P39656 (OST48_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Short name=DDOST 48 kDa subunit
Short name=Oligosaccharyl transferase 48 kDa subunit
EC=2.4.99.18

Gene names

Name:	DDOST
Synonyms:	KIAA0115, OST48
ORF Names:	OK/SW-cl.45

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	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.
Catalytic activity	Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes even after release from the ribosome By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Involvement in disease	Congenital disorder of glycosylation 1R (CDG1R) [MIM:614507]: 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.9
Sequence similarities	Belongs to the DDOST 48 kDa subunit family.
Caution	It is uncertain whether Met-1 or Met-18 is the initiator.
Sequence caution	The sequence BAB93478.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital disorder of glycosylation Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome T cell activation Inferred from direct assay PubMed 9642163. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Inferred by curator PubMed 15835887. Source: HGNC response to cytokine stimulus Inferred from direct assay PubMed 9642163. Source: UniProtKB translation Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TMEM173	Q86WV6	2	EBI-358866,EBI-2800345

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 42	42	By similarity
	Chain	43 – 456	414	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit		PRO_0000021957
Regions
	Topological domain	43 – 427	385	Lumenal Potential
	Transmembrane	428 – 447	20	Helical; Potential
	Topological domain	448 – 456	9	Cytoplasmic Potential
Natural variations
	Natural variant	8	1	R → G. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Corresponds to variant rs537816 [ dbSNP | Ensembl ].		VAR_047911
	Natural variant	217	1	G → D in CDG1R. Ref.9		VAR_067544
Experimental info
	Sequence conflict	343	1	G → A in BAA23670. Ref.1
	Sequence conflict	434	1	S → P in BAA23670. Ref.1
	Sequence conflict	434	1	S → P in BAA06126. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P39656 [UniParc]. Last modified June 16, 2009. Version 4. Checksum: 2707ABAC8FF158CB	FASTA	456	50,801
	10 20 30 40 50 60 MGYFRCARAG SFGRRRKMEP STAARAWALF WLLLPLLGAV CASGPRTLVL LDNLNVRETH 70 80 90 100 110 120 SLFFRSLKDR GFELTFKTAD DPSLSLIKYG EFLYDNLIIF SPSVEDFGGN INVETISAFI 130 140 150 160 170 180 DGGGSVLVAA SSDIGDPLRE LGSECGIEFD EEKTAVIDHH NYDISDLGQH TLIVADTENL 190 200 210 220 230 240 LKAPTIVGKS SLNPILFRGV GMVADPDNPL VLDILTGSST SYSFFPDKPI TQYPHAVGKN 250 260 270 280 290 300 TLLIAGLQAR NNARVIFSGS LDFFSDSFFN SAVQKAAPGS QRYSQTGNYE LAVALSRWVF 310 320 330 340 350 360 KEEGVLRVGP VSHHRVGETA PPNAYTVTDL VEYSIVIQQL SNGKWVPFDG DDIQLEFVRI 370 380 390 400 410 420 DPFVRTFLKK KGGKYSVQFK LPDVYGVFQF KVDYNRLGYT HLYSSTQVSV RPLQHTQYER 430 440 450 FIPSAYPYYA SAFSMMLGLF IFSIVFLHMK EKEKSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome organization of human 48-kDa oligosaccharyltransferase (DDOST)." Yamagata T., Tsuru T., Momoi M.Y., Suwa K., Nozaki Y., Mukasa T., Ohashi H., Fukushima Y., Momoi T. Genomics 45:535-540(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-8.
[2]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-8. Tissue: Bone marrow.
[3]	"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], VARIANT GLY-8. Tissue: Synovium.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-8.
[6]	"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], VARIANT GLY-8. Tissue: Brain.
[7]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-456. Tissue: Colon adenocarcinoma.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"DDOST mutations identified by whole-exome sequencing are implicated in congenital disorders of glycosylation." Jones M.A., Ng B.G., Bhide S., Chin E., Rhodenizer D., He P., Losfeld M.E., He M., Raymond K., Berry G., Freeze H.H., Hegde M.R. Am. J. Hum. Genet. 90:363-368(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDG1R ASP-217.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D89060 Genomic DNA. Translation: BAA23670.1. D29643 mRNA. Translation: BAA06126.1. AK315633 mRNA. Translation: BAG38001.1. AL391357 Genomic DNA. Translation: CAH73476.1. CH471134 Genomic DNA. Translation: EAW94938.1. BC002594 mRNA. Translation: AAH02594.1. AB062391 mRNA. Translation: BAB93478.1. Different initiation.
IPI	IPI00297084.
PIR	A44654. S66254.
RefSeq	NP_005207.2. NM_005216.4.
UniGene	Hs.523145.
3D structure databases
ProteinModelPortal	P39656.
ModBase	Search...
Protein-protein interaction databases
IntAct	P39656. 12 interactions.
MINT	MINT-1144346.
STRING	9606.ENSP00000364188.
PTM databases
PhosphoSite	P39656.
Polymorphism databases
DMDM	239938926.
Proteomic databases
PaxDb	P39656.
PRIDE	P39656.
Protocols and materials databases
DNASU	1650.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375048; ENSP00000364188; ENSG00000244038.
GeneID	1650.
KEGG	hsa:1650.
UCSC	uc001bdo.1. human.
Organism-specific databases
CTD	1650.
GeneCards	GC01M020978.
HGNC	HGNC:2728. DDOST.
HPA	CAB009746.
MIM	602202. gene. 614507. phenotype.
neXtProt	NX_P39656.
Orphanet	300536. DDOST-CDG syndrome.
PharmGKB	PA27195.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG263094.
HOGENOM	HOG000173744.
HOVERGEN	HBG053378.
InParanoid	P39656.
KO	K12670.
OMA	HHNYDVS.
OrthoDB	EOG45HRXC.
PhylomeDB	P39656.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_6900. Immune System. REACT_71. Gene Expression.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	P39656.
Bgee	P39656.
CleanEx	HS_DDOST.
Genevestigator	P39656.
GermOnline	ENSG00000117242. Homo sapiens.
Family and domain databases
InterPro	IPR005013. WBP1. [Graphical view]
PANTHER	PTHR10830. PTHR10830. 1 hit.
Pfam	PF03345. DDOST_48kD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P39656.
ChEMBL	CHEMBL4239.
ChiTaRS	DDOST. human.
GenomeRNAi	1650.
NextBio	6796.
SOURCE	Search...

Entry information

Entry name

OST48_HUMAN

Accession

Primary (citable) accession number: P39656
Secondary accession number(s): B2RDQ4 , O43244, Q5VWA5, Q8NI93, Q9BUI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	June 16, 2009
Last modified:	May 29, 2013
This is version 131 of the entry and version 4 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.