PAR6B_HUMAN
ID PAR6B_HUMAN Reviewed; 372 AA.
AC Q9BYG5; A2A2A7; Q9Y510;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Partitioning defective 6 homolog beta;
DE Short=PAR-6 beta;
DE Short=PAR-6B;
GN Name=PARD6B; Synonyms=PAR6B;
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 INTERACTION WITH PRKCI; PRKCZ;
RP RAC1 AND CDC42.
RC TISSUE=Neuroblastoma;
RX PubMed=11260256; DOI=10.1046/j.1365-2443.2001.00404.x;
RA Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.;
RT "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6
RT as an adaptor that links the small GTPases Rac and Cdc42 to atypical
RT protein kinase C.";
RL Genes Cells 6:107-119(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Noda Y., Kohjima M., Izaki T., Sumimoto H.;
RT "Splicing variants of the cell polarity protein PAR-6.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 PARD3B AND PARD3.
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 [6]
RP INTERACTION WITH LLGL1 AND PRKCI.
RX PubMed=12725730; DOI=10.1016/s0960-9822(03)00244-6;
RA Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A., Hirose T.,
RA Iwamatsu A., Shinohara A., Ohno S.;
RT "Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of
RT PAR-3 to regulate epithelial cell polarity.";
RL Curr. Biol. 13:734-743(2003).
RN [7]
RP INTERACTION WITH ECT2.
RX PubMed=15254234; DOI=10.1128/mcb.24.15.6665-6675.2004;
RA Liu X.F., Ishida H., Raziuddin R., Miki T.;
RT "Nucleotide exchange factor ECT2 interacts with the polarity protein
RT complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta
RT activity.";
RL Mol. Cell. Biol. 24:6665-6675(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes. Probably involved in formation of
CC epithelial tight junctions. Association with PARD3 may prevent the
CC interaction of PARD3 with F11R/JAM1, thereby preventing tight junction
CC assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to
CC atypical protein kinase C proteins.
CC -!- SUBUNIT: Interacts with PARD3. Interacts with GTP-bound forms of CDC42
CC and RAC1. Interacts with GTP-bound RHOQ/TC10. Interacts with PALS1 (By
CC similarity). Interacts with the N-terminal part of PRKCI and PRKCZ.
CC Part of a complex with PARD3, CDC42 or RAC1 and PRKCI or PRKCZ. Part of
CC a complex with LLGL1 and PRKCI. Interacts with PARD3B. Interacts with
CC ECT2. {ECO:0000250, ECO:0000269|PubMed:11260256,
CC ECO:0000269|PubMed:12234671, ECO:0000269|PubMed:12725730,
CC ECO:0000269|PubMed:15254234}.
CC -!- INTERACTION:
CC Q9BYG5; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-295391, EBI-11524452;
CC Q9BYG5; P60953: CDC42; NbExp=18; IntAct=EBI-295391, EBI-81752;
CC Q9BYG5; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-295391, EBI-1773949;
CC Q9BYG5; Q8TAP6: CEP76; NbExp=6; IntAct=EBI-295391, EBI-742887;
CC Q9BYG5; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-295391, EBI-10172181;
CC Q9BYG5; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-295391, EBI-13213391;
CC Q9BYG5; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-295391, EBI-2548508;
CC Q9BYG5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-295391, EBI-618309;
CC Q9BYG5; O75031: HSF2BP; NbExp=3; IntAct=EBI-295391, EBI-7116203;
CC Q9BYG5; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-295391, EBI-746778;
CC Q9BYG5; Q8TEW0: PARD3; NbExp=5; IntAct=EBI-295391, EBI-81968;
CC Q9BYG5; Q8ND90: PNMA1; NbExp=2; IntAct=EBI-295391, EBI-302345;
CC Q9BYG5; P41743: PRKCI; NbExp=22; IntAct=EBI-295391, EBI-286199;
CC Q9BYG5; Q05513: PRKCZ; NbExp=14; IntAct=EBI-295391, EBI-295351;
CC Q9BYG5; P63000: RAC1; NbExp=3; IntAct=EBI-295391, EBI-413628;
CC Q9BYG5; P60763: RAC3; NbExp=3; IntAct=EBI-295391, EBI-767084;
CC Q9BYG5; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-295391, EBI-2845202;
CC Q9BYG5; Q9H4E5: RHOJ; NbExp=6; IntAct=EBI-295391, EBI-6285694;
CC Q9BYG5; P17081: RHOQ; NbExp=3; IntAct=EBI-295391, EBI-689202;
CC Q9BYG5; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-295391, EBI-492476;
CC Q9BYG5; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-295391, EBI-17716262;
CC Q9BYG5; Q04917: YWHAH; NbExp=3; IntAct=EBI-295391, EBI-306940;
CC Q9BYG5; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-295391, EBI-7252920;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BYG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BYG5-2; Sequence=VSP_053311, VSP_053312;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas and in both adult and fetal
CC kidney. Weakly expressed in placenta and lung. Not expressed in other
CC tissues.
CC -!- DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required
CC for the interaction with Rho small GTPases.
CC -!- DOMAIN: The PDZ domain mediates interaction with PALS1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAR6 family. {ECO:0000305}.
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DR EMBL; AB044555; BAB40756.1; -; mRNA.
DR EMBL; AB178534; BAF92013.1; -; mRNA.
DR EMBL; AL031680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060847; AAH60847.1; -; mRNA.
DR CCDS; CCDS33485.1; -. [Q9BYG5-1]
DR RefSeq; NP_115910.1; NM_032521.2. [Q9BYG5-1]
DR AlphaFoldDB; Q9BYG5; -.
DR SMR; Q9BYG5; -.
DR BioGRID; 124145; 105.
DR ComplexPortal; CPX-6193; PAR cell polarity complex, PARD6B-PRKCI variant.
DR ComplexPortal; CPX-6196; PAR cell polarity complex, PARD6B-PRKCZ variant.
DR CORUM; Q9BYG5; -.
DR IntAct; Q9BYG5; 88.
DR MINT; Q9BYG5; -.
DR STRING; 9606.ENSP00000360672; -.
DR iPTMnet; Q9BYG5; -.
DR PhosphoSitePlus; Q9BYG5; -.
DR BioMuta; PARD6B; -.
DR DMDM; 30913176; -.
DR EPD; Q9BYG5; -.
DR jPOST; Q9BYG5; -.
DR MassIVE; Q9BYG5; -.
DR MaxQB; Q9BYG5; -.
DR PaxDb; Q9BYG5; -.
DR PeptideAtlas; Q9BYG5; -.
DR PRIDE; Q9BYG5; -.
DR ProteomicsDB; 187; -.
DR ProteomicsDB; 79639; -. [Q9BYG5-1]
DR Antibodypedia; 2853; 154 antibodies from 29 providers.
DR DNASU; 84612; -.
DR Ensembl; ENST00000371610.7; ENSP00000360672.2; ENSG00000124171.9. [Q9BYG5-1]
DR Ensembl; ENST00000396039.1; ENSP00000379354.1; ENSG00000124171.9. [Q9BYG5-2]
DR GeneID; 84612; -.
DR KEGG; hsa:84612; -.
DR MANE-Select; ENST00000371610.7; ENSP00000360672.2; NM_032521.3; NP_115910.1.
DR UCSC; uc002xvo.3; human. [Q9BYG5-1]
DR CTD; 84612; -.
DR GeneCards; PARD6B; -.
DR HGNC; HGNC:16245; PARD6B.
DR HPA; ENSG00000124171; Tissue enhanced (kidney).
DR MIM; 608975; gene.
DR neXtProt; NX_Q9BYG5; -.
DR OpenTargets; ENSG00000124171; -.
DR PharmGKB; PA32938; -.
DR VEuPathDB; HostDB:ENSG00000124171; -.
DR eggNOG; KOG3606; Eukaryota.
DR GeneTree; ENSGT00950000183211; -.
DR HOGENOM; CLU_040653_2_0_1; -.
DR InParanoid; Q9BYG5; -.
DR OMA; HGASSGC; -.
DR OrthoDB; 825211at2759; -.
DR PhylomeDB; Q9BYG5; -.
DR TreeFam; TF312899; -.
DR PathwayCommons; Q9BYG5; -.
DR Reactome; R-HSA-420029; Tight junction interactions.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR SignaLink; Q9BYG5; -.
DR BioGRID-ORCS; 84612; 89 hits in 1081 CRISPR screens.
DR ChiTaRS; PARD6B; human.
DR GeneWiki; PARD6B; -.
DR GenomeRNAi; 84612; -.
DR Pharos; Q9BYG5; Tbio.
DR PRO; PR:Q9BYG5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BYG5; protein.
DR Bgee; ENSG00000124171; Expressed in germinal epithelium of ovary and 142 other tissues.
DR Genevisible; Q9BYG5; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0070160; C:tight junction; IC:ComplexPortal.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; TAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; TAS:UniProtKB.
DR GO; GO:0060341; P:regulation of cellular localization; IBA:GO_Central.
DR CDD; cd06403; PB1_Par6; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR034873; PAR-6B.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034868; PB1_Par6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14102:SF4; PTHR14102:SF4; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell junction;
KW Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..372
FT /note="Partitioning defective 6 homolog beta"
FT /id="PRO_0000112516"
FT DOMAIN 16..96
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 133..150
FT /note="Pseudo-CRIB"
FT DOMAIN 157..250
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 126..253
FT /note="Interaction with PARD3 and CDC42"
FT /evidence="ECO:0000250"
FT REGION 253..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 97..113
FT /note="EEADYSAFGTDTLIKKK -> GCVLEHSKNNVRMPCLK (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053311"
FT VAR_SEQ 114..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053312"
SQ SEQUENCE 372 AA; 41182 MW; 79B5392D72B15BDC CRC64;
MNRSHRHGAG SGCLGTMEVK SKFGAEFRRF SLERSKPGKF EEFYGLLQHV HKIPNVDVLV
GYADIHGDLL PINNDDNYHK AVSTANPLLR IFIQKKEEAD YSAFGTDTLI KKKNVLTNVL
RPDNHRKKPH IVISMPQDFR PVSSIIDVDI LPETHRRVRL YKYGTEKPLG FYIRDGSSVR
VTPHGLEKVP GIFISRLVPG GLAQSTGLLA VNDEVLEVNG IEVSGKSLDQ VTDMMIANSR
NLIITVRPAN QRNNVVRNSR TSGSSGQSTD NSLLGYPQQI EPSFEPEDED SEEDDIIIED
NGVPQQIPKA VPNTESLESL TQIELSFESG QNGFIPSNEV SLAAIASSSN TEFETHAPDQ
KLLEEDGTII TL
