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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit

Gene

DDOST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • gene expression Source: Reactome
  • innate immune response Source: Reactome
  • post-translational protein modification Source: Reactome
  • protein glycosylation Source: UniProtKB
  • protein N-linked glycosylation Source: UniProtKB
  • protein N-linked glycosylation via asparagine Source: HGNC
  • response to cytokine Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • T cell activation Source: UniProtKB
  • translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_22426. Asparagine N-linked glycosylation.
REACT_25195. Advanced glycosylation endproduct receptor signaling.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit (EC:2.4.99.18)
Short name:
DDOST 48 kDa subunit
Short name:
Oligosaccharyl transferase 48 kDa subunit
Gene namesi
Name:DDOST
Synonyms:KIAA0115, OST48
ORF Names:OK/SW-cl.45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2728. DDOST.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini43 – 427385LumenalSequence AnalysisAdd
BLAST
Transmembranei428 – 44720HelicalSequence AnalysisAdd
BLAST
Topological domaini448 – 4569CytoplasmicSequence Analysis

GO - Cellular componenti

  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: UniProtKB
  • membrane Source: UniProtKB
  • oligosaccharyltransferase complex Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1R (CDG1R)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614507
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171G → D in CDG1R. 1 Publication
VAR_067544

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi614507. phenotype.
Orphaneti300536. DDOST-CDG.
PharmGKBiPA27195.

Polymorphism and mutation databases

BioMutaiDDOST.
DMDMi239938926.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242By similarityAdd
BLAST
Chaini43 – 456414Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunitPRO_0000021957Add
BLAST

Proteomic databases

MaxQBiP39656.
PaxDbiP39656.
PRIDEiP39656.

PTM databases

PhosphoSiteiP39656.

Expressioni

Gene expression databases

BgeeiP39656.
CleanExiHS_DDOST.
ExpressionAtlasiP39656. baseline and differential.
GenevisibleiP39656. HS.

Organism-specific databases

HPAiCAB009746.
HPA046841.
HPA052867.

Interactioni

Subunit structurei

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). Also identified as part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. This contains known members of the OST complex and may be a form of this complex.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TMEM173Q86WV62EBI-358866,EBI-2800345

Protein-protein interaction databases

BioGridi108017. 41 interactions.
IntActiP39656. 19 interactions.
MINTiMINT-1144346.
STRINGi9606.ENSP00000364188.

Structurei

3D structure databases

ProteinModelPortaliP39656.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DDOST 48 kDa subunit family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG263094.
GeneTreeiENSGT00390000017294.
HOGENOMiHOG000173744.
HOVERGENiHBG053378.
InParanoidiP39656.
KOiK12670.
OMAiAFSMMIG.
OrthoDBiEOG7K6PV7.
PhylomeDBiP39656.
TreeFamiTF314821.

Family and domain databases

InterProiIPR005013. WBP1.
[Graphical view]
PANTHERiPTHR10830. PTHR10830. 1 hit.
PfamiPF03345. DDOST_48kD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P39656-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGYFRCARAG SFGRRRKMEP STAARAWALF WLLLPLLGAV CASGPRTLVL
60 70 80 90 100
LDNLNVRETH SLFFRSLKDR GFELTFKTAD DPSLSLIKYG EFLYDNLIIF
110 120 130 140 150
SPSVEDFGGN INVETISAFI DGGGSVLVAA SSDIGDPLRE LGSECGIEFD
160 170 180 190 200
EEKTAVIDHH NYDISDLGQH TLIVADTENL LKAPTIVGKS SLNPILFRGV
210 220 230 240 250
GMVADPDNPL VLDILTGSST SYSFFPDKPI TQYPHAVGKN TLLIAGLQAR
260 270 280 290 300
NNARVIFSGS LDFFSDSFFN SAVQKAAPGS QRYSQTGNYE LAVALSRWVF
310 320 330 340 350
KEEGVLRVGP VSHHRVGETA PPNAYTVTDL VEYSIVIQQL SNGKWVPFDG
360 370 380 390 400
DDIQLEFVRI DPFVRTFLKK KGGKYSVQFK LPDVYGVFQF KVDYNRLGYT
410 420 430 440 450
HLYSSTQVSV RPLQHTQYER FIPSAYPYYA SAFSMMLGLF IFSIVFLHMK

EKEKSD
Length:456
Mass (Da):50,801
Last modified:June 16, 2009 - v4
Checksum:i2707ABAC8FF158CB
GO
Isoform 2 (identifier: P39656-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-105: Missing.

Note: No experimental confirmation available.
Show »
Length:419
Mass (Da):46,577
Checksum:i10E4676DD22C6150
GO
Isoform 3 (identifier: P39656-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-141: Missing.

Note: No experimental confirmation available.
Show »
Length:438
Mass (Da):49,020
Checksum:i1757A69899347B0D
GO

Sequence cautioni

The sequence BAB93478.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291P → R in BAG59544 (PubMed:14702039).Curated
Sequence conflicti343 – 3431G → A in BAA23670 (PubMed:9367678).Curated
Sequence conflicti434 – 4341S → P in BAA23670 (PubMed:9367678).Curated
Sequence conflicti434 – 4341S → P in BAA06126 (PubMed:7788527).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81R → G.5 Publications
Corresponds to variant rs537816 [ dbSNP | Ensembl ].
VAR_047911
Natural varianti217 – 2171G → D in CDG1R. 1 Publication
VAR_067544

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 10537Missing in isoform 2. 1 PublicationVSP_055498Add
BLAST
Alternative sequencei124 – 14118Missing in isoform 3. 1 PublicationVSP_055499Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89060 Genomic DNA. Translation: BAA23670.1.
D29643 mRNA. Translation: BAA06126.1.
AK296041 mRNA. Translation: BAG58805.1.
AK297009 mRNA. Translation: BAG59544.1.
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.
CCDSiCCDS212.1. [P39656-1]
PIRiS66254. A44654.
RefSeqiNP_005207.2. NM_005216.4.
UniGeneiHs.523145.

Genome annotation databases

EnsembliENST00000375048; ENSP00000364188; ENSG00000244038.
ENST00000415136; ENSP00000399457; ENSG00000244038.
GeneIDi1650.
KEGGihsa:1650.
UCSCiuc001bdo.1. human. [P39656-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89060 Genomic DNA. Translation: BAA23670.1.
D29643 mRNA. Translation: BAA06126.1.
AK296041 mRNA. Translation: BAG58805.1.
AK297009 mRNA. Translation: BAG59544.1.
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.
CCDSiCCDS212.1. [P39656-1]
PIRiS66254. A44654.
RefSeqiNP_005207.2. NM_005216.4.
UniGeneiHs.523145.

3D structure databases

ProteinModelPortaliP39656.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108017. 41 interactions.
IntActiP39656. 19 interactions.
MINTiMINT-1144346.
STRINGi9606.ENSP00000364188.

Chemistry

BindingDBiP39656.
ChEMBLiCHEMBL4239.

PTM databases

PhosphoSiteiP39656.

Polymorphism and mutation databases

BioMutaiDDOST.
DMDMi239938926.

Proteomic databases

MaxQBiP39656.
PaxDbiP39656.
PRIDEiP39656.

Protocols and materials databases

DNASUi1650.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375048; ENSP00000364188; ENSG00000244038.
ENST00000415136; ENSP00000399457; ENSG00000244038.
GeneIDi1650.
KEGGihsa:1650.
UCSCiuc001bdo.1. human. [P39656-1]

Organism-specific databases

CTDi1650.
GeneCardsiGC01M020978.
GeneReviewsiDDOST.
HGNCiHGNC:2728. DDOST.
HPAiCAB009746.
HPA046841.
HPA052867.
MIMi602202. gene.
614507. phenotype.
neXtProtiNX_P39656.
Orphaneti300536. DDOST-CDG.
PharmGKBiPA27195.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263094.
GeneTreeiENSGT00390000017294.
HOGENOMiHOG000173744.
HOVERGENiHBG053378.
InParanoidiP39656.
KOiK12670.
OMAiAFSMMIG.
OrthoDBiEOG7K6PV7.
PhylomeDBiP39656.
TreeFamiTF314821.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_22426. Asparagine N-linked glycosylation.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Miscellaneous databases

ChiTaRSiDDOST. human.
GeneWikiiDDOST.
GenomeRNAii1650.
NextBioi35472509.
PROiP39656.
SOURCEiSearch...

Gene expression databases

BgeeiP39656.
CleanExiHS_DDOST.
ExpressionAtlasiP39656. baseline and differential.
GenevisibleiP39656. HS.

Family and domain databases

InterProiIPR005013. WBP1.
[Graphical view]
PANTHERiPTHR10830. PTHR10830. 1 hit.
PfamiPF03345. DDOST_48kD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORMS 1; 2 AND 3), VARIANT GLY-8.
    Tissue: Subthalamic nucleus, Synovium and Umbilical cord blood.
  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. 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] (ISOFORM 1), 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 (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
    Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; RPN1; RPN2; SELK; STT3A; VCP AND VIMP.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "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.

Entry informationi

Entry nameiOST48_HUMAN
AccessioniPrimary (citable) accession number: P39656
Secondary accession number(s): B2RDQ4
, B4DJE3, B4DLI2, O43244, Q5VWA5, Q8NI93, Q9BUI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: July 22, 2015
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-18 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.