TJAP1_HUMAN
ID TJAP1_HUMAN Reviewed; 557 AA.
AC Q5JTD0; Q05BH9; Q5JTD1; Q5JWW1; Q68DB2; Q6P2P3; Q9H7V7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tight junction-associated protein 1;
DE AltName: Full=Protein incorporated later into tight junctions;
DE AltName: Full=Tight junction protein 4;
GN Name=TJAP1 {ECO:0000312|HGNC:HGNC:17949};
GN Synonyms=PILT {ECO:0000303|PubMed:11602598}, TJP4;
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Testis, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Muscle, and Skin;
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 [5]
RP INTERACTION WITH DLG1, AND TISSUE SPECIFICITY.
RX PubMed=11602598; DOI=10.1074/jbc.m107335200;
RA Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K., Takeuchi M.,
RA Takai Y.;
RT "Pilt, a novel peripheral membrane protein at tight junctions in epithelial
RT cells.";
RL J. Biol. Chem. 276:48350-48355(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-320; SER-345 AND
RP SER-545, AND 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300 AND SER-545, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-491 AND SER-545, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-491 AND SER-545, AND
RP IDENTIFICATION BY MASS 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-345; THR-422 AND
RP SER-545, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; THR-422 AND SER-491, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Plays a role in regulating the structure of the Golgi
CC apparatus. {ECO:0000250|UniProtKB:Q9DCD5}.
CC -!- SUBUNIT: Interacts with DLG1 (PubMed:11602598). Interacts with ARF6
CC (GTP-bound form) (By similarity). {ECO:0000250|UniProtKB:Q9DCD5,
CC ECO:0000269|PubMed:11602598}.
CC -!- INTERACTION:
CC Q5JTD0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2814077, EBI-5916454;
CC Q5JTD0; O95678: KRT75; NbExp=3; IntAct=EBI-2814077, EBI-2949715;
CC Q5JTD0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2814077, EBI-16439278;
CC Q5JTD0; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2814077, EBI-2130429;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9DCD5}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9DCD5}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9DCD5}; Peripheral membrane protein
CC {ECO:0000305}. Note=Recruited to tight junctions (TJ) during late
CC stages of maturation of the TJ complexes. Excluded from adherens
CC junctions and desmosomes. {ECO:0000250|UniProtKB:Q9DCD5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5JTD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JTD0-2; Sequence=VSP_016002;
CC Name=3;
CC IsoId=Q5JTD0-3; Sequence=VSP_016000;
CC Name=4;
CC IsoId=Q5JTD0-4; Sequence=VSP_015999, VSP_016001, VSP_016002;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11602598}.
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DR EMBL; AK024269; BAB14867.1; -; mRNA.
DR EMBL; CR749480; CAH18308.1; -; mRNA.
DR EMBL; AL117398; CAI46221.1; -; Transcribed_RNA.
DR EMBL; AL355802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046239; AAH46239.1; -; mRNA.
DR EMBL; BC064401; AAH64401.1; -; mRNA.
DR CCDS; CCDS4898.1; -. [Q5JTD0-2]
DR CCDS; CCDS55004.1; -. [Q5JTD0-1]
DR RefSeq; NP_001139488.1; NM_001146016.1. [Q5JTD0-1]
DR RefSeq; NP_001139489.1; NM_001146017.1. [Q5JTD0-1]
DR RefSeq; NP_001139490.1; NM_001146018.1. [Q5JTD0-2]
DR RefSeq; NP_001139491.1; NM_001146019.1. [Q5JTD0-2]
DR RefSeq; NP_001139492.1; NM_001146020.1. [Q5JTD0-2]
DR RefSeq; NP_542171.2; NM_080604.2. [Q5JTD0-2]
DR RefSeq; XP_006715312.1; XM_006715249.1.
DR RefSeq; XP_006715313.1; XM_006715250.3. [Q5JTD0-1]
DR RefSeq; XP_006715314.1; XM_006715251.2. [Q5JTD0-1]
DR RefSeq; XP_006715315.1; XM_006715252.2.
DR RefSeq; XP_006715317.1; XM_006715254.3. [Q5JTD0-1]
DR RefSeq; XP_006715319.1; XM_006715256.1.
DR RefSeq; XP_006715320.1; XM_006715257.2. [Q5JTD0-1]
DR RefSeq; XP_006715322.1; XM_006715259.3.
DR RefSeq; XP_006715323.1; XM_006715260.1.
DR RefSeq; XP_006715324.1; XM_006715261.1. [Q5JTD0-1]
DR RefSeq; XP_006715325.1; XM_006715262.2. [Q5JTD0-1]
DR RefSeq; XP_006715326.1; XM_006715263.2. [Q5JTD0-1]
DR RefSeq; XP_006715328.1; XM_006715265.1. [Q5JTD0-2]
DR RefSeq; XP_006715329.1; XM_006715266.1. [Q5JTD0-2]
DR RefSeq; XP_011513297.1; XM_011514995.1. [Q5JTD0-1]
DR RefSeq; XP_016866977.1; XM_017011488.1.
DR RefSeq; XP_016866978.1; XM_017011489.1. [Q5JTD0-1]
DR RefSeq; XP_016866979.1; XM_017011490.1.
DR RefSeq; XP_016866980.1; XM_017011491.1.
DR RefSeq; XP_016866981.1; XM_017011492.1. [Q5JTD0-2]
DR RefSeq; XP_016866982.1; XM_017011493.1. [Q5JTD0-2]
DR AlphaFoldDB; Q5JTD0; -.
DR SMR; Q5JTD0; -.
DR BioGRID; 125043; 52.
DR IntAct; Q5JTD0; 29.
DR MINT; Q5JTD0; -.
DR STRING; 9606.ENSP00000361522; -.
DR iPTMnet; Q5JTD0; -.
DR PhosphoSitePlus; Q5JTD0; -.
DR BioMuta; TJAP1; -.
DR DMDM; 74742134; -.
DR EPD; Q5JTD0; -.
DR jPOST; Q5JTD0; -.
DR MassIVE; Q5JTD0; -.
DR MaxQB; Q5JTD0; -.
DR PaxDb; Q5JTD0; -.
DR PeptideAtlas; Q5JTD0; -.
DR PRIDE; Q5JTD0; -.
DR ProteomicsDB; 63213; -. [Q5JTD0-1]
DR ProteomicsDB; 63214; -. [Q5JTD0-2]
DR ProteomicsDB; 63215; -. [Q5JTD0-3]
DR ProteomicsDB; 63216; -. [Q5JTD0-4]
DR Antibodypedia; 16501; 141 antibodies from 24 providers.
DR DNASU; 93643; -.
DR Ensembl; ENST00000259751.5; ENSP00000259751.1; ENSG00000137221.14. [Q5JTD0-2]
DR Ensembl; ENST00000372444.6; ENSP00000361521.2; ENSG00000137221.14. [Q5JTD0-2]
DR Ensembl; ENST00000372445.9; ENSP00000361522.5; ENSG00000137221.14. [Q5JTD0-1]
DR Ensembl; ENST00000372449.5; ENSP00000361527.1; ENSG00000137221.14. [Q5JTD0-1]
DR Ensembl; ENST00000372452.5; ENSP00000361530.1; ENSG00000137221.14. [Q5JTD0-2]
DR Ensembl; ENST00000436109.6; ENSP00000407080.2; ENSG00000137221.14. [Q5JTD0-2]
DR Ensembl; ENST00000438588.6; ENSP00000408769.2; ENSG00000137221.14. [Q5JTD0-1]
DR Ensembl; ENST00000612912.4; ENSP00000484142.1; ENSG00000137221.14. [Q5JTD0-3]
DR GeneID; 93643; -.
DR KEGG; hsa:93643; -.
DR MANE-Select; ENST00000372449.6; ENSP00000361527.1; NM_001350562.2; NP_001337491.1.
DR UCSC; uc003ovc.3; human. [Q5JTD0-1]
DR CTD; 93643; -.
DR DisGeNET; 93643; -.
DR GeneCards; TJAP1; -.
DR HGNC; HGNC:17949; TJAP1.
DR HPA; ENSG00000137221; Low tissue specificity.
DR MIM; 612658; gene.
DR neXtProt; NX_Q5JTD0; -.
DR OpenTargets; ENSG00000137221; -.
DR PharmGKB; PA38268; -.
DR VEuPathDB; HostDB:ENSG00000137221; -.
DR eggNOG; ENOG502QRZ1; Eukaryota.
DR GeneTree; ENSGT00940000161543; -.
DR HOGENOM; CLU_032139_0_0_1; -.
DR InParanoid; Q5JTD0; -.
DR OMA; SQSWIFA; -.
DR OrthoDB; 443898at2759; -.
DR PhylomeDB; Q5JTD0; -.
DR TreeFam; TF331612; -.
DR PathwayCommons; Q5JTD0; -.
DR SignaLink; Q5JTD0; -.
DR BioGRID-ORCS; 93643; 16 hits in 1080 CRISPR screens.
DR ChiTaRS; TJAP1; human.
DR GeneWiki; TJAP1; -.
DR GenomeRNAi; 93643; -.
DR Pharos; Q5JTD0; Tbio.
DR PRO; PR:Q5JTD0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5JTD0; protein.
DR Bgee; ENSG00000137221; Expressed in secondary oocyte and 187 other tissues.
DR ExpressionAtlas; Q5JTD0; baseline and differential.
DR Genevisible; Q5JTD0; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR InterPro; IPR028179; Tjap1.
DR InterPro; IPR043441; Tjap1/BEGAIN.
DR InterPro; IPR043470; Tjap1_dom.
DR PANTHER; PTHR28664; PTHR28664; 1.
DR PANTHER; PTHR28664:SF3; PTHR28664:SF3; 1.
DR Pfam; PF15453; Pilt; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Cell membrane;
KW Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..557
FT /note="Tight junction-associated protein 1"
FT /id="PRO_0000072550"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..171
FT /evidence="ECO:0000255"
FT COMPBIAS 11..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015999"
FT VAR_SEQ 44..557
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016000"
FT VAR_SEQ 66
FT /note="L -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016001"
FT VAR_SEQ 120..129
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_016002"
FT CONFLICT 174
FT /note="L -> P (in Ref. 1; BAB14867)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="HF -> QV (in Ref. 2; CAI46221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61821 MW; 07D41B72E1CB0E20 CRC64;
MTSAAPAKKP YRKAPPEHRE LRLEIPGSRL EQEEPLTDAE RMKLLQEENE ELRRRLASAT
RRTEALEREL EIGQDCLELE LGQSREELDK FKDKFRRLQN SYTASQRTNQ ELEDKLHTLA
SLSHSWIFAI KKAEMDRKTL DWEIVELTNK LLDAKNTINK LEELNERYRL DCNLAVQLLK
CNKSHFRNHK FADLPCELQD MVRKHLHSGQ EAASPGPAPS LAPGAVVPTS VIARVLEKPE
SLLLNSAQSG SAGRPLAEDV FVHVDMSEGV PGDPASPPAP GSPTPQPNGE CHSLGTARGS
PEEELPLPAF EKLNPYPTPS PPHPLYPGRR VIEFSEDKVR IPRNSPLPNC TYATRQAISL
SLVEEGSERA RPSPVPSTPA SAQASPHHQP SPAPLTLSAP ASSASSEEDL LVSWQRAFVD
RTPPPAAVAQ RTAFGRDALP ELQRHFAHSP ADRDEVVQAP SARPEESELL LPTEPDSGFP
REEEELNLPI SPEEERQSLL PINRGTEEGP GTSHTEGRAW PLPSSSRPQR SPKRMGVHHL
HRKDSLTQAQ EQGNLLN
