Q92685 (ALG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
EC=2.4.1.258

Alternative name(s):
Asparagine-linked glycosylation protein 3 homolog
Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
Not56-like protein

Gene names

Name:	ALG3
Synonyms:	NOT, NOT56L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. Ref.5
Catalytic activity	Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.
Involvement in disease	Congenital disorder of glycosylation 1D (CDG1D) [MIM:601110]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.10
Sequence similarities	Belongs to the glycosyltransferase 58 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Disease	Congenital disorder of glycosylation Disease mutation
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.5. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alpha-1,3-mannosyltransferase activity Inferred from direct assay Ref.5. Source: UniProtKB dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92685-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q92685-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MAAGLRKRGR...TFWVIHRVAY → MFPAQAKENAGFSGCGGD

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase		PRO_0000080566
Regions
	Transmembrane	41 – 61	21	Helical; Potential
	Transmembrane	95 – 115	21	Helical; Potential
	Transmembrane	123 – 143	21	Helical; Potential
	Transmembrane	149 – 169	21	Helical; Potential
	Transmembrane	172 – 192	21	Helical; Potential
	Transmembrane	203 – 223	21	Helical; Potential
	Transmembrane	231 – 251	21	Helical; Potential
	Transmembrane	289 – 309	21	Helical; Potential
	Transmembrane	332 – 352	21	Helical; Potential
	Transmembrane	356 – 376	21	Helical; Potential
	Transmembrane	407 – 427	21	Helical; Potential
Natural variations
	Alternative sequence	1 – 66	66	MAAGL…HRVAY → MFPAQAKENAGFSGCGGD in isoform 2.		VSP_042738
	Natural variant	107	1	I → V. Corresponds to variant rs2233463 [ dbSNP | Ensembl ].		VAR_037805
	Natural variant	118	1	G → D in CDG1D. Ref.5 Corresponds to variant rs28940588 [ dbSNP | Ensembl ].		VAR_010306
	Natural variant	171	1	R → Q in CDG1D. Ref.10		VAR_037806

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 687FC8E4A588FD9C	FASTA	438	50,126
	10 20 30 40 50 60 MAAGLRKRGR SGSAAQAEGL CKQWLQRAWQ ERRLLLREPR YTLLVAACLC LAEVGITFWV 70 80 90 100 110 120 IHRVAYTEID WKAYMAEVEG VINGTYDYTQ LQGDTGPLVY PAGFVYIFMG LYYATSRGTD 130 140 150 160 170 180 IRMAQNIFAV LYLATLLLVF LIYHQTCKVP PFVFFFMCCA SYRVHSIFVL RLFNDPVAMV 190 200 210 220 230 240 LLFLSINLLL AQRWGWGCCF FSLAVSVKMN VLLFAPGLLF LLLTQFGFRG ALPKLGICAG 250 260 270 280 290 300 LQVVLGLPFL LENPSGYLSR SFDLGRQFLF HWTVNWRFLP EALFLHRAFH LALLTAHLTL 310 320 330 340 350 360 LLLFALCRWH RTGESILSLL RDPSKRKVPP QPLTPNQIVS TLFTSNFIGI CFSRSLHYQF 370 380 390 400 410 420 YVWYFHTLPY LLWAMPARWL THLLRLLVLG LIELSWNTYP STSCSSAALH ICHAVILLQL 430 WLGPQPFPKS TQHSKKAH
	Isoform 2 [UniParc]. Checksum: CCE950E0FFA23449	FASTA	390	44,370
	10 20 30 40 50 60 MFPAQAKENA GFSGCGGDTE IDWKAYMAEV EGVINGTYDY TQLQGDTGPL VYPAGFVYIF 70 80 90 100 110 120 MGLYYATSRG TDIRMAQNIF AVLYLATLLL VFLIYHQTCK VPPFVFFFMC CASYRVHSIF 130 140 150 160 170 180 VLRLFNDPVA MVLLFLSINL LLAQRWGWGC CFFSLAVSVK MNVLLFAPGL LFLLLTQFGF 190 200 210 220 230 240 RGALPKLGIC AGLQVVLGLP FLLENPSGYL SRSFDLGRQF LFHWTVNWRF LPEALFLHRA 250 260 270 280 290 300 FHLALLTAHL TLLLLFALCR WHRTGESILS LLRDPSKRKV PPQPLTPNQI VSTLFTSNFI 310 320 330 340 350 360 GICFSRSLHY QFYVWYFHTL PYLLWAMPAR WLTHLLRLLV LGLIELSWNT YPSTSCSSAA 370 380 390 LHICHAVILL QLWLGPQPFP KSTQHSKKAH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the human homologue of the Drosophila melanogaster Not56 protein and its expression in various tissues." Kurzik-Dumke U., Kaymer M. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Placenta.
[5]	"Carbohydrate deficient glycoprotein syndrome type IV: deficiency of dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase." Koerner C., Knauer R., Stephani U., Marquardt T., Lehle L., von Figura K. EMBO J. 18:6816-6822(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, VARIANT CDG1D ASP-118, FUNCTION.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Congenital disorder of glycosylation Id presenting with hyperinsulinemic hypoglycemia and islet cell hyperplasia." Sun L., Eklund E.A., Chung W.K., Wang C., Cohen J., Freeze H.H. J. Clin. Endocrinol. Metab. 90:4371-4375(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDG1D GLN-171.

Web resources

GeneReviews

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09022 mRNA. Translation: CAA70220.1. AK289361 mRNA. Translation: BAF82050.1. AC061705 Genomic DNA. No translation available. BC002839 mRNA. Translation: AAH02839.1. BC004313 mRNA. Translation: AAH04313.1.
IPI	IPI00178700. IPI00927184.
RefSeq	NP_001006942.1. NM_001006941.2. NP_005778.1. NM_005787.5.
UniGene	Hs.478481.
3D structure databases
ProteinModelPortal	Q92685.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92685. 1 interaction.
STRING	9606.ENSP00000380793.
Protein family/group databases
CAZy	GT58. Glycosyltransferase Family 58.
PTM databases
PhosphoSite	Q92685.
Polymorphism databases
DMDM	3024226.
Proteomic databases
PaxDb	Q92685.
PRIDE	Q92685.
Protocols and materials databases
DNASU	10195.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397676; ENSP00000380793; ENSG00000214160. ENST00000445626; ENSP00000402744; ENSG00000214160.
GeneID	10195.
KEGG	hsa:10195.
UCSC	uc003fne.2. human.
Organism-specific databases
CTD	10195.
GeneCards	GC03M183960.
HGNC	HGNC:23056. ALG3.
HPA	HPA045103.
MIM	601110. phenotype. 608750. gene.
neXtProt	NX_Q92685.
Orphanet	79321. CDG syndrome type Id.
PharmGKB	PA134897460.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG241920.
HOGENOM	HOG000237555.
HOVERGEN	HBG002070.
InParanoid	Q92685.
KO	K03845.
OMA	LAVSVKM.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q92685.
Bgee	Q92685.
CleanEx	HS_ALG3.
Genevestigator	Q92685.
Family and domain databases
InterPro	IPR007873. Glycosyltransferase_ALG3. [Graphical view]
PANTHER	PTHR12646. PTHR12646. 1 hit.
Pfam	PF05208. ALG3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ALG3. human.
GenomeRNAi	10195.
NextBio	38584.
SOURCE	Search...

Entry information

Entry name

ALG3_HUMAN

Accession

Primary (citable) accession number: Q92685
Secondary accession number(s): A8JZZ6, Q9BT71

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.