AAMP (gene)

Angio-associated, migratory cell protein
Identifiers
Symbols	AAMP;
External IDs	OMIM: 603488 MGI: 107809 HomoloGene: 846 GeneCards: AAMP Gene
Gene Ontology Molecular function • heparin binding Cellular component • cytoplasm • plasma membrane • cell surface Biological process • angiogenesis • multicellular organismal development • positive regulation of endothelial cell migration • smooth muscle cell migration • cell differentiation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	14	227290
Ensembl	ENSG00000127837	ENSMUSG00000006299
UniProt	Q13685	n/a
RefSeq (mRNA)	NM_001087	NM_146110
RefSeq (protein)	NP_001078	NP_666222
Location (UCSC)	Chr 2: 219.13 – 219.13 Mb	Chr 1: 74.33 – 74.33 Mb
PubMed search	[1]	[2]

Angio-associated, migratory cell protein, also known as AAMP, is a protein which in humans is encoded by the AAMP gene.

Function

The gene product is an immunoglobulin-type protein. It is found to be expressed strongly in endothelial cells, cytotrophoblasts, and poorly differentiated colon adenocarcinoma cells found in lymphatics.

The protein contains a WD40 domain and a heparin-binding domain which mediates heparin-sensitive cell adhesion.

Further reading

• Beckner ME, Krutzsch HC, Stracke ML, et al. (1995). "Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence.". Cancer Res. 55 (10): 2140–9. PMID 7743515. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Beckner ME, Krutzsch HC, Klipstein S, et al. (1996). "AAMP, a newly identified protein, shares a common epitope with alpha-actinin and a fast skeletal muscle fiber protein.". Exp. Cell Res. 225 (2): 306–14. doi:10.1006/excr.1996.0181. PMID 8660919. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Beckner ME, Peterson VA, Moul DE (1999). "Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells.". Microvasc. Res. 57 (3): 347–52. doi:10.1006/mvre.1999.2144. PMID 10329261. 
• Beckner ME, Jagannathan S, Peterson VA (2002). "Extracellular angio-associated migratory cell protein plays a positive role in angiogenesis and is regulated by astrocytes in coculture.". Microvasc. Res. 63 (3): 259–69. doi:10.1006/mvre.2001.2384. PMID 11969303. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.