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Protein

Partitioning defective 3 homolog

Gene

Pard3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. 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 similarity). Involved in Schwann cell peripheral myelination.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • apical constriction Source: MGI
  • bicellular tight junction assembly Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • centrosome localization Source: MGI
  • establishment of epithelial cell polarity Source: UniProtKB
  • establishment or maintenance of cell polarity Source: UniProtKB
  • microtubule cytoskeleton organization Source: MGI
  • myelination in peripheral nervous system Source: UniProtKB
  • negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of myelination Source: UniProtKB
  • positive regulation of receptor internalization Source: CACAO
  • protein targeting to membrane Source: UniProtKB
  • regulation of actin filament-based process Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • wound healing, spreading of cells Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Differentiation

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-420029. Tight junction interactions.

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
Ephrin-interacting protein
Short name:
PHIP
Gene namesi
Name:Pard3
Synonyms:Par3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2135608. Pard3.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: MGI
  • apical part of cell Source: MGI
  • bicellular tight junction Source: UniProtKB
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: UniProtKB
  • cell cortex Source: MGI
  • cell junction Source: MGI
  • cytoplasm Source: MGI
  • endomembrane system Source: UniProtKB-SubCell
  • internode region of axon Source: UniProtKB
  • lateral loop Source: BHF-UCL
  • plasma membrane Source: UniProtKB-SubCell
  • protein complex Source: MGI
  • Schmidt-Lanterman incisure Source: BHF-UCL
  • spindle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi824 – 8263SMS → AMA or EME: Strongly reduces phosphorylation by PRKCZ and abolishes interaction with PKRCI. 1 Publication
Mutagenesisi831 – 8311K → A: Inhibits Schwann cell peripheral myelination; when associated with A-848; A-881 and A-1327. 1 Publication
Mutagenesisi848 – 8481K → A: Inhibits Schwann cell peripheral myelination; when associated with A-831; A-881 and A-1327. 1 Publication
Mutagenesisi881 – 8811K → A: Inhibits Schwann cell peripheral myelination; when associated with A-831; A-848 and A-1327. 1 Publication
Mutagenesisi1327 – 13271K → A: Inhibits Schwann cell peripheral myelination; when associated with A-831; A-848 and A-881. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13331333Partitioning defective 3 homologPRO_0000185070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei91 – 911PhosphothreonineBy similarity
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei489 – 4891PhosphotyrosineBy similarity
Modified residuei692 – 6921PhosphoserineBy similarity
Modified residuei695 – 6951PhosphoserineBy similarity
Modified residuei715 – 7151PhosphoserineBy similarity
Modified residuei728 – 7281PhosphoserineCombined sources
Modified residuei806 – 8061PhosphoserineBy similarity
Modified residuei824 – 8241PhosphoserineBy similarity
Modified residuei831 – 8311N6-acetyllysine1 Publication
Modified residuei834 – 8341PhosphoserineBy similarity
Modified residuei848 – 8481N6-acetyllysine1 Publication
Modified residuei849 – 8491PhosphoserineBy similarity
Modified residuei869 – 8691PhosphoserineBy similarity
Modified residuei881 – 8811N6-acetyllysine1 Publication
Modified residuei958 – 9581Phosphoserine; by AURKABy similarity
Modified residuei967 – 9671PhosphoserineBy similarity
Modified residuei969 – 9691PhosphoserineBy similarity
Modified residuei1042 – 10421PhosphoserineBy similarity
Modified residuei1327 – 13271N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann cell peripheral myelination.1 Publication
Phosphorylation at Ser-824 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-1123 phosphorylation mediates dissociation from LIMK2 (By similarity). Phosphorylation by AURKA at Ser-958 is required for the normal establishment of neuronal polarity (By similarity). Isoform 4 and isoform 5 are phosphorylated during oocyte maturation (Probable).By similarityCurated

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99NH2.
PaxDbiQ99NH2.
PeptideAtlasiQ99NH2.
PRIDEiQ99NH2.

PTM databases

iPTMnetiQ99NH2.
PhosphoSiteiQ99NH2.

Expressioni

Tissue specificityi

All isoforms are expressed in heart, while expression in brain is mainly limited to isoform 1, and to isoform 3 to a weaker level.

Developmental stagei

At the protein level, isoform 4 expression increases steadily throughout oocyte maturation, whereas isoform 5 expression decreases in the egg as compared to the oocyte. Isoform 1 and isoform 3 are expressed from E 9.5 to E14.5, while isoform 2 is not expressed.1 Publication

Gene expression databases

BgeeiQ99NH2.
ExpressionAtlasiQ99NH2. baseline and differential.
GenevisibleiQ99NH2. MM.

Interactioni

Subunit structurei

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). 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. Interacts with ECT2 and FBF1 (By similarity). Interacts (via PDZ 1 domain) with F11R/JAM1, PARD6A and PARD6B. Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Directly interacts with TIAM1 and TIAM2. Interacts with SIRT2.By similarity6 Publications

GO - Molecular functioni

  • protein kinase C binding Source: MGI

Protein-protein interaction databases

BioGridi220283. 6 interactions.
DIPiDIP-41727N.
IntActiQ99NH2. 4 interactions.
MINTiMINT-254636.
STRINGi10090.ENSMUSP00000124282.

Structurei

Secondary structure

1
1333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi454 – 4563Combined sources
Beta strandi458 – 4658Combined sources
Beta strandi473 – 4775Combined sources
Beta strandi481 – 4866Combined sources
Beta strandi488 – 4936Combined sources
Beta strandi495 – 4973Combined sources
Helixi498 – 5025Combined sources
Beta strandi510 – 5145Combined sources
Helixi524 – 53310Combined sources
Beta strandi537 – 54610Combined sources
Beta strandi584 – 59512Combined sources
Beta strandi597 – 61014Combined sources
Turni611 – 6144Combined sources
Beta strandi615 – 62410Combined sources
Beta strandi626 – 6283Combined sources
Helixi629 – 6324Combined sources
Beta strandi641 – 6455Combined sources
Helixi655 – 66814Combined sources
Helixi670 – 6734Combined sources
Beta strandi674 – 68310Combined sources
Beta strandi685 – 6873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KOHNMR-A581-689[»]
2KOJNMR-A450-558[»]
ProteinModelPortaliQ99NH2.
SMRiQ99NH2. Positions 2-82, 448-558, 581-689.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99NH2.

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 coili1046 – 107833Sequence analysisAdd
BLAST
Coiled coili1145 – 116824Sequence analysisAdd
BLAST
Coiled coili1195 – 121824Sequence analysisAdd
BLAST
Coiled coili1274 – 129522Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi980 – 103859Lys-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

eggNOGiENOG410ITAJ. Eukaryota.
ENOG410ZDVK. LUCA.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000232109.
HOVERGENiHBG053508.
InParanoidiQ99NH2.
KOiK04237.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
InterProiIPR021922. DUF3534.
IPR001478. PDZ.
[Graphical view]
PfamiPF12053. DUF3534. 1 hit.
PF00595. PDZ. 2 hits.
[Graphical view]
SMARTiSM00228. PDZ. 3 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 3 hits.
PROSITEiPS50106. PDZ. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99NH2-1) [UniParc]FASTAAdd to basket

Also known as: 180 kDa

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 RVVVPCGDGR MKVFSLIQQA VTRYRKAVAK DPNYWIQVHR
60 70 80 90 100
LEHGDGGILD LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASFTGTQS
110 120 130 140 150
PEIFGSELGT NNVSAFQPYQ ATSEIEVTPS VLRANMPLHV RRSSDPALTG
160 170 180 190 200
LSTSVSDNNF SSEEPSRKNP TRWSTTAGFL KQNTAGSPKT CDRKKDENYR
210 220 230 240 250
SLPRDPSSWS NQFQRDNARS SLSASHPMVD RWLEKQEQDE EGTEEDSSRV
260 270 280 290 300
EPVGHADTGL ENMPNFSLDD MVKLVQVPND GGPLGIHVVP FSARGGRTLG
310 320 330 340 350
LLVKRLEKGG KAEQENLFHE NDCIVRINDG DLRNRRFEQA QHMFRQAMRA
360 370 380 390 400
RVIWFHVVPA ANKEQYEQLS QREKNNYSPG RFSPDSHCVA NRSVANNAPQ
410 420 430 440 450
ALPRAPRLSQ PPEQLDAHPR LPHSAHASTK PPAAPALAPP SVLSTNVGSV
460 470 480 490 500
YNTKKVGKRL NIQLKKGTEG LGFSITSRDV TIGGSAPIYV KNILPRGAAI
510 520 530 540 550
QDGRLKAGDR LIEVNGVDLA GKSQEEVVSL LRSTKMEGTV SLLVFRQEEA
560 570 580 590 600
FHPREMNAEP SQMQTPKETK AEDEDVVLTP DGTREFLTFE VPLNDSGSAG
610 620 630 640 650
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL
660 670 680 690 700
LGKANQEAME TLRRSMSTEG NKRGMIQLIV ARRISRCNEL RSPGSPAAPE
710 720 730 740 750
LPIETELDDR ERRISHSLYS GIEGLDESPT RNAALSRIMG KCQLSPTVNM
760 770 780 790 800
PHDDTVMIED DRLPVLPPHL SDQSSSSSHD DVGFIMTEAG TWAKATISDS
810 820 830 840 850
ADCSLSPDVD PVLAFQREGF GRQSMSEKRT KQFSDASQLD FVKTRKSKSM
860 870 880 890 900
DLVADETKLN TVDDQRAGSP SRDVGPSLGL KKSSSLESLQ TAVAEVTLNG
910 920 930 940 950
NIPFHRPRPR IIRGRGCNES FRAAIDKSYD KPMVDDDDEG METLEEDTEE
960 970 980 990 1000
SSRSGRESVS TSSDQPSYSL ERQMNGDPEK RDKTERKKDK AGKDKKKDRE
1010 1020 1030 1040 1050
KEKDKLKAKK GMLKGLGDMF RFGKHRKDDK MEKMGRIKIQ DSFTSEEDRV
1060 1070 1080 1090 1100
RMKEEQERIQ AKTREFRERQ ARERDYAEIQ DFHRTFGCDD ELLYGGMSSY
1110 1120 1130 1140 1150
EGCLALNARP QSPREGHLMD TLYAQVKKPR SSKPGDSNRS TPSNHDRIQR
1160 1170 1180 1190 1200
LRQEFQQAKQ DEDVEDRRRT YSFEQSWSSS RPASQSGRHS VSVEVQVQRQ
1210 1220 1230 1240 1250
RQEERESFQQ AQRQYSSLPR QSRKNASSIS QDSWEQNYAP GEGFQSAKEN
1260 1270 1280 1290 1300
PRYSSYQGSR NGYLGGHGFN ARVMLETQEL LRQEQRRKEQ QLKKQPPADG
1310 1320 1330
VRGPFRQDVP PSPSQVARLN RLQTPEKGRP FYS
Length:1,333
Mass (Da):149,075
Last modified:November 25, 2008 - v2
Checksum:i1DD680EE824C3837
GO
Isoform 2 (identifier: Q99NH2-2) [UniParc]FASTAAdd to basket

Also known as: 150 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1030-1333: Missing.

Show »
Length:1,029
Mass (Da):113,505
Checksum:i39B0912262E1EFCB
GO
Isoform 3 (identifier: Q99NH2-3) [UniParc]FASTAAdd to basket

Also known as: 100 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     741-744: KCQL → ESGT
     745-1333: Missing.

Show »
Length:744
Mass (Da):81,660
Checksum:i1B857E25F96A6C2B
GO
Isoform 4 (identifier: Q99NH2-4) [UniParc]FASTAAdd to basket

Also known as: PAR-3o1, Partitioning defective 3 oocyte form 1

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
     1021-1030: RFGKHRKDDK → SLAKLKPEKR
     1031-1333: Missing.

Show »
Length:895
Mass (Da):98,737
Checksum:i12807D70707852A3
GO
Isoform 5 (identifier: Q99NH2-5) [UniParc]FASTAAdd to basket

Also known as: PAR-3o2, Partitioning defective 3 oocyte form 2

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
     741-741: K → T
     742-1333: Missing.

Show »
Length:606
Mass (Da):66,609
Checksum:iEAA4320A1C682CAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti477 – 4771S → C in BAC29670 (PubMed:16141072).Curated
Sequence conflicti853 – 8531V → GI in AAX48909 (PubMed:15766746).Curated
Sequence conflicti1009 – 10091K → N in AAK07669 (PubMed:10934475).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 135135Missing in isoform 4 and isoform 5. 1 PublicationVSP_035895Add
BLAST
Alternative sequencei741 – 7444KCQL → ESGT in isoform 3. 2 PublicationsVSP_007472
Alternative sequencei741 – 7411K → T in isoform 5. 1 PublicationVSP_035896
Alternative sequencei742 – 1333592Missing in isoform 5. 1 PublicationVSP_035897Add
BLAST
Alternative sequencei745 – 1333589Missing in isoform 3. 2 PublicationsVSP_007473Add
BLAST
Alternative sequencei1021 – 103010RFGKHRKDDK → SLAKLKPEKR in isoform 4. 1 PublicationVSP_035898
Alternative sequencei1030 – 1333304Missing in isoform 2. 1 PublicationVSP_007474Add
BLAST
Alternative sequencei1031 – 1333303Missing in isoform 4. 1 PublicationVSP_035899Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY026057 mRNA. Translation: AAK07669.1.
AY856081 mRNA. Translation: AAX48908.1.
AY856082 mRNA. Translation: AAX48909.1.
AK037015 mRNA. Translation: BAC29670.1.
CCDSiCCDS22788.1. [Q99NH2-1]
CCDS40523.1. [Q99NH2-5]
RefSeqiNP_001013598.1. NM_001013580.3. [Q99NH2-5]
NP_001013599.1. NM_001013581.2.
UniGeneiMm.299254.

Genome annotation databases

EnsembliENSMUST00000108752; ENSMUSP00000104383; ENSMUSG00000025812. [Q99NH2-5]
ENSMUST00000160717; ENSMUSP00000125612; ENSMUSG00000025812. [Q99NH2-5]
GeneIDi93742.
KEGGimmu:93742.
UCSCiuc009nzk.2. mouse. [Q99NH2-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY026057 mRNA. Translation: AAK07669.1.
AY856081 mRNA. Translation: AAX48908.1.
AY856082 mRNA. Translation: AAX48909.1.
AK037015 mRNA. Translation: BAC29670.1.
CCDSiCCDS22788.1. [Q99NH2-1]
CCDS40523.1. [Q99NH2-5]
RefSeqiNP_001013598.1. NM_001013580.3. [Q99NH2-5]
NP_001013599.1. NM_001013581.2.
UniGeneiMm.299254.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KOHNMR-A581-689[»]
2KOJNMR-A450-558[»]
ProteinModelPortaliQ99NH2.
SMRiQ99NH2. Positions 2-82, 448-558, 581-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220283. 6 interactions.
DIPiDIP-41727N.
IntActiQ99NH2. 4 interactions.
MINTiMINT-254636.
STRINGi10090.ENSMUSP00000124282.

PTM databases

iPTMnetiQ99NH2.
PhosphoSiteiQ99NH2.

Proteomic databases

MaxQBiQ99NH2.
PaxDbiQ99NH2.
PeptideAtlasiQ99NH2.
PRIDEiQ99NH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108752; ENSMUSP00000104383; ENSMUSG00000025812. [Q99NH2-5]
ENSMUST00000160717; ENSMUSP00000125612; ENSMUSG00000025812. [Q99NH2-5]
GeneIDi93742.
KEGGimmu:93742.
UCSCiuc009nzk.2. mouse. [Q99NH2-5]

Organism-specific databases

CTDi56288.
MGIiMGI:2135608. Pard3.

Phylogenomic databases

eggNOGiENOG410ITAJ. Eukaryota.
ENOG410ZDVK. LUCA.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000232109.
HOVERGENiHBG053508.
InParanoidiQ99NH2.
KOiK04237.

Enzyme and pathway databases

ReactomeiR-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-420029. Tight junction interactions.

Miscellaneous databases

ChiTaRSiPard3. mouse.
EvolutionaryTraceiQ99NH2.
PROiQ99NH2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99NH2.
ExpressionAtlasiQ99NH2. baseline and differential.
GenevisibleiQ99NH2. MM.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
InterProiIPR021922. DUF3534.
IPR001478. PDZ.
[Graphical view]
PfamiPF12053. DUF3534. 1 hit.
PF00595. PDZ. 2 hits.
[Graphical view]
SMARTiSM00228. PDZ. 3 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 3 hits.
PROSITEiPS50106. PDZ. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif."
    Lin D., Gish G.D., Songyang Z., Pawson T.
    J. Biol. Chem. 274:3726-3733(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Strain: NIH Swiss.
    Tissue: Embryo.
  2. "A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity."
    Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.
    Nat. Cell Biol. 2:540-547(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, PHOSPHORYLATION BY PRKCZ, INTERACTION WITH PRKCI AND PARD6A, SUBUNIT OF A COMPLEX CONTAINING PARD6A AND CDC42, MUTAGENESIS OF 824-SER--SER-826.
    Strain: NIH Swiss.
  3. "PAR-3 defines a central subdomain of the cortical actin cap in mouse eggs."
    Duncan F.E., Moss S.B., Schultz R.M., Williams C.J.
    Dev. Biol. 280:38-47(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PTM.
    Strain: C57BL/6J x SJL/J.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 458-1333 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Vagina.
  5. "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: INTERACTION WITH PARD6B, SUBUNIT OF A COMPLEX CONTAINING PARD6B; PRKCI AND CDC42.
  6. "The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)."
    Ebnet K., Suzuki A., Horikoshi Y., Hirose T., Meyer zu Brickwedde M.-K., Ohno S., Vestweber D.
    EMBO J. 20:3738-3748(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH F11R.
  7. "Assembly of epithelial tight junctions is negatively regulated by Par6."
    Gao L., Joberty G., Macara I.G.
    Curr. Biol. 12:221-225(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH F11R AND PARD6B.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-156 AND SER-728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Spleen.
  10. "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module."
    Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T., Kaibuchi K., Hakoshima T.
    EMBO J. 29:236-250(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIAM1 AND TIAM2.
  11. "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: FUNCTION IN REGULATION OF PERIPHERAL MYELINATION, ACETYLATION AT LYS-831; LYS-848; LYS-881 AND LYS-1327, DEACETYLATION BY SIRT2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-831; LYS-848; LYS-881 AND LYS-1327, MASS SPECTROMETRY.
  12. "Macromolecular structure determination by NMR sepectroscopy."
    Center for eukaryotic structural genomics (CESG)
    Submitted (NOV-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 448-558.
  13. "Distal interactions within the par3-VE-cadherin complex."
    Tyler R.C., Peterson F.C., Volkman B.F.
    Biochemistry 49:951-957(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 581-689 IN COMPLEX WITH CDH5 PEPTIDE, SUBUNIT.

Entry informationi

Entry nameiPARD3_MOUSE
AccessioniPrimary (citable) accession number: Q99NH2
Secondary accession number(s): Q58T10, Q58T11, Q8CB21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: November 25, 2008
Last modified: July 6, 2016
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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.