P48449 (ERG7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LSS
Synonyms:	OSC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. Ref.1
Catalytic activity	(3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol. Ref.1 Ref.9
Pathway	Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 3/3.
Subunit structure	Monomer. Ref.9
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein Ref.9 Ref.12.
Sequence similarities	Belongs to the terpene cyclase/mutase family. Contains 4 PFTB repeats.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol biosynthetic process Inferred from mutant phenotype PubMed 17186944. Source: BHF-UCL
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome lipid particle Inferred from direct assay PubMed 14741744. Source: UniProtKB
Molecular_function	lanosterol synthase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P48449-1)

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: P48449-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P48449-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 732

731

Lanosterol synthase

PRO_0000072659

Regions

Repeat

124 – 165

42

PFTB 1

Repeat

483 – 528

46

PFTB 2

Repeat

560 – 600

41

PFTB 3

Repeat

612 – 653

42

PFTB 4

Sites

Active site

232

1

Proton acceptor

Active site

455

1

Proton donor Probable

Natural variations

Alternative sequence

1 – 80

80

Missing in isoform 2.

VSP_045407

Alternative sequence

133 – 143

11

Missing in isoform 3.

VSP_046188

Natural variant

175

1

R → Q.
Corresponds to variant rs2839158 [ dbSNP | Ensembl ].

VAR_024648

Natural variant

310

1

H → R.
Corresponds to variant rs34115287 [ dbSNP | Ensembl ].

VAR_052057

Natural variant

614

1

R → W.
Corresponds to variant rs35785446 [ dbSNP | Ensembl ].

VAR_052058

Natural variant

642

1

L → V. Ref.3 Ref.5 Ref.8
Corresponds to variant rs2254524 [ dbSNP | Ensembl ].

VAR_021522

Natural variant

688

1

P → L.
Corresponds to variant rs17293705 [ dbSNP | Ensembl ].

VAR_052059

Experimental info

Sequence conflict

348

1

W → R in CAB42828. Ref.4

Secondary structure

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732

Helix Strand Turn

Details...

Helix

22 – 24

3

Beta strand

25 – 30

6

Beta strand

33 – 38

6

Beta strand

40 – 45

6

Helix

50 – 56

7

Turn

61 – 63

3

Helix

73 – 85

13

Beta strand

101 – 103

3

Helix

104 – 115

12

Helix

123 – 134

12

Helix

151 – 163

13

Helix

171 – 182

12

Helix

186 – 188

3

Helix

191 – 199

9

Helix

205 – 207

3

Helix

213 – 217

5

Helix

226 – 228

3

Helix

231 – 245

15

Helix

254 – 260

7

Helix

268 – 270

3

Helix

274 – 276

3

Helix

282 – 284

3

Helix

291 – 305

15

Helix

309 – 330

22

Helix

337 – 351

15

Helix

356 – 363

8

Helix

366 – 368

3

Beta strand

369 – 372

4

Beta strand

375 – 378

4

Beta strand

380 – 382

3

Helix

385 – 398

14

Helix

401 – 403

3

Helix

405 – 407

3

Helix

408 – 421

14

Helix

430 – 433

4

Beta strand

443 – 445

3

Turn

447 – 449

3

Helix

454 – 470

17

Helix

480 – 491

12

Beta strand

502 – 504

3

Helix

510 – 515

6

Helix

531 – 547

17

Helix

553 – 570

18

Beta strand

580 – 584

5

Helix

585 – 598

14

Helix

610 – 620

11

Helix

634 – 638

5

Helix

649 – 661

13

Helix

667 – 680

14

Beta strand

694 – 696

3

Turn

697 – 699

3

Beta strand

700 – 702

3

Helix

707 – 722

16

Helix

727 – 729

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: E4708A5AE53585ED	FASTA	732	83,309
	10 20 30 40 50 60 MTEGTCLRRR GGPYKTEPAT DLGRWRLNCE RGRQTWTYLQ DERAGREQTG LEAYALGLDT 70 80 90 100 110 120 KNYFKDLPKA HTAFEGALNG MTFYVGLQAE DGHWTGDYGG PLFLLPGLLI TCHVARIPLP 130 140 150 160 170 180 AGYREEIVRY LRSVQLPDGG WGLHIEDKST VFGTALNYVS LRILGVGPDD PDLVRARNIL 190 200 210 220 230 240 HKKGGAVAIP SWGKFWLAVL NVYSWEGLNT LFPEMWLFPD WAPAHPSTLW CHCRQVYLPM 250 260 270 280 290 300 SYCYAVRLSA AEDPLVQSLR QELYVEDFAS IDWLAQRNNV APDELYTPHS WLLRVVYALL 310 320 330 340 350 360 NLYEHHHSAH LRQRAVQKLY EHIVADDRFT KSISIGPISK TINMLVRWYV DGPASTAFQE 370 380 390 400 410 420 HVSRIPDYLW MGLDGMKMQG TNGSQIWDTA FAIQALLEAG GHHRPEFSSC LQKAHEFLRL 430 440 450 460 470 480 SQVPDNPPDY QKYYRQMRKG GFSFSTLDCG WIVSDCTAEA LKAVLLLQEK CPHVTEHIPR 490 500 510 520 530 540 ERLCDAVAVL LNMRNPDGGF ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA 550 560 570 580 590 600 LKYFHKRFPE HRAAEIRETL TQGLEFCRRQ QRADGSWEGS WGVCFTYGTW FGLEAFACMG 610 620 630 640 650 660 QTYRDGTACA EVSRACDFLL SRQMADGGWG EDFESCEERR YLQSAQSQIH NTCWAMMGLM 670 680 690 700 710 720 AVRHPDIEAQ ERGVRCLLEK QLPNGDWPQE NIAGVFNKSC AISYTSYRNI FPIWALGRFS 730 QLYPERALAG HP
	Isoform 2 [UniParc]. Checksum: 89E4851E8F451100	FASTA	652	74,218
	10 20 30 40 50 60 MTFYVGLQAE DGHWTGDYGG PLFLLPGLLI TCHVARIPLP AGYREEIVRY LRSVQLPDGG 70 80 90 100 110 120 WGLHIEDKST VFGTALNYVS LRILGVGPDD PDLVRARNIL HKKGGAVAIP SWGKFWLAVL 130 140 150 160 170 180 NVYSWEGLNT LFPEMWLFPD WAPAHPSTLW CHCRQVYLPM SYCYAVRLSA AEDPLVQSLR 190 200 210 220 230 240 QELYVEDFAS IDWLAQRNNV APDELYTPHS WLLRVVYALL NLYEHHHSAH LRQRAVQKLY 250 260 270 280 290 300 EHIVADDRFT KSISIGPISK TINMLVRWYV DGPASTAFQE HVSRIPDYLW MGLDGMKMQG 310 320 330 340 350 360 TNGSQIWDTA FAIQALLEAG GHHRPEFSSC LQKAHEFLRL SQVPDNPPDY QKYYRQMRKG 370 380 390 400 410 420 GFSFSTLDCG WIVSDCTAEA LKAVLLLQEK CPHVTEHIPR ERLCDAVAVL LNMRNPDGGF 430 440 450 460 470 480 ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA LKYFHKRFPE HRAAEIRETL 490 500 510 520 530 540 TQGLEFCRRQ QRADGSWEGS WGVCFTYGTW FGLEAFACMG QTYRDGTACA EVSRACDFLL 550 560 570 580 590 600 SRQMADGGWG EDFESCEERR YLQSAQSQIH NTCWAMMGLM AVRHPDIEAQ ERGVRCLLEK 610 620 630 640 650 QLPNGDWPQE NIAGVFNKSC AISYTSYRNI FPIWALGRFS QLYPERALAG HP
	Isoform 3 [UniParc]. Checksum: EE5504BCAF3EEE27	FASTA	721	82,199
	10 20 30 40 50 60 MTEGTCLRRR GGPYKTEPAT DLGRWRLNCE RGRQTWTYLQ DERAGREQTG LEAYALGLDT 70 80 90 100 110 120 KNYFKDLPKA HTAFEGALNG MTFYVGLQAE DGHWTGDYGG PLFLLPGLLI TCHVARIPLP 130 140 150 160 170 180 AGYREEIVRY LRHIEDKSTV FGTALNYVSL RILGVGPDDP DLVRARNILH KKGGAVAIPS 190 200 210 220 230 240 WGKFWLAVLN VYSWEGLNTL FPEMWLFPDW APAHPSTLWC HCRQVYLPMS YCYAVRLSAA 250 260 270 280 290 300 EDPLVQSLRQ ELYVEDFASI DWLAQRNNVA PDELYTPHSW LLRVVYALLN LYEHHHSAHL 310 320 330 340 350 360 RQRAVQKLYE HIVADDRFTK SISIGPISKT INMLVRWYVD GPASTAFQEH VSRIPDYLWM 370 380 390 400 410 420 GLDGMKMQGT NGSQIWDTAF AIQALLEAGG HHRPEFSSCL QKAHEFLRLS QVPDNPPDYQ 430 440 450 460 470 480 KYYRQMRKGG FSFSTLDCGW IVSDCTAEAL KAVLLLQEKC PHVTEHIPRE RLCDAVAVLL 490 500 510 520 530 540 NMRNPDGGFA TYETKRGGHL LELLNPSEVF GDIMIDYTYV ECTSAVMQAL KYFHKRFPEH 550 560 570 580 590 600 RAAEIRETLT QGLEFCRRQQ RADGSWEGSW GVCFTYGTWF GLEAFACMGQ TYRDGTACAE 610 620 630 640 650 660 VSRACDFLLS RQMADGGWGE DFESCEERRY LQSAQSQIHN TCWAMMGLMA VRHPDIEAQE 670 680 690 700 710 720 RGVRCLLEKQ LPNGDWPQEN IAGVFNKSCA ISYTSYRNIF PIWALGRFSQ LYPERALAGH P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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. , 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].
[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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00009747.
IPI00923506.

PIR

JC4194.

RefSeq

NP_001001438.1. NM_001001438.2.
NP_001138908.1. NM_001145436.1.
NP_001138909.1. NM_001145437.1.
NP_002331.3. NM_002340.5.

UniGene

Hs.596543.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W6J	X-ray	2.20	A	1-732	[»]
1W6K	X-ray	2.10	A	1-732	[»]

ProteinModelPortal

P48449.

ModBase

Search...

Protein-protein interaction databases

IntAct

P48449. 1 interaction.

STRING

9606.ENSP00000348762.

PTM databases

PhosphoSite

P48449.

Polymorphism databases

DMDM

1352387.

Proteomic databases

PaxDb

P48449.

PeptideAtlas

P48449.

PRIDE

P48449.

Protocols and materials databases

DNASU

4047.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356396; ENSP00000348762; ENSG00000160285.
ENST00000397728; ENSP00000380837; ENSG00000160285.
ENST00000457828; ENSP00000409191; ENSG00000160285.
ENST00000522411; ENSP00000429133; ENSG00000160285.

GeneID

4047.

KEGG

hsa:4047.

UCSC

uc002zij.3. human.

Organism-specific databases

CTD

4047.

GeneCards

GC21M047608.

HGNC

HGNC:6708. LSS.

HPA

HPA032060.

MIM

600909. gene.

neXtProt

NX_P48449.

PharmGKB

PA30473.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1657.

HOGENOM

HOG000234317.

HOVERGEN

HBG005604.

InParanoid

P48449.

KO

K01852.

OMA

SWLLHVV.

OrthoDB

EOG4SQWW4.

PhylomeDB

P48449.

Enzyme and pathway databases

BioCyc

MetaCyc:HS08480-MONOMER.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00767; UER00753.

Gene expression databases

ArrayExpress

P48449.

Bgee

P48449.

CleanEx

HS_LSS.

Genevestigator

P48449.

GermOnline

ENSG00000160285. Homo sapiens.

Family and domain databases

InterPro

IPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR002365. Terpene_synthase_CS.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]

Pfam

PF00432. Prenyltrans. 3 hits.
[Graphical view]

SUPFAM

SSF48239. Terp_cyc_toroid. 2 hits.

TIGRFAMs

TIGR01787. squalene_cyclas. 1 hit.

PROSITE

PS01074. TERPENE_SYNTHASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P48449.

ChEMBL

CHEMBL3593.

ChiTaRS

LSS. human.

EvolutionaryTrace

P48449.

GenomeRNAi

4047.

NextBio

15850.

SOURCE

Search...

Entry information

Entry name

ERG7_HUMAN

Accession

Primary (citable) accession number: P48449
Secondary accession number(s): B4DJZ9 , D3DSN0, E9PEI9, G5E9Q9, Q8IYL6, Q9UEZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.