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Q99KU1

- DHDDS_MOUSE

UniProt

Q99KU1 - DHDDS_MOUSE

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Protein
Dehydrodolichyl diphosphate synthase
Gene
Dhdds
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

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.UniRule annotation

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_202113. 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
Gene namesi
Name:Dhdds
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1914672. Dhdds.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity
Note: colocalizes with calnexin By similarity.UniRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Dehydrodolichyl diphosphate synthaseUniRule annotation
PRO_0000123750Add
BLAST

Proteomic databases

PRIDEiQ99KU1.

PTM databases

PhosphoSiteiQ99KU1.

Expressioni

Gene expression databases

ArrayExpressiQ99KU1.
BgeeiQ99KU1.
CleanExiMM_DHDDS.
GenevestigatoriQ99KU1.

Interactioni

Subunit structurei

Interacts with NUS1/NgBR, the interaction is required for efficient activity. Interacts with NPC2 By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000101511.

Structurei

3D structure databases

ProteinModelPortaliQ99KU1.
SMRiQ99KU1. Positions 27-235.

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.

Phylogenomic databases

eggNOGiCOG0020.
GeneTreeiENSGT00390000007879.
HOGENOMiHOG000006053.
HOVERGENiHBG051350.
InParanoidiA3KGL4.
KOiK11778.
OMAiRIEGHKR.
OrthoDBiEOG7HTHHB.
PhylomeDBiQ99KU1.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99KU1-1) [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 KAGPVPKHIA FIMDGNRRYA KKCQVERQEG    50
HTQGFNKLAE TLRWCLNLGI LEVTVYAFSI ENFKRSKSEV DGLLDLARQK 100
FSCLMEEQEK LQKHGVCIRV LGDLHLLPLD LQEKIAHAIQ ATKNYNKCFL 150
NVCFAYTSRH EIANAVREMA WGVEQGLLEP SDVSESLLDK CLYSNHSPHP 200
DILIRTSGEV RLSDFLLWQT SHSCLVFQPV LWPEYTFWNL CEAILQFQRN 250
HGALQKARDM YAEERKRRQL ERDQAAVTEQ LLREGLQASG DAQLRRTRLH 300
KLSTKREERV QGFLKALELK RANWLALWGT ASA 333
Length:333
Mass (Da):38,509
Last modified:June 1, 2001 - v1
Checksum:i53992F5E92D3F2C9
GO
Isoform 2 (identifier: Q99KU1-2) [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):38,637
Checksum:iB4574B527D0D8C1B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei255 – 2551Q → QQ in isoform 2.
VSP_010032

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301A → L in BAC29643. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK034277 mRNA. Translation: BAC28657.1.
AK036929 mRNA. Translation: BAC29643.1.
AK049991 mRNA. Translation: BAC34020.1.
AK135087 mRNA. Translation: BAE22416.1.
AK149138 mRNA. Translation: BAE28748.1.
AK171207 mRNA. Translation: BAE42313.1.
AL837508, AL670680 Genomic DNA. Translation: CAM46083.1.
BC004011 mRNA. Translation: AAH04011.1.
CCDSiCCDS18760.1. [Q99KU1-1]
RefSeqiNP_080420.2. NM_026144.4. [Q99KU1-1]
UniGeneiMm.100290.

Genome annotation databases

EnsembliENSMUST00000012262; ENSMUSP00000012262; ENSMUSG00000012117. [Q99KU1-1]
ENSMUST00000105887; ENSMUSP00000101511; ENSMUSG00000012117. [Q99KU1-2]
ENSMUST00000144668; ENSMUSP00000116098; ENSMUSG00000012117. [Q99KU1-1]
GeneIDi67422.
KEGGimmu:67422.
UCSCiuc008vds.1. mouse. [Q99KU1-1]
uc008vdv.1. mouse. [Q99KU1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK034277 mRNA. Translation: BAC28657.1 .
AK036929 mRNA. Translation: BAC29643.1 .
AK049991 mRNA. Translation: BAC34020.1 .
AK135087 mRNA. Translation: BAE22416.1 .
AK149138 mRNA. Translation: BAE28748.1 .
AK171207 mRNA. Translation: BAE42313.1 .
AL837508 , AL670680 Genomic DNA. Translation: CAM46083.1 .
BC004011 mRNA. Translation: AAH04011.1 .
CCDSi CCDS18760.1. [Q99KU1-1 ]
RefSeqi NP_080420.2. NM_026144.4. [Q99KU1-1 ]
UniGenei Mm.100290.

3D structure databases

ProteinModelPortali Q99KU1.
SMRi Q99KU1. Positions 27-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000101511.

PTM databases

PhosphoSitei Q99KU1.

Proteomic databases

PRIDEi Q99KU1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000012262 ; ENSMUSP00000012262 ; ENSMUSG00000012117 . [Q99KU1-1 ]
ENSMUST00000105887 ; ENSMUSP00000101511 ; ENSMUSG00000012117 . [Q99KU1-2 ]
ENSMUST00000144668 ; ENSMUSP00000116098 ; ENSMUSG00000012117 . [Q99KU1-1 ]
GeneIDi 67422.
KEGGi mmu:67422.
UCSCi uc008vds.1. mouse. [Q99KU1-1 ]
uc008vdv.1. mouse. [Q99KU1-2 ]

Organism-specific databases

CTDi 79947.
MGIi MGI:1914672. Dhdds.

Phylogenomic databases

eggNOGi COG0020.
GeneTreei ENSGT00390000007879.
HOGENOMi HOG000006053.
HOVERGENi HBG051350.
InParanoidi A3KGL4.
KOi K11778.
OMAi RIEGHKR.
OrthoDBi EOG7HTHHB.
PhylomeDBi Q99KU1.
TreeFami TF323753.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_202113. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

NextBioi 324524.
PROi Q99KU1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99KU1.
Bgeei Q99KU1.
CleanExi MM_DHDDS.
Genevestigatori Q99KU1.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Diencephalon, Hippocampus, Olfactory bulb, Sympathetic ganglion and Vagina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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).
    Tissue: Mammary tumor.

Entry informationi

Entry nameiDHDDS_MOUSE
AccessioniPrimary (citable) accession number: Q99KU1
Secondary accession number(s): A3KGL4
, Q3UF13, Q8BZ16, Q8BZK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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