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Protein

Phosphatase and actin regulator 1

Gene

PHACTR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 cell motility. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival.2 Publications

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actomyosin structure organization Source: UniProtKB
  • cell motility Source: UniProtKB
  • 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
Synonyms:KIAA1733, RPEL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:20990. PHACTR1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell junctionsynapse By similarity
  • Nucleus By similarity

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134923900.

Polymorphism and mutation databases

BioMutaiPHACTR1.
DMDMi97536946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Phosphatase and actin regulator 1PRO_0000126634Add
BLAST

Proteomic databases

PaxDbiQ9C0D0.
PRIDEiQ9C0D0.

PTM databases

PhosphoSiteiQ9C0D0.

Expressioni

Tissue specificityi

Detected in umbilical vein endothelial cells.1 Publication

Inductioni

Up-regulated by VEGFA.2 Publications

Gene expression databases

BgeeiQ9C0D0.
CleanExiHS_PHACTR1.
ExpressionAtlasiQ9C0D0. baseline and differential.
GenevisibleiQ9C0D0. HS.

Organism-specific databases

HPAiHPA029755.
HPA029756.
HPA029757.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi128746. 3 interactions.
IntActiQ9C0D0. 1 interaction.
MINTiMINT-6781379.
STRINGi9606.ENSP00000329880.

Structurei

3D structure databases

ProteinModelPortaliQ9C0D0.
SMRiQ9C0D0. 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 – 48425RPEL 3Add
BLAST
Repeati498 – 52326RPEL 4Add
BLAST

Motif

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

Domaini

Binds three actin monomers via the three C-terminal RPEL repeats.By similarity

Sequence similaritiesi

Contains 4 RPEL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG275065.
GeneTreeiENSGT00390000004420.
HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ9C0D0.
OMAiSCRMIDE.
PhylomeDBiQ9C0D0.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9C0D0-1) [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 ISNEEDSLEN GQSLSSSQLS LPALSEMEPV
210 220 230 240 250
PMPRDPCSYE VLQPSDIMDG PDPGAPVKLP CLPVKLSPPL PPKKVMICMP
260 270 280 290 300
VGGPDLSLVS YTAQKSGQQG VAQHHHTVLP SQIQHQLQYG SHGQHLPSTT
310 320 330 340 350
GSLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSGDG
360 370 380 390 400
VTKAGPMGLP EIRQVPTVVI ECDDNKENVP HESDYEDSSC LYTREEEEEE
410 420 430 440 450
EDEDDDSSLY 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):66,308
Last modified:May 16, 2006 - v3
Checksum:i5111973836BBEA39
GO
Isoform 2 (identifier: Q9C0D0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     483-484: PR → RK
     485-580: Missing.

Note: No experimental confirmation available.
Show »
Length:484
Mass (Da):54,608
Checksum:i073BD94AB00339F5
GO

Sequence cautioni

The sequence BAB21824.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471I → M.
Corresponds to variant rs17602409 [ dbSNP | Ensembl ].
VAR_053645
Natural varianti521 – 5211R → C Found in a patient with mental retardation, seizures, severely delayed psychomotor development, spastic tetraparesis, joint contractures and scoliosis. 1 Publication
VAR_069379

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei483 – 4842PR → RK in isoform 2. 1 PublicationVSP_018529
Alternative sequencei485 – 58096Missing in isoform 2. 1 PublicationVSP_018530Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051520 mRNA. Translation: BAB21824.1. Different initiation.
AK090769 mRNA. Translation: BAG52223.1.
AK290017 mRNA. Translation: BAF82706.1.
Z99495
, AL391385, AL008729, AL354680, AL591682 Genomic DNA. Translation: CAI20986.1.
AL591682
, Z99495, AL391385, AL354680, AL008729 Genomic DNA. Translation: CAI40399.1.
AL354680
, AL008729, AL391385, Z99495, AL591682 Genomic DNA. Translation: CAI41067.1.
AL008729
, Z99495, AL591682, AL391385, AL354680 Genomic DNA. Translation: CAI95669.1.
BC101526 mRNA. Translation: AAI01527.1.
BC101528 mRNA. Translation: AAI01529.1.
CCDSiCCDS75401.1. [Q9C0D0-1]
RefSeqiNP_001229577.1. NM_001242648.1. [Q9C0D0-1]
NP_112210.1. NM_030948.2. [Q9C0D0-1]
UniGeneiHs.436996.

Genome annotation databases

EnsembliENST00000332995; ENSP00000329880; ENSG00000112137.
ENST00000379350; ENSP00000368655; ENSG00000112137. [Q9C0D0-2]
GeneIDi221692.
KEGGihsa:221692.
UCSCiuc003nag.2. human. [Q9C0D0-2]
uc003nah.2. human. [Q9C0D0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051520 mRNA. Translation: BAB21824.1. Different initiation.
AK090769 mRNA. Translation: BAG52223.1.
AK290017 mRNA. Translation: BAF82706.1.
Z99495
, AL391385, AL008729, AL354680, AL591682 Genomic DNA. Translation: CAI20986.1.
AL591682
, Z99495, AL391385, AL354680, AL008729 Genomic DNA. Translation: CAI40399.1.
AL354680
, AL008729, AL391385, Z99495, AL591682 Genomic DNA. Translation: CAI41067.1.
AL008729
, Z99495, AL591682, AL391385, AL354680 Genomic DNA. Translation: CAI95669.1.
BC101526 mRNA. Translation: AAI01527.1.
BC101528 mRNA. Translation: AAI01529.1.
CCDSiCCDS75401.1. [Q9C0D0-1]
RefSeqiNP_001229577.1. NM_001242648.1. [Q9C0D0-1]
NP_112210.1. NM_030948.2. [Q9C0D0-1]
UniGeneiHs.436996.

3D structure databases

ProteinModelPortaliQ9C0D0.
SMRiQ9C0D0. Positions 133-162, 419-560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128746. 3 interactions.
IntActiQ9C0D0. 1 interaction.
MINTiMINT-6781379.
STRINGi9606.ENSP00000329880.

PTM databases

PhosphoSiteiQ9C0D0.

Polymorphism and mutation databases

BioMutaiPHACTR1.
DMDMi97536946.

Proteomic databases

PaxDbiQ9C0D0.
PRIDEiQ9C0D0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332995; ENSP00000329880; ENSG00000112137.
ENST00000379350; ENSP00000368655; ENSG00000112137. [Q9C0D0-2]
GeneIDi221692.
KEGGihsa:221692.
UCSCiuc003nag.2. human. [Q9C0D0-2]
uc003nah.2. human. [Q9C0D0-1]

Organism-specific databases

CTDi221692.
GeneCardsiGC06P012717.
H-InvDBHIX0019503.
HGNCiHGNC:20990. PHACTR1.
HPAiHPA029755.
HPA029756.
HPA029757.
MIMi608723. gene.
neXtProtiNX_Q9C0D0.
PharmGKBiPA134923900.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275065.
GeneTreeiENSGT00390000004420.
HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ9C0D0.
OMAiSCRMIDE.
PhylomeDBiQ9C0D0.

Miscellaneous databases

ChiTaRSiPHACTR1. human.
GenomeRNAii221692.
NextBioi91417.
PROiQ9C0D0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9C0D0.
CleanExiHS_PHACTR1.
ExpressionAtlasiQ9C0D0. baseline and differential.
GenevisibleiQ9C0D0. HS.

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. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala and Hippocampus.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Cerebellum.
  5. "Depletion of the novel protein PHACTR-1 from human endothelial cells abolishes tube formation and induces cell death receptor apoptosis."
    Jarray R., Allain B., Borriello L., Biard D., Loukaci A., Larghero J., Hadj-Slimane R., Garbay C., Lepelletier Y., Raynaud F.
    Biochimie 93:1668-1675(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  6. "Neuropilin-1 regulates a new VEGF-induced gene, Phactr-1, which controls tubulogenesis and modulates lamellipodial dynamics in human endothelial cells."
    Allain B., Jarray R., Borriello L., Leforban B., Dufour S., Liu W.Q., Pamonsinlapatham P., Bianco S., Larghero J., Hadj-Slimane R., Garbay C., Raynaud F., Lepelletier Y.
    Cell. Signal. 24:214-223(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  7. Cited for: VARIANT CYS-521.

Entry informationi

Entry nameiPHAR1_HUMAN
AccessioniPrimary (citable) accession number: Q9C0D0
Secondary accession number(s): A8K1V2, Q3MJ93, Q5JSJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 16, 2006
Last modified: July 22, 2015
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.