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Protein

Cytochrome P450 26B1

Gene

CYP26B1

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

Functioni

Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA. Essential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints.2 Publications
Has also a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo.1 Publication

Cofactori

hemeBy similarity

Kineticsi

  1. KM=1.01 µM for tazarotenic acid (measured in vitro by the production of tazarotenic acid-sulfoxide)1 Publication
  2. KM=0.56 µM for tazarotenic acid (measured in vitro by the production of hydroxytazarotenic acid production)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi441 – 4411Iron (heme axial ligand)Sequence analysis

    GO - Molecular functioni

    • heme binding Source: BHF-UCL
    • iron ion binding Source: InterPro
    • retinoic acid 4-hydroxylase activity Source: BHF-UCL
    • retinoic acid binding Source: BHF-UCL

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiR-HSA-211916. Vitamins.
    R-HSA-5365859. RA biosynthesis pathway.
    R-HSA-5579015. Defective CYP26B1 causes Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome P450 26B1 (EC:1.14.13.-2 Publications)
    Alternative name(s):
    Cytochrome P450 26A2
    Cytochrome P450 retinoic acid-inactivating 2
    Short name:
    Cytochrome P450RAI-2
    Retinoic acid-metabolizing cytochrome
    Gene namesi
    Name:CYP26B1
    Synonyms:CYP26A2, P450RAI2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20581. CYP26B1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • endoplasmic reticulum membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disease characterized by craniofacial malformations, occipital encephalocele, radiohumeral fusions, oligodactyly, advanced osseous maturation, and calvarial mineralization defects.
    See also OMIM:614416
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti146 – 1461S → P in RHFCA. 1 Publication
    Corresponds to variant rs281875232 [ dbSNP | Ensembl ].
    VAR_067923
    Natural varianti363 – 3631R → L in RHFCA. 1 Publication
    Corresponds to variant rs281875231 [ dbSNP | Ensembl ].
    VAR_067924

    Keywords - Diseasei

    Craniosynostosis, Disease mutation

    Organism-specific databases

    MalaCardsiCYP26B1.
    MIMi614416. phenotype.
    Orphaneti293925. Lethal occipital encephalocele-skeletal dysplasia syndrome.
    PharmGKBiPA134879191.

    Polymorphism and mutation databases

    DMDMi20137526.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 512512Cytochrome P450 26B1PRO_0000051985Add
    BLAST

    Proteomic databases

    MaxQBiQ9NR63.
    PaxDbiQ9NR63.
    PeptideAtlasiQ9NR63.
    PRIDEiQ9NR63.

    PTM databases

    iPTMnetiQ9NR63.
    PhosphoSiteiQ9NR63.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, particularly in the cerebellum and pons.1 Publication

    Inductioni

    By retinoic acid.1 Publication

    Gene expression databases

    BgeeiQ9NR63.
    CleanExiHS_CYP26B1.
    ExpressionAtlasiQ9NR63. baseline and differential.
    GenevisibleiQ9NR63. HS.

    Organism-specific databases

    HPAiHPA012567.

    Interactioni

    Protein-protein interaction databases

    BioGridi121153. 2 interactions.
    STRINGi9606.ENSP00000001146.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NR63.
    SMRiQ9NR63. Positions 32-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiKOG0157. Eukaryota.
    COG2124. LUCA.
    GeneTreeiENSGT00800000124060.
    HOGENOMiHOG000220829.
    HOVERGENiHBG051099.
    InParanoidiQ9NR63.
    KOiK12664.
    OMAiNQNEILP.
    OrthoDBiEOG7F24SP.
    PhylomeDBiQ9NR63.
    TreeFamiTF105093.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NR63-1) [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
    MLFEGLDLVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP
    60 70 80 90 100
    KGSMGFPLIG ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE
    110 120 130 140 150
    NVRKILMGEH HLVSTEWPRS TRMLLGPNTV SNSIGDIHRN KRKVFSKIFS
    160 170 180 190 200
    HEALESYLPK IQLVIQDTLR AWSSHPEAIN VYQEAQKLTF RMAIRVLLGF
    210 220 230 240 250
    SIPEEDLGHL FEVYQQFVDN VFSLPVDLPF SGYRRGIQAR QILQKGLEKA
    260 270 280 290 300
    IREKLQCTQG KDYLDALDLL IESSKEHGKE MTMQELKDGT LELIFAAYAT
    310 320 330 340 350
    TASASTSLIM QLLKHPTVLE KLRDELRAHG ILHSGGCPCE GTLRLDTLSG
    360 370 380 390 400
    LRYLDCVIKE VMRLFTPISG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH
    410 420 430 440 450
    DTAPVFKDVN VFDPDRFSQA RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF
    460 470 480 490 500
    LKVLAVELAS TSRFELATRT FPRITLVPVL HPVDGLSVKF FGLDSNQNEI
    510
    LPETEAMLSA TV
    Length:512
    Mass (Da):57,513
    Last modified:October 1, 2000 - v1
    Checksum:iA06D1D9944E6726F
    GO
    Isoform 2 (identifier: Q9NR63-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-143: Missing.

    Show »
    Length:437
    Mass (Da):49,007
    Checksum:i85CA080EB0045520
    GO
    Isoform 3 (identifier: Q9NR63-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-67: MLFEGLDLVS...LIGETGHWLL → MKNKTCVLVC...TLRETRVWLP

    Note: No experimental confirmation available.
    Show »
    Length:495
    Mass (Da):55,756
    Checksum:iF5BBD7200E20573B
    GO

    Sequence cautioni

    The sequence BAH12154.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti265 – 2651D → G in BAH11930 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641H → R.1 Publication
    VAR_075982
    Natural varianti146 – 1461S → P in RHFCA. 1 Publication
    Corresponds to variant rs281875232 [ dbSNP | Ensembl ].
    VAR_067923
    Natural varianti181 – 1811V → M.1 Publication
    Corresponds to variant rs142999899 [ dbSNP | Ensembl ].
    VAR_038722
    Natural varianti185 – 1851A → V.1 Publication
    Corresponds to variant rs765423228 [ dbSNP | Ensembl ].
    VAR_038723
    Natural varianti191 – 1911R → H.1 Publication
    Corresponds to variant rs76025186 [ dbSNP | Ensembl ].
    VAR_038724
    Natural varianti227 – 2271D → N.1 Publication
    Corresponds to variant rs143738797 [ dbSNP | Ensembl ].
    VAR_038725
    Natural varianti264 – 2641L → S.3 Publications
    Corresponds to variant rs2241057 [ dbSNP | Ensembl ].
    VAR_024383
    Natural varianti363 – 3631R → L in RHFCA. 1 Publication
    Corresponds to variant rs281875231 [ dbSNP | Ensembl ].
    VAR_067924
    Natural varianti380 – 3801E → K.1 Publication
    Corresponds to variant rs2286965 [ dbSNP | Ensembl ].
    VAR_038726
    Natural varianti420 – 4201A → G.1 Publication
    Corresponds to variant rs7568553 [ dbSNP | Ensembl ].
    VAR_038727
    Natural varianti473 – 4731R → C.1 Publication
    Corresponds to variant rs61751056 [ dbSNP | Ensembl ].
    VAR_038728
    Natural varianti479 – 4791V → I.1 Publication
    Corresponds to variant rs148075682 [ dbSNP | Ensembl ].
    VAR_038729

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6767MLFEG…GHWLL → MKNKTCVLVCVSVFGGERGQ VTVPRVGVRRPSLAGPLQKC TLRETRVWLP in isoform 3. 1 PublicationVSP_042967Add
    BLAST
    Alternative sequencei69 – 14375Missing in isoform 2. 2 PublicationsVSP_042968Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF252297 mRNA. Translation: AAF76003.1.
    FJ467289 mRNA. Translation: ACR19332.1.
    AK294814 mRNA. Translation: BAH11892.1.
    AK294933 mRNA. Translation: BAH11930.1.
    AK295683 mRNA. Translation: BAH12154.1. Different initiation.
    AK313433 mRNA. Translation: BAG36224.1.
    AC007002 Genomic DNA. Translation: AAY14690.1.
    BC069443 mRNA. Translation: AAH69443.1.
    BC109205 mRNA. Translation: AAI09206.1.
    CCDSiCCDS1919.1. [Q9NR63-1]
    CCDS62934.1. [Q9NR63-2]
    RefSeqiNP_001264671.1. NM_001277742.1. [Q9NR63-2]
    NP_063938.1. NM_019885.3. [Q9NR63-1]
    UniGeneiHs.91546.

    Genome annotation databases

    EnsembliENST00000001146; ENSP00000001146; ENSG00000003137. [Q9NR63-1]
    ENST00000546307; ENSP00000443304; ENSG00000003137. [Q9NR63-2]
    GeneIDi56603.
    KEGGihsa:56603.
    UCSCiuc002sih.3. human. [Q9NR63-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF252297 mRNA. Translation: AAF76003.1.
    FJ467289 mRNA. Translation: ACR19332.1.
    AK294814 mRNA. Translation: BAH11892.1.
    AK294933 mRNA. Translation: BAH11930.1.
    AK295683 mRNA. Translation: BAH12154.1. Different initiation.
    AK313433 mRNA. Translation: BAG36224.1.
    AC007002 Genomic DNA. Translation: AAY14690.1.
    BC069443 mRNA. Translation: AAH69443.1.
    BC109205 mRNA. Translation: AAI09206.1.
    CCDSiCCDS1919.1. [Q9NR63-1]
    CCDS62934.1. [Q9NR63-2]
    RefSeqiNP_001264671.1. NM_001277742.1. [Q9NR63-2]
    NP_063938.1. NM_019885.3. [Q9NR63-1]
    UniGeneiHs.91546.

    3D structure databases

    ProteinModelPortaliQ9NR63.
    SMRiQ9NR63. Positions 32-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121153. 2 interactions.
    STRINGi9606.ENSP00000001146.

    PTM databases

    iPTMnetiQ9NR63.
    PhosphoSiteiQ9NR63.

    Polymorphism and mutation databases

    DMDMi20137526.

    Proteomic databases

    MaxQBiQ9NR63.
    PaxDbiQ9NR63.
    PeptideAtlasiQ9NR63.
    PRIDEiQ9NR63.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000001146; ENSP00000001146; ENSG00000003137. [Q9NR63-1]
    ENST00000546307; ENSP00000443304; ENSG00000003137. [Q9NR63-2]
    GeneIDi56603.
    KEGGihsa:56603.
    UCSCiuc002sih.3. human. [Q9NR63-1]

    Organism-specific databases

    CTDi56603.
    GeneCardsiCYP26B1.
    HGNCiHGNC:20581. CYP26B1.
    HPAiHPA012567.
    MalaCardsiCYP26B1.
    MIMi605207. gene.
    614416. phenotype.
    neXtProtiNX_Q9NR63.
    Orphaneti293925. Lethal occipital encephalocele-skeletal dysplasia syndrome.
    PharmGKBiPA134879191.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0157. Eukaryota.
    COG2124. LUCA.
    GeneTreeiENSGT00800000124060.
    HOGENOMiHOG000220829.
    HOVERGENiHBG051099.
    InParanoidiQ9NR63.
    KOiK12664.
    OMAiNQNEILP.
    OrthoDBiEOG7F24SP.
    PhylomeDBiQ9NR63.
    TreeFamiTF105093.

    Enzyme and pathway databases

    ReactomeiR-HSA-211916. Vitamins.
    R-HSA-5365859. RA biosynthesis pathway.
    R-HSA-5579015. Defective CYP26B1 causes Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA).

    Miscellaneous databases

    GeneWikiiCYP26B1.
    GenomeRNAii56603.
    PROiQ9NR63.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NR63.
    CleanExiHS_CYP26B1.
    ExpressionAtlasiQ9NR63. baseline and differential.
    GenevisibleiQ9NR63. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of the human cytochrome P450, P450RAI-2, which is predominantly expressed in the adult cerebellum and is responsible for all-trans-retinoic acid metabolism."
      White J.A., Ramshaw H., Taimi M., Stangle W., Zhang A., Everingham S., Creighton S., Tam S.-P., Jones G., Petkovich M.
      Proc. Natl. Acad. Sci. U.S.A. 97:6403-6408(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION.
      Tissue: Retina.
    2. "A spliced version of the human cytochrome P450 26B1 has an alternative function in retinoic acid metabolism."
      Savenstrand H., Kumawat A., Karlsson M., Eriksson L.A., Sirsjo A., Strid A.
      Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT SER-264.
      Tissue: Vascular smooth muscle.
    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; 2 AND 3), VARIANT SER-264.
      Tissue: Brain, Cerebellum and Hippocampus.
    4. SeattleSNPs variation discovery resource
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-181; VAL-185; HIS-191; ASN-227; SER-264; LYS-380; GLY-420; CYS-473 AND ILE-479.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      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).
    7. "Craniosynostosis and multiple skeletal anomalies in humans and zebrafish result from a defect in the localized degradation of retinoic acid."
      Laue K., Pogoda H.M., Daniel P.B., van Haeringen A., Alanay Y., von Ameln S., Rachwalski M., Morgan T., Gray M.J., Breuning M.H., Sawyer G.M., Sutherland-Smith A.J., Nikkels P.G., Kubisch C., Bloch W., Wollnik B., Hammerschmidt M., Robertson S.P.
      Am. J. Hum. Genet. 89:595-606(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, VARIANTS RHFCA PRO-146 AND LEU-363.
    8. "Identification of tazarotenic acid as the first xenobiotic substrate of human retinoic acid hydroxylase CYP26A1 and CYP26B1."
      Foti R.S., Isoherranen N., Zelter A., Dickmann L.J., Buttrick B.R., Diaz P., Douguet D.
      J. Pharmacol. Exp. Ther. 357:281-292(2016) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT ARG-64.

    Entry informationi

    Entry nameiCP26B_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR63
    Secondary accession number(s): B2R8M7
    , B7Z2K6, B7Z2P4, B7Z3B8, E4W5W7, Q32MC0, Q53TW1, Q9NP41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: October 1, 2000
    Last modified: July 6, 2016
    This is version 138 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.