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O15528

- CP27B_HUMAN

UniProt

O15528 - CP27B_HUMAN

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Protein
25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Gene
CYP27B1, CYP1ALPHA, CYP27B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation.

Catalytic activityi

Calcidiol + NADPH + O2 = calcitriol + NADP+ + H2O.

Cofactori

Heme group By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi455 – 4551Iron (heme axial ligand) By similarity

GO - Molecular functioni

  1. calcidiol 1-monooxygenase activity Source: BHF-UCL
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. G1 to G0 transition Source: BHF-UCL
  2. bone mineralization Source: BHF-UCL
  3. calcitriol biosynthetic process from calciol Source: BHF-UCL
  4. calcium ion homeostasis Source: BHF-UCL
  5. calcium ion transport Source: BHF-UCL
  6. decidualization Source: BHF-UCL
  7. negative regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  8. negative regulation of cell growth Source: BHF-UCL
  9. negative regulation of cell proliferation Source: BHF-UCL
  10. positive regulation of keratinocyte differentiation Source: BHF-UCL
  11. positive regulation of vitamin D 24-hydroxylase activity Source: BHF-UCL
  12. positive regulation of vitamin D receptor signaling pathway Source: BHF-UCL
  13. regulation of bone mineralization Source: BHF-UCL
  14. response to estrogen Source: BHF-UCL
  15. response to interferon-gamma Source: BHF-UCL
  16. response to lipopolysaccharide Source: BHF-UCL
  17. response to vitamin D Source: BHF-UCL
  18. small molecule metabolic process Source: Reactome
  19. steroid metabolic process Source: Reactome
  20. vitamin D catabolic process Source: Ensembl
  21. vitamin D metabolic process Source: BHF-UCL
  22. vitamin metabolic process Source: Reactome
  23. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.14.13.13. 2681.
ReactomeiREACT_13450. Vitamins.
REACT_13523. Vitamin D (calciferol) metabolism.
UniPathwayiUPA00955.

Names & Taxonomyi

Protein namesi
Recommended name:
25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC:1.14.13.13)
Alternative name(s):
25-OHD-1 alpha-hydroxylase
25-hydroxyvitamin D(3) 1-alpha-hydroxylase
Short name:
VD3 1A hydroxylase
Calcidiol 1-monooxygenase
Cytochrome P450 subfamily XXVIIB polypeptide 1
Cytochrome P450C1 alpha
Cytochrome P450VD1-alpha
Cytochrome p450 27B1
Gene namesi
Name:CYP27B1
Synonyms:CYP1ALPHA, CYP27B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2606. CYP27B1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. mitochondrial outer membrane Source: Reactome
  3. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Rickets vitamin D-dependent 1A (VDDR1A) [MIM:264700]: A disorder caused by a selective deficiency of the active form of vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective bone mineralization and clinical features of rickets.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651Q → H in VDDR1A. 1 Publication
VAR_016969
Natural varianti107 – 1071R → H in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934604 [ dbSNP | Ensembl ].
VAR_016952
Natural varianti125 – 1251G → E in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934605 [ dbSNP | Ensembl ].
VAR_016953
Natural varianti189 – 1891E → G in VDDR1A; 22% of wild-type activity. 1 Publication
VAR_016954
Natural varianti189 – 1891E → K in VDDR1A; 11% of wild-type activity. 1 Publication
VAR_016967
Natural varianti321 – 3211T → R in VDDR1A; complete loss of activity. 1 Publication
VAR_016955
Natural varianti323 – 3231S → Y in VDDR1A. 1 Publication
VAR_016970
Natural varianti335 – 3351R → P in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934606 [ dbSNP | Ensembl ].
VAR_016956
Natural varianti343 – 3431L → F in VDDR1A; 2.3% of wild-type activity. 1 Publication
VAR_016957
Natural varianti382 – 3821P → S in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934607 [ dbSNP | Ensembl ].
VAR_016958
Natural varianti389 – 3891R → C in VDDR1A; complete loss of activity. 1 Publication
VAR_016968
Natural varianti389 – 3891R → G in VDDR1A; complete loss of activity. 1 Publication
VAR_016960
Natural varianti389 – 3891R → H in VDDR1A; complete loss of activity. 2 Publications
VAR_016959
Natural varianti409 – 4091T → I in VDDR1A. 2 Publications
VAR_016961
Natural varianti429 – 4291R → P in VDDR1A. 1 Publication
VAR_016971
Natural varianti453 – 4531R → C in VDDR1A. 1 Publication
VAR_016972
Natural varianti478 – 4781V → G in VDDR1A. 1 Publication
VAR_016973
Natural varianti497 – 4971P → R in VDDR1A. 1 Publication
VAR_016974

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi264700. phenotype.
Orphaneti289157. Hypocalcemic vitamin D-dependent rickets.
PharmGKBiPA27099.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 50825-hydroxyvitamin D-1 alpha hydroxylase, mitochondrialPRO_0000003622
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Proteomic databases

PaxDbiO15528.
PRIDEiO15528.

PTM databases

PhosphoSiteiO15528.

Expressioni

Tissue specificityi

Kidney.

Gene expression databases

ArrayExpressiO15528.
BgeeiO15528.
CleanExiHS_CYP27B1.
GenevestigatoriO15528.

Organism-specific databases

HPAiHPA043358.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000228606.

Structurei

3D structure databases

ProteinModelPortaliO15528.
SMRiO15528. Positions 35-505.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000253961.
HOVERGENiHBG106909.
InParanoidiO15528.
KOiK07438.
OMAiLHSEITA.
OrthoDBiEOG7ZGX4B.
PhylomeDBiO15528.
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]

Sequencei

Sequence statusi: Complete.

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

O15528-1 [UniParc]FASTAAdd to Basket

« Hide

MTQTLKYASR VFHRVRWAPE LGASLGYREY HSARRSLADI PGPSTPSFLA    50
ELFCKGGLSR LHELQVQGAA HFGPVWLASF GTVRTVYVAA PALVEELLRQ 100
EGPRPERCSF SPWTEHRRCR QRACGLLTAE GEEWQRLRSL LAPLLLRPQA 150
AARYAGTLNN VVCDLVRRLR RQRGRGTGPP ALVRDVAGEF YKFGLEGIAA 200
VLLGSRLGCL EAQVPPDTET FIRAVGSVFV STLLTMAMPH WLRHLVPGPW 250
GRLCRDWDQM FAFAQRHVER REAEAAMRNG GQPEKDLESG AHLTHFLFRE 300
ELPAQSILGN VTELLLAGVD TVSNTLSWAL YELSRHPEVQ TALHSEITAA 350
LSPGSSAYPS ATVLSQLPLL KAVVKEVLRL YPVVPGNSRV PDKDIHVGDY 400
IIPKNTLVTL CHYATSRDPA QFPEPNSFRP ARWLGEGPTP HPFASLPFGF 450
GKRSCMGRRL AELELQMALA QILTHFEVQP EPGAAPVRPK TRTVLVPERS 500
INLQFLDR 508
Length:508
Mass (Da):56,504
Last modified:January 1, 1998 - v1
Checksum:i7F0611EFAD1B5C1C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651Q → H in VDDR1A. 1 Publication
VAR_016969
Natural varianti107 – 1071R → H in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934604 [ dbSNP | Ensembl ].
VAR_016952
Natural varianti125 – 1251G → E in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934605 [ dbSNP | Ensembl ].
VAR_016953
Natural varianti166 – 1661V → L.1 Publication
Corresponds to variant rs8176344 [ dbSNP | Ensembl ].
VAR_018841
Natural varianti189 – 1891E → G in VDDR1A; 22% of wild-type activity. 1 Publication
VAR_016954
Natural varianti189 – 1891E → K in VDDR1A; 11% of wild-type activity. 1 Publication
VAR_016967
Natural varianti321 – 3211T → R in VDDR1A; complete loss of activity. 1 Publication
VAR_016955
Natural varianti323 – 3231S → Y in VDDR1A. 1 Publication
VAR_016970
Natural varianti335 – 3351R → P in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934606 [ dbSNP | Ensembl ].
VAR_016956
Natural varianti343 – 3431L → F in VDDR1A; 2.3% of wild-type activity. 1 Publication
VAR_016957
Natural varianti382 – 3821P → S in VDDR1A; complete loss of activity. 1 Publication
Corresponds to variant rs28934607 [ dbSNP | Ensembl ].
VAR_016958
Natural varianti389 – 3891R → C in VDDR1A; complete loss of activity. 1 Publication
VAR_016968
Natural varianti389 – 3891R → G in VDDR1A; complete loss of activity. 1 Publication
VAR_016960
Natural varianti389 – 3891R → H in VDDR1A; complete loss of activity. 2 Publications
VAR_016959
Natural varianti409 – 4091T → I in VDDR1A. 2 Publications
VAR_016961
Natural varianti429 – 4291R → P in VDDR1A. 1 Publication
VAR_016971
Natural varianti453 – 4531R → C in VDDR1A. 1 Publication
VAR_016972
Natural varianti478 – 4781V → G in VDDR1A. 1 Publication
VAR_016973
Natural varianti497 – 4971P → R in VDDR1A. 1 Publication
VAR_016974

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201D → N in BAG37458. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF027152 Genomic DNA. Translation: AAC51854.1.
AB005038 mRNA. Translation: BAA23416.1.
AB005989 mRNA. Translation: BAA22656.1.
AB005990 Genomic DNA. Translation: BAA22657.1.
AB006987 Genomic DNA. Translation: BAA23418.1.
AF020192 mRNA. Translation: AAC51853.1.
AF256213 Genomic DNA. Translation: AAG00416.1.
AF246895 mRNA. Translation: AAF64299.1.
AY288916 Genomic DNA. Translation: AAP31972.1.
AK314953 mRNA. Translation: BAG37458.1.
CH471054 Genomic DNA. Translation: EAW97067.1.
BC136386 mRNA. Translation: AAI36387.1.
CCDSiCCDS8954.1.
PIRiJC5713.
RefSeqiNP_000776.1. NM_000785.3.
UniGeneiHs.524528.

Genome annotation databases

EnsembliENST00000228606; ENSP00000228606; ENSG00000111012.
GeneIDi1594.
KEGGihsa:1594.
UCSCiuc001spz.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF027152 Genomic DNA. Translation: AAC51854.1 .
AB005038 mRNA. Translation: BAA23416.1 .
AB005989 mRNA. Translation: BAA22656.1 .
AB005990 Genomic DNA. Translation: BAA22657.1 .
AB006987 Genomic DNA. Translation: BAA23418.1 .
AF020192 mRNA. Translation: AAC51853.1 .
AF256213 Genomic DNA. Translation: AAG00416.1 .
AF246895 mRNA. Translation: AAF64299.1 .
AY288916 Genomic DNA. Translation: AAP31972.1 .
AK314953 mRNA. Translation: BAG37458.1 .
CH471054 Genomic DNA. Translation: EAW97067.1 .
BC136386 mRNA. Translation: AAI36387.1 .
CCDSi CCDS8954.1.
PIRi JC5713.
RefSeqi NP_000776.1. NM_000785.3.
UniGenei Hs.524528.

3D structure databases

ProteinModelPortali O15528.
SMRi O15528. Positions 35-505.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000228606.

Chemistry

BindingDBi O15528.
ChEMBLi CHEMBL5993.
DrugBanki DB00146. Calcidiol.
DB00136. Calcitriol.
DB00153. Ergocalciferol.

PTM databases

PhosphoSitei O15528.

Proteomic databases

PaxDbi O15528.
PRIDEi O15528.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228606 ; ENSP00000228606 ; ENSG00000111012 .
GeneIDi 1594.
KEGGi hsa:1594.
UCSCi uc001spz.1. human.

Organism-specific databases

CTDi 1594.
GeneCardsi GC12M058156.
H-InvDB HIX0171662.
HGNCi HGNC:2606. CYP27B1.
HPAi HPA043358.
MIMi 264700. phenotype.
609506. gene.
neXtProti NX_O15528.
Orphaneti 289157. Hypocalcemic vitamin D-dependent rickets.
PharmGKBi PA27099.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
HOGENOMi HOG000253961.
HOVERGENi HBG106909.
InParanoidi O15528.
KOi K07438.
OMAi LHSEITA.
OrthoDBi EOG7ZGX4B.
PhylomeDBi O15528.
TreeFami TF105094.

Enzyme and pathway databases

UniPathwayi UPA00955 .
BRENDAi 1.14.13.13. 2681.
Reactomei REACT_13450. Vitamins.
REACT_13523. Vitamin D (calciferol) metabolism.

Miscellaneous databases

GeneWikii 25-Hydroxyvitamin_D3_1-alpha-hydroxylase.
GenomeRNAii 1594.
NextBioi 35468145.
PROi O15528.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15528.
Bgeei O15528.
CleanExi HS_CYP27B1.
Genevestigatori O15528.

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. "Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha."
    Fu G.K., Portale A.P., Miller W.L.
    DNA Cell Biol. 16:1499-1507(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase."
    Monkawa T., Yoshida T., Wakino S., Shinki T., Anazawa H., Deluca H.F., Suda T., Hayashi M., Saruta T.
    Biochem. Biophys. Res. Commun. 239:527-533(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Kidney.
  3. "Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1."
    Fu G.K., Lin D., Zhang Y.H., Bikle D.D., Shackleton C.H., Miller W.L., Portale A.A.
    Mol. Endocrinol. 11:1961-1970(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Targeted disruption of the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in ras-transformed keratinocytes demonstrates that locally produced 1alpha,25-dihydroxyvitamin D3 suppresses growth and induces differentiation in an autocrine fashion."
    Huang D.C., Papavasiliou V., Rhim J.S., Horst R.L., Kremer R.
    Mol. Cancer Res. 1:56-67(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Targeted disruption of the 25-hydroxyvitamin D3 1 a-hydroxylase gene in a Ras-transformed human keratinocyte cell line: evidence for an autocrine growth regulatory function of 1 alpha, 25-dihydroxyvitamin D3 in vitro and in vivo."
    Huang D.C., Papavasiliou J., Rhim J., Kremer R.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-166.
  7. "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].
    Tissue: Kidney.
  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].
  10. "Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets."
    Kitanaka S., Takeyama K., Murayama A., Sato T., Okumura K., Nogami M., Hasegawa Y., Niimi H., Yanagisawa J., Tanaka T., Kato S.
    N. Engl. J. Med. 338:653-661(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VDDR1A HIS-107; GLU-125; PRO-335 AND SER-382.
  11. "Genetics of vitamin D 1-alpha-hydroxylase deficiency in 17 families."
    Wang J.T., Lin C.-J., Burridge S.M., Fu G.K., Labuda M., Portale A.A., Miller W.L.
    Am. J. Hum. Genet. 63:1694-1702(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VDDR1A HIS-65; LYS-189; HIS-389; ILE-409; PRO-429; CYS-453 AND ARG-497.
  12. "Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages."
    Smith S.J., Rucka A.K., Berry J.L., Davies M., Mylchreest S., Paterson C.R., Heath D.A., Tassabehji M., Read A.P., Mee A.P., Mawer E.B.
    J. Bone Miner. Res. 14:730-739(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VDDR1A TYR-323 AND GLY-478.
  13. "No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation."
    Kitanaka S., Murayama A., Sakaki T., Inouye K., Seino Y., Fukumoto S., Shima M., Yukizane S., Takayanagi M., Niimi H., Takeyama K., Kato S.
    J. Clin. Endocrinol. Metab. 84:4111-4117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VDDR1A ARG-321 AND CYS-389.
  14. "Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro."
    Wang X., Zhang M.Y., Miller W.L., Portale A.A.
    J. Clin. Endocrinol. Metab. 87:2424-2430(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VDDR1A GLY-189; PHE-343; GLY-389; HIS-389 AND ILE-409.

Entry informationi

Entry nameiCP27B_HUMAN
AccessioniPrimary (citable) accession number: O15528
Secondary accession number(s): B2RC61, Q548T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 139 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 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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