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Protein

Dehydrodolichyl diphosphate syntase complex subunit DHDDS

Gene

DHDDS

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

Functioni

With DHDDS, forms the dehydrodolichyl diphosphate syntase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol.1 Publication1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).1 Publication

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
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

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.87. 2681.
ReactomeiREACT_22230. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrodolichyl diphosphate syntase complex subunit DHDDSCurated (EC:2.5.1.871 Publication)
Alternative name(s):
Cis-isoprenyltransferase
Short name:
CIT
Short name:
Cis-IPTase
Epididymis tissue protein Li 189m
Gene namesi
Name:DHDDS
Synonyms:HDS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20603. DHDDS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 59 (RP59)1 Publication

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

Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

See also OMIM:613861
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421K → E in RP59. 1 Publication
VAR_065356

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi613861. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA134867119.

Polymorphism and mutation databases

BioMutaiDHDDS.
DMDMi116241329.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Dehydrodolichyl diphosphate syntase complex subunit DHDDSPRO_0000123749Add
BLAST

Proteomic databases

MaxQBiQ86SQ9.
PaxDbiQ86SQ9.
PRIDEiQ86SQ9.

PTM databases

PhosphoSiteiQ86SQ9.

Expressioni

Tissue specificityi

Expressed at high levels in testis and kidney. Expressed in epididymis (at protein level). Slightly expressed in heart, spleen and thymus.1 Publication

Gene expression databases

BgeeiQ86SQ9.
CleanExiHS_DHDDS.
ExpressionAtlasiQ86SQ9. baseline and differential.
GenevisibleiQ86SQ9. HS.

Organism-specific databases

HPAiHPA026721.
HPA026727.

Interactioni

Subunit structurei

Forms an active dehydrodolichyl diphosphate syntase complex with NUS1. Interacts with NPC2.2 Publications

Protein-protein interaction databases

BioGridi123018. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ86SQ9.
SMRiQ86SQ9. Positions 27-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Phylogenomic databases

eggNOGiCOG0020.
GeneTreeiENSGT00390000007879.
HOVERGENiHBG051350.
InParanoidiQ86SQ9.
KOiK11778.
OMAiNLGICEV.
PhylomeDBiQ86SQ9.
TreeFamiTF323753.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86SQ9-1) [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
MSWIKEGELS LWERFCANII KAGPMPKHIA FIMDGNRRYA KKCQVERQEG
60 70 80 90 100
HSQGFNKLAE TLRWCLNLGI LEVTVYAFSI ENFKRSKSEV DGLMDLARQK
110 120 130 140 150
FSRLMEEKEK LQKHGVCIRV LGDLHLLPLD LQELIAQAVQ ATKNYNKCFL
160 170 180 190 200
NVCFAYTSRH EISNAVREMA WGVEQGLLDP SDISESLLDK CLYTNRSPHP
210 220 230 240 250
DILIRTSGEV RLSDFLLWQT SHSCLVFQPV LWPEYTFWNL FEAILQFQMN
260 270 280 290 300
HSVLQKARDM YAEERKRQQL ERDQATVTEQ LLREGLQASG DAQLRRTRLH
310 320 330
KLSARREERV QGFLQALELK RADWLARLGT ASA
Length:333
Mass (Da):38,657
Last modified:October 17, 2006 - v3
Checksum:i12EF3A15437A2583
GO
Isoform 2 (identifier: Q86SQ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     255-255: Q → QQ

Show »
Length:334
Mass (Da):38,786
Checksum:i8B91F530F1E538E2
GO
Isoform 3 (identifier: Q86SQ9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-147: Missing.

Note: May be due to exon skipping.
Show »
Length:294
Mass (Da):34,264
Checksum:i1EF92BC4658FFDF9
GO
Isoform 4 (identifier: Q86SQ9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     147-181: KCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPS → N

Note: No experimental confirmation available.
Show »
Length:299
Mass (Da):34,817
Checksum:i55AE4DA2A326CA58
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511N → Y in BAB14439 (PubMed:14702039).Curated
Sequence conflicti277 – 2771V → E in AAH34152 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421K → E in RP59. 1 Publication
VAR_065356
Natural varianti253 – 2531V → M.3 Publications
Corresponds to variant rs3816539 [ dbSNP | Ensembl ].
VAR_028088

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei109 – 14739Missing in isoform 3. 1 PublicationVSP_010030Add
BLAST
Alternative sequencei147 – 18135KCFLN…LLDPS → N in isoform 4. 1 PublicationVSP_045007Add
BLAST
Alternative sequencei255 – 2551Q → QQ in isoform 2. 1 PublicationVSP_010031

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB090852 mRNA. Translation: BAC57588.1.
GU727641 mRNA. Translation: ADU87642.1.
AK023164 mRNA. Translation: BAB14439.1.
AK297134 mRNA. Translation: BAH12505.1.
AK316485 mRNA. Translation: BAH14856.1.
AL513365 Genomic DNA. Translation: CAI21495.1.
CH471059 Genomic DNA. Translation: EAX07806.1.
CH471059 Genomic DNA. Translation: EAX07808.1.
CH471059 Genomic DNA. Translation: EAX07809.1.
CH471059 Genomic DNA. Translation: EAX07810.1.
CH471059 Genomic DNA. Translation: EAX07811.1.
CH471059 Genomic DNA. Translation: EAX07812.1.
BC003643 mRNA. Translation: AAH03643.1.
BC004117 mRNA. Translation: AAH04117.1.
BC034152 mRNA. Translation: AAH34152.1.
CCDSiCCDS281.1. [Q86SQ9-2]
CCDS282.1. [Q86SQ9-1]
CCDS57983.1. [Q86SQ9-4]
CCDS57984.1. [Q86SQ9-3]
RefSeqiNP_001230493.1. NM_001243564.1. [Q86SQ9-4]
NP_001230494.1. NM_001243565.1. [Q86SQ9-3]
NP_079163.2. NM_024887.3. [Q86SQ9-2]
NP_995583.1. NM_205861.2. [Q86SQ9-1]
XP_006710975.1. XM_006710912.1. [Q86SQ9-2]
XP_006710976.1. XM_006710913.1. [Q86SQ9-2]
XP_006710977.1. XM_006710914.1. [Q86SQ9-2]
UniGeneiHs.369385.

Genome annotation databases

EnsembliENST00000236342; ENSP00000236342; ENSG00000117682. [Q86SQ9-1]
ENST00000360009; ENSP00000353104; ENSG00000117682. [Q86SQ9-2]
ENST00000525682; ENSP00000434984; ENSG00000117682. [Q86SQ9-4]
ENST00000526219; ENSP00000434219; ENSG00000117682. [Q86SQ9-3]
GeneIDi79947.
KEGGihsa:79947.
UCSCiuc001bmk.3. human. [Q86SQ9-2]
uc001bml.3. human. [Q86SQ9-1]
uc001bmn.3. human. [Q86SQ9-3]
uc010ofd.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB090852 mRNA. Translation: BAC57588.1.
GU727641 mRNA. Translation: ADU87642.1.
AK023164 mRNA. Translation: BAB14439.1.
AK297134 mRNA. Translation: BAH12505.1.
AK316485 mRNA. Translation: BAH14856.1.
AL513365 Genomic DNA. Translation: CAI21495.1.
CH471059 Genomic DNA. Translation: EAX07806.1.
CH471059 Genomic DNA. Translation: EAX07808.1.
CH471059 Genomic DNA. Translation: EAX07809.1.
CH471059 Genomic DNA. Translation: EAX07810.1.
CH471059 Genomic DNA. Translation: EAX07811.1.
CH471059 Genomic DNA. Translation: EAX07812.1.
BC003643 mRNA. Translation: AAH03643.1.
BC004117 mRNA. Translation: AAH04117.1.
BC034152 mRNA. Translation: AAH34152.1.
CCDSiCCDS281.1. [Q86SQ9-2]
CCDS282.1. [Q86SQ9-1]
CCDS57983.1. [Q86SQ9-4]
CCDS57984.1. [Q86SQ9-3]
RefSeqiNP_001230493.1. NM_001243564.1. [Q86SQ9-4]
NP_001230494.1. NM_001243565.1. [Q86SQ9-3]
NP_079163.2. NM_024887.3. [Q86SQ9-2]
NP_995583.1. NM_205861.2. [Q86SQ9-1]
XP_006710975.1. XM_006710912.1. [Q86SQ9-2]
XP_006710976.1. XM_006710913.1. [Q86SQ9-2]
XP_006710977.1. XM_006710914.1. [Q86SQ9-2]
UniGeneiHs.369385.

3D structure databases

ProteinModelPortaliQ86SQ9.
SMRiQ86SQ9. Positions 27-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123018. 6 interactions.

PTM databases

PhosphoSiteiQ86SQ9.

Polymorphism and mutation databases

BioMutaiDHDDS.
DMDMi116241329.

Proteomic databases

MaxQBiQ86SQ9.
PaxDbiQ86SQ9.
PRIDEiQ86SQ9.

Protocols and materials databases

DNASUi79947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236342; ENSP00000236342; ENSG00000117682. [Q86SQ9-1]
ENST00000360009; ENSP00000353104; ENSG00000117682. [Q86SQ9-2]
ENST00000525682; ENSP00000434984; ENSG00000117682. [Q86SQ9-4]
ENST00000526219; ENSP00000434219; ENSG00000117682. [Q86SQ9-3]
GeneIDi79947.
KEGGihsa:79947.
UCSCiuc001bmk.3. human. [Q86SQ9-2]
uc001bml.3. human. [Q86SQ9-1]
uc001bmn.3. human. [Q86SQ9-3]
uc010ofd.2. human.

Organism-specific databases

CTDi79947.
GeneCardsiGC01P026758.
GeneReviewsiDHDDS.
HGNCiHGNC:20603. DHDDS.
HPAiHPA026721.
HPA026727.
MIMi608172. gene.
613861. phenotype.
neXtProtiNX_Q86SQ9.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA134867119.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0020.
GeneTreeiENSGT00390000007879.
HOVERGENiHBG051350.
InParanoidiQ86SQ9.
KOiK11778.
OMAiNLGICEV.
PhylomeDBiQ86SQ9.
TreeFamiTF323753.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.5.1.87. 2681.
ReactomeiREACT_22230. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

ChiTaRSiDHDDS. human.
GeneWikiiDehydrodolichyl_diphosphate_synthase.
DHDDS.
GenomeRNAii79947.
NextBioi69906.
PROiQ86SQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ86SQ9.
CleanExiHS_DHDDS.
ExpressionAtlasiQ86SQ9. baseline and differential.
GenevisibleiQ86SQ9. HS.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of human dehydrodolichyl diphosphate synthase gene."
    Endo S., Zhang Y.-W., Takahashi S., Koyama T.
    Biochim. Biophys. Acta 1625:291-295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
    Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
    Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-253, TISSUE SPECIFICITY.
    Tissue: Epididymis.
  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 2 AND 4), VARIANT MET-253.
    Tissue: Teratocarcinoma and Thyroid.
  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].
  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] (ISOFORMS 1 AND 3), VARIANT MET-253.
    Tissue: Lung, Muscle and Placenta.
  7. "Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltransferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells."
    Shridas P., Rush J.S., Waechter C.J.
    Biochem. Biophys. Res. Commun. 312:1349-1356(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Nogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylation."
    Harrison K.D., Park E.J., Gao N., Kuo A., Rush J.S., Waechter C.J., Lehrman M.A., Sessa W.C.
    EMBO J. 30:2490-2500(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUS1.
  9. "Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation."
    Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H., Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N., Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S., Sessa W.C.
    Cell Metab. 20:448-457(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
  10. Cited for: VARIANT RP59 GLU-42.

Entry informationi

Entry nameiDHDDS_HUMAN
AccessioniPrimary (citable) accession number: Q86SQ9
Secondary accession number(s): B7Z4B9
, B7ZB20, D3DPK7, D3DPK8, D3DPK9, E9KL43, Q5T0A4, Q8NE90, Q9BTG5, Q9BTK3, Q9H905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 116 of the entry and version 3 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

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.