AFAP1

Actin filament-associated protein 1 is a protein that in humans is encoded by the AFAP1 gene.[5][6][7][8]

AFAP1
Identifiers
Aliases	AFAP1, AFAP, AFAP-110, AFAP110, actin filament associated protein 1
External IDs	OMIM: 608252 MGI: 1917542 HomoloGene: 11009 GeneCards: AFAP1
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p16.1 Start 7,758,714 bp[1] End 7,939,926 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 B3 Start 35,893,319 bp[2] End 36,003,923 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • actin binding • SH3 domain binding • SH2 domain binding Cellular component • cytoplasm • cytoskeleton • focal adhesion • cytosol • actin cytoskeleton Biological process • regulation of signal transduction • regulation of cytoskeleton organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	60312	70292
Ensembl	ENSG00000196526	ENSMUSG00000029094
UniProt	Q8N556	Q80YS6
RefSeq (mRNA)	NM_001134647 NM_021638 NM_198595 NM_001371090 NM_001371091	NM_027373
RefSeq (protein)	NP_001128119 NP_940997 NP_001358019 NP_001358020	NP_081649
Location (UCSC)	Chr 4: 7.76 – 7.94 Mb	Chr 5: 35.89 – 36 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene is a Src binding partner. It may represent a potential modulator of actin filament integrity in response to cellular signals, and may function as an adaptor protein by linking Src family members and/or other signaling proteins to actin filaments. Two alternative transcripts encoding the same protein have been identified.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000196526 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029094 - Ensembl, 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. Qian Y, Gatesman AS, Baisden JM, Zot HG, Cherezova L, Qazi I, Mazloum N, Lee MY, Guappone-Koay A, Flynn DC (Feb 2004). "Analysis of the role of the leucine zipper motif in regulating the ability of AFAP-110 to alter actin filament integrity". J Cell Biochem. 91 (3): 602–20. doi:10.1002/jcb.10725. PMID 14755689. S2CID 38130241.
6. Baisden JM, Gatesman AS, Cherezova L, Jiang BH, Flynn DC (Oct 2001). "The intrinsic ability of AFAP-110 to alter actin filament integrity is linked with its ability to also activate cellular tyrosine kinases". Oncogene. 20 (45): 6607–16. doi:10.1038/sj.onc.1204802. PMID 11641786.
7. Baisden JM, Qian Y, Zot HM, Flynn DC (Oct 2001). "The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity". Oncogene. 20 (44): 6435–47. doi:10.1038/sj.onc.1204784. PMID 11607843.
8. "Entrez Gene: AFAP1 actin filament associated protein 1".

External links

• Human AFAP1 genome location and AFAP1 gene details page in the UCSC Genome Browser.

Further reading

• Ishida Y, Hadano S, Nagayama T, et al. (1995). "Isolation and characterization of 21 novel expressed DNA sequences from the distal region of human chromosome 4p". Genomics. 22 (2): 302–12. doi:10.1006/geno.1994.1388. PMID 7545969.
• Qian Y, Baisden JM, Westin EH, et al. (1998). "Src can regulate carboxy terminal interactions with AFAP-110, which influence self-association, cell localization and actin filament integrity". Oncogene. 16 (17): 2185–95. doi:10.1038/sj.onc.1201753. PMID 9619827.
• Guappone AC, Weimer T, Flynn DC (1998). "Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif". Mol. Carcinog. 22 (2): 110–9. doi:10.1002/(SICI)1098-2744(199806)22:2<110::AID-MC6>3.0.CO;2-Q. PMID 9655255.
• Qian Y, Baisden JM, Zot HG, et al. (2000). "The carboxy terminus of AFAP-110 modulates direct interactions with actin filaments and regulates its ability to alter actin filament integrity and induce lamellipodia formation". Exp. Cell Res. 255 (1): 102–13. doi:10.1006/excr.1999.4795. PMID 10666339.
• Qian Y, Baisden JM, Cherezova L, et al. (2003). "PC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments". Mol. Biol. Cell. 13 (7): 2311–22. doi:10.1091/mbc.E01-12-0148. PMC 117315. PMID 12134071.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Dorfleutner A, Stehlik C, Zhang J, et al. (2007). "AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells". J. Cell. Physiol. 213 (3): 740–9. CiteSeerX 10.1.1.636.3591. doi:10.1002/jcp.21143. PMID 17520695. S2CID 15344259.