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Identification
HMDB Protein ID HMDBP02363
Secondary Accession Numbers
  • 7852
Name Chitobiosyldiphosphodolichol beta-mannosyltransferase
Synonyms
  1. Asparagine-linked glycosylation protein 1 homolog
  2. Beta-1,4-mannosyltransferase
  3. GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
  4. GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
  5. MT-1
  6. Mannosyltransferase-1
  7. hMat-1
Gene Name ALG1
Protein Type Enzyme
Biological Properties
General Function Involved in biosynthetic process
Specific Function Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Pathways
  • N-Glycan biosynthesis
  • protein glycosylation
Reactions
Guanosine diphosphate mannose + (N-Acetylglucosaminyl)2-diphosphodolichol → Guanosine diphosphate + beta-1,4-D-mannosylchitobiosyldiphosphodolichol details
GDP-D-mannose + N,N'-Chitobiosyldiphosphodolichol → GDP + details
GO Classification
Biological Process
lipopolysaccharide biosynthetic process
dolichol-linked oligosaccharide biosynthetic process
post-translational protein modification
protein N-linked glycosylation via asparagine
Cellular Component
endoplasmic reticulum membrane
integral to membrane
Molecular Function
chitobiosyldiphosphodolichol beta-mannosyltransferase activity
mannosyltransferase activity
Process
metabolic process
biosynthetic process
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Single-pass type II membrane protein (Probable)
Gene Properties
Chromosome Location 16
Locus 16p13.3
SNPs ALG1
Gene Sequence
>1395 bp
ATGGCGGCCTCATGCTTGGTCCTGCTGGCGCTGTGTCTGCTGCTGCCGCTGCTGCTGCTG
GGAGGATGGAAGCGCTGGCGCCGGGGGCGGGCGGCCCGGCATGTAGTAGCGGTGGTGCTG
GGCGACGTGGGCCGCAGCCCCCGTATGCAGTACCACGCGCTGTCGTTGGCCATGCACGGC
TTCTCGGTGACCCTCCTGGGGTTCTGCAACTCCAAACCCCATGATGAGCTCTTGCAGAAC
AACAGAATTCAGATTGTGGGGTTGACAGAACTTCAGAGTCTTGCAGTTGGGCCCCGAGTT
TTCCAGTACGGAGTCAAAGTTGTACTTCAGGCTATGTACTTGCTGTGGAAGTTGATGTGG
AGGGAGCCAGGTGCCTATATCTTTCTCCAGAACCCCCCAGGTCTGCCTAGCATTGCTGTC
TGCTGGTTCGTGGGCTGCCTTTGTGGAAGCAAGCTCGTCATTGACTGGCACAACTATGGC
TACTCCATCATGGGTCTGGTGCATGGCCCCAACCATCCCCTCGTTCTGCTGGCCAAGTGG
TACGAGAAGTTCTTTGGGCGCCTGTCCCACCTGAACCTGTGTGTTACCAATGCTATGCGA
GAAGACCTGGCGGATAACTGGCACATCAGGGCTGTGACCGTCTACGACAAGCCCGCATCT
TTCTTTAAAGAGACACCTCTGGACCTGCAGCACCGGCTCTTCATGAAGCTGGGCAGCATG
CACTCTCCGTTCAGGGCCCGCTCAGAACCTGAGGACCCAGTCACGGAGCGGTCGGCCTTC
ACGGAGCGGGATGCTGGGAGCGGGCTGGTGACGCGTCTCCGTGAGCGGCCAGCCCTGCTG
GTCAGCAGCACGAGCTGGACAGAGGACGAAGACTTCTCCATCCTGCTGGCAGCTTTAGAA
AAGTTTGAACAACTGACTCTTGATGGACACAACCTTCCTTCTCTCGTCTGTGTGATAACA
GGCAAAGGGCCTCTGAGGGAGTATTATAGCCGCCTCATCCACCAGAAGCACTTCCAGCAC
ATCCAGGTCTGCACCCCCTGGCTGGAGGCCGAGGACTACCCCCTGCTTCTAGGGTCGGCG
GACCTGGGTGTCTGTCTGCACACGTCCTCCAGTGGCCTGGACCTGCCCATGAAGGTGGTG
GACATGTTCGGGTGCTGTTTGCCTGTGTGTGCTGTGAACTTCAAGTGTTTACATGAGCTG
GTGAAACATGAAGAAAATGGCCTGGTCTTTGAGGACTCAGAGGAACTGGCAGCTCAGCTG
CAGATGCTTTTCTCAAACTTTCCTGATCCTGCGGGCAAGCTAAACCAGTTCCGGAAGAAC
CTGCGGGAGTCGCAGCAGCTCCGATGGGATGAGAGCTGGGTGCAGACTGTGCTCCCTTTG
GTTATGGACACATAA
Protein Properties
Number of Residues 464
Molecular Weight 52517.685
Theoretical pI 7.228
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Chitobiosyldiphosphodolichol beta-mannosyltransferase
MAASCLVLLALCLLLPLLLLGGWKRWRRGRAARHVVAVVLGDVGRSPRMQYHALSLAMHG
FSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMW
REPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKW
YEKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLGSM
HSPFRARSEPEDPVTERSAFTERDAGSGLVTRLRERPALLVSSTSWTEDEDFSILLAALE
KFEQLTLDGHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSA
DLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQL
QMLFSNFPDPAGKLNQFRKNLRESQQLRWDESWVQTVLPLVMDT
GenBank ID Protein 6970470
UniProtKB/Swiss-Prot ID Q9BT22
UniProtKB/Swiss-Prot Entry Name ALG1_HUMAN
PDB IDs Not Available
GenBank Gene ID AB019038
GeneCard ID ALG1
GenAtlas ID ALG1
HGNC ID HGNC:18294
References
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. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed:12975309 ]
  4. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed:16303743 ]
  5. Takahashi T, Honda R, Nishikawa Y: Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1. Glycobiology. 2000 Mar;10(3):321-7. [PubMed:10704531 ]
  6. Schwarz M, Thiel C, Lubbehusen J, Dorland B, de Koning T, von Figura K, Lehle L, Korner C: Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik. Am J Hum Genet. 2004 Mar;74(3):472-81. Epub 2004 Feb 16. [PubMed:14973778 ]
  7. Kranz C, Denecke J, Lehle L, Sohlbach K, Jeske S, Meinhardt F, Rossi R, Gudowius S, Marquardt T: Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I. Am J Hum Genet. 2004 Mar;74(3):545-51. Epub 2004 Feb 17. [PubMed:14973782 ]
  8. Grubenmann CE, Frank CG, Hulsmeier AJ, Schollen E, Matthijs G, Mayatepek E, Berger EG, Aebi M, Hennet T: Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik. Hum Mol Genet. 2004 Mar 1;13(5):535-42. Epub 2004 Jan 6. [PubMed:14709599 ]