Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P48449

- ERG7_HUMAN

UniProt

P48449 - ERG7_HUMAN

Protein

Lanosterol synthase

Gene

LSS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus.1 Publication

    Catalytic activityi

    (3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321Proton acceptor
    Active sitei455 – 4551Proton donorCurated

    GO - Molecular functioni

    1. lanosterol synthase activity Source: ProtInc

    GO - Biological processi

    1. cholesterol biosynthetic process Source: BHF-UCL
    2. small molecule metabolic process Source: Reactome
    3. steroid metabolic process Source: ProtInc

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08480-MONOMER.
    ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_9405. Cholesterol biosynthesis.
    UniPathwayiUPA00767; UER00753.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lanosterol synthase (EC:5.4.99.7)
    Alternative name(s):
    2,3-epoxysqualene--lanosterol cyclase
    Oxidosqualene--lanosterol cyclase
    Short name:
    OSC
    Short name:
    hOSC
    Gene namesi
    Name:LSS
    Synonyms:OSC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:6708. LSS.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Peripheral membrane protein 2 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. lipid particle Source: UniProtKB
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30473.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 732731Lanosterol synthasePRO_0000072659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48449.
    PaxDbiP48449.
    PeptideAtlasiP48449.
    PRIDEiP48449.

    PTM databases

    PhosphoSiteiP48449.

    Expressioni

    Gene expression databases

    ArrayExpressiP48449.
    BgeeiP48449.
    CleanExiHS_LSS.
    GenevestigatoriP48449.

    Organism-specific databases

    HPAiCAB034116.
    HPA032060.
    HPA032062.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi110225. 6 interactions.
    IntActiP48449. 1 interaction.
    STRINGi9606.ENSP00000348762.

    Structurei

    Secondary structure

    1
    732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Beta strandi25 – 306
    Beta strandi33 – 386
    Beta strandi40 – 456
    Helixi50 – 567
    Turni61 – 633
    Helixi73 – 8513
    Beta strandi101 – 1033
    Helixi104 – 11512
    Helixi123 – 13412
    Helixi151 – 16313
    Helixi171 – 18212
    Helixi186 – 1883
    Helixi191 – 1999
    Helixi205 – 2073
    Helixi213 – 2175
    Helixi226 – 2283
    Helixi231 – 24515
    Helixi254 – 2607
    Helixi268 – 2703
    Helixi274 – 2763
    Helixi282 – 2843
    Helixi291 – 30515
    Helixi309 – 33022
    Helixi337 – 35115
    Helixi356 – 3638
    Helixi366 – 3683
    Beta strandi369 – 3724
    Beta strandi375 – 3784
    Beta strandi380 – 3823
    Helixi385 – 39814
    Helixi401 – 4033
    Helixi405 – 4073
    Helixi408 – 42114
    Helixi430 – 4334
    Beta strandi443 – 4453
    Turni447 – 4493
    Helixi454 – 47017
    Helixi480 – 49112
    Beta strandi502 – 5043
    Helixi510 – 5156
    Helixi531 – 54717
    Helixi553 – 57018
    Beta strandi580 – 5845
    Helixi585 – 59814
    Helixi610 – 62011
    Helixi634 – 6385
    Helixi649 – 66113
    Helixi667 – 68014
    Beta strandi694 – 6963
    Turni697 – 6993
    Beta strandi700 – 7023
    Helixi707 – 72216
    Helixi727 – 7293

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W6JX-ray2.20A1-732[»]
    1W6KX-ray2.10A1-732[»]
    ProteinModelPortaliP48449.
    SMRiP48449. Positions 6-732.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48449.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati124 – 16542PFTB 1Add
    BLAST
    Repeati483 – 52846PFTB 2Add
    BLAST
    Repeati560 – 60041PFTB 3Add
    BLAST
    Repeati612 – 65342PFTB 4Add
    BLAST

    Sequence similaritiesi

    Belongs to the terpene cyclase/mutase family.Curated
    Contains 4 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1657.
    HOGENOMiHOG000234317.
    HOVERGENiHBG005604.
    InParanoidiP48449.
    KOiK01852.
    OMAiLHKFGGA.
    OrthoDBiEOG70W3CN.
    PhylomeDBiP48449.
    TreeFamiTF300406.

    Family and domain databases

    Gene3Di1.50.10.20. 2 hits.
    InterProiIPR001330. Prenyltrans.
    IPR018333. Squalene_cyclase.
    IPR002365. Terpene_synthase_CS.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF00432. Prenyltrans. 3 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 2 hits.
    TIGRFAMsiTIGR01787. squalene_cyclas. 1 hit.
    PROSITEiPS01074. TERPENE_SYNTHASES. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48449-1) [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

    MTEGTCLRRR GGPYKTEPAT DLGRWRLNCE RGRQTWTYLQ DERAGREQTG    50
    LEAYALGLDT KNYFKDLPKA HTAFEGALNG MTFYVGLQAE DGHWTGDYGG 100
    PLFLLPGLLI TCHVARIPLP AGYREEIVRY LRSVQLPDGG WGLHIEDKST 150
    VFGTALNYVS LRILGVGPDD PDLVRARNIL HKKGGAVAIP SWGKFWLAVL 200
    NVYSWEGLNT LFPEMWLFPD WAPAHPSTLW CHCRQVYLPM SYCYAVRLSA 250
    AEDPLVQSLR QELYVEDFAS IDWLAQRNNV APDELYTPHS WLLRVVYALL 300
    NLYEHHHSAH LRQRAVQKLY EHIVADDRFT KSISIGPISK TINMLVRWYV 350
    DGPASTAFQE HVSRIPDYLW MGLDGMKMQG TNGSQIWDTA FAIQALLEAG 400
    GHHRPEFSSC LQKAHEFLRL SQVPDNPPDY QKYYRQMRKG GFSFSTLDCG 450
    WIVSDCTAEA LKAVLLLQEK CPHVTEHIPR ERLCDAVAVL LNMRNPDGGF 500
    ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA LKYFHKRFPE 550
    HRAAEIRETL TQGLEFCRRQ QRADGSWEGS WGVCFTYGTW FGLEAFACMG 600
    QTYRDGTACA EVSRACDFLL SRQMADGGWG EDFESCEERR YLQSAQSQIH 650
    NTCWAMMGLM AVRHPDIEAQ ERGVRCLLEK QLPNGDWPQE NIAGVFNKSC 700
    AISYTSYRNI FPIWALGRFS QLYPERALAG HP 732
    Length:732
    Mass (Da):83,309
    Last modified:February 1, 1996 - v1
    Checksum:iE4708A5AE53585ED
    GO
    Isoform 2 (identifier: P48449-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:652
    Mass (Da):74,218
    Checksum:i89E4851E8F451100
    GO
    Isoform 3 (identifier: P48449-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         133-143: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:721
    Mass (Da):82,199
    Checksum:iEE5504BCAF3EEE27
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti348 – 3481W → R in CAB42828. (PubMed:10598817)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751R → Q.
    Corresponds to variant rs2839158 [ dbSNP | Ensembl ].
    VAR_024648
    Natural varianti310 – 3101H → R.
    Corresponds to variant rs34115287 [ dbSNP | Ensembl ].
    VAR_052057
    Natural varianti614 – 6141R → W.
    Corresponds to variant rs35785446 [ dbSNP | Ensembl ].
    VAR_052058
    Natural varianti642 – 6421L → V.3 Publications
    Corresponds to variant rs2254524 [ dbSNP | Ensembl ].
    VAR_021522
    Natural varianti688 – 6881P → L.
    Corresponds to variant rs17293705 [ dbSNP | Ensembl ].
    VAR_052059

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080Missing in isoform 2. 1 PublicationVSP_045407Add
    BLAST
    Alternative sequencei133 – 14311Missing in isoform 3. 1 PublicationVSP_046188Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22526 mRNA. Translation: AAC50184.1.
    D63807 mRNA. Translation: BAA09875.1.
    S81221 mRNA. Translation: AAB36220.1.
    AJ239031
    , AJ239021, AJ239022, AJ239023, AJ239024, AJ239025, AJ239026, AJ239027, AJ239028, AJ239029, AJ239030 Genomic DNA. Translation: CAB42828.1.
    AK296313 mRNA. Translation: BAG59011.1.
    AK226141 mRNA. No translation available.
    AP001468 Genomic DNA. No translation available.
    AP001469 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09299.1.
    CH471079 Genomic DNA. Translation: EAX09301.1.
    CH471079 Genomic DNA. Translation: EAX09302.1.
    CH471079 Genomic DNA. Translation: EAX09303.1.
    BC035638 mRNA. Translation: AAH35638.1.
    X87809 mRNA. Translation: CAA61078.1.
    CCDSiCCDS13733.1. [P48449-1]
    CCDS46654.1. [P48449-3]
    CCDS54489.1. [P48449-2]
    PIRiJC4194.
    RefSeqiNP_001001438.1. NM_001001438.2. [P48449-1]
    NP_001138908.1. NM_001145436.1. [P48449-3]
    NP_001138909.1. NM_001145437.1. [P48449-2]
    NP_002331.3. NM_002340.5. [P48449-1]
    XP_006724066.1. XM_006724003.1. [P48449-1]
    UniGeneiHs.596543.

    Genome annotation databases

    EnsembliENST00000356396; ENSP00000348762; ENSG00000160285. [P48449-1]
    ENST00000397728; ENSP00000380837; ENSG00000160285. [P48449-1]
    ENST00000457828; ENSP00000409191; ENSG00000160285. [P48449-2]
    ENST00000522411; ENSP00000429133; ENSG00000160285. [P48449-3]
    GeneIDi4047.
    KEGGihsa:4047.
    UCSCiuc002zij.3. human. [P48449-1]

    Polymorphism databases

    DMDMi1352387.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22526 mRNA. Translation: AAC50184.1 .
    D63807 mRNA. Translation: BAA09875.1 .
    S81221 mRNA. Translation: AAB36220.1 .
    AJ239031
    , AJ239021 , AJ239022 , AJ239023 , AJ239024 , AJ239025 , AJ239026 , AJ239027 , AJ239028 , AJ239029 , AJ239030 Genomic DNA. Translation: CAB42828.1 .
    AK296313 mRNA. Translation: BAG59011.1 .
    AK226141 mRNA. No translation available.
    AP001468 Genomic DNA. No translation available.
    AP001469 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09299.1 .
    CH471079 Genomic DNA. Translation: EAX09301.1 .
    CH471079 Genomic DNA. Translation: EAX09302.1 .
    CH471079 Genomic DNA. Translation: EAX09303.1 .
    BC035638 mRNA. Translation: AAH35638.1 .
    X87809 mRNA. Translation: CAA61078.1 .
    CCDSi CCDS13733.1. [P48449-1 ]
    CCDS46654.1. [P48449-3 ]
    CCDS54489.1. [P48449-2 ]
    PIRi JC4194.
    RefSeqi NP_001001438.1. NM_001001438.2. [P48449-1 ]
    NP_001138908.1. NM_001145436.1. [P48449-3 ]
    NP_001138909.1. NM_001145437.1. [P48449-2 ]
    NP_002331.3. NM_002340.5. [P48449-1 ]
    XP_006724066.1. XM_006724003.1. [P48449-1 ]
    UniGenei Hs.596543.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W6J X-ray 2.20 A 1-732 [» ]
    1W6K X-ray 2.10 A 1-732 [» ]
    ProteinModelPortali P48449.
    SMRi P48449. Positions 6-732.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110225. 6 interactions.
    IntActi P48449. 1 interaction.
    STRINGi 9606.ENSP00000348762.

    Chemistry

    BindingDBi P48449.
    ChEMBLi CHEMBL3593.
    GuidetoPHARMACOLOGYi 2434.

    PTM databases

    PhosphoSitei P48449.

    Polymorphism databases

    DMDMi 1352387.

    Proteomic databases

    MaxQBi P48449.
    PaxDbi P48449.
    PeptideAtlasi P48449.
    PRIDEi P48449.

    Protocols and materials databases

    DNASUi 4047.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356396 ; ENSP00000348762 ; ENSG00000160285 . [P48449-1 ]
    ENST00000397728 ; ENSP00000380837 ; ENSG00000160285 . [P48449-1 ]
    ENST00000457828 ; ENSP00000409191 ; ENSG00000160285 . [P48449-2 ]
    ENST00000522411 ; ENSP00000429133 ; ENSG00000160285 . [P48449-3 ]
    GeneIDi 4047.
    KEGGi hsa:4047.
    UCSCi uc002zij.3. human. [P48449-1 ]

    Organism-specific databases

    CTDi 4047.
    GeneCardsi GC21M047608.
    HGNCi HGNC:6708. LSS.
    HPAi CAB034116.
    HPA032060.
    HPA032062.
    MIMi 600909. gene.
    neXtProti NX_P48449.
    PharmGKBi PA30473.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1657.
    HOGENOMi HOG000234317.
    HOVERGENi HBG005604.
    InParanoidi P48449.
    KOi K01852.
    OMAi LHKFGGA.
    OrthoDBi EOG70W3CN.
    PhylomeDBi P48449.
    TreeFami TF300406.

    Enzyme and pathway databases

    UniPathwayi UPA00767 ; UER00753 .
    BioCyci MetaCyc:HS08480-MONOMER.
    Reactomei REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_9405. Cholesterol biosynthesis.

    Miscellaneous databases

    ChiTaRSi LSS. human.
    EvolutionaryTracei P48449.
    GeneWikii Lanosterol_synthase.
    GenomeRNAii 4047.
    NextBioi 15850.
    PROi P48449.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48449.
    Bgeei P48449.
    CleanExi HS_LSS.
    Genevestigatori P48449.

    Family and domain databases

    Gene3Di 1.50.10.20. 2 hits.
    InterProi IPR001330. Prenyltrans.
    IPR018333. Squalene_cyclase.
    IPR002365. Terpene_synthase_CS.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    Pfami PF00432. Prenyltrans. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 2 hits.
    TIGRFAMsi TIGR01787. squalene_cyclas. 1 hit.
    PROSITEi PS01074. TERPENE_SYNTHASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the human gene encoding lanosterol synthase from a liver cDNA library."
      Baker C.H., Matsuda S.P.T., Liu D.R., Corey E.J.
      Biochem. Biophys. Res. Commun. 213:154-160(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY.
      Tissue: Liver.
    2. "Molecular cloning of cDNA encoding human lanosterol synthase."
      Sung C.K., Shibuya M., Sankawa U., Ebizuka Y.
      Biol. Pharm. Bull. 18:1459-1461(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    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] (ISOFORM 3), VARIANT VAL-642.
      Tissue: Thalamus.
    4. "Structure of the human lanosterol synthase gene and its analysis as a candidate for holoprosencephaly."
      Roessler E., Mittaz L., Du Y., Scott H.S., Chang J., Rossier C., Guipponi M., Matsuda S.P., Muenke M., Antonarakis S.E.
      Hum. Genet. 105:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-642.
      Tissue: Brain.
    6. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT VAL-642.
      Tissue: Eye.
    9. "The monotopic membrane protein human oxidosqualene cyclase is active as monomer."
      Ruf A., Muller F., D'Arcy B., Stihle M., Kusznir E., Handschin C., Morand O.H., Thoma R.
      Biochem. Biophys. Res. Commun. 315:247-254(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-5, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION.
    10. "The human lanosterol synthase gene maps to chromosome 21q22.3."
      Young M., Chen H., Lalioti M.D., Antonarakis S.E.
      Hum. Genet. 97:620-624(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-630 (ISOFORM 1).
      Tissue: Fetal brain.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "Insight into steroid scaffold formation from the structure of human oxidosqualene cyclase."
      Thoma R., Schulz-Gasch T., D'Arcy B., Benz J., Aebi J., Dehmlow H., Hennig M., Stihle M., Ruf A.
      Nature 432:118-122(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH LANOSTEROL AND RO 48-807, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiERG7_HUMAN
    AccessioniPrimary (citable) accession number: P48449
    Secondary accession number(s): B4DJZ9
    , D3DSN0, E9PEI9, G5E9Q9, Q8IYL6, Q9UEZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3