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Q8TEW0

- PARD3_HUMAN

UniProt

Q8TEW0 - PARD3_HUMAN

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Protein

Partitioning defective 3 homolog

Gene

PARD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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: Ensembl
  6. cell junction Source: HPA
  7. cytosol Source: Reactome
  8. internode region of axon Source: UniProtKB
  9. neuronal cell body Source: Ensembl
  10. plasma membrane Source: Reactome
  11. protein complex Source: Ensembl
  12. spindle Source: Ensembl
  13. tight junction Source: UniProtKB
Complete GO annotation...

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

BgeeiQ8TEW0.
ExpressionAtlasiQ8TEW0. baseline and differential.
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. 49 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 – 4658Combined sources
Beta strandi473 – 4764Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi488 – 4936Combined sources
Helixi498 – 5014Combined sources
Beta strandi507 – 5148Combined sources
Helixi524 – 53310Combined sources
Beta strandi539 – 5468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KOMNMR-A451-549[»]
ProteinModelPortaliQ8TEW0.
SMRiQ8TEW0. Positions 2-82, 280-348, 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.
GeneTreeiENSGT00760000119017.
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

        10         20         30         40         50
MKVTVCFGRT RVVVPCGDGH MKVFSLIQQA VTRYRKAIAK DPNYWIQVHR
60 70 80 90 100
LEHGDGGILD LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS
110 120 130 140 150
PEIFGSELGT NNVSAFQPYQ ATSEIEVTPS VLRANMPLHV RRSSDPALIG
160 170 180 190 200
LSTSVSDSNF SSEEPSRKNP TRWSTTAGFL KQNTAGSPKT CDRKKDENYR
210 220 230 240 250
SLPRDTSNWS NQFQRDNARS SLSASHPMVG KWLEKQEQDE DGTEEDNSRV
260 270 280 290 300
EPVGHADTGL EHIPNFSLDD MVKLVEVPND GGPLGIHVVP FSARGGRTLG
310 320 330 340 350
LLVKRLEKGG KAEHENLFRE NDCIVRINDG DLRNRRFEQA QHMFRQAMRT
360 370 380 390 400
PIIWFHVVPA ANKEQYEQLS QSEKNNYYSS RFSPDSQYID NRSVNSAGLH
410 420 430 440 450
TVQRAPRLNH PPEQIDSHSR LPHSAHPSGK PPSAPASAPQ NVFSTTVSSG
460 470 480 490 500
YNTKKIGKRL NIQLKKGTEG LGFSITSRDV TIGGSAPIYV KNILPRGAAI
510 520 530 540 550
QDGRLKAGDR LIEVNGVDLV GKSQEEVVSL LRSTKMEGTV SLLVFRQEDA
560 570 580 590 600
FHPRELNAEP SQMQIPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG
610 620 630 640 650
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL
660 670 680 690 700
LGKTNQDAME TLRRSMSTEG NKRGMIQLIV ARRISKCNEL KSPGSPPGPE
710 720 730 740 750
LPIETALDDR ERRISHSLYS GIEGLDESPS RNAALSRIMG ESGKYQLSPT
760 770 780 790 800
VNMPQDDTVI IEDDRLPVLP PHLSDQSSSS SHDDVGFVTA DAGTWAKAAI
810 820 830 840 850
SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSDAS QLDFVKTRKS
860 870 880 890 900
KSMDLGIADE TKLNTVDDQK AGSPSRDVGP SLGLKKSSSL ESLQTAVAEV
910 920 930 940 950
TLNGDIPFHR PRPRIIRGRG CNESFRAAID KSYDKPAVDD DDEGMETLEE
960 970 980 990 1000
DTEESSRSGR ESVSTASDQP SHSLERQMNG NQEKGDKTDR KKDKTGKEKK
1010 1020 1030 1040 1050
KDRDKEKDKM KAKKGMLKGL GDMFRFGKHR KDDKIEKTGK IKIQESFTSE
1060 1070 1080 1090 1100
EERIRMKQEQ ERIQAKTREF RERQARERDY AEIQDFHRTF GCDDELMYGG
1110 1120 1130 1140 1150
VSSYEGSMAL NARPQSPREG HMMDALYAQV KKPRNSKPSP VDSNRSTPSN
1160 1170 1180 1190 1200
HDRIQRLRQE FQQAKQDEDV EDRRRTYSFE QPWPNARPAT QSGRHSVSVE
1210 1220 1230 1240 1250
VQMQRQRQEE RESSQQAQRQ YSSLPRQSRK NASSVSQDSW EQNYSPGEGF
1260 1270 1280 1290 1300
QSAKENPRYS SYQGSRNGYL GGHGFNARVM LETQELLRQE QRRKEQQMKK
1310 1320 1330 1340 1350
QPPSEGPSNY DSYKKVQDPS YAPPKGPFRQ DVPPSPSQVA RLNRLQTPEK

GRPFYS
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.Curated
The sequence BAA91366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB55330.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KOM NMR - A 451-549 [» ]
ProteinModelPortali Q8TEW0.
SMRi Q8TEW0. Positions 2-82, 280-348, 451-719.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121134. 49 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.
GeneTreei ENSGT00760000119017.
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

Bgeei Q8TEW0.
ExpressionAtlasi Q8TEW0. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 138 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