P53868

Name	Alpha-1,2-mannosyltransferase ALG9 (EC 2.4.1.259) (EC 2.4.1.261) (Asparagine-linked glycosylation protein 9) (Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase)
Uniprot ID	P53868
Systematic gene name	YNL219C
Standard gene name	ALG9
Gene names	ALG9 YNL219C N1295
Description from SGD	YNL219C ALG9 SGDID:S000005163, Chr XIV from 237663-235996, Genome Release 64-3-1, reverse complement, Verified ORF, "Mannosyltransferase, involved in N-linked glycosylation; catalyzes the transfer of both the seventh mannose residue on B-arm and ninth mannose residue on the C-arm from Dol-P-Man to lipid-linked oligosaccharides; human homolog ALG9 can complement yeast null mutant; mutation of human homolog causes type 1 congenital disorders of glycosylation"
Protein length	555
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MNCKAVTISL LLLLFLTRVY IQPTFSLISD CDETFNYWEP LNLLVRGFGK
QTWEYSPEYS IRSWAFLLPF YCILYPVNKF TDLESHWNFF ITRACLGFFS
FIMEFKLHRE IAGSLALQIA NIWIIFQLFN PGWFHASVEL LPSAVAMLLY
VGATRHSLRY LSTGSTSNFT KSLAYNFLAS ILGWPFVLIL SLPLCLHYLF
NHRIISTIRT AFDCCLIFSL TAFAVIVTDS IFYGKLAPVS WNILFYNVIN
ASEESGPNIF GVEPWYYYPL NLLLNFPLPV LVLAILGIFH LRLWPLWASL
FTWIAVFTQQ PHKEERFLYP IYGLITLSAS IAFYKVLNLF NRKPILKKGI
KLSVLLIVAG QAMSRIVALV NNYTAPIAVY EQFSSLNQGG VKAPVVNVCT
GREWYHFPSS FLLPDNHRLK FVKSGFDGLL PGDFPESGSI FKKIRTLPKG
MNNKNIYDTG KEWPITRCDY FIDIVAPINL TKDVFNPLHL MDNWNKLACA
AFIDGENSKI LGRAFYVPEP INRIMQIVLP KQWNQVYGVR YIDYCLFEKP
TETTN

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[50, Ubi]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[479, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[509, Ubi]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)