Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q86SQ9 (DHDDS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dehydrodolichyl diphosphate synthase

Short name=Dedol-PP synthase
EC=2.5.1.-
Alternative name(s):
Cis-isoprenyltransferase
Short name=CIT
Short name=Cis-IPTase
Epididymis tissue protein Li 189m
Gene names
Name:DHDDS
Synonyms:HDS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein. Ref.7

Pathway

Protein modification; protein glycosylation. HAMAP-Rule MF_01139

Subunit structure

Interacts with NUS1/NgBR, the interaction is required for efficient activity. Interacts with NPC2. Ref.8

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Note: colocalizes with calnexin. Ref.7

Tissue specificity

Expressed at high levels in testis and kidney. Expressed in epididymis (at protein level). Slightly expressed in heart, spleen and thymus. Ref.2

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the UPP synthase family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86SQ9-1)

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: Q86SQ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     255-255: Q → QQ
Isoform 3 (identifier: Q86SQ9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     109-147: Missing.
Note: May be due to exon skipping.
Isoform 4 (identifier: Q86SQ9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     147-181: KCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPS → N
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Dehydrodolichyl diphosphate synthase HAMAP-Rule MF_01139
PRO_0000123749

Natural variations

Alternative sequence109 – 14739Missing in isoform 3.
VSP_010030
Alternative sequence147 – 18135KCFLN…LLDPS → N in isoform 4.
VSP_045007
Alternative sequence2551Q → QQ in isoform 2.
VSP_010031
Natural variant421K → E in RP59. Ref.9
VAR_065356
Natural variant2531V → M. Ref.2 Ref.3 Ref.6
Corresponds to variant rs3816539 [ dbSNP | Ensembl ].
VAR_028088

Experimental info

Sequence conflict1511N → Y in BAB14439. Ref.3
Sequence conflict2771V → E in AAH34152. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 12EF3A15437A2583

FASTA33338,657
        10         20         30         40         50         60 
MSWIKEGELS LWERFCANII KAGPMPKHIA FIMDGNRRYA KKCQVERQEG HSQGFNKLAE 

        70         80         90        100        110        120 
TLRWCLNLGI LEVTVYAFSI ENFKRSKSEV DGLMDLARQK FSRLMEEKEK LQKHGVCIRV 

       130        140        150        160        170        180 
LGDLHLLPLD LQELIAQAVQ ATKNYNKCFL NVCFAYTSRH EISNAVREMA WGVEQGLLDP 

       190        200        210        220        230        240 
SDISESLLDK CLYTNRSPHP DILIRTSGEV RLSDFLLWQT SHSCLVFQPV LWPEYTFWNL 

       250        260        270        280        290        300 
FEAILQFQMN HSVLQKARDM YAEERKRQQL ERDQATVTEQ LLREGLQASG DAQLRRTRLH 

       310        320        330 
KLSARREERV QGFLQALELK RADWLARLGT ASA 

« Hide

Isoform 2 [UniParc].

Checksum: 8B91F530F1E538E2
Show »

FASTA33438,786
Isoform 3 [UniParc].

Checksum: 1EF92BC4658FFDF9
Show »

FASTA29434,264
Isoform 4 [UniParc].

Checksum: 55AE4DA2A326CA58
Show »

FASTA29934,817

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Whole-exome sequencing links a variant in DHDDS to retinitis pigmentosa."
Zuchner S., Dallman J., Wen R., Beecham G., Naj A., Farooq A., Kohli M.A., Whitehead P.L., Hulme W., Konidari I., Edwards Y.J., Cai G., Peter I., Seo D., Buxbaum J.D., Haines J.L., Blanton S., Young J. expand/collapse author list , Alfonso E., Vance J.M., Lam B.L., Pericak-Vance M.A.
Am. J. Hum. Genet. 88:201-206(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP59 GLU-42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS281.1. [Q86SQ9-2]
CCDS282.1. [Q86SQ9-1]
CCDS57983.1. [Q86SQ9-4]
CCDS57984.1. [Q86SQ9-3]
RefSeqNP_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]
UniGeneHs.369385.

3D structure databases

ProteinModelPortalQ86SQ9.
SMRQ86SQ9. Positions 27-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123018. 5 interactions.
STRING9606.ENSP00000353104.

PTM databases

PhosphoSiteQ86SQ9.

Polymorphism databases

DMDM116241329.

Proteomic databases

MaxQBQ86SQ9.
PaxDbQ86SQ9.
PRIDEQ86SQ9.

Protocols and materials databases

DNASU79947.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236342; ENSP00000236342; ENSG00000117682. [Q86SQ9-1]
ENST00000360009; ENSP00000353104; ENSG00000117682. [Q86SQ9-2]
ENST00000525682; ENSP00000434984; ENSG00000117682. [Q86SQ9-4]
ENST00000526219; ENSP00000434219; ENSG00000117682. [Q86SQ9-3]
GeneID79947.
KEGGhsa:79947.
UCSCuc001bmk.3. human. [Q86SQ9-2]
uc001bml.3. human. [Q86SQ9-1]
uc001bmn.3. human. [Q86SQ9-3]
uc010ofd.2. human.

Organism-specific databases

CTD79947.
GeneCardsGC01P026758.
GeneReviewsDHDDS.
HGNCHGNC:20603. DHDDS.
HPAHPA026721.
HPA026727.
MIM608172. gene.
613861. phenotype.
neXtProtNX_Q86SQ9.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA134867119.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0020.
HOVERGENHBG051350.
KOK11778.
OMARIEGHKR.
PhylomeDBQ86SQ9.
TreeFamTF323753.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ86SQ9.
BgeeQ86SQ9.
CleanExHS_DHDDS.
GenevestigatorQ86SQ9.

Family and domain databases

Gene3D3.40.1180.10. 1 hit.
HAMAPMF_01139. ISPT.
InterProIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERPTHR10291. PTHR10291. 1 hit.
PfamPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMSSF64005. SSF64005. 1 hit.
TIGRFAMsTIGR00055. uppS. 1 hit.
PROSITEPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDehydrodolichyl_diphosphate_synthase.
DHDDS.
GenomeRNAi79947.
NextBio69906.
PROQ86SQ9.
SOURCESearch...

Entry information

Entry nameDHDDS_HUMAN
AccessionPrimary (citable) accession number: Q86SQ9
Secondary accession number(s): B7Z4B9 expand/collapse secondary AC list , B7ZB20, D3DPK7, D3DPK8, D3DPK9, E9KL43, Q5T0A4, Q8NE90, Q9BTG5, Q9BTK3, Q9H905
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM