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P48449

- ERG7_HUMAN

UniProt

P48449 - ERG7_HUMAN

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Protein

Lanosterol synthase

Gene

LSS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP48449.
CleanExiHS_LSS.
ExpressionAtlasiP48449. baseline and differential.
GenevestigatoriP48449.

Organism-specific databases

HPAiCAB034116.
HPA032060.
HPA032062.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi110225. 7 interactions.
IntActiP48449. 1 interaction.
STRINGi9606.ENSP00000348762.

Structurei

Secondary structure

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

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.
GeneTreeiENSGT00390000011570.
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

        10         20         30         40         50
MTEGTCLRRR GGPYKTEPAT DLGRWRLNCE RGRQTWTYLQ DERAGREQTG
60 70 80 90 100
LEAYALGLDT KNYFKDLPKA HTAFEGALNG MTFYVGLQAE DGHWTGDYGG
110 120 130 140 150
PLFLLPGLLI TCHVARIPLP AGYREEIVRY LRSVQLPDGG WGLHIEDKST
160 170 180 190 200
VFGTALNYVS LRILGVGPDD PDLVRARNIL HKKGGAVAIP SWGKFWLAVL
210 220 230 240 250
NVYSWEGLNT LFPEMWLFPD WAPAHPSTLW CHCRQVYLPM SYCYAVRLSA
260 270 280 290 300
AEDPLVQSLR QELYVEDFAS IDWLAQRNNV APDELYTPHS WLLRVVYALL
310 320 330 340 350
NLYEHHHSAH LRQRAVQKLY EHIVADDRFT KSISIGPISK TINMLVRWYV
360 370 380 390 400
DGPASTAFQE HVSRIPDYLW MGLDGMKMQG TNGSQIWDTA FAIQALLEAG
410 420 430 440 450
GHHRPEFSSC LQKAHEFLRL SQVPDNPPDY QKYYRQMRKG GFSFSTLDCG
460 470 480 490 500
WIVSDCTAEA LKAVLLLQEK CPHVTEHIPR ERLCDAVAVL LNMRNPDGGF
510 520 530 540 550
ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA LKYFHKRFPE
560 570 580 590 600
HRAAEIRETL TQGLEFCRRQ QRADGSWEGS WGVCFTYGTW FGLEAFACMG
610 620 630 640 650
QTYRDGTACA EVSRACDFLL SRQMADGGWG EDFESCEERR YLQSAQSQIH
660 670 680 690 700
NTCWAMMGLM AVRHPDIEAQ ERGVRCLLEK QLPNGDWPQE NIAGVFNKSC
710 720 730
AISYTSYRNI FPIWALGRFS QLYPERALAG HP
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. 7 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.
GeneTreei ENSGT00390000011570.
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

Bgeei P48449.
CleanExi HS_LSS.
ExpressionAtlasi P48449. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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