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Protein

Phosphatase and actin regulator 1

Gene

Phactr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival (By similarity). Plays a role in cell motility.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actomyosin structure organization Source: UniProtKB
  • cell motility Source: MGI
  • stress fiber assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatase and actin regulator 1
Gene namesi
Name:Phactr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2659021. Phactr1.

Subcellular locationi

  • Cytoplasm
  • Cell junctionsynapse By similarity
  • Nucleus

  • Note: Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import.By similarity

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi108 – 110RRR → AAA: Abolishes nuclear import. 3
Mutagenesisi127 – 129KKK → AAA: Abolishes nuclear import. 3
Mutagenesisi147R → A: Reduces affinity for actin. 1 Publication1
Mutagenesisi431R → A: Constitutively nuclear; when associated with A-469 and A-507. Strongly reduced affinity for actin. 1 Publication1
Mutagenesisi459G → K: Increases affinity for actin. 1 Publication1
Mutagenesisi469R → A: Constitutively nuclear; when associated with A-431 and A-507. Strongly reduced affinity for actin. 1 Publication1
Mutagenesisi496I → A: Reduces affinity for actin. 1 Publication1
Mutagenesisi507R → A: Constitutively nuclear; when associated with A-431 and A-469. Strongly reduced affinity for actin. 1 Publication1
Mutagenesisi516R → A: Reduces affinity for actin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002359901 – 580Phosphatase and actin regulator 1Add BLAST580

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67PhosphoserineCombined sources1
Modified residuei78PhosphoserineCombined sources1
Modified residuei104PhosphothreonineCombined sources1
Modified residuei467PhosphoserineBy similarity1
Modified residuei505PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ2M3X8.
PeptideAtlasiQ2M3X8.
PRIDEiQ2M3X8.

PTM databases

iPTMnetiQ2M3X8.
PhosphoSitePlusiQ2M3X8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000054728.
CleanExiMM_PHACTR1.
ExpressionAtlasiQ2M3X8. baseline and differential.
GenevisibleiQ2M3X8. MM.

Interactioni

Subunit structurei

Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and PPP1CA compete for the same binding site.2 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi229998. 1 interactor.
IntActiQ2M3X8. 1 interactor.

Structurei

Secondary structure

1580
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi138 – 145Combined sources8
Helixi150 – 155Combined sources6
Helixi422 – 429Combined sources8
Helixi434 – 438Combined sources5
Turni439 – 441Combined sources3
Helixi458 – 467Combined sources10
Helixi472 – 477Combined sources6
Helixi495 – 505Combined sources11
Helixi510 – 515Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B1UX-ray2.00M133-164[»]
4B1VX-ray1.75M/N133-164[»]
4B1WX-ray1.95M417-448[»]
4B1XX-ray1.80M455-486[»]
4B1YX-ray1.29M493-524[»]
4B1ZX-ray3.30M/N414-528[»]
ProteinModelPortaliQ2M3X8.
SMRiQ2M3X8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati138 – 163RPEL 1Add BLAST26
Repeati422 – 447RPEL 2Add BLAST26
Repeati460 – 485RPEL 3Add BLAST26
Repeati498 – 523RPEL 4Add BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi108 – 129Nuclear localization signalAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi395 – 403Poly-Glu9

Domaini

Binds three actin monomers via the three C-terminal RPEL repeats.1 Publication

Sequence similaritiesi

Contains 4 RPEL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000004420.
HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ2M3X8.
OMAiSCRMIDE.
OrthoDBiEOG091G0HBF.
PhylomeDBiQ2M3X8.
TreeFamiTF316316.

Family and domain databases

InterProiIPR029987. Phactr1.
IPR004018. RPEL_repeat.
[Graphical view]
PANTHERiPTHR12751:SF6. PTHR12751:SF6. 1 hit.
PfamiPF02755. RPEL. 4 hits.
[Graphical view]
SMARTiSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEiPS51073. RPEL. 4 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2M3X8-1) [UniParc]FASTAAdd to basket

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
MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS
60 70 80 90 100
SEDDIDRRPI RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP
110 120 130 140 150
GTHTPPIRRR SKFANLGRIF KPWKWRKKKS EKFKHTSAAL ERKISMRQSR
160 170 180 190 200
EELIKRGVLK EIYDKDGELS ISNEDDSLEN GQSLSSSQLS LPALSEMEPV
210 220 230 240 250
PMPRDPCSYE VLQASDIMDG PDPGAPVKLP CLPVKLSPPL PPKKVLICMP
260 270 280 290 300
VGGPELTLAS YAAQKSSQQA VAQHHHTVLP SQMQHQLQYG SHGQHLPSST
310 320 330 340 350
GTLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSSDG
360 370 380 390 400
ITKAGPMGLP EIRQVPTVVI ECDDNKENVP HEPDYEDSPC LYGREEEEEE
410 420 430 440 450
EDEDDDASLY TSSLAMKVCR KDSLAIKLSN RPSKRELEEK NILPRQTDEE
460 470 480 490 500
RLELRQQIGT KLTRRLSQRP TAEELEQRNI LKPRNEQEEQ EEKREIKRRL
510 520 530 540 550
TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK PWTRLTAADK
560 570 580
AAIRKELNEF KSTEMEVHEL SRHLTRFHRP
Length:580
Mass (Da):66,286
Last modified:February 21, 2006 - v1
Checksum:i367DD2393117EC89
GO
Isoform 2 (identifier: Q2M3X8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQ → MCVSLLLSPPPPFRLSPSPSLHLLLLS

Show »
Length:573
Mass (Da):65,143
Checksum:i077C19321C16FE26
GO
Isoform 3 (identifier: Q2M3X8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQ → MCVSLLLSPPPPFRLSPSPSLHLLLLS
     221-221: P → PVSEESPSASESGVLLSQDPSAKPVLFLPPKKSAAFPGDHEETPVKQLSLHKQPPALPPKPTARIANHLT

Show »
Length:642
Mass (Da):72,427
Checksum:i825EA76DBE9A8CD2
GO
Isoform 4 (identifier: Q2M3X8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-221: P → PVSEESPSASESGVLLSQDPSAKPVLFLPPKKSAAFPGDHEETPVKQLSLHKQPPALPPKPTARIANHLT

Show »
Length:649
Mass (Da):73,570
Checksum:i05238060A2217537
GO

Sequence cautioni

The sequence AAH48407 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH61691 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC33272 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0185591 – 34MDYPK…SQGAQ → MCVSLLLSPPPPFRLSPSPS LHLLLLS in isoform 2 and isoform 3. 2 PublicationsAdd BLAST34
Alternative sequenceiVSP_018560221P → PVSEESPSASESGVLLSQDP SAKPVLFLPPKKSAAFPGDH EETPVKQLSLHKQPPALPPK PTARIANHLT in isoform 3 and isoform 4. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY993932 mRNA. Translation: AAY42814.1.
CT025549
, AC140415, AC154505, AC164878 Genomic DNA. Translation: CAO78135.1.
CT025549
, AC140415, AC154505, AC164878 Genomic DNA. Translation: CAO78137.1.
CT025549
, AC140415, AC154505, AC164878 Genomic DNA. Translation: CAO78138.1.
CH466546 Genomic DNA. Translation: EDL40986.1.
BC048407 mRNA. Translation: AAH48407.1. Different initiation.
BC061691 mRNA. Translation: AAH61691.1. Different initiation.
AK048208 mRNA. Translation: BAC33272.1. Different initiation.
CCDSiCCDS49251.1. [Q2M3X8-3]
CCDS79181.1. [Q2M3X8-1]
RefSeqiNP_001005740.1. NM_001005740.1. [Q2M3X8-3]
NP_001289564.1. NM_001302635.1. [Q2M3X8-1]
NP_001289565.1. NM_001302636.1.
XP_006516968.1. XM_006516905.3. [Q2M3X8-4]
XP_006516969.1. XM_006516906.3. [Q2M3X8-4]
XP_011242697.1. XM_011244395.2. [Q2M3X8-4]
XP_017170971.1. XM_017315482.1. [Q2M3X8-1]
XP_017170972.1. XM_017315483.1. [Q2M3X8-1]
UniGeneiMm.160124.

Genome annotation databases

EnsembliENSMUST00000066928; ENSMUSP00000066663; ENSMUSG00000054728. [Q2M3X8-2]
ENSMUST00000110161; ENSMUSP00000105790; ENSMUSG00000054728. [Q2M3X8-4]
ENSMUST00000128646; ENSMUSP00000122232; ENSMUSG00000054728. [Q2M3X8-1]
ENSMUST00000148891; ENSMUSP00000115228; ENSMUSG00000054728. [Q2M3X8-3]
ENSMUST00000149235; ENSMUSP00000115207; ENSMUSG00000054728. [Q2M3X8-1]
GeneIDi218194.
KEGGimmu:218194.
UCSCiuc007qfo.2. mouse. [Q2M3X8-1]
uc007qfp.1. mouse. [Q2M3X8-3]
uc007qfq.1. mouse. [Q2M3X8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY993932 mRNA. Translation: AAY42814.1.
CT025549
, AC140415, AC154505, AC164878 Genomic DNA. Translation: CAO78135.1.
CT025549
, AC140415, AC154505, AC164878 Genomic DNA. Translation: CAO78137.1.
CT025549
, AC140415, AC154505, AC164878 Genomic DNA. Translation: CAO78138.1.
CH466546 Genomic DNA. Translation: EDL40986.1.
BC048407 mRNA. Translation: AAH48407.1. Different initiation.
BC061691 mRNA. Translation: AAH61691.1. Different initiation.
AK048208 mRNA. Translation: BAC33272.1. Different initiation.
CCDSiCCDS49251.1. [Q2M3X8-3]
CCDS79181.1. [Q2M3X8-1]
RefSeqiNP_001005740.1. NM_001005740.1. [Q2M3X8-3]
NP_001289564.1. NM_001302635.1. [Q2M3X8-1]
NP_001289565.1. NM_001302636.1.
XP_006516968.1. XM_006516905.3. [Q2M3X8-4]
XP_006516969.1. XM_006516906.3. [Q2M3X8-4]
XP_011242697.1. XM_011244395.2. [Q2M3X8-4]
XP_017170971.1. XM_017315482.1. [Q2M3X8-1]
XP_017170972.1. XM_017315483.1. [Q2M3X8-1]
UniGeneiMm.160124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B1UX-ray2.00M133-164[»]
4B1VX-ray1.75M/N133-164[»]
4B1WX-ray1.95M417-448[»]
4B1XX-ray1.80M455-486[»]
4B1YX-ray1.29M493-524[»]
4B1ZX-ray3.30M/N414-528[»]
ProteinModelPortaliQ2M3X8.
SMRiQ2M3X8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229998. 1 interactor.
IntActiQ2M3X8. 1 interactor.

PTM databases

iPTMnetiQ2M3X8.
PhosphoSitePlusiQ2M3X8.

Proteomic databases

MaxQBiQ2M3X8.
PeptideAtlasiQ2M3X8.
PRIDEiQ2M3X8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066928; ENSMUSP00000066663; ENSMUSG00000054728. [Q2M3X8-2]
ENSMUST00000110161; ENSMUSP00000105790; ENSMUSG00000054728. [Q2M3X8-4]
ENSMUST00000128646; ENSMUSP00000122232; ENSMUSG00000054728. [Q2M3X8-1]
ENSMUST00000148891; ENSMUSP00000115228; ENSMUSG00000054728. [Q2M3X8-3]
ENSMUST00000149235; ENSMUSP00000115207; ENSMUSG00000054728. [Q2M3X8-1]
GeneIDi218194.
KEGGimmu:218194.
UCSCiuc007qfo.2. mouse. [Q2M3X8-1]
uc007qfp.1. mouse. [Q2M3X8-3]
uc007qfq.1. mouse. [Q2M3X8-2]

Organism-specific databases

CTDi221692.
MGIiMGI:2659021. Phactr1.

Phylogenomic databases

GeneTreeiENSGT00390000004420.
HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ2M3X8.
OMAiSCRMIDE.
OrthoDBiEOG091G0HBF.
PhylomeDBiQ2M3X8.
TreeFamiTF316316.

Miscellaneous databases

ChiTaRSiPhactr1. mouse.
PROiQ2M3X8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000054728.
CleanExiMM_PHACTR1.
ExpressionAtlasiQ2M3X8. baseline and differential.
GenevisibleiQ2M3X8. MM.

Family and domain databases

InterProiIPR029987. Phactr1.
IPR004018. RPEL_repeat.
[Graphical view]
PANTHERiPTHR12751:SF6. PTHR12751:SF6. 1 hit.
PfamiPF02755. RPEL. 4 hits.
[Graphical view]
SMARTiSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEiPS51073. RPEL. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHAR1_MOUSE
AccessioniPrimary (citable) accession number: Q2M3X8
Secondary accession number(s): B1B1B5
, B1B1B6, B1B1B7, G5E8P7, Q80VL9, Q8C873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 21, 2006
Last modified: November 2, 2016
This is version 85 of the entry and version 1 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.