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Q16850

- CP51A_HUMAN

UniProt

Q16850 - CP51A_HUMAN

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Protein

Lanosterol 14-alpha demethylase

Gene

CYP51A1

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

Functioni

Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.1 Publication

Catalytic activityi

A 14-alpha-methylsteroid + 3 O2 + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP+ + 4 H2O.1 Publication

Cofactori

heme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi449 – 4491Iron (heme axial ligand)

GO - Molecular functioni

  1. heme binding Source: UniProtKB
  2. iron ion binding Source: InterPro
  3. sterol 14-demethylase activity Source: UniProtKB

GO - Biological processi

  1. cholesterol biosynthetic process Source: Reactome
  2. cholesterol biosynthetic process via 24,25-dihydrolanosterol Source: Ensembl
  3. demethylation Source: GOC
  4. small molecule metabolic process Source: Reactome
  5. steroid biosynthetic process Source: UniProtKB
  6. sterol metabolic process Source: Reactome
  7. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS00076-MONOMER.
ReactomeiREACT_13812. Endogenous sterols.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
UniPathwayiUPA00770; UER00754.

Names & Taxonomyi

Protein namesi
Recommended name:
Lanosterol 14-alpha demethylase (EC:1.14.13.70)
Short name:
LDM
Alternative name(s):
CYPLI
Cytochrome P450 51A1
Cytochrome P450-14DM
Short name:
Cytochrome P45014DM
Cytochrome P450LI
Sterol 14-alpha demethylase
Gene namesi
Name:CYP51A1
Synonyms:CYP51
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2649. CYP51A1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei24 – 4421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Lanosterol 14-alpha demethylasePRO_0000051998Add
BLAST

Proteomic databases

MaxQBiQ16850.
PaxDbiQ16850.
PRIDEiQ16850.

PTM databases

PhosphoSiteiQ16850.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in testis, ovary, adrenal, prostate, liver, kidney and lung.1 Publication

Gene expression databases

BgeeiQ16850.
CleanExiHS_CYP51A1.
ExpressionAtlasiQ16850. baseline.
GenevestigatoriQ16850.

Organism-specific databases

HPAiHPA041325.
HPA043508.

Interactioni

Protein-protein interaction databases

BioGridi107967. 18 interactions.
IntActiQ16850. 3 interactions.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni69 – 713Combined sources
Helixi74 – 796Combined sources
Helixi81 – 9212Combined sources
Beta strandi94 – 1007Combined sources
Beta strandi103 – 1086Combined sources
Helixi111 – 1199Combined sources
Turni122 – 1243Combined sources
Beta strandi125 – 1273Combined sources
Helixi128 – 13912Combined sources
Helixi144 – 1463Combined sources
Helixi149 – 16214Combined sources
Helixi165 – 18218Combined sources
Helixi183 – 1864Combined sources
Beta strandi188 – 1936Combined sources
Helixi194 – 21017Combined sources
Helixi213 – 2175Combined sources
Helixi221 – 23111Combined sources
Helixi236 – 2405Combined sources
Helixi248 – 27124Combined sources
Helixi281 – 2866Combined sources
Helixi298 – 32932Combined sources
Helixi331 – 34515Combined sources
Helixi354 – 3585Combined sources
Helixi361 – 37313Combined sources
Beta strandi380 – 3867Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi400 – 4034Combined sources
Helixi405 – 4084Combined sources
Turni412 – 4143Combined sources
Turni416 – 4194Combined sources
Helixi423 – 4275Combined sources
Helixi431 – 4344Combined sources
Beta strandi435 – 4395Combined sources
Helixi445 – 4473Combined sources
Helixi452 – 46918Combined sources
Beta strandi470 – 4734Combined sources
Beta strandi475 – 4773Combined sources
Beta strandi485 – 4884Combined sources
Beta strandi491 – 4933Combined sources
Beta strandi495 – 5006Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JUSX-ray2.90A/B54-502[»]
3JUVX-ray3.12A54-502[»]
3LD6X-ray2.80A/B54-502[»]
ProteinModelPortaliQ16850.
SMRiQ16850. Positions 58-502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16850.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00660000095370.
HOVERGENiHBG051102.
InParanoidiQ16850.
KOiK05917.
OrthoDBiEOG7PZRX3.
PhylomeDBiQ16850.
TreeFamiTF105091.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00465. EP450IV.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16850-1) [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
MLLLGLLQAG GSVLGQAMEK VTGGNLLSML LIACAFTLSL VYLIRLAAGH
60 70 80 90 100
LVQLPAGVKS PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM
110 120 130 140 150
VGKTFTYLLG SDAAALLFNS KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP
160 170 180 190 200
VFLEQKKMLK SGLNIAHFKQ HVSIIEKETK EYFESWGESG EKNVFEALSE
210 220 230 240 250
LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL LPGWLPLPSF
260 270 280 290 300
RRRDRAHREI KDIFYKAIQK RRQSQEKIDD ILQTLLDATY KDGRPLTDDE
310 320 330 340 350
VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQKKCYLE QKTVCGENLP
360 370 380 390 400
PLTYDQLKDL NLLDRCIKET LRLRPPIMIM MRMARTPQTV AGYTIPPGHQ
410 420 430 440 450
VCVSPTVNQR LKDSWVERLD FNPDRYLQDN PASGEKFAYV PFGAGRHRCI
460 470 480 490 500
GENFAYVQIK TIWSTMLRLY EFDLIDGYFP TVNYTTMIHT PENPVIRYKR

RSK
Length:503
Mass (Da):56,806
Last modified:December 15, 1998 - v3
Checksum:i4FCEC147FB4DED86
GO
Isoform 2 (identifier: Q16850-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Note: No experimental confirmation available.

Show »
Length:404
Mass (Da):46,312
Checksum:i2D5198C9B55ED478
GO

Sequence cautioni

The sequence AAB39951.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAB46356.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH32322.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA09512.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG36881.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAL24154.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAW76858.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701K → E in BAG36881. (PubMed:14702039)Curated
Sequence conflicti272 – 2721R → T in AAC50951. (PubMed:8975714)Curated
Sequence conflicti368 – 3681K → R in AAC50951. (PubMed:8975714)Curated
Sequence conflicti377 – 3771I → V in AAH32322. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131V → A.
Corresponds to variant rs2229188 [ dbSNP | Ensembl ].
VAR_023470

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9999Missing in isoform 2. 1 PublicationVSP_037413Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23942 mRNA. Translation: AAB39951.1. Different initiation.
D55653 mRNA. Translation: BAA09512.1. Different initiation.
U51692
, U51684, U51685, U51686, U51687, U51688, U51689, U51690, U51691 Genomic DNA. Translation: AAC50951.1.
AK314205 mRNA. Translation: BAG36881.1. Different initiation.
AK295932 mRNA. Translation: BAG58717.1.
AC000120 Genomic DNA. Translation: AAB46356.1. Different initiation.
CH236949 Genomic DNA. Translation: EAL24154.1. Different initiation.
CH471091 Genomic DNA. Translation: EAW76858.1. Different initiation.
CH471091 Genomic DNA. Translation: EAW76859.1.
BC032322 mRNA. Translation: AAH32322.1. Different initiation.
CCDSiCCDS55123.1. [Q16850-2]
PIRiJC4759.
S68855.
RefSeqiNP_000777.1. NM_000786.3.
NP_001139624.1. NM_001146152.1. [Q16850-2]
UniGeneiHs.417077.

Genome annotation databases

EnsembliENST00000003100; ENSP00000003100; ENSG00000001630.
ENST00000450723; ENSP00000406757; ENSG00000001630. [Q16850-2]
GeneIDi1595.
KEGGihsa:1595.
UCSCiuc003ulm.4. human. [Q16850-1]

Polymorphism databases

DMDMi3915660.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23942 mRNA. Translation: AAB39951.1 . Different initiation.
D55653 mRNA. Translation: BAA09512.1 . Different initiation.
U51692
, U51684 , U51685 , U51686 , U51687 , U51688 , U51689 , U51690 , U51691 Genomic DNA. Translation: AAC50951.1 .
AK314205 mRNA. Translation: BAG36881.1 . Different initiation.
AK295932 mRNA. Translation: BAG58717.1 .
AC000120 Genomic DNA. Translation: AAB46356.1 . Different initiation.
CH236949 Genomic DNA. Translation: EAL24154.1 . Different initiation.
CH471091 Genomic DNA. Translation: EAW76858.1 . Different initiation.
CH471091 Genomic DNA. Translation: EAW76859.1 .
BC032322 mRNA. Translation: AAH32322.1 . Different initiation.
CCDSi CCDS55123.1. [Q16850-2 ]
PIRi JC4759.
S68855.
RefSeqi NP_000777.1. NM_000786.3.
NP_001139624.1. NM_001146152.1. [Q16850-2 ]
UniGenei Hs.417077.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3JUS X-ray 2.90 A/B 54-502 [» ]
3JUV X-ray 3.12 A 54-502 [» ]
3LD6 X-ray 2.80 A/B 54-502 [» ]
ProteinModelPortali Q16850.
SMRi Q16850. Positions 58-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107967. 18 interactions.
IntActi Q16850. 3 interactions.

Chemistry

BindingDBi Q16850.
ChEMBLi CHEMBL3849.
DrugBanki DB01167. Itraconazole.
DB01026. Ketoconazole.
DB01153. Sertaconazole.
DB01007. Tioconazole.

PTM databases

PhosphoSitei Q16850.

Polymorphism databases

DMDMi 3915660.

Proteomic databases

MaxQBi Q16850.
PaxDbi Q16850.
PRIDEi Q16850.

Protocols and materials databases

DNASUi 1595.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000003100 ; ENSP00000003100 ; ENSG00000001630 .
ENST00000450723 ; ENSP00000406757 ; ENSG00000001630 . [Q16850-2 ]
GeneIDi 1595.
KEGGi hsa:1595.
UCSCi uc003ulm.4. human. [Q16850-1 ]

Organism-specific databases

CTDi 1595.
GeneCardsi GC07M091741.
HGNCi HGNC:2649. CYP51A1.
HPAi HPA041325.
HPA043508.
MIMi 601637. gene.
neXtProti NX_Q16850.
PharmGKBi PA27123.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00660000095370.
HOVERGENi HBG051102.
InParanoidi Q16850.
KOi K05917.
OrthoDBi EOG7PZRX3.
PhylomeDBi Q16850.
TreeFami TF105091.

Enzyme and pathway databases

UniPathwayi UPA00770 ; UER00754 .
BioCyci MetaCyc:HS00076-MONOMER.
Reactomei REACT_13812. Endogenous sterols.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

EvolutionaryTracei Q16850.
GenomeRNAii 1595.
NextBioi 6556.
PROi Q16850.
SOURCEi Search...

Gene expression databases

Bgeei Q16850.
CleanExi HS_CYP51A1.
ExpressionAtlasi Q16850. baseline.
Genevestigatori Q16850.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00465. EP450IV.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols."
    Stroemstedt M., Rozman D., Waterman M.R.
    Arch. Biochem. Biophys. 329:73-81(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient and conserved P450 species."
    Aoyama Y., Noshiro M., Gotoh O., Imaoka S., Funae Y., Kurosawa N., Horiuchi T., Yoshida Y.
    J. Biochem. 119:926-933(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family."
    Rozman D., Stroemstedt M., Waterman M.R.
    Arch. Biochem. Biophys. 333:466-474(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  4. "Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes."
    Rozman D., Stroemstedt M., Tsui L.-C., Scherer S.W., Waterman M.R.
    Genomics 38:371-381(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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).
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural basis of human CYP51 inhibition by antifungal azoles."
    Strushkevich N., Usanov S.A., Park H.W.
    J. Mol. Biol. 397:1067-1078(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 54-502 IN COMPLEXES WITH HEME; KETOCONAZOLE AND ECONAZOLE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.

Entry informationi

Entry nameiCP51A_HUMAN
AccessioniPrimary (citable) accession number: Q16850
Secondary accession number(s): A4D1F8
, B2RAI4, B4DJ55, O00770, O00772, Q16784, Q8N1A8, Q99868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: November 26, 2014
This is version 142 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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