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Q86SQ9

- DHDDS_HUMAN

UniProt

Q86SQ9 - DHDDS_HUMAN

Protein

Dehydrodolichyl diphosphate synthase

Gene

DHDDS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. 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

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_22230. Synthesis of Dolichyl-phosphate.
    UniPathwayiUPA00378.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dehydrodolichyl diphosphate synthase (EC:2.5.1.-)
    Short name:
    Dedol-PP synthase
    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

    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 synthasePRO_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

    ArrayExpressiQ86SQ9.
    BgeeiQ86SQ9.
    CleanExiHS_DHDDS.
    GenevestigatoriQ86SQ9.

    Organism-specific databases

    HPAiHPA026721.
    HPA026727.

    Interactioni

    Subunit structurei

    Interacts with NUS1/NgBR, the interaction is required for efficient activity. Interacts with NPC2.1 Publication

    Protein-protein interaction databases

    BioGridi123018. 5 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.
    HOVERGENiHBG051350.
    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

    MSWIKEGELS LWERFCANII KAGPMPKHIA FIMDGNRRYA KKCQVERQEG    50
    HSQGFNKLAE TLRWCLNLGI LEVTVYAFSI ENFKRSKSEV DGLMDLARQK 100
    FSRLMEEKEK LQKHGVCIRV LGDLHLLPLD LQELIAQAVQ ATKNYNKCFL 150
    NVCFAYTSRH EISNAVREMA WGVEQGLLDP SDISESLLDK CLYTNRSPHP 200
    DILIRTSGEV RLSDFLLWQT SHSCLVFQPV LWPEYTFWNL FEAILQFQMN 250
    HSVLQKARDM YAEERKRQQL ERDQATVTEQ LLREGLQASG DAQLRRTRLH 300
    KLSARREERV QGFLQALELK RADWLARLGT ASA 333
    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. 5 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.
    HOVERGENi HBG051350.
    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

    ArrayExpressi Q86SQ9.
    Bgeei Q86SQ9.
    CleanExi HS_DHDDS.
    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

    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. 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 1, 2014
    This is version 110 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