ID PAR3L_HUMAN Reviewed; 1205 AA. AC Q8TEW8; E9PE87; Q8IUC7; Q8IUC9; Q96DK9; Q96N09; Q96NX6; Q96NX7; Q96Q29; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 02-SEP-2026, entry version 197. DE RecName: Full=Partitioning defective 3 homolog B; DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein; DE AltName: Full=PAR3-beta; DE AltName: Full=Partitioning defective 3-like protein; DE Short=PAR3-L protein; GN Name=PARD3B; Synonyms=ALS2CR19, PAR3B, PAR3L; 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 4). RX PubMed=11586298; DOI=10.1038/ng1001-166; RA Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S., RA Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A., RA Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr., RA Scherer S.W., Rouleau G.A., Hayden M.R., Ikeda J.-E.; RT "A gene encoding a putative GTPase regulator is mutated in familial RT amyotrophic lateral sclerosis 2."; RL Nat. Genet. 29:166-173(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), AND VARIANT PRO-165. RX PubMed=12459187; DOI=10.1016/s0006-291x(02)02698-0; RA Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.; RT "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes RT to tight junctions."; RL Biochem. Biophys. Res. Commun. 299:641-646(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), CHARACTERIZATION, AND RP INTERACTION WITH PARD6B. RX PubMed=12234671; DOI=10.1016/s0378-1119(02)00681-9; RA Gao L., Macara I.G., Joberty G.; RT "Multiple splice variants of Par3 and of a novel related gene, Par3L, RT produce proteins with different binding properties."; RL Gene 294:99-107(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-901 (ISOFORM 1), AND VARIANTS RP PRO-165 AND LYS-192. RC TISSUE=Gastric mucosa, and Neuron; 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 [6] RP INTERACTION WITH INSC. RX PubMed=16458856; DOI=10.1016/j.bbrc.2006.01.050; RA Izaki T., Kamakura S., Kohjima M., Sumimoto H.; RT "Two forms of human Inscuteable-related protein that links Par3 to the Pins RT homologues LGN and AGS3."; RL Biochem. Biophys. Res. Commun. 341:1001-1006(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746 AND SER-801, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-368 AND SER-746, AND RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-1184, 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: Putative adapter protein involved in asymmetrical cell CC division and cell polarization processes. May play a role in the CC formation of epithelial tight junctions. CC -!- SUBUNIT: Interacts with PARD6B. Interacts with INSC/inscuteable. CC {ECO:0000269|PubMed:12234671, ECO:0000269|PubMed:16458856}. CC -!- INTERACTION: CC Q8TEW8; O15439: ABCC4; NbExp=3; IntAct=EBI-2861929, EBI-4319622; CC Q8TEW8; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-2861929, EBI-1057448; CC Q8TEW8; Q9UHC3: ASIC3; NbExp=3; IntAct=EBI-2861929, EBI-66903811; CC Q8TEW8; P23634: ATP2B4; NbExp=3; IntAct=EBI-2861929, EBI-1174388; CC Q8TEW8; O75838: CIB2; NbExp=2; IntAct=EBI-2861929, EBI-25770403; CC Q8TEW8; Q9NS75: CYSLTR2; NbExp=3; IntAct=EBI-2861929, EBI-3843579; CC Q8TEW8; Q5KSL6: DGKK; NbExp=3; IntAct=EBI-2861929, EBI-4401920; CC Q8TEW8; Q13574: DGKZ; NbExp=3; IntAct=EBI-2861929, EBI-715507; CC Q8TEW8; Q8N1I0: DOCK4; NbExp=3; IntAct=EBI-2861929, EBI-1059186; CC Q8TEW8; Q14CM0: FRMPD4; NbExp=2; IntAct=EBI-2861929, EBI-311279; CC Q8TEW8; O75084: FZD7; NbExp=2; IntAct=EBI-2861929, EBI-746917; CC Q8TEW8; P22460: KCNA5; NbExp=3; IntAct=EBI-2861929, EBI-6426121; CC Q8TEW8; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-2861929, EBI-17272405; CC Q8TEW8; P36507: MAP2K2; NbExp=3; IntAct=EBI-2861929, EBI-1056930; CC Q8TEW8; Q96KB5: PBK; NbExp=3; IntAct=EBI-2861929, EBI-536853; CC Q8TEW8; P60484: PTEN; NbExp=2; IntAct=EBI-2861929, EBI-696162; CC Q8TEW8; Q6ZTQ3: RASSF6; NbExp=3; IntAct=EBI-2861929, EBI-2933412; CC Q8TEW8; Q15418: RPS6KA1; NbExp=6; IntAct=EBI-2861929, EBI-963034; CC Q8TEW8; A6NIM6: SLC15A5; NbExp=3; IntAct=EBI-2861929, EBI-11792220; CC Q8TEW8; Q9NYB5: SLCO1C1; NbExp=2; IntAct=EBI-2861929, EBI-11792007; CC Q8TEW8; Q7Z6J2: TAMALIN; NbExp=3; IntAct=EBI-2861929, EBI-2806496; CC Q8TEW8; Q9UDY2: TJP2; NbExp=3; IntAct=EBI-2861929, EBI-1042602; CC Q8TEW8; P0DTC3: 3a; Xeno; NbExp=2; IntAct=EBI-2861929, EBI-25475894; CC Q8TEW8; P26554: E6; Xeno; NbExp=3; IntAct=EBI-2861929, EBI-11793986; CC Q8TEW8; P36809: E6; Xeno; NbExp=3; IntAct=EBI-2861929, EBI-63979783; CC Q8TEW8; Q9IR59: E6; Xeno; NbExp=3; IntAct=EBI-2861929, EBI-64093585; CC Q8TEW8; Q9Q6P4: GP1; Xeno; NbExp=2; IntAct=EBI-2861929, EBI-66910636; CC Q8TEW8; Q81964: ORF putative E6; Xeno; NbExp=3; IntAct=EBI-2861929, EBI-64093422; CC Q8TEW8; P03409: Tax; Xeno; NbExp=2; IntAct=EBI-2861929, EBI-5236464; CC -!- SUBCELLULAR LOCATION: Endomembrane system. Cell junction. Cell CC junction, tight junction. Note=Partially localized along the cell-cell CC contact region. Colocalizes with TJP1 to epithelial tight junctions. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=Par3La, a; CC IsoId=Q8TEW8-1; Sequence=Displayed; CC Name=2; Synonyms=Par3Lb, b; CC IsoId=Q8TEW8-2; Sequence=VSP_007478; CC Name=3; Synonyms=Par3Lc, c; CC IsoId=Q8TEW8-3; Sequence=VSP_007479; CC Name=4; CC IsoId=Q8TEW8-4; Sequence=VSP_007476, VSP_007477; CC Name=5; CC IsoId=Q8TEW8-5; Sequence=VSP_007543; CC Name=6; CC IsoId=Q8TEW8-6; Sequence=VSP_054048; CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, lung and skeletal CC muscle. Expressed at intermediate levels in brain, heart, placenta, CC liver and pancreas. Isoform 1 is predominant, while isoform 2 and CC isoform 3 are expressed at lower levels. CC -!- DOMAIN: The N-terminal part (1-351) part blocks the association of the CC tight junction marker TJP1 with the cell-cell boundary when it is CC overexpressed. CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB71106.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB71623.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB053321; BAB69028.1; -; mRNA. DR EMBL; AB073472; BAC54035.1; -; mRNA. DR EMBL; AB092439; BAC54285.1; -; mRNA. DR EMBL; AF428250; AAL30664.1; -; mRNA. DR EMBL; AF428251; AAL30665.1; -; mRNA. DR EMBL; AF466152; AAL79827.1; -; mRNA. DR EMBL; AC007385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007736; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007746; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008171; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC009316; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC016903; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108468; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK056157; BAB71106.1; ALT_FRAME; mRNA. DR EMBL; AK057965; BAB71623.1; ALT_INIT; mRNA. DR CCDS; CCDS42804.1; -. [Q8TEW8-5] DR CCDS; CCDS42805.1; -. [Q8TEW8-6] DR CCDS; CCDS42806.1; -. [Q8TEW8-2] DR CCDS; CCDS77511.1; -. [Q8TEW8-1] DR RefSeq; NP_001289698.1; NM_001302769.2. [Q8TEW8-1] DR RefSeq; NP_476518.4; NM_057177.7. [Q8TEW8-6] DR RefSeq; NP_689739.4; NM_152526.6. [Q8TEW8-2] DR RefSeq; NP_995585.2; NM_205863.4. [Q8TEW8-5] DR AlphaFoldDB; Q8TEW8; -. DR SMR; Q8TEW8; -. DR BioGRID; 125592; 52. DR CORUM; Q8TEW8; -. DR DIP; DIP-42276N; -. DR FunCoup; Q8TEW8; 339. DR IntAct; Q8TEW8; 380. DR MINT; Q8TEW8; -. DR STRING; 9606.ENSP00000385848; -. DR GlyGen; Q8TEW8; 2 sites. DR iPTMnet; Q8TEW8; -. DR PhosphoSitePlus; Q8TEW8; -. DR BioMuta; PARD3B; -. DR DMDM; 30913163; -. DR jPOST; Q8TEW8; -. DR MassIVE; Q8TEW8; -. DR PaxDb; 9606-ENSP00000385848; -. DR PeptideAtlas; Q8TEW8; -. DR ProteomicsDB; 19836; -. DR ProteomicsDB; 74517; -. [Q8TEW8-1] DR ProteomicsDB; 74518; -. [Q8TEW8-2] DR ProteomicsDB; 74519; -. [Q8TEW8-3] DR ProteomicsDB; 74520; -. [Q8TEW8-4] DR ProteomicsDB; 74521; -. [Q8TEW8-5] DR Antibodypedia; 34169; 41 antibodies from 18 providers. DR DNASU; 117583; -. DR Ensembl; ENST00000349953.7; ENSP00000340280.3; ENSG00000116117.20. [Q8TEW8-5] DR Ensembl; ENST00000351153.5; ENSP00000317261.2; ENSG00000116117.20. [Q8TEW8-6] DR Ensembl; ENST00000358768.6; ENSP00000351618.2; ENSG00000116117.20. [Q8TEW8-2] DR Ensembl; ENST00000406610.7; ENSP00000385848.2; ENSG00000116117.20. [Q8TEW8-1] DR Ensembl; ENST00000415947.1; ENSP00000407718.1; ENSG00000116117.20. [Q8TEW8-4] DR GeneID; 117583; -. DR KEGG; hsa:117583; -. DR MANE-Select; ENST00000406610.7; ENSP00000385848.2; NM_001302769.2; NP_001289698.1. DR UCSC; uc002vao.3; human. [Q8TEW8-1] DR AGR; HGNC:14446; -. DR ClinPGx; PA162398721; -. DR CTD; 117583; -. DR DisGeNET; 117583; -. DR GeneCards; PARD3B; -. DR HGNC; HGNC:14446; PARD3B. DR HPA; ENSG00000116117; Low tissue specificity. DR MIM; 619353; gene. DR OpenTargets; ENSG00000116117; -. DR VEuPathDB; HostDB:ENSG00000116117; -. DR eggNOG; KOG3528; Eukaryota. DR GeneTree; ENSGT00950000183214; -. DR HOGENOM; CLU_2605385_0_0_1; -. DR InParanoid; Q8TEW8; -. DR OMA; QFQHIKA; -. DR OrthoDB; 6264899at2759; -. DR PAN-GO; Q8TEW8; 10 GO annotations based on evolutionary models. DR PhylomeDB; Q8TEW8; -. DR PathwayCommons; Q8TEW8; -. DR SignaLink; Q8TEW8; -. DR Agora; ENSG00000116117; -. DR BioGRID-ORCS; 117583; 9 hits in 1155 CRISPR screens. DR ChiTaRS; PARD3B; human. DR GeneWiki; PARD3B; -. DR GenomeRNAi; 117583; -. DR Pharos; Q8TEW8; Tbio. DR PRO; PR:Q8TEW8; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8TEW8; protein. DR Bgee; ENSG00000116117; Expressed in sural nerve and 149 other cell types or tissues. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005938; C:cell cortex; IBA:GO_Central. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central. DR GO; GO:0008104; P:intracellular protein localization; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR CDD; cd06691; PDZ1_Par3-like; 1. DR CDD; cd23058; PDZ2_Par3-like; 1. DR CDD; cd23059; PDZ3_Par3-like; 1. DR FunFam; 2.30.42.10:FF:000078; Partitioning defective 3 homolog B; 1. DR FunFam; 2.30.42.10:FF:000117; partitioning defective 3 homolog B isoform X2; 1. DR FunFam; 2.30.42.10:FF:000011; partitioning defective 3 homolog isoform X1; 1. DR FunFam; 3.10.20.90:FF:000017; partitioning defective 3 homolog isoform X2; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR InterPro; IPR052213; PAR3. DR InterPro; IPR021922; Par3/HAL_N. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR16484:SF4; PARTITIONING DEFECTIVE 3 HOMOLOG B; 1. DR PANTHER; PTHR16484; PARTITIONING DEFECTIVE 3 RELATED; 1. DR Pfam; PF12053; Par3_HAL_N_term; 1. DR Pfam; PF00595; PDZ; 2. DR SMART; SM00228; PDZ; 3. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR PROSITE; PS50106; PDZ; 3. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Cell junction; Membrane; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW Tight junction. FT CHAIN 1..1205 FT /note="Partitioning defective 3 homolog B" FT /id="PRO_0000185072" FT DOMAIN 201..289 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 383..468 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 498..585 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 83..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 137..165 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 707..743 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 784..921 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1111..1205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 329..352 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..374 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 806..822 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 838..865 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 881..921 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 100 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CSB4" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 635 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CSB4" FT MOD_RES 710 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CSB4" FT MOD_RES 728 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CSB4" FT MOD_RES 730 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CSB4" FT MOD_RES 746 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 749 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CSB4" FT MOD_RES 801 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 41..79 FT /note="GPGYWVKIHHLEYTDGGILDPDDVLADVVEDKDKLIAVF -> VSAARRSGA FT RLQPRHLPGSWLLGEDSSLRIYRWRNPGSR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11586298" FT /id="VSP_007476" FT VAR_SEQ 80..1205 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11586298" FT /id="VSP_007477" FT VAR_SEQ 479..540 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12234671" FT /id="VSP_007478" FT VAR_SEQ 729..797 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_054048" FT VAR_SEQ 730..798 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12234671" FT /id="VSP_007479" FT VAR_SEQ 914..1014 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:12459187" FT /id="VSP_007543" FT VARIANT 165 FT /note="L -> P (in dbSNP:rs1510765)" FT /evidence="ECO:0000269|PubMed:12459187, FT ECO:0000269|PubMed:14702039" FT /id="VAR_015664" FT VARIANT 192 FT /note="R -> K (in dbSNP:rs2289025)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_015665" FT VARIANT 295 FT /note="Q -> K (in dbSNP:rs1061522)" FT /id="VAR_015666" FT VARIANT 317 FT /note="K -> R (in dbSNP:rs34751010)" FT /id="VAR_056642" FT CONFLICT 893..901 FT /note="GTLKHGGLR -> WLINFVLIW (in Ref. 5; BAB71623)" FT /evidence="ECO:0000305" SQ SEQUENCE 1205 AA; 132494 MW; 26E6704CCDCE8CD8 CRC64; MKVTVCFGRT GIVVPCKEGQ LRVGELTQQA LQRYLKTREK GPGYWVKIHH LEYTDGGILD PDDVLADVVE DKDKLIAVFE EQEPLHKIES PSGNPADRQS PDAFETEVAA QLAAFKPIGG EIEVTPSALK LGTPLLVRRS SDPVPGPPAD TQPSASHPGG QSLKLVVPDS TQNLEDREVL NGVQTELLTS PRTKDTLSDM TRTVEISGEG GPLGIHVVPF FSSLSGRILG LFIRGIEDNS RSKREGLFHE NECIVKINNV DLVDKTFAQA QDVFRQAMKS PSVLLHVLPP QNREQYEKSV IGSLNIFGNN DGVLKTKVPP PVHGKSGLKT ANLTGTDSPE TDASASLQQN KSPRVPRLGG KPSSPSLSPL MGFGSNKNAK KIKIDLKKGP EGLGFTVVTR DSSIHGPGPI FVKNILPKGA AIKDGRLQSG DRILEVNGRD VTGRTQEELV AMLRSTKQGE TASLVIARQE GHFLPRELKG EPDCCALSLE TSEQLTFEIP LNDSGSAGLG VSLKGNKSRE TGTDLGIFIK SIIHGGAAFK DGRLRMNDQL IAVNGESLLG KSNHEAMETL RRSMSMEGNI RGMIQLVILR RPERPMEDPA ECGAFSKPCF ENCQNAVTTS RRNDNSILHP LGTCSPQDKQ KGLLLPNDGW AESEVPPSPT PHSALGLGLE DYSHSSGVDS AVYFPDQHIN FRSVTPARQP ESINLKASKS MDLVPDESKV HSLAGQKSES PSKDFGPTLG LKKSSSLESL QTAVAEVRKN DLPFHRPRPH MVRGRGCNES FRAAIDKSYD GPEEIEADGL SDKSSHSGQG ALNCESAPQG NSELEDMENK ARKVKKTKEK EKKKEKGKLK VKEKKRKEEN EDPERKIKKK GFGAMLRFGK KKEDKGGKAE QKGTLKHGGL REEELEKMKE ERERIGAKHQ ELREKQARGL LDYATGAIGS VYDMDDDEMD PNYARVNHFR EPCTSANVFR SPSPPRAGPF GYPRDGHPLS PERDHLEGLY AKVNKPYHPL VPADSGRPTG GSTDRIQKLR KEYYQARREG FPLYEDDEGR ARPSEYDLLW VPGRGPDGNA HNLRFEGMER QYASLPRGGP ADPVDYLPAA PRGLYKEREL PYYPGAHPMH PPKGSYPRPT ELRVADLRYP QHYPPPPAPQ HKGPFRQDVP PSPPQHQRMP AYQETGRPGP RGGSPDQYPY RTQDSRQKNP MTAAV //