PFN2

Protein-coding gene in the species Homo sapiens
PFN2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1D1J

Identifiers
AliasesPFN2, D3S1319E, PFL, profilin 2
External IDsOMIM: 176590; MGI: 97550; HomoloGene: 1974; GeneCards: PFN2; OMA:PFN2 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PFN2
Genomic location for PFN2
Band3q25.1Start149,964,904 bp[1]
End150,050,788 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • frontal pole

  • superior frontal gyrus

  • postcentral gyrus

  • Brodmann area 10

  • pons

  • middle temporal gyrus

  • orbitofrontal cortex

  • ganglionic eminence

  • glutes

  • ventricular zone
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • actin binding
  • phosphatidylinositol-4,5-bisphosphate binding
  • actin monomer binding
  • protein binding
  • ATPase activity
Cellular component
  • cytoplasm
  • terminal bouton
  • extracellular exosome
  • cytoskeleton
  • Schaffer collateral - CA1 synapse
  • presynapse
  • postsynapse
  • glutamatergic synapse
Biological process
  • regulation of actin filament polymerization
  • regulation of synaptic vesicle exocytosis
  • protein stabilization
  • positive regulation of actin filament bundle assembly
  • positive regulation of actin filament polymerization
  • negative regulation of actin filament polymerization
  • positive regulation of ATP-dependent activity
  • negative regulation of epithelial cell migration
  • positive regulation of stress fiber assembly
  • actin cytoskeleton organization
  • positive regulation of peptidyl-serine phosphorylation
  • negative regulation of ruffle assembly
  • modification of postsynaptic actin cytoskeleton
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5217

18645

Ensembl

ENSG00000070087

ENSMUSG00000027805

UniProt

P35080

Q9JJV2

RefSeq (mRNA)

NM_053024
NM_002628

NM_019410

RefSeq (protein)

NP_002619
NP_444252

NP_062283

Location (UCSC)Chr 3: 149.96 – 150.05 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Profilin-2 is a protein that in humans is encoded by the PFN2 gene.[4][5][6]

The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. There are two alternatively spliced transcript variants encoding different isoforms described for this gene.[6]

Interactions

PFN2 has been shown to interact with ROCK1,[7] Vasodilator-stimulated phosphoprotein,[8][9] CCDC113[10] and FMNL1.[11]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000070087 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Joensuu T, Blanco G, Pakarinen L, Sistonen P, Kaariainen H, Brown S, Chapelle A, Sankila EM (March 1997). "Refined mapping of the Usher syndrome type III locus on chromosome 3, exclusion of candidate genes, and identification of the putative mouse homologous region". Genomics. 38 (3): 255–63. doi:10.1006/geno.1996.0626. PMID 8975700.
  5. ^ Honore B, Madsen P, Andersen AH, Leffers H (October 1993). "Cloning and expression of a novel human profilin variant, profilin II". FEBS Lett. 330 (2): 151–5. doi:10.1016/0014-5793(93)80262-S. PMID 8365484. S2CID 46347046.
  6. ^ a b "Entrez Gene: PFN2 profilin 2".
  7. ^ Da Silva JS, Medina Miguel, Zuliani Cecilia, Di Nardo Alessia, Witke Walter, Dotti Carlos G (September 2003). "RhoA/ROCK regulation of neuritogenesis via profilin IIa–mediated control of actin stability". J. Cell Biol. 162 (7). United States: 1267–79. doi:10.1083/jcb.200304021. ISSN 0021-9525. PMC 2173969. PMID 14517206.
  8. ^ Reinhard M, Giehl K, Abel K, Haffner C, Jarchau T, Hoppe V, Jockusch B M, Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8). ENGLAND: 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. ISSN 0261-4189. PMC 398250. PMID 7737110.
  9. ^ Harbeck B, Hüttelmaier S, Schluter K, Jockusch B M, Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40). UNITED STATES: 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.
  10. ^ "Coiled-Coil Domain Containing 113". GeneCards. Retrieved May 8, 2013.
  11. ^ Yayoshi-Yamamoto S, Taniuchi I, Watanabe T (September 2000). "FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages". Mol. Cell. Biol. 20 (18). UNITED STATES: 6872–81. doi:10.1128/MCB.20.18.6872-6881.2000. ISSN 0270-7306. PMC 86228. PMID 10958683.

Further reading

  • Qualmann B, Kessels MM (2003). "Endocytosis and the cytoskeleton". Int. Rev. Cytol. International Review of Cytology. 220: 93–144. doi:10.1016/S0074-7696(02)20004-2. ISBN 978-0-12-364624-8. PMID 12224553.
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
  • Kwiatkowski DJ, Bruns GA (1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis". J. Biol. Chem. 263 (12): 5910–5. doi:10.1016/S0021-9258(18)60651-9. PMID 3356709.
  • Reinhard M, Giehl K, Abel K, et al. (1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. PMC 398250. PMID 7737110.
  • Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W (1995). "Distinct biochemical characteristics of the two human profilin isoforms". Eur. J. Biochem. 229 (3): 621–8. doi:10.1111/j.1432-1033.1995.tb20506.x. PMID 7758455.
  • Naylor SL, Carritt B, Boileau C, et al. (1996). "Report of the sixth international workshop on human chromosome 3 mapping 1995". Cytogenet. Cell Genet. 72 (4): 255–70. doi:10.1159/000134204. PMID 8641130.
  • Witke W, Podtelejnikov AV, Di Nardo A, et al. (1998). "In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly". EMBO J. 17 (4): 967–76. doi:10.1093/emboj/17.4.967. PMC 1170446. PMID 9463375.
  • Nodelman IM, Bowman GD, Lindberg U, Schutt CE (2000). "X-ray structure determination of human profilin II: A comparative structural analysis of human profilins". J. Mol. Biol. 294 (5): 1271–85. doi:10.1006/jmbi.1999.3318. PMID 10600384.
  • Harbeck B, Hüttelmaier S, Schluter K, et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
  • Lambrechts A, Kwiatkowski AV, Lanier LM, et al. (2000). "cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains". J. Biol. Chem. 275 (46): 36143–51. doi:10.1074/jbc.M006274200. PMID 10945997.
  • Lambrechts A, Braun A, Jonckheere V, et al. (2000). "Profilin II Is Alternatively Spliced, Resulting in Profilin Isoforms That Are Differentially Expressed and Have Distinct Biochemical Properties". Mol. Cell. Biol. 20 (21): 8209–19. doi:10.1128/MCB.20.21.8209-8219.2000. PMC 86430. PMID 11027290.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Tojo H, Kaieda I, Hattori H, et al. (2004). "The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa". Mol. Endocrinol. 17 (7): 1216–29. doi:10.1210/me.2003-0056. PMID 12677009.
  • Da Silva JS, Medina M, Zuliani C, et al. (2003). "RhoA/ROCK regulation of neuritogenesis via profilin IIa–mediated control of actin stability". J. Cell Biol. 162 (7): 1267–79. doi:10.1083/jcb.200304021. PMC 2173969. PMID 14517206.
  • Goehler H, Lalowski M, Stelzl U, et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Lederer M, Jockusch BM, Rothkegel M (2005). "Profilin regulates the activity of p42POP, a novel Myb-related transcription factor". J. Cell Sci. 118 (Pt 2): 331–41. doi:10.1242/jcs.01618. PMID 15615774. S2CID 14624003.

External links

  • Overview of all the structural information available in the PDB for UniProt: P35080 (Human Profilin-2) at the PDBe-KB.
  • Overview of all the structural information available in the PDB for UniProt: Q9JJV2 (Mouse Profilin-2) at the PDBe-KB.


  • v
  • t
  • e
  • 1d1j: CRYSTAL STRUCTURE OF HUMAN PROFILIN II
    1d1j: CRYSTAL STRUCTURE OF HUMAN PROFILIN II
  • v
  • t
  • e
Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects
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