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Q16850

- CP51A_HUMAN

UniProt

Q16850 - CP51A_HUMAN

Protein

Lanosterol 14-alpha demethylase

Gene

CYP51A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    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

    Heme group.1 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

    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

    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

    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

    ArrayExpressiQ16850.
    BgeeiQ16850.
    CleanExiHS_CYP51A1.
    GenevestigatoriQ16850.

    Organism-specific databases

    HPAiHPA041325.
    HPA043508.

    Interactioni

    Protein-protein interaction databases

    BioGridi107967. 3 interactions.
    IntActiQ16850. 3 interactions.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2124.
    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

    MLLLGLLQAG GSVLGQAMEK VTGGNLLSML LIACAFTLSL VYLIRLAAGH    50
    LVQLPAGVKS PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM 100
    VGKTFTYLLG SDAAALLFNS KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP 150
    VFLEQKKMLK SGLNIAHFKQ HVSIIEKETK EYFESWGESG EKNVFEALSE 200
    LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL LPGWLPLPSF 250
    RRRDRAHREI KDIFYKAIQK RRQSQEKIDD ILQTLLDATY KDGRPLTDDE 300
    VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQKKCYLE QKTVCGENLP 350
    PLTYDQLKDL NLLDRCIKET LRLRPPIMIM MRMARTPQTV AGYTIPPGHQ 400
    VCVSPTVNQR LKDSWVERLD FNPDRYLQDN PASGEKFAYV PFGAGRHRCI 450
    GENFAYVQIK TIWSTMLRLY EFDLIDGYFP TVNYTTMIHT PENPVIRYKR 500
    RSK 503
    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.
    The sequence AAB46356.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH32322.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA09512.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAG36881.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAL24154.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW76858.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 3 interactions.
    IntActi Q16850. 3 interactions.

    Chemistry

    BindingDBi Q16850.
    ChEMBLi CHEMBL3849.
    DrugBanki DB00196. Fluconazole.
    DB01167. Itraconazole.
    DB01026. Ketoconazole.
    DB01110. Miconazole.
    DB00251. Terconazole.

    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.
    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

    ArrayExpressi Q16850.
    Bgeei Q16850.
    CleanExi HS_CYP51A1.
    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

    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: October 1, 2014
    This is version 140 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