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Q8TEW0

- PARD3_HUMAN

UniProt

Q8TEW0 - PARD3_HUMAN

Protein

Partitioning defective 3 homolog

Gene

PARD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
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    Functioni

    Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Targets the phosphatase PTEN to cell junctions. Involved in Schwann cell peripheral myelination By similarity. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of neuronal polarity and normal axon formation in cultured hippocampal neurons.By similarity1 Publication

    GO - Molecular functioni

    1. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    2. phosphatidylinositol-3-phosphate binding Source: UniProtKB
    3. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. apical constriction Source: Ensembl
    2. asymmetric cell division Source: ProtInc
    3. axonogenesis Source: UniProtKB
    4. cell-cell junction organization Source: Reactome
    5. cell cycle Source: UniProtKB-KW
    6. cell junction assembly Source: Reactome
    7. centrosome localization Source: Ensembl
    8. establishment of epithelial cell polarity Source: UniProtKB
    9. establishment or maintenance of cell polarity Source: UniProtKB
    10. microtubule cytoskeleton organization Source: Ensembl
    11. myelination in peripheral nervous system Source: UniProtKB
    12. negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    13. positive regulation of myelination Source: UniProtKB
    14. protein complex assembly Source: ProtInc
    15. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    16. protein targeting to membrane Source: UniProtKB
    17. regulation of actin filament-based process Source: Ensembl
    18. regulation of cellular localization Source: Ensembl
    19. tight junction assembly Source: UniProtKB
    20. transforming growth factor beta receptor signaling pathway Source: Reactome
    21. wound healing, spreading of cells Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_19373. Tight junction interactions.
    SignaLinkiQ8TEW0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Partitioning defective 3 homolog
    Short name:
    PAR-3
    Short name:
    PARD-3
    Alternative name(s):
    Atypical PKC isotype-specific-interacting protein
    Short name:
    ASIP
    CTCL tumor antigen se2-5
    PAR3-alpha
    Gene namesi
    Name:PARD3
    Synonyms:PAR3, PAR3A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:16051. PARD3.

    Subcellular locationi

    Cytoplasm By similarity. Endomembrane system 1 Publication. Cell junction 1 Publication. Cell junctiontight junction 1 Publication. Cell membrane 1 Publication. Cytoplasmcell cortex By similarity. Cytoplasmcytoskeleton 1 Publication
    Note: Localized along the cell-cell contact region. Colocalizes with PARD6A and PRKCI at epithelial tight junctions. Colocalizes with the cortical actin that overlays the meiotic spindle during metaphase I and metaphase II. Colocalized with SIRT2 in internode region of myelin sheat By similarity. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. axonal growth cone Source: Ensembl
    3. cell-cell adherens junction Source: Ensembl
    4. cell-cell junction Source: UniProtKB
    5. cell cortex Source: UniProtKB-SubCell
    6. cell junction Source: HPA
    7. cytosol Source: Reactome
    8. endomembrane system Source: UniProtKB-SubCell
    9. internode region of axon Source: UniProtKB
    10. neuronal cell body Source: Ensembl
    11. plasma membrane Source: Reactome
    12. protein complex Source: Ensembl
    13. spindle Source: Ensembl
    14. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi962 – 9621S → A: Abolishes phosphorylation by AURKA. 1 Publication
    Mutagenesisi1127 – 11271Y → F: Delayed epithelial tight junction assembly.

    Organism-specific databases

    PharmGKBiPA32936.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13561356Partitioning defective 3 homologPRO_0000185069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei383 – 3831Phosphoserine5 Publications
    Modified residuei692 – 6921Phosphoserine1 Publication
    Modified residuei695 – 6951Phosphoserine2 Publications
    Modified residuei728 – 7281Phosphoserine3 Publications
    Modified residuei809 – 8091Phosphoserine1 Publication
    Modified residuei827 – 8271PhosphoserineBy similarity
    Modified residuei834 – 8341N6-acetyllysineBy similarity
    Modified residuei851 – 8511N6-acetyllysineBy similarity
    Modified residuei852 – 8521Phosphoserine4 Publications
    Modified residuei873 – 8731Phosphoserine3 Publications
    Modified residuei885 – 8851N6-acetyllysineBy similarity
    Modified residuei962 – 9621Phosphoserine; by AURKA1 Publication
    Modified residuei1350 – 13501N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann cell peripheral myelination.1 Publication
    Phosphorylation at Ser-827 by PRKCZ and PRKCI occurs at the most apical tip of epithelial cell-cell contacts during the initial phase of tight junction formation and may promote dissociation of the complex with PARD6. EGF-induced Tyr-1127 phosphorylation mediates dissociation from LIMK2 By similarity. Phosphorylation by AURKA at Ser-962 is required for the normal establishment of neuronal polarity.By similarity6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8TEW0.
    PaxDbiQ8TEW0.
    PRIDEiQ8TEW0.

    PTM databases

    PhosphoSiteiQ8TEW0.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ8TEW0.
    BgeeiQ8TEW0.
    GenevestigatoriQ8TEW0.

    Organism-specific databases

    HPAiHPA030443.

    Interactioni

    Subunit structurei

    Interacts (via PDZ 1 domain) with F11R/JAM1, PARD6A and PARD6B. Isoform 2, but not at least isoform 3 interacts with PRKCZ. Interacts with PRCKI and CDH5. Interacts (via PDZ 3 domain) with PTEN (via C-terminus) By similarity. Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with LIMK2, AURKA and AURKB. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Directly interacts with TIAM1 and TIAM2. Interacts with ECT2, FBF1 and SIRT2.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDH5P331515EBI-81968,EBI-2903122
    CTNNB1P352222EBI-81968,EBI-491549
    F11RQ9Y6242EBI-81968,EBI-742600
    PARD6AQ9NPB68EBI-81968,EBI-81876
    PARD6BQ9BYG54EBI-81968,EBI-295391
    Pard6bQ9JK832EBI-81968,EBI-81861From a different organism.
    PARD6GQ9BYG43EBI-81968,EBI-295417
    PNMA1Q8ND904EBI-81968,EBI-302345
    PRKCIP417433EBI-81968,EBI-286199
    Tiam2Q6ZPF36EBI-9118204,EBI-7565978From a different organism.
    TP53P046373EBI-81968,EBI-366083
    YWHAHQ049176EBI-81968,EBI-306940
    YWHAZP631044EBI-81968,EBI-347088

    Protein-protein interaction databases

    BioGridi121134. 47 interactions.
    DIPiDIP-31315N.
    IntActiQ8TEW0. 38 interactions.
    MINTiMINT-7711810.

    Structurei

    Secondary structure

    1
    1356
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi458 – 4658
    Beta strandi473 – 4764
    Beta strandi481 – 4855
    Beta strandi488 – 4936
    Helixi498 – 5014
    Beta strandi507 – 5148
    Helixi524 – 53310
    Beta strandi539 – 5468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KOMNMR-A451-549[»]
    ProteinModelPortaliQ8TEW0.
    SMRiQ8TEW0. Positions 2-82, 272-358, 451-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TEW0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini271 – 35989PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini461 – 54686PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini590 – 67788PDZ 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni712 – 936225Interacts with PRKCI and PRKCZBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1049 – 107729Sequence AnalysisAdd
    BLAST
    Coiled coili1151 – 117424Sequence AnalysisAdd
    BLAST
    Coiled coili1201 – 122424Sequence AnalysisAdd
    BLAST
    Coiled coili1280 – 130122Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi984 – 104259Lys-richAdd
    BLAST

    Domaini

    Contains a conserved N-terminal oligomerization domain (NTD) that is involved in oligomerization and is essential for proper subapical membrane localization.By similarity
    The second PDZ domain mediates interaction with membranes containing phosphoinositol lipids.By similarity

    Sequence similaritiesi

    Belongs to the PAR3 family.Curated
    Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG268288.
    HOVERGENiHBG053508.
    InParanoidiQ8TEW0.
    KOiK04237.
    OMAiDEQDPHH.
    OrthoDBiEOG7WHH92.
    PhylomeDBiQ8TEW0.
    TreeFamiTF323729.

    Family and domain databases

    Gene3Di2.30.42.10. 3 hits.
    InterProiIPR021922. DUF3534.
    IPR001478. PDZ.
    [Graphical view]
    PfamiPF12053. DUF3534. 1 hit.
    PF00595. PDZ. 3 hits.
    [Graphical view]
    SMARTiSM00228. PDZ. 3 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 3 hits.
    PROSITEiPS50106. PDZ. 3 hits.
    [Graphical view]

    Sequences (11)i

    Sequence statusi: Complete.

    This entry describes 11 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TEW0-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKVTVCFGRT RVVVPCGDGH MKVFSLIQQA VTRYRKAIAK DPNYWIQVHR     50
    LEHGDGGILD LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS 100
    PEIFGSELGT NNVSAFQPYQ ATSEIEVTPS VLRANMPLHV RRSSDPALIG 150
    LSTSVSDSNF SSEEPSRKNP TRWSTTAGFL KQNTAGSPKT CDRKKDENYR 200
    SLPRDTSNWS NQFQRDNARS SLSASHPMVG KWLEKQEQDE DGTEEDNSRV 250
    EPVGHADTGL EHIPNFSLDD MVKLVEVPND GGPLGIHVVP FSARGGRTLG 300
    LLVKRLEKGG KAEHENLFRE NDCIVRINDG DLRNRRFEQA QHMFRQAMRT 350
    PIIWFHVVPA ANKEQYEQLS QSEKNNYYSS RFSPDSQYID NRSVNSAGLH 400
    TVQRAPRLNH PPEQIDSHSR LPHSAHPSGK PPSAPASAPQ NVFSTTVSSG 450
    YNTKKIGKRL NIQLKKGTEG LGFSITSRDV TIGGSAPIYV KNILPRGAAI 500
    QDGRLKAGDR LIEVNGVDLV GKSQEEVVSL LRSTKMEGTV SLLVFRQEDA 550
    FHPRELNAEP SQMQIPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG 600
    LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL 650
    LGKTNQDAME TLRRSMSTEG NKRGMIQLIV ARRISKCNEL KSPGSPPGPE 700
    LPIETALDDR ERRISHSLYS GIEGLDESPS RNAALSRIMG ESGKYQLSPT 750
    VNMPQDDTVI IEDDRLPVLP PHLSDQSSSS SHDDVGFVTA DAGTWAKAAI 800
    SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSDAS QLDFVKTRKS 850
    KSMDLGIADE TKLNTVDDQK AGSPSRDVGP SLGLKKSSSL ESLQTAVAEV 900
    TLNGDIPFHR PRPRIIRGRG CNESFRAAID KSYDKPAVDD DDEGMETLEE 950
    DTEESSRSGR ESVSTASDQP SHSLERQMNG NQEKGDKTDR KKDKTGKEKK 1000
    KDRDKEKDKM KAKKGMLKGL GDMFRFGKHR KDDKIEKTGK IKIQESFTSE 1050
    EERIRMKQEQ ERIQAKTREF RERQARERDY AEIQDFHRTF GCDDELMYGG 1100
    VSSYEGSMAL NARPQSPREG HMMDALYAQV KKPRNSKPSP VDSNRSTPSN 1150
    HDRIQRLRQE FQQAKQDEDV EDRRRTYSFE QPWPNARPAT QSGRHSVSVE 1200
    VQMQRQRQEE RESSQQAQRQ YSSLPRQSRK NASSVSQDSW EQNYSPGEGF 1250
    QSAKENPRYS SYQGSRNGYL GGHGFNARVM LETQELLRQE QRRKEQQMKK 1300
    QPPSEGPSNY DSYKKVQDPS YAPPKGPFRQ DVPPSPSQVA RLNRLQTPEK 1350
    GRPFYS 1356
    Length:1,356
    Mass (Da):151,423
    Last modified:May 16, 2003 - v2
    Checksum:iA4FD3F4F9AD8B92A
    GO
    Isoform 2 (identifier: Q8TEW0-2) [UniParc]FASTAAdd to Basket

    Also known as: B, La

    The sequence of this isoform differs from the canonical sequence as follows:
         740-742: Missing.

    Show »
    Length:1,353
    Mass (Da):151,150
    Checksum:iBC531577B9C31AE3
    GO
    Isoform 3 (identifier: Q8TEW0-3) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         195-238: Missing.
         557-569: Missing.
         740-742: Missing.
         827-856: Missing.

    Show »
    Length:1,266
    Mass (Da):141,072
    Checksum:i92DF51B68081A4A2
    GO
    Isoform 4 (identifier: Q8TEW0-4) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         1025-1061: Missing.

    Show »
    Length:1,319
    Mass (Da):146,877
    Checksum:iF5FBF3CE4E67163B
    GO
    Isoform 5 (identifier: Q8TEW0-5) [UniParc]FASTAAdd to Basket

    Also known as: E

    The sequence of this isoform differs from the canonical sequence as follows:
         195-238: Missing.
         557-569: Missing.
         740-742: Missing.
         857-857: I → S
         858-872: Missing.
         1025-1061: Missing.

    Show »
    Length:1,244
    Mass (Da):138,332
    Checksum:iC3C156C8811D49C2
    GO
    Isoform 6 (identifier: Q8TEW0-6) [UniParc]FASTAAdd to Basket

    Also known as: F

    The sequence of this isoform differs from the canonical sequence as follows:
         557-569: Missing.
         740-742: Missing.
         827-856: Missing.

    Show »
    Length:1,310
    Mass (Da):146,276
    Checksum:i57361092A273AC60
    GO
    Isoform 7 (identifier: Q8TEW0-7) [UniParc]FASTAAdd to Basket

    Also known as: Lb

    The sequence of this isoform differs from the canonical sequence as follows:
         557-569: Missing.
         740-742: Missing.
         827-856: Missing.
         1025-1061: Missing.

    Show »
    Length:1,273
    Mass (Da):141,730
    Checksum:i53C1A94D8CB7341E
    GO
    Isoform 8 (identifier: Q8TEW0-8) [UniParc]FASTAAdd to Basket

    Also known as: Sa

    The sequence of this isoform differs from the canonical sequence as follows:
         740-742: Missing.
         1025-1034: RFGKHRKDDK → SLAKLKPEKR
         1035-1356: Missing.

    Show »
    Length:1,031
    Mass (Da):113,419
    Checksum:i40DD593636EAE999
    GO
    Isoform 9 (identifier: Q8TEW0-9) [UniParc]FASTAAdd to Basket

    Also known as: Sb

    The sequence of this isoform differs from the canonical sequence as follows:
         557-569: Missing.
         740-742: Missing.
         827-856: Missing.
         1025-1034: RFGKHRKDDK → SLAKLKPEKR
         1035-1356: Missing.

    Show »
    Length:988
    Mass (Da):108,545
    Checksum:i89F2139B096F7F7F
    GO
    Isoform 10 (identifier: Q8TEW0-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         740-742: Missing.
         827-856: Missing.
         857-858: IA → T
         1025-1034: RFGKHRKDDK → SLAKLKPEKR
         1035-1356: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,000
    Mass (Da):109,917
    Checksum:i135A54F80C144606
    GO
    Isoform 11 (identifier: Q8TEW0-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         557-569: Missing.
         740-742: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,340
    Mass (Da):149,695
    Checksum:i3DAB16557C6BBA86
    GO

    Sequence cautioni

    The sequence AAG33676.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAA91366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB55330.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901T → A in BAB55330. (PubMed:14702039)Curated
    Sequence conflicti233 – 2331L → Q in BAB55330. (PubMed:14702039)Curated
    Sequence conflicti594 – 5941N → S in BAB55330. (PubMed:14702039)Curated
    Sequence conflicti764 – 7641D → N in AAH71566. (PubMed:15489334)Curated
    Sequence conflicti996 – 10005GKEKK → VELHE in BAA91366. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071E → D.
    Corresponds to variant rs1436731 [ dbSNP | Ensembl ].
    VAR_015663
    Natural varianti575 – 5751D → N.
    Corresponds to variant rs3758459 [ dbSNP | Ensembl ].
    VAR_050453

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei195 – 23844Missing in isoform 3 and isoform 5. 4 PublicationsVSP_007462Add
    BLAST
    Alternative sequencei557 – 56913Missing in isoform 3, isoform 5, isoform 6, isoform 7, isoform 9 and isoform 11. 6 PublicationsVSP_007463Add
    BLAST
    Alternative sequencei740 – 7423Missing in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11. 6 PublicationsVSP_007464
    Alternative sequencei827 – 85630Missing in isoform 3, isoform 6, isoform 7, isoform 9 and isoform 10. 4 PublicationsVSP_007465Add
    BLAST
    Alternative sequencei857 – 8582IA → T in isoform 10. 1 PublicationVSP_007467
    Alternative sequencei857 – 8571I → S in isoform 5. 2 PublicationsVSP_007466
    Alternative sequencei858 – 87215Missing in isoform 5. 2 PublicationsVSP_007468Add
    BLAST
    Alternative sequencei1025 – 106137Missing in isoform 4, isoform 5 and isoform 7. 3 PublicationsVSP_007469Add
    BLAST
    Alternative sequencei1025 – 103410RFGKHRKDDK → SLAKLKPEKR in isoform 8, isoform 9 and isoform 10. 2 PublicationsVSP_007470
    Alternative sequencei1035 – 1356322Missing in isoform 8, isoform 9 and isoform 10. 2 PublicationsVSP_007471Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF252293 mRNA. Translation: AAF71530.1.
    AF196185 mRNA. Translation: AAK27891.1.
    AF196186 mRNA. Translation: AAK27892.1.
    AF332592 mRNA. Translation: AAK69192.1.
    AF332593 mRNA. Translation: AAK69193.1.
    AB073671 mRNA. Translation: BAC54037.1.
    AF467002 mRNA. Translation: AAL76042.1.
    AF467003 mRNA. Translation: AAL76043.1.
    AF467004 mRNA. Translation: AAL76044.1.
    AF467005 mRNA. Translation: AAL76045.1.
    AF467006 mRNA. Translation: AAL76046.1.
    AL360233
    , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71161.1.
    AL360233
    , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71162.1.
    AL360233
    , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71163.1.
    AL360233
    , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71165.1.
    AL360233
    , AL138768, AL160409, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71166.1.
    AL360233
    , AL138768, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH71167.1.
    AL160409
    , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73524.1.
    AL160409
    , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73525.1.
    AL160409
    , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73526.1.
    AL160409
    , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73528.1.
    AL160409
    , AL138768, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAH73529.1.
    AL450337
    , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15036.1.
    AL450337
    , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15037.1.
    AL450337
    , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15038.1.
    AL450337
    , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15039.1.
    AL450337
    , AL138768, AL160409, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15040.1.
    AL450337
    , AL138768, AL360233, AL390766, AL392123 Genomic DNA. Translation: CAI15041.1.
    AL138768
    , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16985.1.
    AL138768
    , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16986.1.
    AL138768
    , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16987.1.
    AL138768
    , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16988.1.
    AL138768
    , AL160409, AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16989.1.
    AL138768
    , AL360233, AL390766, AL392123, AL450337 Genomic DNA. Translation: CAI16991.1.
    AL390766
    , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17304.1.
    AL390766
    , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17305.1.
    AL390766
    , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17306.1.
    AL390766
    , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17308.1.
    AL390766
    , AL138768, AL160409, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17309.1.
    AL390766
    , AL138768, AL360233, AL392123, AL450337 Genomic DNA. Translation: CAI17310.1.
    AL392123
    , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17327.1.
    AL392123
    , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17328.1.
    AL392123
    , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17329.1.
    AL392123
    , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17331.1.
    AL392123
    , AL138768, AL160409, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17332.1.
    AL392123
    , AL138768, AL360233, AL390766, AL450337 Genomic DNA. Translation: CAI17333.1.
    CH471072 Genomic DNA. Translation: EAW85932.1.
    CH471072 Genomic DNA. Translation: EAW85934.1.
    BC011711 mRNA. Translation: AAH11711.2.
    BC071566 mRNA. Translation: AAH71566.1.
    AK000761 mRNA. Translation: BAA91366.1. Different initiation.
    AK027735 mRNA. Translation: BAB55330.1. Different initiation.
    AF177228 mRNA. Translation: AAG33676.1. Sequence problems.
    CCDSiCCDS53509.1. [Q8TEW0-5]
    CCDS53510.1. [Q8TEW0-3]
    CCDS53511.1. [Q8TEW0-11]
    CCDS53512.1. [Q8TEW0-6]
    CCDS53513.1. [Q8TEW0-9]
    CCDS53514.1. [Q8TEW0-4]
    CCDS53515.1. [Q8TEW0-2]
    CCDS53516.1. [Q8TEW0-8]
    CCDS7178.1. [Q8TEW0-1]
    RefSeqiNP_001171714.1. NM_001184785.1. [Q8TEW0-2]
    NP_001171715.1. NM_001184786.1. [Q8TEW0-11]
    NP_001171716.1. NM_001184787.1. [Q8TEW0-4]
    NP_001171717.1. NM_001184788.1. [Q8TEW0-6]
    NP_001171718.1. NM_001184789.1. [Q8TEW0-7]
    NP_001171719.1. NM_001184790.1. [Q8TEW0-3]
    NP_001171720.1. NM_001184791.1. [Q8TEW0-5]
    NP_001171721.1. NM_001184792.1. [Q8TEW0-8]
    NP_001171722.1. NM_001184793.1. [Q8TEW0-10]
    NP_001171723.1. NM_001184794.1. [Q8TEW0-9]
    NP_062565.2. NM_019619.3. [Q8TEW0-1]
    UniGeneiHs.131489.

    Genome annotation databases

    EnsembliENST00000340077; ENSP00000341844; ENSG00000148498. [Q8TEW0-8]
    ENST00000346874; ENSP00000340591; ENSG00000148498. [Q8TEW0-4]
    ENST00000350537; ENSP00000311986; ENSG00000148498. [Q8TEW0-6]
    ENST00000374776; ENSP00000363908; ENSG00000148498. [Q8TEW0-9]
    ENST00000374788; ENSP00000363920; ENSG00000148498. [Q8TEW0-2]
    ENST00000374789; ENSP00000363921; ENSG00000148498. [Q8TEW0-1]
    ENST00000374794; ENSP00000363926; ENSG00000148498. [Q8TEW0-5]
    ENST00000545260; ENSP00000440857; ENSG00000148498. [Q8TEW0-3]
    ENST00000545693; ENSP00000443147; ENSG00000148498. [Q8TEW0-11]
    GeneIDi56288.
    KEGGihsa:56288.
    UCSCiuc001ixp.2. human. [Q8TEW0-10]
    uc001ixq.2. human. [Q8TEW0-9]
    uc001ixr.2. human. [Q8TEW0-8]
    uc010qej.2. human. [Q8TEW0-1]
    uc010qek.2. human. [Q8TEW0-2]
    uc010qel.2. human. [Q8TEW0-4]
    uc010qen.2. human. [Q8TEW0-6]
    uc010qeo.2. human. [Q8TEW0-7]
    uc010qep.2. human. [Q8TEW0-3]
    uc010qeq.2. human. [Q8TEW0-5]

    Polymorphism databases

    DMDMi30913162.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF252293 mRNA. Translation: AAF71530.1 .
    AF196185 mRNA. Translation: AAK27891.1 .
    AF196186 mRNA. Translation: AAK27892.1 .
    AF332592 mRNA. Translation: AAK69192.1 .
    AF332593 mRNA. Translation: AAK69193.1 .
    AB073671 mRNA. Translation: BAC54037.1 .
    AF467002 mRNA. Translation: AAL76042.1 .
    AF467003 mRNA. Translation: AAL76043.1 .
    AF467004 mRNA. Translation: AAL76044.1 .
    AF467005 mRNA. Translation: AAL76045.1 .
    AF467006 mRNA. Translation: AAL76046.1 .
    AL360233
    , AL138768 , AL160409 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH71161.1 .
    AL360233
    , AL138768 , AL160409 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH71162.1 .
    AL360233
    , AL138768 , AL160409 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH71163.1 .
    AL360233
    , AL138768 , AL160409 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH71165.1 .
    AL360233
    , AL138768 , AL160409 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH71166.1 .
    AL360233
    , AL138768 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH71167.1 .
    AL160409
    , AL138768 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH73524.1 .
    AL160409
    , AL138768 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH73525.1 .
    AL160409
    , AL138768 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH73526.1 .
    AL160409
    , AL138768 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH73528.1 .
    AL160409
    , AL138768 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAH73529.1 .
    AL450337
    , AL138768 , AL160409 , AL360233 , AL390766 , AL392123 Genomic DNA. Translation: CAI15036.1 .
    AL450337
    , AL138768 , AL160409 , AL360233 , AL390766 , AL392123 Genomic DNA. Translation: CAI15037.1 .
    AL450337
    , AL138768 , AL160409 , AL360233 , AL390766 , AL392123 Genomic DNA. Translation: CAI15038.1 .
    AL450337
    , AL138768 , AL160409 , AL360233 , AL390766 , AL392123 Genomic DNA. Translation: CAI15039.1 .
    AL450337
    , AL138768 , AL160409 , AL360233 , AL390766 , AL392123 Genomic DNA. Translation: CAI15040.1 .
    AL450337
    , AL138768 , AL360233 , AL390766 , AL392123 Genomic DNA. Translation: CAI15041.1 .
    AL138768
    , AL160409 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAI16985.1 .
    AL138768
    , AL160409 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAI16986.1 .
    AL138768
    , AL160409 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAI16987.1 .
    AL138768
    , AL160409 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAI16988.1 .
    AL138768
    , AL160409 , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAI16989.1 .
    AL138768
    , AL360233 , AL390766 , AL392123 , AL450337 Genomic DNA. Translation: CAI16991.1 .
    AL390766
    , AL138768 , AL160409 , AL360233 , AL392123 , AL450337 Genomic DNA. Translation: CAI17304.1 .
    AL390766
    , AL138768 , AL160409 , AL360233 , AL392123 , AL450337 Genomic DNA. Translation: CAI17305.1 .
    AL390766
    , AL138768 , AL160409 , AL360233 , AL392123 , AL450337 Genomic DNA. Translation: CAI17306.1 .
    AL390766
    , AL138768 , AL160409 , AL360233 , AL392123 , AL450337 Genomic DNA. Translation: CAI17308.1 .
    AL390766
    , AL138768 , AL160409 , AL360233 , AL392123 , AL450337 Genomic DNA. Translation: CAI17309.1 .
    AL390766
    , AL138768 , AL360233 , AL392123 , AL450337 Genomic DNA. Translation: CAI17310.1 .
    AL392123
    , AL138768 , AL160409 , AL360233 , AL390766 , AL450337 Genomic DNA. Translation: CAI17327.1 .
    AL392123
    , AL138768 , AL160409 , AL360233 , AL390766 , AL450337 Genomic DNA. Translation: CAI17328.1 .
    AL392123
    , AL138768 , AL160409 , AL360233 , AL390766 , AL450337 Genomic DNA. Translation: CAI17329.1 .
    AL392123
    , AL138768 , AL160409 , AL360233 , AL390766 , AL450337 Genomic DNA. Translation: CAI17331.1 .
    AL392123
    , AL138768 , AL160409 , AL360233 , AL390766 , AL450337 Genomic DNA. Translation: CAI17332.1 .
    AL392123
    , AL138768 , AL360233 , AL390766 , AL450337 Genomic DNA. Translation: CAI17333.1 .
    CH471072 Genomic DNA. Translation: EAW85932.1 .
    CH471072 Genomic DNA. Translation: EAW85934.1 .
    BC011711 mRNA. Translation: AAH11711.2 .
    BC071566 mRNA. Translation: AAH71566.1 .
    AK000761 mRNA. Translation: BAA91366.1 . Different initiation.
    AK027735 mRNA. Translation: BAB55330.1 . Different initiation.
    AF177228 mRNA. Translation: AAG33676.1 . Sequence problems.
    CCDSi CCDS53509.1. [Q8TEW0-5 ]
    CCDS53510.1. [Q8TEW0-3 ]
    CCDS53511.1. [Q8TEW0-11 ]
    CCDS53512.1. [Q8TEW0-6 ]
    CCDS53513.1. [Q8TEW0-9 ]
    CCDS53514.1. [Q8TEW0-4 ]
    CCDS53515.1. [Q8TEW0-2 ]
    CCDS53516.1. [Q8TEW0-8 ]
    CCDS7178.1. [Q8TEW0-1 ]
    RefSeqi NP_001171714.1. NM_001184785.1. [Q8TEW0-2 ]
    NP_001171715.1. NM_001184786.1. [Q8TEW0-11 ]
    NP_001171716.1. NM_001184787.1. [Q8TEW0-4 ]
    NP_001171717.1. NM_001184788.1. [Q8TEW0-6 ]
    NP_001171718.1. NM_001184789.1. [Q8TEW0-7 ]
    NP_001171719.1. NM_001184790.1. [Q8TEW0-3 ]
    NP_001171720.1. NM_001184791.1. [Q8TEW0-5 ]
    NP_001171721.1. NM_001184792.1. [Q8TEW0-8 ]
    NP_001171722.1. NM_001184793.1. [Q8TEW0-10 ]
    NP_001171723.1. NM_001184794.1. [Q8TEW0-9 ]
    NP_062565.2. NM_019619.3. [Q8TEW0-1 ]
    UniGenei Hs.131489.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KOM NMR - A 451-549 [» ]
    ProteinModelPortali Q8TEW0.
    SMRi Q8TEW0. Positions 2-82, 272-358, 451-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121134. 47 interactions.
    DIPi DIP-31315N.
    IntActi Q8TEW0. 38 interactions.
    MINTi MINT-7711810.

    PTM databases

    PhosphoSitei Q8TEW0.

    Polymorphism databases

    DMDMi 30913162.

    Proteomic databases

    MaxQBi Q8TEW0.
    PaxDbi Q8TEW0.
    PRIDEi Q8TEW0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340077 ; ENSP00000341844 ; ENSG00000148498 . [Q8TEW0-8 ]
    ENST00000346874 ; ENSP00000340591 ; ENSG00000148498 . [Q8TEW0-4 ]
    ENST00000350537 ; ENSP00000311986 ; ENSG00000148498 . [Q8TEW0-6 ]
    ENST00000374776 ; ENSP00000363908 ; ENSG00000148498 . [Q8TEW0-9 ]
    ENST00000374788 ; ENSP00000363920 ; ENSG00000148498 . [Q8TEW0-2 ]
    ENST00000374789 ; ENSP00000363921 ; ENSG00000148498 . [Q8TEW0-1 ]
    ENST00000374794 ; ENSP00000363926 ; ENSG00000148498 . [Q8TEW0-5 ]
    ENST00000545260 ; ENSP00000440857 ; ENSG00000148498 . [Q8TEW0-3 ]
    ENST00000545693 ; ENSP00000443147 ; ENSG00000148498 . [Q8TEW0-11 ]
    GeneIDi 56288.
    KEGGi hsa:56288.
    UCSCi uc001ixp.2. human. [Q8TEW0-10 ]
    uc001ixq.2. human. [Q8TEW0-9 ]
    uc001ixr.2. human. [Q8TEW0-8 ]
    uc010qej.2. human. [Q8TEW0-1 ]
    uc010qek.2. human. [Q8TEW0-2 ]
    uc010qel.2. human. [Q8TEW0-4 ]
    uc010qen.2. human. [Q8TEW0-6 ]
    uc010qeo.2. human. [Q8TEW0-7 ]
    uc010qep.2. human. [Q8TEW0-3 ]
    uc010qeq.2. human. [Q8TEW0-5 ]

    Organism-specific databases

    CTDi 56288.
    GeneCardsi GC10M034438.
    HGNCi HGNC:16051. PARD3.
    HPAi HPA030443.
    MIMi 606745. gene.
    neXtProti NX_Q8TEW0.
    PharmGKBi PA32936.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268288.
    HOVERGENi HBG053508.
    InParanoidi Q8TEW0.
    KOi K04237.
    OMAi DEQDPHH.
    OrthoDBi EOG7WHH92.
    PhylomeDBi Q8TEW0.
    TreeFami TF323729.

    Enzyme and pathway databases

    Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_19373. Tight junction interactions.
    SignaLinki Q8TEW0.

    Miscellaneous databases

    ChiTaRSi PARD3. human.
    EvolutionaryTracei Q8TEW0.
    GeneWikii PARD3.
    GenomeRNAii 56288.
    NextBioi 61959.
    PROi Q8TEW0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TEW0.
    Bgeei Q8TEW0.
    Genevestigatori Q8TEW0.

    Family and domain databases

    Gene3Di 2.30.42.10. 3 hits.
    InterProi IPR021922. DUF3534.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF12053. DUF3534. 1 hit.
    PF00595. PDZ. 3 hits.
    [Graphical view ]
    SMARTi SM00228. PDZ. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 3 hits.
    PROSITEi PS50106. PDZ. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
      Joberty G., Petersen C., Gao L., Macara I.G.
      Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PARD6B.
      Tissue: Kidney.
    2. "Down-regulated expression of atypical PKC-binding domain deleted asip isoforms in human hepatocellular carcinomas."
      Fang C.M., Xu Y.H.
      Cell Res. 11:223-229(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 7; 8 AND 9).
    3. "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions."
      Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.
      Biochem. Biophys. Res. Commun. 299:641-646(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    4. "Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties."
      Gao L., Macara I.G., Joberty G.
      Gene 294:99-107(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION WITH PARD6B AND PRKCZ, TISSUE SPECIFICITY.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1356 (ISOFORM 1).
      Tissue: Lung and Placenta.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 955-1356 (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1356 (ISOFORM 10).
      Tissue: Hepatoma and Ovarian carcinoma.
    9. "Serological detection of cutaneous T-cell lymphoma-associated antigens."
      Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.
      Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 313-992.
      Tissue: Testis.
    10. "The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1."
      Johansson A.-S., Driessens M., Aspenstroem P.
      J. Cell Sci. 113:3267-3275(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARD6A.
    11. "Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures."
      Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., Ohno S.
      J. Cell Biol. 152:1183-1196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B AND PRKCI.
      Tissue: Kidney.
    12. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity."
      Liu X.F., Ishida H., Raziuddin R., Miki T.
      Mol. Cell. Biol. 24:6665-6675(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECT2.
    14. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
      Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
      Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; MPP5 AND INADL.
    15. "The keratin-binding protein Albatross regulates polarization of epithelial cells."
      Sugimoto M., Inoko A., Shiromizu T., Nakayama M., Zou P., Yonemura S., Hayashi Y., Izawa I., Sasoh M., Uji Y., Kaibuchi K., Kiyono T., Inagaki M.
      J. Cell Biol. 183:19-28(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBF1.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-692; SER-695; SER-728; SER-809; SER-852 AND SER-873, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Phosphorylation of the par polarity complex protein Par3 at serine 962 is mediated by aurora A and regulates its function in neuronal polarity."
      Khazaei M.R., Puschel A.W.
      J. Biol. Chem. 284:33571-33579(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AURKA AND AURKB, FUNCTION, MUTAGENESIS OF SER-962, PHOSPHORYLATION AT SER-962.
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-728 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "CCM1 regulates vascular-lumen organization by inducing endothelial polarity."
      Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E.
      J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-728; SER-852 AND SER-873, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling."
      Beirowski B., Gustin J., Armour S.M., Yamamoto H., Viader A., North B.J., Michan S., Baloh R.H., Golden J.P., Schmidt R.E., Sinclair D.A., Auwerx J., Milbrandt J.
      Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, DEACETYLATION BY SIRT2, INTERACTION WITH SIRT2.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-852 AND SER-873, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "High-resolution structure of the Tiam1 PHn-CC-Ex domain."
      Joshi M., Gakhar L., Fuentes E.J.
      Acta Crystallogr. F 69:744-752(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIAM1.
    26. "Rapid, robotic, small-scale protein production for NMR screening and structure determination."
      Jensen D.R., Woytovich C., Li M., Duvnjak P., Cassidy M.S., Frederick R.O., Bergeman L.F., Peterson F.C., Volkman B.F.
      Protein Sci. 19:570-578(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 451-549.

    Entry informationi

    Entry nameiPARD3_HUMAN
    AccessioniPrimary (citable) accession number: Q8TEW0
    Secondary accession number(s): F5H5T0
    , Q5T2U1, Q5VUA2, Q5VUA3, Q5VWV0, Q5VWV1, Q5VWV3, Q5VWV4, Q5VWV5, Q6IQ47, Q8TCZ9, Q8TEW1, Q8TEW2, Q8TEW3, Q96K28, Q96RM6, Q96RM7, Q9BY57, Q9BY58, Q9HC48, Q9NWL4, Q9NYE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Antibodies against PARD3 are present in sera from patients with cutaneous T-cell lymphomas.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3