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Profilin 1

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Protein-coding gene in the species Homo sapiens
PFN1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1AWI, 1CF0, 1CJF, 1FIK, 1FIL, 1PFL, 2PAV, 2PBD, 3CHW, 4X1L, 4X1M, 4X25

Identifiers
AliasesPFN1, ALS18, Profilin 1
External IDsOMIM: 176610; MGI: 97549; HomoloGene: 3684; GeneCards: PFN1; OMA:PFN1 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)
Chromosome 17 (human)Genomic location for PFN1Genomic location for PFN1
Band17p13.2Start4,945,652 bp
End4,949,061 bp
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)
Chromosome 11 (mouse)Genomic location for PFN1Genomic location for PFN1
Band11 B3|11 43.21 cMStart70,542,676 bp
End70,545,470 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • mucosa of transverse colon

  • muscle layer of sigmoid colon

  • mucosa of ileum

  • monocyte

  • thoracic aorta

  • ascending aorta

  • stromal cell of endometrium

  • Descending thoracic aorta

  • left coronary artery
Top expressed in
  • granulocyte

  • yolk sac

  • tail of embryo

  • thymus

  • tibiofemoral joint

  • lymph node

  • mesenteric lymph nodes

  • genital tubercle

  • epiblast

  • ascending aorta
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5216

18643

Ensembl

ENSG00000108518

ENSMUSG00000018293

UniProt

P07737

P62962

RefSeq (mRNA)

NM_005022
NM_001375991

NM_011072

RefSeq (protein)

NP_005013
NP_001362920

NP_035202

Location (UCSC)Chr 17: 4.95 – 4.95 MbChr 11: 70.54 – 70.55 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Profilin-1 is a protein that in humans is encoded by the PFN1 gene.

Function

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. Deletion of this gene is associated with Miller-Dieker syndrome. Mutations in this gene may be a rare cause of amyotrophic lateral sclerosis, also called Lou Gehrig's disease.

Profilin-1 is a pseudouridine-binding protein and contributes to stability and translation efficiency of certain mRNAs.

Interactions

Profilin 1 has been shown to interact with:

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000108518Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000018293Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Kwiatkowski DJ, Bruns GA (May 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.
  6. Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC (April 1990). "Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome". Am J Hum Genet. 46 (3): 559–67. PMC 1683621. PMID 1968707.
  7. "Entrez Gene: PFN1 profilin 1".
  8. Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, et al. (August 2012). "Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis". Nature. 488 (7412): 499–503. Bibcode:2012Natur.488..499W. doi:10.1038/nature11280. PMC 3575525. PMID 22801503.
  9. Daoud H, Dobrzeniecka S, Camu W, Meininger V, Dupré N, Dion PA, Rouleau GA (April 2013). "Mutation analysis of PFN1 in familial amyotrophic lateral sclerosis patients". Neurobiology of Aging. 34 (4): 1311.e1–2. doi:10.1016/j.neurobiolaging.2012.09.001. PMID 23062600. S2CID 42137823.
  10. Tiloca C, Ticozzi N, Pensato V, Corrado L, Del Bo R, Bertolin C, et al. (May 2013). "Screening of the PFN1 gene in sporadic amyotrophic lateral sclerosis and in frontotemporal dementia". Neurobiology of Aging. 34 (5): 1517.e9–10. doi:10.1016/j.neurobiolaging.2012.09.016. PMC 3548975. PMID 23063648.
  11. Ingre C, Landers JE, Rizik N, Volk AE, Akimoto C, Birve A, et al. (June 2013). "A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts". Neurobiology of Aging. 34 (6): 1708.e1–6. doi:10.1016/j.neurobiolaging.2012.10.009. PMC 6591725. PMID 23141414.
  12. Lattante S, Le Ber I, Camuzat A, Brice A, Kabashi E (June 2013). "Mutations in the PFN1 gene are not a common cause in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration in France". Neurobiology of Aging. 34 (6): 1709.e1–2. doi:10.1016/j.neurobiolaging.2012.10.026. PMID 23182804. S2CID 37470475.
  13. Dillen L, Van Langenhove T, Engelborghs S, Vandenbulcke M, Sarafov S, Tournev I, et al. (June 2013). "Explorative genetic study of UBQLN2 and PFN1 in an extended Flanders-Belgian cohort of frontotemporal lobar degeneration patients". Neurobiology of Aging. 34 (6): 1711.e1–5. doi:10.1016/j.neurobiolaging.2012.12.007. PMID 23312802. S2CID 8448562.
  14. Zou ZY, Sun Q, Liu MS, Li XG, Cui LY (June 2013). "Mutations in the profilin 1 gene are not common in amyotrophic lateral sclerosis of Chinese origin". Neurobiology of Aging. 34 (6): 1713.e5–6. doi:10.1016/j.neurobiolaging.2012.12.024. PMID 23357624. S2CID 9675956.
  15. Chen Y, Zheng ZZ, Huang R, Chen K, Song W, Zhao B, et al. (July 2013). "PFN1 mutations are rare in Han Chinese populations with amyotrophic lateral sclerosis". Neurobiology of Aging. 34 (7): 1922.e1–5. doi:10.1016/j.neurobiolaging.2013.01.013. PMID 23428184. S2CID 25016105.
  16. van Blitterswijk M, Baker MC, Bieniek KF, Knopman DS, Josephs KA, Boeve B, et al. (September 2013). "Profilin-1 mutations are rare in patients with amyotrophic lateral sclerosis and frontotemporal dementia". Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration. 14 (5–6): 463–9. doi:10.3109/21678421.2013.787630. PMC 3923463. PMID 23634771.
  17. Yang S, Fifita JA, Williams KL, Warraich ST, Pamphlett R, Nicholson GA, et al. (September 2013). "Mutation analysis and immunopathological studies of PFN1 in familial and sporadic amyotrophic lateral sclerosis". Neurobiology of Aging. 34 (9): 2235.e7–10. doi:10.1016/j.neurobiolaging.2013.04.003. PMID 23635659. S2CID 19339337.
  18. Fratta P, Charnock J, Collins T, Devoy A, Howard R, Malaspina A, et al. (May 2014). "Profilin1 E117G is a moderate risk factor for amyotrophic lateral sclerosis". Journal of Neurology, Neurosurgery, and Psychiatry. 85 (5): 506–8. doi:10.1136/jnnp-2013-306761. PMC 3995330. PMID 24309268.
  19. Syriani E, Salvans C, Salvadó M, Morales M, Lorenzo L, Cazorla S, Gamez J (December 2014). "PFN1 mutations are also rare in the Catalan population with amyotrophic lateral sclerosis". Journal of Neurology. 261 (12): 2387–92. doi:10.1007/s00415-014-7501-x. PMID 25249294. S2CID 21281429.
  20. Smith BN, Vance C, Scotter EL, Troakes C, Wong CH, Topp S, et al. (March 2015). "Novel mutations support a role for Profilin 1 in the pathogenesis of ALS". Neurobiology of Aging. 36 (3): 1602.e17–27. doi:10.1016/j.neurobiolaging.2014.10.032. PMC 4357530. PMID 25499087.
  21. Wei S, Dai X, Yuan J, He S, Shah K, Guo S, Duan Z, Murn J, Wang Y (2024-12-31). "Quantitative Proteomics Identifies Profilin-1 as a Pseudouridine-Binding Protein". Journal of the American Chemical Society. doi:10.1021/jacs.4c17659. ISSN 0002-7863.
  22. 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): 6872–81. doi:10.1128/mcb.20.18.6872-6881.2000. PMC 86228. PMID 10958683.
  23. Boettner B, Govek EE, Cross J, Van Aelst L (August 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
  24. Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 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.
  25. Miki H, Suetsugu S, Takenawa T (December 1998). "WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac". EMBO J. 17 (23): 6932–41. doi:10.1093/emboj/17.23.6932. PMC 1171041. PMID 9843499.
  26. Mimuro H, Suzuki T, Suetsugu S, Miki H, Takenawa T, Sasakawa C (September 2000). "Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri". J. Biol. Chem. 275 (37): 28893–901. doi:10.1074/jbc.M003882200. PMID 10867004.
  27. Suetsugu S, Miki H, Takenawa T (November 1998). "The essential role of profilin in the assembly of actin for microspike formation". EMBO J. 17 (22): 6516–26. doi:10.1093/emboj/17.22.6516. PMC 1170999. PMID 9822597.

Further reading

PDB gallery
  • 1awi: HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE 1awi: HUMAN PLATELET PROFILIN COMPLEXED WITH THE L-PRO10 PEPTIDE
  • 1cf0: HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE 1cf0: HUMAN PLATELET PROFILIN COMPLEXED WITH AN L-PRO10-IODOTYROSINE PEPTIDE
  • 1cjf: PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS 1cjf: PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS
  • 1fik: HUMAN PLATELET PROFILIN I CRYSTALLIZED IN LOW SALT 1fik: HUMAN PLATELET PROFILIN I CRYSTALLIZED IN LOW SALT
  • 1fil: HUMAN PLATELET PROFILIN I CRYSTALLIZED IN HIGH SALT ACTIN-BINDING PROTEIN 1fil: HUMAN PLATELET PROFILIN I CRYSTALLIZED IN HIGH SALT ACTIN-BINDING PROTEIN
  • 1hlu: STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE 1hlu: STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE
  • 1pfl: REFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I 1pfl: REFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I
  • 1pne: CRYSTALLIZATION AND STRUCTURE DETERMINATION OF BOVINE PROFILIN AT 2.0 ANGSTROMS RESOLUTION 1pne: CRYSTALLIZATION AND STRUCTURE DETERMINATION OF BOVINE PROFILIN AT 2.0 ANGSTROMS RESOLUTION
  • 2btf: THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN 2btf: THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN
Proteins of the cytoskeleton
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
Category: