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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1103RRR → AAA: Abolishes nuclear import.
Mutagenesisi127 – 1293KKK → AAA: Abolishes nuclear import.
Mutagenesisi147 – 1471R → A: Reduces affinity for actin. 1 Publication
Mutagenesisi431 – 4311R → A: Constitutively nuclear; when associated with A-469 and A-507. Strongly reduced affinity for actin. 1 Publication
Mutagenesisi459 – 4591G → K: Increases affinity for actin. 1 Publication
Mutagenesisi469 – 4691R → A: Constitutively nuclear; when associated with A-431 and A-507. Strongly reduced affinity for actin. 1 Publication
Mutagenesisi496 – 4961I → A: Reduces affinity for actin. 1 Publication
Mutagenesisi507 – 5071R → A: Constitutively nuclear; when associated with A-431 and A-469. Strongly reduced affinity for actin. 1 Publication
Mutagenesisi516 – 5161R → A: Reduces affinity for actin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Phosphatase and actin regulator 1PRO_0000235990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei78 – 781PhosphoserineCombined sources
Modified residuei104 – 1041PhosphothreonineCombined sources
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei505 – 5051PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ2M3X8.
MaxQBiQ2M3X8.
PeptideAtlasiQ2M3X8.
PRIDEiQ2M3X8.

PTM databases

iPTMnetiQ2M3X8.
PhosphoSiteiQ2M3X8.

Expressioni

Gene expression databases

BgeeiQ2M3X8.
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 interaction.
IntActiQ2M3X8. 1 interaction.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 1458Combined sources
Helixi150 – 1556Combined sources
Helixi422 – 4298Combined sources
Helixi434 – 4385Combined sources
Turni439 – 4413Combined sources
Helixi458 – 46710Combined sources
Helixi472 – 4776Combined sources
Helixi495 – 50511Combined sources
Helixi510 – 5156Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 133-162, 419-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati138 – 16326RPEL 1Add
BLAST
Repeati422 – 44726RPEL 2Add
BLAST
Repeati460 – 48526RPEL 3Add
BLAST
Repeati498 – 52326RPEL 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi108 – 12922Nuclear localization signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi395 – 4039Poly-Glu

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.
OrthoDBiEOG7QG44R.
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 AAH48407.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH61691.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC33272.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MDYPK…SQGAQ → MCVSLLLSPPPPFRLSPSPS LHLLLLS in isoform 2 and isoform 3. 2 PublicationsVSP_018559Add
BLAST
Alternative sequencei221 – 2211P → PVSEESPSASESGVLLSQDP SAKPVLFLPPKKSAAFPGDH EETPVKQLSLHKQPPALPPK PTARIANHLT in isoform 3 and isoform 4. 2 PublicationsVSP_018560

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_006516905.2. [Q2M3X8-4]
XP_006516969.1. XM_006516906.2. [Q2M3X8-4]
XP_011242697.1. XM_011244395.1. [Q2M3X8-4]
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_006516905.2. [Q2M3X8-4]
XP_006516969.1. XM_006516906.2. [Q2M3X8-4]
XP_011242697.1. XM_011244395.1. [Q2M3X8-4]
UniGeneiMm.160124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 133-162, 419-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229998. 1 interaction.
IntActiQ2M3X8. 1 interaction.

PTM databases

iPTMnetiQ2M3X8.
PhosphoSiteiQ2M3X8.

Proteomic databases

EPDiQ2M3X8.
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.
OrthoDBiEOG7QG44R.
PhylomeDBiQ2M3X8.
TreeFamiTF316316.

Miscellaneous databases

ChiTaRSiPhactr1. mouse.
PROiQ2M3X8.
SOURCEiSearch...

Gene expression databases

BgeeiQ2M3X8.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Capucin: a novel striatal marker down-regulated in rodent models of Huntington disease."
    de Chaldee M., Brochier C., Van de Vel A., Caudy N., Luthi-Carter R., Gaillard M.-C., Elalouf J.-M.
    Genomics 87:200-207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Corpus striatum.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 4).
  4. "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] (ISOFORMS 2 AND 3).
    Tissue: Eye and Olfactory epithelium.
  5. "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 30-580 (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Head.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-78 AND THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Kidney.
  7. "G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly."
    Wiezlak M., Diring J., Abella J., Mouilleron S., Way M., McDonald N.Q., Treisman R.
    J. Cell Sci. 125:5860-5872(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1CA AND ACTA1, SUBCELLULAR LOCATION, MUTAGENESIS OF 108-ARG--LYS-129; ARG-147; ARG-431; ARG-469 AND ARG-507.
  8. "Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity."
    Mouilleron S., Wiezlak M., O'Reilly N., Treisman R., McDonald N.Q.
    Structure 20:1960-1970(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 133-164 AND 414-528 IN COMPLEXES WITH ACTA1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF GLY-459; ILE-496 AND ARG-516, IDENTIFICATION BY MASS SPECTROMETRY.

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: July 6, 2016
This is version 82 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.