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Identification
HMDB Protein ID HMDBP02106
Secondary Accession Numbers
  • 7588
Name Annexin A5
Synonyms
  1. Anchorin CII
  2. Annexin V
  3. Annexin-5
  4. CBP-I
  5. Calphobindin I
  6. Endonexin II
  7. Lipocortin V
  8. PAP-I
  9. PP4
  10. Placental anticoagulant protein 4
  11. Placental anticoagulant protein I
  12. Thromboplastin inhibitor
  13. VAC-alpha
  14. Vascular anticoagulant-alpha
Gene Name ANXA5
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific Function This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
calcium-dependent phospholipid binding
calcium ion binding
lipid binding
phospholipid binding
Process
regulation of coagulation
negative regulation of coagulation
biological regulation
regulation of biological process
regulation of multicellular organismal process
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:4
Locus 4q26-q28|4q27
SNPs ANXA5
Gene Sequence
>963 bp
ATGGCACAGGTTCTCAGAGGCACTGTGACTGACTTCCCTGGATTTGATGAGCGGGCTGAT
GCAGAAACTCTTCGGAAGGCTATGAAAGGCTTGGGCACAGATGAGGAGAGCATCCTGACT
CTGTTGACATCCCGAAGTAATGCTCAGCGCCAGGAAATCTCTGCAGCTTTTAAGACTCTG
TTTGGCAGGGATCTTCTGGATGACCTGAAATCAGAACTAACTGGAAAATTTGAAAAATTA
ATTGTGGCTCTGATGAAACCCTCTCGGCTTTATGATGCTTATGAACTGAAACATGCCTTG
AAGGGAGCTGGAACAAATGAAAAAGTACTGACAGAAATTATTGCTTCAAGGACACCTGAA
GAACTGAGAGCCATCAAACAAGTTTATGAAGAAGAATATGGCTCAAGCCTGGAAGATGAC
GTGGTGGGGGACACTTCAGGGTACTACCAGCGGATGTTGGTGGTTCTCCTTCAGGCTAAC
AGAGACCCTGATGCTGGAATTGATGAAGCTCAAGTTGAACAAGATGCTCAGGCTTTATTT
CAGGCTGGAGAACTTAAATGGGGGACAGATGAAGAAAAGTTTATCACCATCTTTGGAACA
CGAAGTGTGTCTCATTTGAGAAAGGTGTTTGACAAGTACATGACTATATCAGGATTTCAA
ATTGAGGAAACCATTGACCGCGAGACTTCTGGCAATTTAGAGCAACTACTCCTTGCTGTT
GTGAAATCTATTCGAAGTATACCTGCCTACCTTGCAGAGACCCTCTATTATGCTATGAAG
GGAGCTGGGACAGATGATCATACCCTCATCAGAGTCATGGTTTCCAGGAGTGAGATTGAT
CTGTTTAACATCAGGAAGGAGTTTAGGAAGAATTTTGCCACCTCTCTTTATTCCATGATT
AAGGGAGATACATCTGGGGACTATAAGAAAGCTCTTCTGCTGCTCTGTGGAGAAGATGAC
TAA
Protein Properties
Number of Residues 320
Molecular Weight 35936.4
Theoretical pI 4.66
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Annexin A5
MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTL
FGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPE
ELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALF
QAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAV
VKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMI
KGDTSGDYKKALLLLCGEDD
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P08758
UniProtKB/Swiss-Prot Entry Name ANXA5_HUMAN
PDB IDs
GenBank Gene ID M18366
GeneCard ID ANXA5
GenAtlas ID ANXA5
HGNC ID HGNC:543
References
General References
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  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed:16916647 ]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  8. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed:15242332 ]
  9. Pepinsky RB, Tizard R, Mattaliano RJ, Sinclair LK, Miller GT, Browning JL, Chow EP, Burne C, Huang KS, Pratt D, et al.: Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. J Biol Chem. 1988 Aug 5;263(22):10799-811. [PubMed:2968983 ]
  10. Funakoshi T, Hendrickson LE, McMullen BA, Fujikawa K: Primary structure of human placental anticoagulant protein. Biochemistry. 1987 Dec 15;26(25):8087-92. [PubMed:2964863 ]
  11. Iwasaki A, Suda M, Nakao H, Nagoya T, Saino Y, Arai K, Mizoguchi T, Sato F, Yoshizaki H, Hirata M, et al.: Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein. J Biochem. 1987 Nov;102(5):1261-73. [PubMed:2963810 ]
  12. Maurer-Fogy I, Reutelingsperger CP, Pieters J, Bodo G, Stratowa C, Hauptmann R: Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein. Eur J Biochem. 1988 Jul 1;174(4):585-92. [PubMed:2455636 ]
  13. Kaplan R, Jaye M, Burgess WH, Schlaepfer DD, Haigler HT: Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein. J Biol Chem. 1988 Jun 15;263(17):8037-43. [PubMed:2967291 ]
  14. Grundmann U, Abel KJ, Bohn H, Lobermann H, Lottspeich F, Kupper H: Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3708-12. [PubMed:2967495 ]
  15. Fernandez MP, Morgan RO, Fernandez MR, Carcedo MT: The gene encoding human annexin V has a TATA-less promoter with a high G+C content. Gene. 1994 Nov 18;149(2):253-60. [PubMed:7958998 ]
  16. Cookson BT, Engelhardt S, Smith C, Bamford HA, Prochazka M, Tait JF: Organization of the human annexin V (ANX5) gene. Genomics. 1994 Apr;20(3):463-7. [PubMed:8034319 ]
  17. Rothhut B, Comera C, Cortial S, Haumont PY, Diep Le KH, Cavadore JC, Conard J, Russo-Marie F, Lederer F: A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation. Biochem J. 1989 Nov 1;263(3):929-35. [PubMed:2532007 ]
  18. Hertogs K, Leenders WP, Depla E, De Bruin WC, Meheus L, Raymackers J, Moshage H, Yap SH: Endonexin II, present on human liver plasma membranes, is a specific binding protein of small hepatitis B virus (HBV) envelope protein. Virology. 1993 Dec;197(2):549-57. [PubMed:8249278 ]
  19. Schlaepfer DD, Mehlman T, Burgess WH, Haigler HT: Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6078-82. [PubMed:2957692 ]
  20. Ahn NG, Teller DC, Bienkowski MJ, McMullen BA, Lipkin EW, de Haen C: Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor. J Biol Chem. 1988 Dec 15;263(35):18657-63. [PubMed:2974032 ]
  21. Huber R, Romisch J, Paques EP: The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 1990 Dec;9(12):3867-74. [PubMed:2147412 ]
  22. Huber R, Schneider M, Mayr I, Romisch J, Paques EP: The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. FEBS Lett. 1990 Nov 26;275(1-2):15-21. [PubMed:2148156 ]
  23. Huber R, Berendes R, Burger A, Schneider M, Karshikov A, Luecke H, Romisch J, Paques E: Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J Mol Biol. 1992 Feb 5;223(3):683-704. [PubMed:1311770 ]
  24. Kaneko N, Ago H, Matsuda R, Inagaki E, Miyano M: Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor. J Mol Biol. 1997 Nov 21;274(1):16-20. [PubMed:9398511 ]
  25. Budisa N, Minks C, Medrano FJ, Lutz J, Huber R, Moroder L: Residue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: structure and stability of the per-thiaproline mutant of annexin V. Proc Natl Acad Sci U S A. 1998 Jan 20;95(2):455-9. [PubMed:9435213 ]