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HMDB Protein ID HMDBP00372
Secondary Accession Numbers
  • 5608
Name Alpha-lactalbumin
  1. Lactose synthase B protein
  2. Lysozyme-like protein 7
Gene Name LALBA
Protein Type Enzyme
Biological Properties
General Function Involved in lactose synthase activity
Specific Function Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
  • Congenital disorder of glycosylation CDG-IId
  • Galactose metabolism
  • GLUT-1 deficiency syndrome
  • Lactose Synthesis
Uridine diphosphategalactose + D-Glucose → Uridine 5'-diphosphate + beta-Lactose details
GO Classification
Biological Process
signal transduction
cell-cell signaling
lactose biosynthetic process
defense response to bacterium
induction of apoptosis
Cellular Component
extracellular space
ion binding
cation binding
metal ion binding
catalytic activity
transferase activity
udp-glycosyltransferase activity
udp-galactosyltransferase activity
lactose synthase activity
transferase activity, transferring glycosyl groups
calcium ion binding
Molecular Function
lactose synthase activity
calcium ion binding
metabolic process
primary metabolic process
carbohydrate metabolic process
oligosaccharide metabolic process
disaccharide metabolic process
lactose metabolic process
lactose biosynthetic process
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Not Available
Locus Not Available
Gene Sequence
>429 bp
Protein Properties
Number of Residues 142
Molecular Weight Not Available
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
GenBank ID Protein 307104
UniProtKB/Swiss-Prot ID P00709
UniProtKB/Swiss-Prot Entry Name LALBA_HUMAN
GenBank Gene ID J00270
General References
  1. 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 ]
  2. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. doi: 10.1002/pmic.200701057. [PubMed:18780401 ]
  3. Hall L, Craig RK, Edbrooke MR, Campbell PN: Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene. Nucleic Acids Res. 1982 Jun 11;10(11):3503-15. [PubMed:6285305 ]
  4. Hall L, Emery DC, Davies MS, Parker D, Craig RK: Organization and sequence of the human alpha-lactalbumin gene. Biochem J. 1987 Mar 15;242(3):735-42. [PubMed:2954544 ]
  5. Findlay JB, Brew K: The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65-86. [PubMed:5049057 ]
  6. Maynard F: Identification of a new molecular form of human alpha-lactalbumin. J Dairy Res. 1992 Aug;59(3):425-9. [PubMed:1401360 ]
  7. Acharya KR, Ren JS, Stuart DI, Phillips DC, Fenna RE: Crystal structure of human alpha-lactalbumin at 1.7 A resolution. J Mol Biol. 1991 Sep 20;221(2):571-81. [PubMed:1920433 ]
  8. Ren J, Stuart DI, Acharya KR: Alpha-lactalbumin possesses a distinct zinc binding site. J Biol Chem. 1993 Sep 15;268(26):19292-8. [PubMed:8366079 ]
  9. Chandra N, Brew K, Acharya KR: Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 1998 Apr 7;37(14):4767-72. [PubMed:9537992 ]
  10. Harata K, Abe Y, Muraki M: Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method. J Mol Biol. 1999 Mar 26;287(2):347-58. [PubMed:10080897 ]
  11. Chowanadisai W, Kelleher SL, Nemeth JF, Yachetti S, Kuhlman CF, Jackson JG, Davis AM, Lien EL, Lonnerdal B: Detection of a single nucleotide polymorphism in the human alpha-lactalbumin gene: implications for human milk proteins. J Nutr Biochem. 2005 May;16(5):272-8. [PubMed:15866226 ]