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P05108

- CP11A_HUMAN

UniProt

P05108 - CP11A_HUMAN

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Protein

Cholesterol side-chain cleavage enzyme, mitochondrial

Gene

CYP11A1

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

Functioni

Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.1 Publication

Catalytic activityi

Cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O.1 Publication

Cofactori

Heme group.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi462 – 4621Iron (heme axial ligand)

GO - Molecular functioni

  1. cholesterol binding Source: Ensembl
  2. cholesterol monooxygenase (side-chain-cleaving) activity Source: UniProtKB
  3. heme binding Source: UniProtKB
  4. iron ion binding Source: InterPro

GO - Biological processi

  1. biphenyl metabolic process Source: Ensembl
  2. C21-steroid hormone biosynthetic process Source: UniProtKB
  3. cellular response to antibiotic Source: Ensembl
  4. cellular response to cadmium ion Source: Ensembl
  5. cellular response to cAMP Source: Ensembl
  6. cellular response to fibroblast growth factor stimulus Source: Ensembl
  7. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
  8. cellular response to interleukin-1 Source: Ensembl
  9. cellular response to lipopolysaccharide Source: Ensembl
  10. cellular response to peptide hormone stimulus Source: Ensembl
  11. cellular response to transforming growth factor beta stimulus Source: Ensembl
  12. cellular response to tumor necrosis factor Source: Ensembl
  13. cerebellum development Source: Ensembl
  14. cholesterol metabolic process Source: UniProtKB
  15. dibenzo-p-dioxin metabolic process Source: Ensembl
  16. estrogen biosynthetic process Source: Ensembl
  17. fractalkine metabolic process Source: Ensembl
  18. granulosa cell differentiation Source: Ensembl
  19. hippocampus development Source: Ensembl
  20. Leydig cell differentiation Source: Ensembl
  21. maternal process involved in female pregnancy Source: Ensembl
  22. mating behavior Source: Ensembl
  23. phenol-containing compound metabolic process Source: Ensembl
  24. phthalate metabolic process Source: Ensembl
  25. progesterone biosynthetic process Source: Ensembl
  26. response to alkaloid Source: Ensembl
  27. response to corticosterone Source: Ensembl
  28. response to drug Source: Ensembl
  29. response to fungicide Source: Ensembl
  30. response to gamma radiation Source: Ensembl
  31. response to genistein Source: Ensembl
  32. response to hydrogen peroxide Source: Ensembl
  33. response to insecticide Source: Ensembl
  34. response to L-ascorbic acid Source: Ensembl
  35. response to salt stress Source: Ensembl
  36. response to vitamin E Source: Ensembl
  37. Schwann cell differentiation Source: Ensembl
  38. small molecule metabolic process Source: Reactome
  39. steroid metabolic process Source: Reactome
  40. sterol metabolic process Source: Reactome
  41. testosterone biosynthetic process Source: Ensembl
  42. vitamin D metabolic process Source: UniProtKB
  43. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06719-MONOMER.
ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
SABIO-RKP05108.
UniPathwayiUPA00229.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesterol side-chain cleavage enzyme, mitochondrial (EC:1.14.15.6)
Alternative name(s):
CYPXIA1
Cholesterol desmolase
Cytochrome P450 11A1
Cytochrome P450(scc)
Gene namesi
Name:CYP11A1
Synonyms:CYP11A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:2590. CYP11A1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial crista Source: Ensembl
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
  4. perikaryon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR) [MIM:613743]: A rare disorder that can present as acute adrenal insufficiency in infancy or childhood. ACTH and plasma renin activity are elevated and adrenal steroids are inappropriately low or absent; the 46,XY patients have female external genitalia, sometimes with clitoromegaly. The phenotypic spectrum ranges from prematurity, complete underandrogenization, and severe early-onset adrenal failure to term birth with clitoromegaly and later-onset adrenal failure. Patients with congenital adrenal insufficiency do not manifest the massive adrenal enlargement typical of congenital lipoid adrenal hyperplasia.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411L → W in AICSR; reduced activity. 1 Publication
VAR_065241
Natural varianti189 – 1891A → V in AICSR; no loss of activity. 1 Publication
VAR_016949
Natural varianti222 – 2221L → P in AICSR; markedly reduced activity. 1 Publication
VAR_065242
Natural varianti271 – 2711D → DGD in AICSR; complete loss of activity. 1 Publication
VAR_016950
Natural varianti353 – 3531R → W in AICSR; loss of activity. 1 Publication
VAR_016951
Natural varianti359 – 3591A → V in AICSR; markedly reduced activity. 1 Publication
VAR_065243
Natural varianti415 – 4151V → E in AICSR; complete loss of activity. 1 Publication
VAR_065244

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613743. phenotype.
Orphaneti168558. 46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency.
289548. Inherited isolated adrenal insufficiency due to CYP11A1 deficiency.
PharmGKBiPA27089.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionAdd
BLAST
Chaini40 – 521482Cholesterol side-chain cleavage enzyme, mitochondrialPRO_0000003585Add
BLAST

Proteomic databases

PaxDbiP05108.
PRIDEiP05108.

PTM databases

PhosphoSiteiP05108.

Expressioni

Inductioni

By 8-bromo cyclic AMP.1 Publication

Gene expression databases

BgeeiP05108.
CleanExiHS_CYP11A1.
ExpressionAtlasiP05108. baseline and differential.
GenevestigatoriP05108.

Organism-specific databases

HPAiHPA016436.

Interactioni

Subunit structurei

Interacts with FDX1/adrenodoxin.1 Publication

Protein-protein interaction databases

BioGridi107955. 4 interactions.
IntActiP05108. 4 interactions.
MINTiMINT-1200919.
STRINGi9606.ENSP00000268053.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503
Helixi58 – 6811
Helixi71 – 733
Helixi74 – 8512
Beta strandi87 – 937
Beta strandi96 – 1016
Helixi104 – 1129
Helixi124 – 1329
Helixi139 – 1413
Helixi144 – 15815
Helixi161 – 1644
Helixi167 – 18923
Beta strandi190 – 1967
Helixi199 – 21517
Beta strandi223 – 2253
Helixi228 – 24417
Helixi245 – 2473
Helixi252 – 2587
Helixi260 – 29132
Helixi301 – 3077
Helixi313 – 32816
Helixi330 – 34415
Helixi346 – 36217
Turni363 – 3653
Helixi367 – 3704
Helixi375 – 38713
Beta strandi390 – 3978
Beta strandi402 – 4043
Beta strandi407 – 4093
Beta strandi414 – 4185
Helixi419 – 4235
Turni426 – 4283
Beta strandi429 – 4313
Helixi437 – 4404
Turni449 – 4513
Helixi458 – 4603
Helixi465 – 48218
Beta strandi483 – 4864
Beta strandi495 – 50511
Beta strandi509 – 5135

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9YX-ray2.10A/B41-521[»]
3N9ZX-ray2.17A/B41-521[»]
3NA0X-ray2.50A/B44-514[»]
3NA1X-ray2.25A/B41-521[»]
ProteinModelPortaliP05108.
SMRiP05108. Positions 44-514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05108.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP05108.
KOiK00498.
OMAiYQRPIGV.
OrthoDBiEOG7MKW5S.
PhylomeDBiP05108.
TreeFamiTF105094.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P05108-1) [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
MLAKGLPPRS VLVKGCQTFL SAPREGLGRL RVPTGEGAGI STRSPRPFNE
60 70 80 90 100
IPSPGDNGWL NLYHFWRETG THKVHLHHVQ NFQKYGPIYR EKLGNVESVY
110 120 130 140 150
VIDPEDVALL FKSEGPNPER FLIPPWVAYH QYYQRPIGVL LKKSAAWKKD
160 170 180 190 200
RVALNQEVMA PEATKNFLPL LDAVSRDFVS VLHRRIKKAG SGNYSGDISD
210 220 230 240 250
DLFRFAFESI TNVIFGERQG MLEEVVNPEA QRFIDAIYQM FHTSVPMLNL
260 270 280 290 300
PPDLFRLFRT KTWKDHVAAW DVIFSKADIY TQNFYWELRQ KGSVHHDYRG
310 320 330 340 350
ILYRLLGDSK MSFEDIKANV TEMLAGGVDT TSMTLQWHLY EMARNLKVQD
360 370 380 390 400
MLRAEVLAAR HQAQGDMATM LQLVPLLKAS IKETLRLHPI SVTLQRYLVN
410 420 430 440 450
DLVLRDYMIP AKTLVQVAIY ALGREPTFFF DPENFDPTRW LSKDKNITYF
460 470 480 490 500
RNLGFGWGVR QCLGRRIAEL EMTIFLINML ENFRVEIQHL SDVGTTFNLI
510 520
LMPEKPISFT FWPFNQEATQ Q
Length:521
Mass (Da):60,102
Last modified:April 3, 2007 - v2
Checksum:iAB0501E7A5665D8B
GO
Isoform 2 (identifier: P05108-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.

Note: No experimental confirmation available.

Show »
Length:363
Mass (Da):42,152
Checksum:i8CA4719AAC24EF8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161C → Y in AAA52162. (PubMed:3024157)Curated
Sequence conflicti274 – 2741F → L in CAA28965. (PubMed:3038854)Curated
Sequence conflicti283 – 2831N → H in AAA36404. (PubMed:2419119)Curated
Sequence conflicti301 – 3011I → M in AAA52162. (PubMed:3024157)Curated
Sequence conflicti301 – 3011I → M in AAA36404. (PubMed:2419119)Curated
Sequence conflicti505 – 5051K → E in BAG51810. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411L → W in AICSR; reduced activity. 1 Publication
VAR_065241
Natural varianti189 – 1891A → V in AICSR; no loss of activity. 1 Publication
VAR_016949
Natural varianti222 – 2221L → P in AICSR; markedly reduced activity. 1 Publication
VAR_065242
Natural varianti271 – 2711D → DGD in AICSR; complete loss of activity. 1 Publication
VAR_016950
Natural varianti314 – 3141E → K.1 Publication
Corresponds to variant rs6161 [ dbSNP | Ensembl ].
VAR_013944
Natural varianti353 – 3531R → W in AICSR; loss of activity. 1 Publication
VAR_016951
Natural varianti359 – 3591A → V in AICSR; markedly reduced activity. 1 Publication
VAR_065243
Natural varianti415 – 4151V → E in AICSR; complete loss of activity. 1 Publication
VAR_065244

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158Missing in isoform 2. 1 PublicationVSP_045695Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14565 mRNA. Translation: AAA52162.1.
X05367
, X05368, X05369, X05370, X05371, X05372, X05373, X05374 Genomic DNA. Translation: CAA28965.1.
AK056794 mRNA. Translation: BAG51810.1.
AK292300 mRNA. Translation: BAF84989.1.
AC090826 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99341.1.
CH471136 Genomic DNA. Translation: EAW99342.1.
BC032329 mRNA. Translation: AAH32329.1.
X14257 Genomic DNA. Translation: CAA32471.1.
M28253 mRNA. Translation: AAA36404.1.
CCDSiCCDS32291.1. [P05108-1]
CCDS45303.1. [P05108-2]
PIRiA25922.
RefSeqiNP_000772.2. NM_000781.2. [P05108-1]
NP_001093243.1. NM_001099773.1. [P05108-2]
UniGeneiHs.303980.

Genome annotation databases

EnsembliENST00000268053; ENSP00000268053; ENSG00000140459. [P05108-1]
ENST00000358632; ENSP00000351455; ENSG00000140459. [P05108-2]
GeneIDi1583.
KEGGihsa:1583.
UCSCiuc002axs.2. human. [P05108-1]

Polymorphism databases

DMDMi143811381.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14565 mRNA. Translation: AAA52162.1 .
X05367
, X05368 , X05369 , X05370 , X05371 , X05372 , X05373 , X05374 Genomic DNA. Translation: CAA28965.1 .
AK056794 mRNA. Translation: BAG51810.1 .
AK292300 mRNA. Translation: BAF84989.1 .
AC090826 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99341.1 .
CH471136 Genomic DNA. Translation: EAW99342.1 .
BC032329 mRNA. Translation: AAH32329.1 .
X14257 Genomic DNA. Translation: CAA32471.1 .
M28253 mRNA. Translation: AAA36404.1 .
CCDSi CCDS32291.1. [P05108-1 ]
CCDS45303.1. [P05108-2 ]
PIRi A25922.
RefSeqi NP_000772.2. NM_000781.2. [P05108-1 ]
NP_001093243.1. NM_001099773.1. [P05108-2 ]
UniGenei Hs.303980.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3N9Y X-ray 2.10 A/B 41-521 [» ]
3N9Z X-ray 2.17 A/B 41-521 [» ]
3NA0 X-ray 2.50 A/B 44-514 [» ]
3NA1 X-ray 2.25 A/B 41-521 [» ]
ProteinModelPortali P05108.
SMRi P05108. Positions 44-514.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107955. 4 interactions.
IntActi P05108. 4 interactions.
MINTi MINT-1200919.
STRINGi 9606.ENSP00000268053.

Chemistry

ChEMBLi CHEMBL2033.
DrugBanki DB00357. Aminoglutethimide.
DB00169. Cholecalciferol.
DB00882. Clomifene.
DB00257. Clotrimazole.
DB01234. Dexamethasone.
DB01396. Digitoxin.
DB00390. Digoxin.
DB00917. Dinoprostone.
DB01437. Glutethimide.
DB01026. Ketoconazole.
DB00338. Omeprazole.
DB01232. Saquinavir.
DB00857. Terbinafine.
DB00624. Testosterone.
GuidetoPHARMACOLOGYi 1358.

PTM databases

PhosphoSitei P05108.

Polymorphism databases

DMDMi 143811381.

Proteomic databases

PaxDbi P05108.
PRIDEi P05108.

Protocols and materials databases

DNASUi 1583.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268053 ; ENSP00000268053 ; ENSG00000140459 . [P05108-1 ]
ENST00000358632 ; ENSP00000351455 ; ENSG00000140459 . [P05108-2 ]
GeneIDi 1583.
KEGGi hsa:1583.
UCSCi uc002axs.2. human. [P05108-1 ]

Organism-specific databases

CTDi 1583.
GeneCardsi GC15M074630.
HGNCi HGNC:2590. CYP11A1.
HPAi HPA016436.
MIMi 118485. gene.
613743. phenotype.
neXtProti NX_P05108.
Orphaneti 168558. 46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency.
289548. Inherited isolated adrenal insufficiency due to CYP11A1 deficiency.
PharmGKBi PA27089.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000119243.
HOGENOMi HOG000013161.
HOVERGENi HBG051098.
InParanoidi P05108.
KOi K00498.
OMAi YQRPIGV.
OrthoDBi EOG7MKW5S.
PhylomeDBi P05108.
TreeFami TF105094.

Enzyme and pathway databases

UniPathwayi UPA00229 .
BioCyci MetaCyc:HS06719-MONOMER.
Reactomei REACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
SABIO-RK P05108.

Miscellaneous databases

ChiTaRSi CYP11A1. human.
EvolutionaryTracei P05108.
GeneWikii Cholesterol_side-chain_cleavage_enzyme.
GenomeRNAii 1583.
NextBioi 35469259.
PROi P05108.
SOURCEi Search...

Gene expression databases

Bgeei P05108.
CleanExi HS_CYP11A1.
ExpressionAtlasi P05108. baseline and differential.
Genevestigatori P05108.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning, assignment of the gene to chromosome 15, and expression in the placenta."
    Chung B.-C., Matteson K.J., Voutilainen R., Mohandas T.K., Miller W.L.
    Proc. Natl. Acad. Sci. U.S.A. 83:8962-8966(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Gene structure of human cytochrome P-450(SCC), cholesterol desmolase."
    Morohashi K., Sogawa K., Omura T., Fujii-Kuriyama Y.
    J. Biochem. 101:879-887(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  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 1 AND 2).
    Tissue: Placenta and Testis.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(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] (ISOFORM 1).
    Tissue: Brain.
  7. Chung B.-C.
    Submitted (JAN-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
  8. "Regulated expression of cytochrome P-450scc (cholesterol-side-chain cleavage enzyme) in cultured cell lines detected by antibody against bacterially expressed human protein."
    Hu M.C., Guo I.C., Lin J.H., Chung B.-C.
    Biochem. J. 274:813-817(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-54, INDUCTION.
    Tissue: Choriocarcinoma.
  9. "Study of cholesterol side-chain cleavage (20,22 desmolase) deficiency causing congenital lipoid adrenal hyperplasia using bovine-sequence P450scc oligodeoxyribonucleotide probes."
    Matteson K.J., Chung B.-C., Urdea M.S., Miller W.L.
    Endocrinology 118:1296-1305(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 283-521 (ISOFORM 1).
  10. "Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system."
    Strushkevich N., MacKenzie F., Cherkesova T., Grabovec I., Usanov S., Park H.W.
    Proc. Natl. Acad. Sci. U.S.A. 108:10139-10143(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 41-521 IN COMPLEXES WITH FDX1; HEME AND CHOLESTEROL, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, INTERACTION WITH FDX1.
  11. Cited for: VARIANT LYS-314.
  12. "Heterozygous mutation in the cholesterol side chain cleavage enzyme (P450scc) gene in a patient with 46,XY sex reversal and adrenal insufficiency."
    Tajima T., Fujieda K., Kouda N., Nakae J., Miller W.L.
    J. Clin. Endocrinol. Metab. 86:3820-3825(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AICSR GLY-ASP-271 INS.
  13. "Compound heterozygous mutations in the cholesterol side-chain cleavage enzyme gene (CYP11A) cause congenital adrenal insufficiency in humans."
    Katsumata N., Ohtake M., Hojo T., Ogawa E., Hara T., Sato N., Tanaka T.
    J. Clin. Endocrinol. Metab. 87:3808-3813(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AICSR VAL-189 AND TRP-353.
  14. "Homozygous mutation of P450 side-chain cleavage enzyme gene (CYP11A1) in 46, XY patient with adrenal insufficiency, complete sex reversal, and agenesis of corpus callosum."
    al Kandari H., Katsumata N., Alexander S., Rasoul M.A.
    J. Clin. Endocrinol. Metab. 91:2821-2826(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AICSR VAL-359, CHARACTERIZATION OF VARIANT AICSR VAL-359.
  15. "Severe combined adrenal and gonadal deficiency caused by novel mutations in the cholesterol side chain cleavage enzyme, P450scc."
    Kim C.J., Lin L., Huang N., Quigley C.A., Avruskin T.W., Achermann J.C., Miller W.L.
    J. Clin. Endocrinol. Metab. 93:696-702(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AICSR TRP-141 AND GLU-415, CHARACTERIZATION OF VARIANTS AICSR TRP-141 AND GLU-415.
  16. "A novel homozygous mutation in CYP11A1 gene is associated with late-onset adrenal insufficiency and hypospadias in a 46,XY patient."
    Rubtsov P., Karmanov M., Sverdlova P., Spirin P., Tiulpakov A.
    J. Clin. Endocrinol. Metab. 94:936-939(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AICSR PRO-222, CHARACTERIZATION OF VARIANT AICSR PRO-222.

Entry informationi

Entry nameiCP11A_HUMAN
AccessioniPrimary (citable) accession number: P05108
Secondary accession number(s): A8K8D5
, B3KPU8, G3XAD7, Q15081, Q16805, Q8N1A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 167 of the entry and version 2 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 15
    Human chromosome 15: 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