Estes M.K., Hecht G.A.;
RT "Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and
RT Contributes to Formation of Filopodia and Lamellipodia.";
RL Gastroenterology 157:1544-1555(2019).
CC -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC tight junction (TJ) paracellular permeability barrier.
CC -!- SUBUNIT: Homodimer (PubMed:11042084). Interacts with TJP1/ZO1
CC (PubMed:12023291). Interacts with SPEF1 (PubMed:31473225).
CC {ECO:0000269|PubMed:12023291, ECO:0000269|PubMed:31473225,
CC ECO:0000303|PubMed:11042084}.
CC -!- INTERACTION:
CC Q9P2M7; P31947: SFN; NbExp=4; IntAct=EBI-79537, EBI-476295;
CC Q9P2M7; P63104: YWHAZ; NbExp=4; IntAct=EBI-79537, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P59242}. Note=Localizes to the apical junction
CC complex composed of tight and adherens junctions (By similarity).
CC Colocalizes with SPEF1 at sites of cell-cell contact in intestinal
CC epithelial cells (PubMed:12023291). {ECO:0000250|UniProtKB:P59242,
CC ECO:0000269|PubMed:12023291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2M7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2M7-2; Sequence=VSP_037039, VSP_037040;
CC -!- TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight
CC junctions of polarized epithelia and some endothelia. Expressed in
CC pancreas, kidney, liver and lung, but not in skeletal muscle, placenta,
CC brain or heart.
CC -!- DOMAIN: Deletion of the TJP1/ZO1 interaction motif (ZIM) decreases but
CC does not abolish colocalization with TJP1/ZO1.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI46658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92557.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF263462; AAF74498.1; -; mRNA.
DR EMBL; AB037740; BAA92557.1; ALT_INIT; mRNA.
DR EMBL; AK290007; BAF82696.1; -; mRNA.
DR EMBL; AL365436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53434.1; -; Genomic_DNA.
DR EMBL; BC146657; AAI46658.1; ALT_INIT; mRNA.
DR EMBL; BC152445; AAI52446.1; -; mRNA.
DR CCDS; CCDS999.1; -. [Q9P2M7-1]
DR RefSeq; NP_065821.1; NM_020770.2. [Q9P2M7-1]
DR RefSeq; XP_005245422.1; XM_005245365.4. [Q9P2M7-1]
DR AlphaFoldDB; Q9P2M7; -.
DR SMR; Q9P2M7; -.
DR BioGRID; 121589; 149.
DR DIP; DIP-30947N; -.
DR IntAct; Q9P2M7; 40.
DR MINT; Q9P2M7; -.
DR STRING; 9606.ENSP00000271636; -.
DR iPTMnet; Q9P2M7; -.
DR MetOSite; Q9P2M7; -.
DR PhosphoSitePlus; Q9P2M7; -.
DR BioMuta; CGN; -.
DR DMDM; 27923755; -.
DR EPD; Q9P2M7; -.
DR jPOST; Q9P2M7; -.
DR MassIVE; Q9P2M7; -.
DR MaxQB; Q9P2M7; -.
DR PaxDb; 9606-ENSP00000271636; -.
DR PeptideAtlas; Q9P2M7; -.
DR ProteomicsDB; 83849; -. [Q9P2M7-1]
DR ProteomicsDB; 83850; -. [Q9P2M7-2]
DR Pumba; Q9P2M7; -.
DR Antibodypedia; 34064; 127 antibodies from 23 providers.
DR DNASU; 57530; -.
DR Ensembl; ENST00000271636.12; ENSP00000271636.7; ENSG00000143375.15. [Q9P2M7-1]
DR GeneID; 57530; -.
DR KEGG; hsa:57530; -.
DR MANE-Select; ENST00000271636.12; ENSP00000271636.7; NM_020770.3; NP_065821.1.
DR UCSC; uc009wmw.4; human. [Q9P2M7-1]
DR AGR; HGNC:17429; -.
DR CTD; 57530; -.
DR DisGeNET; 57530; -.
DR GeneCards; CGN; -.
DR HGNC; HGNC:17429; CGN.
DR HPA; ENSG00000143375; Tissue enhanced (intestine).
DR MIM; 609473; gene.
DR neXtProt; NX_Q9P2M7; -.
DR OpenTargets; ENSG00000143375; -.
DR PharmGKB; PA134938123; -.
DR VEuPathDB; HostDB:ENSG00000143375; -.
DR eggNOG; ENOG502R9EI; Eukaryota.
DR GeneTree; ENSGT00940000154489; -.
DR HOGENOM; CLU_002036_0_0_1; -.
DR InParanoid; Q9P2M7; -.
DR OMA; HWREMFQ; -.
DR OrthoDB; 4226071at2759; -.
DR PhylomeDB; Q9P2M7; -.
DR TreeFam; TF332247; -.
DR PathwayCommons; Q9P2M7; -.
DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR SignaLink; Q9P2M7; -.
DR BioGRID-ORCS; 57530; 12 hits in 1149 CRISPR screens.
DR ChiTaRS; CGN; human.
DR GeneWiki; Cingulin; -.
DR GenomeRNAi; 57530; -.
DR Pharos; Q9P2M7; Tbio.
DR PRO; PR:Q9P2M7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P2M7; Protein.
DR Bgee; ENSG00000143375; Expressed in pancreatic ductal cell and 148 other cell types or tissues.
DR ExpressionAtlas; Q9P2M7; baseline and differential.
DR Genevisible; Q9P2M7; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR002928; Myosin_tail.
DR PANTHER; PTHR46349:SF4; CINGULIN; 1.
DR PANTHER; PTHR46349; CINGULIN-LIKE PROTEIN 1-RELATED; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Coiled coil;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..1203
FT /note="Cingulin"
FT /id="PRO_0000089763"
FT REGION 7..357
FT /note="Head"
FT REGION 25..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..67
FT /note="Interaction with TJP1/ZO1"
FT /evidence="ECO:0000269|PubMed:12023291"
FT REGION 89..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1203
FT /note="Tail"
FT COILED 358..1160
FT /evidence="ECO:0000255"
FT MOTIF 48..62
FT /note="ZIM"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59242"
FT MOD_RES 579
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 712
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 704..777
FT /note="KMVAEAEATVLGQRRAAVETTLRETQEENDEFRRRILGLEQQLKETRGLVDG
FT GEAVEARLRDKLQRLEAEKQQL -> RGVGTGLRRWRLRVSGGLRSQRVWKVTCHGYVL
FT TSSWVLGMWFKEARIWQGEDTCICVGVGFSEKRLAGGSCSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037039"
FT VAR_SEQ 778..1203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037040"
FT VARIANT 485
FT /note="R -> Q (in dbSNP:rs12038198)"
FT /id="VAR_057809"
SQ SEQUENCE 1203 AA; 137057 MW; 0AE294110E605765 CRC64;
MEQAPNMAEP RGPVDHGVQI RFITEPVSGA EMGTLRRGGR RPAKDARAST YGVAVRVQGI
AGQPFVVLNS GEKGGDSFGV QIKGANDQGA SGALSSDLEL PENPYSQVKG FPAPSQSSTS
DEEPGAYWNG KLLRSHSQAS LAGPGPVDPS NRSNSMLELA PKVASPGSTI DTAPLSSVDS
LINKFDSQLG GQARGRTGRR TRMLPPEQRK RSKSLDSRLP RDTFEERERQ STNHWTSSTK
YDNHVGTSKQ PAQSQNLSPL SGFSRSRQTQ DWVLQSFEEP RRSAQDPTML QFKSTPDLLR
DQQEAAPPGS VDHMKATIYG ILREGSSESE TSVRRKVSLV LEKMQPLVMV SSGSTKAVAG
QGELTRKVEE LQRKLDEEVK KRQKLEPSQV GLERQLEEKT EECSRLQELL ERRKGEAQQS
NKELQNMKRL LDQGEDLRHG LETQVMELQN KLKHVQGPEP AKEVLLKDLL ETRELLEEVL
EGKQRVEEQL RLRERELTAL KGALKEEVAS RDQEVEHVRQ QYQRDTEQLR RSMQDATQDH
AVLEAERQKM SALVRGLQRE LEETSEETGH WQSMFQKNKE DLRATKQELL QLRMEKEEME
EELGEKIEVL QRELEQARAS AGDTRQVEVL KKELLRTQEE LKELQAERQS QEVAGRHRDR
ELEKQLAVLR VEADRGRELE EQNLQLQKTL QQLRQDCEEA SKAKMVAEAE ATVLGQRRAA
VETTLRETQE ENDEFRRRIL GLEQQLKETR GLVDGGEAVE ARLRDKLQRL EAEKQQLEEA
LNASQEEEGS LAAAKRALEA RLEEAQRGLA RLGQEQQTLN RALEEEGKQR EVLRRGKAEL
EEQKRLLDRT VDRLNKELEK IGEDSKQALQ QLQAQLEDYK EKARREVADA QRQAKDWASE
AEKTSGGLSR LQDEIQRLRQ ALQASQAERD TARLDKELLA QRLQGLEQEA ENKKRSQDDR
ARQLKGLEEK VSRLETELDE EKNTVELLTD RVNRGRDQVD QLRTELMQER SARQDLECDK
ISLERQNKDL KTRLASSEGF QKPSASLSQL ESQNQLLQER LQAEEREKTV LQSTNRKLER
KVKELSIQIE DERQHVNDQK DQLSLRVKAL KRQVDEAEEE IERLDGLRKK AQREVEEQHE
VNEQLQARIK SLEKDSWRKA SRSAAESALK NEGLSSDEEF DSVYDPSSIA SLLTESNLQT
SSC
//
