Pard3 par-3 family cell polarity regulator [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Pard3provided by MGI
Official Full Name: par-3 family cell polarity regulatorprovided by MGI
Primary source: MGI:MGI:2135608
See related: Ensembl:ENSMUSG00000025812 AllianceGenome:MGI:2135608
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Asip; Par3; Phip; Par-3; Pard-3; Pard3a; D8Ertd580e
Summary: Predicted to enable identical protein binding activity; phosphatidylinositol phosphate binding activity; and protein phosphatase binding activity. Involved in several processes, including negative regulation of peptidyl-threonine phosphorylation; positive regulation of myelination; and positive regulation of receptor internalization. Acts upstream of or within several processes, including apical constriction; centrosome localization; and wound healing, spreading of cells. Located in several cellular components, including Schmidt-Lanterman incisure; internode region of axon; and lateral loop. Is expressed in several structures, including alimentary system; central nervous system; genitourinary system; respiratory system; and sensory organ. Orthologous to human PARD3 (par-3 family cell polarity regulator). [provided by Alliance of Genome Resources, Nov 2024]
Annotation information: Note: Par3 (Gene ID: 112235) and Pard3 (Gene ID: 93742) share the Par3 symbol/alias in common. Par3 is a widely used alternative name for par-3 family cell polarity regulator (Pard3), which can be confused with the official symbol for pulmonary adenoma resistance 3 (Par3). [13 May 2019]
Expression: Ubiquitous expression in ovary adult (RPKM 7.1), bladder adult (RPKM 6.3) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 8 E2; 8 74.66 cM

Exon count:: 28

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	8	NC_000074.7 (127790131..128338767)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	8	NC_000074.6 (127063381..127612286)

Chromosome 8 - NC_000074.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The effect of Par3 on the cellular junctions and biological functions of odontoblast-lineage cells.
Title: The effect of Par3 on the cellular junctions and biological functions of odontoblast-lineage cells.
TAZ stimulates exercise-induced muscle satellite cell activation via Pard3-p38 MAPK-TAZ signalling axis.
Title: TAZ stimulates exercise-induced muscle satellite cell activation via Pard3-p38 MAPK-TAZ signalling axis.
Syndecan-4/PAR-3 signaling regulates focal adhesion dynamics in mesenchymal cells.
Title: Syndecan-4/PAR-3 signaling regulates focal adhesion dynamics in mesenchymal cells.
Loss of endothelial PAR-3 disrupts regional axial cell polarity and increases pro-inflammatory response of endothelial cells.
Title: PAR-3 controls endothelial planar polarity and vascular inflammation under laminar flow.
mammary morphogenesis is dependent on the ability of Par3 to directly bind aPKC
Title: The Par3/aPKC interaction is essential for end bud remodeling and progenitor differentiation during mammary gland morphogenesis.
The structure of par3-PDZ3 peptide bound to the C-terminal tail of vascular endothelial cadherin clearly shows that both canonical and distal interactions are utilized in binding and suggests a mechanism for ligand specificity within the polarity network.
Title: Distal interactions within the par3-VE-cadherin complex.
results suggest that ERK2 phosphorylates Par3 and inhibits its binding with KIF3A, thereby controlling Par3 transport and neuronal polarity
Title: ERK2-mediated phosphorylation of Par3 regulates neuronal polarization.
Polycystin-1 binds Par3/PKCalpha and controls convergent extension during renal tubular morphogenesis.
Title: Polycystin-1 binds Par3/aPKC and controls convergent extension during renal tubular morphogenesis.
Rassf5 and Ndr1 or Ndr2 kinases regulate neuronal polarity through Par3 phosphorylation.
Title: Rassf5 and Ndr kinases regulate neuronal polarity through Par3 phosphorylation in a novel pathway.
support for the hitherto untested model that Par3-mInsc and Galphai3 act cooperatively to polarize LGN and promote perpendicular divisions
Title: Par3-mInsc and Gαi3 cooperate to promote oriented epidermal cell divisions through LGN.

Submit: New GeneRIF Correction See all GeneRIFs (44)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Targeted (7) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:236046

48.MMHAP66FRH12.seq (e-PCR)
- UniSTS:124694

AA960621 (e-PCR)
- UniSTS:159847

D8Mit245 (e-PCR), detects polymorphism
- UniSTS:131456

D8Mit93 (e-PCR), detects polymorphism
- UniSTS:116354

RH136057 (e-PCR)
- UniSTS:210052

D8Ertd580e (e-PCR), detects polymorphism
- UniSTS:167582

D8Mit326 (e-PCR), detects polymorphism
- UniSTS:131542

RH143682 (e-PCR)
- UniSTS:232928

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables phosphatidylinositol binding	IBA Inferred from Biological aspect of Ancestor more info
enables phosphatidylinositol-3,4,5-trisphosphate binding	ISO Inferred from Sequence Orthology more info
enables phosphatidylinositol-3,4,5-trisphosphate binding	ISS Inferred from Sequence or Structural Similarity more info
enables phosphatidylinositol-3-phosphate binding	ISO Inferred from Sequence Orthology more info
enables phosphatidylinositol-3-phosphate binding	ISS Inferred from Sequence or Structural Similarity more info
enables phosphatidylinositol-4,5-bisphosphate binding	ISO Inferred from Sequence Orthology more info
enables phosphatidylinositol-4,5-bisphosphate binding	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein phosphatase binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within apical constriction	IGI Inferred from Genetic Interaction more info	PubMed
involved_in bicellular tight junction assembly	ISO Inferred from Sequence Orthology more info
involved_in bicellular tight junction assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in cell adhesion	IBA Inferred from Biological aspect of Ancestor more info
involved_in cell division	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cell-cell adhesion	IC Inferred by Curator more info	PubMed
acts_upstream_of_or_within centrosome localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in establishment of cell polarity	IBA Inferred from Biological aspect of Ancestor more info
involved_in establishment of centrosome localization	IBA Inferred from Biological aspect of Ancestor more info
involved_in establishment of epithelial cell polarity	ISO Inferred from Sequence Orthology more info
involved_in establishment of epithelial cell polarity	ISS Inferred from Sequence or Structural Similarity more info
involved_in establishment or maintenance of cell polarity	TAS Traceable Author Statement more info	PubMed
involved_in establishment or maintenance of epithelial cell apical/basal polarity	IBA Inferred from Biological aspect of Ancestor more info
involved_in establishment or maintenance of epithelial cell apical/basal polarity	ISO Inferred from Sequence Orthology more info
involved_in microtubule cytoskeleton organization	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within microtubule cytoskeleton organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in myelination in peripheral nervous system	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of peptidyl-threonine phosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of myelination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of receptor internalization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein targeting to membrane	ISO Inferred from Sequence Orthology more info
involved_in protein targeting to membrane	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within regulation of actin filament-based process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of cellular localization	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within wound healing, spreading of cells	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of PAR polarity complex	ISO Inferred from Sequence Orthology more info
located_in Schmidt-Lanterman incisure	IDA Inferred from Direct Assay more info	PubMed
is_active_in adherens junction	IBA Inferred from Biological aspect of Ancestor more info
located_in adherens junction	IDA Inferred from Direct Assay more info	PubMed
is_active_in apical junction complex	IBA Inferred from Biological aspect of Ancestor more info
located_in apical junction complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in apical plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in axonal growth cone	ISO Inferred from Sequence Orthology more info
located_in bicellular tight junction	IDA Inferred from Direct Assay more info	PubMed
located_in bicellular tight junction	ISO Inferred from Sequence Orthology more info
located_in bicellular tight junction	ISS Inferred from Sequence or Structural Similarity more info
is_active_in cell cortex	IBA Inferred from Biological aspect of Ancestor more info
located_in cell cortex	IEA Inferred from Electronic Annotation more info
located_in cell junction	IDA Inferred from Direct Assay more info	PubMed
located_in cell junction	ISO Inferred from Sequence Orthology more info
located_in cell-cell junction	IDA Inferred from Direct Assay more info	PubMed
located_in cell-cell junction	ISO Inferred from Sequence Orthology more info
located_in cell-cell junction	ISS Inferred from Sequence or Structural Similarity more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in endomembrane system	IEA Inferred from Electronic Annotation more info
located_in internode region of axon	IDA Inferred from Direct Assay more info	PubMed
located_in lateral loop	IDA Inferred from Direct Assay more info	PubMed
located_in neuronal cell body	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info
located_in spindle	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: partitioning defective 3 homolog

Names: atypical PKC isotype-specific-interacting protein; ephrin-interacting protein; par-3 (partitioning defective 3) homolog

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001013580.4 → NP_001013598.1 partitioning defective 3 homolog isoform 2

See identical proteins and their annotated locations for NP_001013598.1

Status: VALIDATED

Description

Transcript Variant: This variant (2, also called PAR-3o2) differs in the 5' and 3' UTR and has multiple coding region differences compared to variant 5. These differences cause translation initiation at a downstream AUG and an isoform (2) with a shorter N-terminus and shorter and distinct C-terminus compared to isoform 5.

Source sequence(s)

AC105981, AC132321

Consensus CDS

CCDS40523.1

UniProtKB/TrEMBL

Q8BPQ6

Related

ENSMUSP00000125612.2, ENSMUST00000160717.8

Conserved Domains (1) summary

cd00992
Location:330 → 409

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...
NM_001013581.3 → NP_001013599.1 partitioning defective 3 homolog isoform 1

See identical proteins and their annotated locations for NP_001013599.1

Status: VALIDATED

Description

Transcript Variant: This variant (1, also called PAR-3o1) differs in the 5' and 3' UTR and has multiple coding region differences compared to variant 5. These differences cause translation initiation at a downstream AUG and an isoform (1) with a shorter N-terminus and shorter and distinct C-terminus compared to isoform 5.

Source sequence(s)

AC105981, AC132321

Consensus CDS

CCDS22789.1

UniProtKB/TrEMBL

A0A0R4J1Y4, E0CZE2

Related

ENSMUSP00000124162.2, ENSMUST00000162456.8

Conserved Domains (1) summary

cd00992
Location:330 → 409

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...
NM_001122850.2 → NP_001116322.1 partitioning defective 3 homolog isoform 4

Status: VALIDATED

Description

Transcript Variant: This variant (4) differs in the 3' UTR and coding region compared to variant 5. The resulting isoform (4) has a shorter and distinct C-terminus compared to isoform 5.

Source sequence(s)

AC105981, AC132321, AC155818, AC165964

Consensus CDS

CCDS52712.1

UniProtKB/TrEMBL

E9PYJ2, Q8BPQ4

Related

ENSMUSP00000124319.2, ENSMUST00000162907.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:1 → 146

DUF3534; Domain of unknown function (DUF3534)
NM_001309391.1 → NP_001296320.1 partitioning defective 3 homolog isoform 5

See identical proteins and their annotated locations for NP_001296320.1

Status: VALIDATED

Description

Transcript Variant: This variant (5) encodes isoform 5.

Source sequence(s)

BC090616

Consensus CDS

CCDS80945.1

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

UniProtKB/TrEMBL

A5D6P2

Related

ENSMUSP00000125453.2, ENSMUST00000160272.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:1 → 146

DUF3534; Domain of unknown function (DUF3534)
NM_001309392.1 → NP_001296321.1 partitioning defective 3 homolog isoform 6

See identical proteins and their annotated locations for NP_001296321.1

Status: VALIDATED

Description

Transcript Variant: This variant (6) lacks an in-frame exon in the central coding region, compared to variant 5. The encoded isoform (6) is shorter than isoform 5.

Source sequence(s)

BC090616

Consensus CDS

CCDS80946.1

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

UniProtKB/TrEMBL

B7ZNY3

Related

ENSMUSP00000026921.7, ENSMUST00000026921.13

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:1 → 146

DUF3534; Domain of unknown function (DUF3534)
NM_001363431.1 → NP_001350360.1 partitioning defective 3 homolog isoform 7

Status: VALIDATED

Description

Transcript Variant: This variant (7) uses an alternate in-frame splice junction compared to variant 5. The resulting isoform (7) has the same N- and C-termini but is shorter compared to isoform 5.

Source sequence(s)

AC102819, AC105981, AC132321, AC155818, AC165964

UniProtKB/TrEMBL

B2RUK1, F6S7Z1

Related

ENSMUSP00000124718.2, ENSMUST00000162665.8

Conserved Domains (3) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam06495
Location:1117 → 1187

Transformer; Fruit fly transformer protein

pfam12053
Location:1 → 146

DUF3534; Domain of unknown function (DUF3534)
NM_001363432.1 → NP_001350361.1 partitioning defective 3 homolog isoform 8

Status: VALIDATED

Description

Transcript Variant: This variant (8) represents the longest transcript and encodes the longest isoform (8).

Source sequence(s)

AC102819, AC105981, AC132321, AC155818, AC165964

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:1 → 146

DUF3534; Domain of unknown function (DUF3534)
NM_033620.2 → NP_296369.2 partitioning defective 3 homolog isoform 3

See identical proteins and their annotated locations for NP_296369.2

Status: VALIDATED

Description

Transcript Variant: This variant (3) uses an alternate in-frame splice site in the central coding region, compared to variant 5. The encoded isoform (3) is shorter than isoform 5.

Source sequence(s)

BC090616

Consensus CDS

CCDS22788.1

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

UniProtKB/TrEMBL

G3XA13

Related

ENSMUSP00000124282.2, ENSMUST00000162309.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:1 → 146

DUF3534; Domain of unknown function (DUF3534)

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000074.7 Reference GRCm39 C57BL/6J

Range

127790131..128338767

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006531520.3 → XP_006531583.1 partitioning defective 3 homolog isoform X1

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531523.3 → XP_006531586.1 partitioning defective 3 homolog isoform X2

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531524.3 → XP_006531587.1 partitioning defective 3 homolog isoform X3

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531527.3 → XP_006531590.1 partitioning defective 3 homolog isoform X5

UniProtKB/TrEMBL

F6S7Z1

Conserved Domains (3) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam06495
Location:1120 → 1190

Transformer; Fruit fly transformer protein

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531529.3 → XP_006531592.1 partitioning defective 3 homolog isoform X10

UniProtKB/TrEMBL

E0CZE2

Related

ENSMUSP00000125450.2, ENSMUST00000162602.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531530.3 → XP_006531593.1 partitioning defective 3 homolog isoform X11

UniProtKB/TrEMBL

E0CZE2

Related

ENSMUSP00000124934.2, ENSMUST00000159537.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_030243870.1 → XP_030099730.1 partitioning defective 3 homolog isoform X13

UniProtKB/TrEMBL

E0CXR8

Related

ENSMUSP00000124141.2, ENSMUST00000160581.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531532.3 → XP_006531595.1 partitioning defective 3 homolog isoform X14

UniProtKB/TrEMBL

E0CXR8

Related

ENSMUSP00000125064.2, ENSMUST00000161355.8

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531531.3 → XP_006531594.1 partitioning defective 3 homolog isoform X12

UniProtKB/TrEMBL

E0CZE2

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531533.3 → XP_006531596.1 partitioning defective 3 homolog isoform X15

UniProtKB/TrEMBL

Q8BPQ4

Conserved Domains (2) summary

cd00992
Location:465 → 544

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_006531526.3 → XP_006531589.1 partitioning defective 3 homolog isoform X4

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_030243868.1 → XP_030099728.1 partitioning defective 3 homolog isoform X8

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_030243867.1 → XP_030099727.1 partitioning defective 3 homolog isoform X6

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_030243869.1 → XP_030099729.1 partitioning defective 3 homolog isoform X9

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_036154397.1 → XP_036010290.1 partitioning defective 3 homolog isoform X7

UniProtKB/Swiss-Prot

Q58T10, Q58T11, Q8CB21, Q99NH2

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_030243872.1 → XP_030099732.1 partitioning defective 3 homolog isoform X17

UniProtKB/TrEMBL

Q8BPQ4

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins
XM_030243871.1 → XP_030099731.1 partitioning defective 3 homolog isoform X16

UniProtKB/TrEMBL

Q8BPQ4

Conserved Domains (2) summary

cd00992
Location:437 → 516

PDZ_signaling; PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) ...

pfam12053
Location:2 → 83

DUF3534; N-terminal of Par3 and HAL proteins