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Protein

Phosphatase and actin regulator 3

Gene

Phactr3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • actin binding Source: RGD
  • protein phosphatase inhibitor activity Source: RGD
  • protein phosphatase type 1 regulator activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatase and actin regulator 3
Alternative name(s):
Scaffold-associated PP1-inhibiting protein
Short name:
Scapinin
Gene namesi
Name:Phactr3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303029. Phactr3.

Subcellular locationi

  • Nucleus matrix By similarity

  • Note: Localized to the nuclear matrix-intermediate filament scaffold.By similarity

GO - Cellular componenti

  • nuclear matrix Source: UniProtKB-SubCell
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001266401 – 517Phosphatase and actin regulator 3Add BLAST517

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29PhosphothreonineBy similarity1
Modified residuei188PhosphoserineCombined sources1
Modified residuei194PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ6RFY2.

PTM databases

iPTMnetiQ6RFY2.
PhosphoSitePlusiQ6RFY2.

Expressioni

Tissue specificityi

Diffusely expressed throughout the brain cortex, with highest levels in the cortex and the hippocampus and lower levels in the striatum and thalamus.1 Publication

Interactioni

Subunit structurei

Binds actin and PPP1CA; thus inhibiting the protein phosphatase 1 (PP1) activity.By similarity

GO - Molecular functioni

  • actin binding Source: RGD

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati52 – 77RPEL 1Add BLAST26
Repeati359 – 384RPEL 2Add BLAST26
Repeati397 – 422RPEL 3Add BLAST26
Repeati435 – 460RPEL 4Add BLAST26

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili408 – 444Sequence analysisAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi175 – 197Pro-richAdd BLAST23

Sequence similaritiesi

Contains 4 RPEL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ6RFY2.
KOiK17594.
PhylomeDBiQ6RFY2.

Family and domain databases

InterProiIPR029990. Phactr3.
IPR004018. RPEL_repeat.
[Graphical view]
PANTHERiPTHR12751:SF7. PTHR12751:SF7. 1 hit.
PfamiPF02755. RPEL. 2 hits.
[Graphical view]
SMARTiSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEiPS51073. RPEL. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6RFY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQTPPARSE PLVSGIRTPP VRRNSKLATL GRIFKPWKWR KKKNEKLKQT
60 70 80 90 100
TSALEKKMAG RQGREELIKQ GLLEMMEQDS ESKACSPKEG SQPAQSEPSA
110 120 130 140 150
GEQETLTSEG VQPGSPSASG TDQASQDELL SSDAHPDDTA KMSSASSGEE
160 170 180 190 200
ADAGNLLPTT DEPSQEALSG SLDSPPRTLE RSASQLPSPP LLPTPPPKAS
210 220 230 240 250
SKATKNVTGQ AALFQGSSMK NNEPVLRGQL PTPTGSPHLT TVHRPLPPSR
260 270 280 290 300
VIEELHRALA TKHRQDSFQG RECRGSPKKR MDVRLSRTSS MERGKERDEA
310 320 330 340 350
WSFDGASENK WTAAKDSEEN KENLILSSEL KDDLLLYQDE EALNDSIISG
360 370 380 390 400
TLPRKCKKEL LAVKLRNRPS KQELEDRNIF PRRTDEERQE IRQQIEMKLS
410 420 430 440 450
KRLSQRPAVE ELERRNILKQ RNDQTEQEER REIKQRLTRK LNQRPTVDEL
460 470 480 490 500
RDRKILIRFS DYVEVARAQD YDRRADKPWT RLSAADKAAI RKELNEYKSN
510
EMEVHASSKH LTRFHRP
Length:517
Mass (Da):58,461
Last modified:July 5, 2004 - v1
Checksum:i8016593B93B3B43C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY500157 mRNA. Translation: AAS86431.1.
RefSeqiNP_999624.1. NM_214459.2.
UniGeneiRn.27183.

Genome annotation databases

GeneIDi362284.
KEGGirno:362284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY500157 mRNA. Translation: AAS86431.1.
RefSeqiNP_999624.1. NM_214459.2.
UniGeneiRn.27183.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ6RFY2.
PhosphoSitePlusiQ6RFY2.

Proteomic databases

PRIDEiQ6RFY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi362284.
KEGGirno:362284.

Organism-specific databases

CTDi116154.
RGDi1303029. Phactr3.

Phylogenomic databases

HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ6RFY2.
KOiK17594.
PhylomeDBiQ6RFY2.

Miscellaneous databases

PROiQ6RFY2.

Family and domain databases

InterProiIPR029990. Phactr3.
IPR004018. RPEL_repeat.
[Graphical view]
PANTHERiPTHR12751:SF7. PTHR12751:SF7. 1 hit.
PfamiPF02755. RPEL. 2 hits.
[Graphical view]
SMARTiSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEiPS51073. RPEL. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHAR3_RAT
AccessioniPrimary (citable) accession number: Q6RFY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 77 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

Complete proteome, Reference proteome

Documents

  1. 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.