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Q86SQ9

- DHDDS_HUMAN

UniProt

Q86SQ9 - DHDDS_HUMAN

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Protein

Dehydrodolichyl diphosphate syntase complex subunit DHDDS

Gene

DHDDS

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

GO - Molecular functioni

  1. transferase activity, transferring alkyl or aryl (other than methyl) groups Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. dolichyl diphosphate biosynthetic process Source: Reactome
  4. post-translational protein modification Source: Reactome
  5. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

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: Chromosome 1

Organism-specific databases

HGNCiHGNC:20603. DHDDS.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication
Note: colocalizes with calnexin.

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 59 (RP59) [MIM:613861]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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.
GenevestigatoriQ86SQ9.

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. 7 interactions.
STRINGi9606.ENSP00000353104.

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.
OMAiRIEGHKR.
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. Align

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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi116241329.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS281.1. [Q86SQ9-2 ]
CCDS282.1. [Q86SQ9-1 ]
CCDS57983.1. [Q86SQ9-4 ]
CCDS57984.1. [Q86SQ9-3 ]
RefSeqi NP_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 ]
UniGenei Hs.369385.

3D structure databases

ProteinModelPortali Q86SQ9.
SMRi Q86SQ9. Positions 27-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123018. 7 interactions.
STRINGi 9606.ENSP00000353104.

PTM databases

PhosphoSitei Q86SQ9.

Polymorphism databases

DMDMi 116241329.

Proteomic databases

MaxQBi Q86SQ9.
PaxDbi Q86SQ9.
PRIDEi Q86SQ9.

Protocols and materials databases

DNASUi 79947.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000236342 ; ENSP00000236342 ; ENSG00000117682 . [Q86SQ9-1 ]
ENST00000360009 ; ENSP00000353104 ; ENSG00000117682 . [Q86SQ9-2 ]
ENST00000525682 ; ENSP00000434984 ; ENSG00000117682 . [Q86SQ9-4 ]
ENST00000526219 ; ENSP00000434219 ; ENSG00000117682 . [Q86SQ9-3 ]
GeneIDi 79947.
KEGGi hsa:79947.
UCSCi uc001bmk.3. human. [Q86SQ9-2 ]
uc001bml.3. human. [Q86SQ9-1 ]
uc001bmn.3. human. [Q86SQ9-3 ]
uc010ofd.2. human.

Organism-specific databases

CTDi 79947.
GeneCardsi GC01P026758.
GeneReviewsi DHDDS.
HGNCi HGNC:20603. DHDDS.
HPAi HPA026721.
HPA026727.
MIMi 608172. gene.
613861. phenotype.
neXtProti NX_Q86SQ9.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA134867119.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0020.
GeneTreei ENSGT00390000007879.
HOVERGENi HBG051350.
InParanoidi Q86SQ9.
KOi K11778.
OMAi RIEGHKR.
PhylomeDBi Q86SQ9.
TreeFami TF323753.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_22230. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

GeneWikii Dehydrodolichyl_diphosphate_synthase.
DHDDS.
GenomeRNAii 79947.
NextBioi 69906.
PROi Q86SQ9.
SOURCEi Search...

Gene expression databases

Bgeei Q86SQ9.
CleanExi HS_DHDDS.
ExpressionAtlasi Q86SQ9. baseline and differential.
Genevestigatori Q86SQ9.

Family and domain databases

Gene3Di 3.40.1180.10. 1 hit.
HAMAPi MF_01139. ISPT.
InterProi IPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view ]
PANTHERi PTHR10291. PTHR10291. 1 hit.
Pfami PF01255. Prenyltransf. 1 hit.
[Graphical view ]
SUPFAMi SSF64005. SSF64005. 1 hit.
TIGRFAMsi TIGR00055. uppS. 1 hit.
PROSITEi PS01066. UPP_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 0:0-0(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: October 29, 2014
This is version 111 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