Skip Header

Contribute Send feedback
Read comments (?) or add your own

P08686 (CP21A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Steroid 21-hydroxylase
EC=1.14.99.10
Alternative name(s):
21-OHase
Cytochrome P-450c21
Cytochrome P450 21
Cytochrome P450 XXI
Cytochrome P450-C21
Cytochrome P450-C21B
Gene names
Name:CYP21A2
Synonyms:CYP21, CYP21B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids.

Catalytic activity

A C21 steroid + (reduced NADPH--hemoprotein reductase) + O2 = a 21-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + H2O.

Cofactor

Heme group.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Domain

The leucine-rich hydrophobic amino acid N-terminal region probably helps to anchor the protein to the microsomal membrane.

Polymorphism

Seven non deleterious alleles are known: CYP21A2*1A, CYP21A2*1B, CYP21A2*2, CYP21A2*3, CYP21A2*4, CYP21A2*5 and CYP21A2*6. The sequence shown corresponds to allele CYP21A2*1B. Deleterious alleles are mostly generated by recombinations between CYP21A2 and the pseudogene CYP21A1P through gene conversion. This process consists of recombination events that either delete CYP21A2 or transfer deleterious mutations from CYP21A1P to CYP21A2.

Involvement in disease

Adrenal hyperplasia 3 (AH3) [MIM:201910]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late-onset (NC or LOAH)and 'cryptic' (asymptomatic).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.4 Ref.5 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61

Sequence similarities

Belongs to the cytochrome P450 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08686-1)

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.
Isoform 2 (identifier: P08686-2)

The sequence of this isoform differs from the canonical sequence as follows:
     6-6: L → LL
     68-102: VVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSK → KLVSR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Steroid 21-hydroxylase
PRO_0000051976

Regions

Region342 – 35817Steroid-binding By similarity

Sites

Metal binding4281Iron (heme axial ligand)

Natural variations

Alternative sequence61L → LL in isoform 2.
VSP_046264
Alternative sequence68 – 10235VVVLN…KLVSK → KLVSR in isoform 2.
VSP_046265
Natural variant91L → LL in allele CYP21A2*2. Ref.3 Ref.4 Ref.5 Ref.19
VAR_018363
Natural variant151A → T in AH3; salt wasting form; no significant difference in activity compared with the wild-type. Ref.50 Ref.55
Corresponds to variant rs63749090 [ dbSNP | Ensembl ].
VAR_026059
Natural variant301P → L in AH3; non-classic form; 50% activity; 10% of non-classic AH3 Texan patients. Ref.21 Ref.22 Ref.33 Ref.35 Ref.36 Ref.38 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47 Ref.50 Ref.51 Ref.55 Ref.56 Ref.57 Ref.58
VAR_001281
Natural variant301P → Q in AH3; does not affect membrane binding; enzyme function abolished. Ref.32
VAR_026060
Natural variant561G → R in AH3; loss of activity. Ref.59
VAR_065668
Natural variant621H → L in AH3; non-classic form; simple virilizing form when associated with a second mild mutation such as S-453 or L-30; activity is significantly reduced in association with S-453. Ref.51 Ref.58 Ref.59
VAR_018364
Natural variant641G → E in AH3; no activity. Ref.35
VAR_007923
Natural variant771I → T in AH3; simple virilizing form. Ref.61
VAR_065669
Natural variant901G → V in AH3. Ref.33
VAR_026061
Natural variant981K → R.
VAR_001282
Natural variant1021K → R in allele CYP21A2*3. Ref.3 Ref.5 Ref.56
VAR_001283
Natural variant1051P → L in AH3. Ref.24 Ref.29
VAR_001284
Natural variant1071L → R in AH3; loss of activity. Ref.59
VAR_065670
Natural variant1211K → Q in AH3; non-classic form; reduced activity; decreased affinity for 17-hydroxyprogesterone and progesterone. Ref.60
VAR_065671
Natural variant1241R → H in AH3. Ref.54
Corresponds to variant rs72552750 [ dbSNP | Ensembl ].
VAR_026062
Natural variant1421L → P in AH3; loss of activity. Ref.59
VAR_065672
Natural variant1671L → P in AH3; salt wasting form; loss of activity. Ref.61
VAR_065673
Natural variant1691C → Y in AH3. Ref.34
VAR_001285
Natural variant1721I → N in AH3; simple virilizing form; 1-4% activity. Ref.11 Ref.12 Ref.13 Ref.19 Ref.20 Ref.22 Ref.26 Ref.33 Ref.35 Ref.36 Ref.38 Ref.39 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47 Ref.50 Ref.51 Ref.52 Ref.53 Ref.56 Ref.57 Ref.58 Ref.59 Ref.61
VAR_001286
Natural variant1781G → A in AH3. Ref.33
Corresponds to variant rs72552751 [ dbSNP | Ensembl ].
VAR_026063
Natural variant1831D → E in allele CYP21A2*4.
Corresponds to variant rs1040310 [ dbSNP | Ensembl ].
VAR_001287
Natural variant1961Missing in AH3; moderate. Ref.31
VAR_008688
Natural variant2111V → L in AH3; non-classic form; pathogenicity uncertain. Ref.18
VAR_026064
Natural variant2301I → T in AH3. Ref.61
VAR_065674
Natural variant2331R → K in AH3. Ref.61
VAR_065675
Natural variant2361I → N in AH3; salt wasting form. Ref.22 Ref.26 Ref.35 Ref.36 Ref.56
VAR_001288
Natural variant2371V → E in AH3; salt wasting form. Ref.22 Ref.36 Ref.56
Corresponds to variant rs12530380 [ dbSNP | Ensembl ].
VAR_001289
Natural variant2391M → K in AH3; salt wasting form. Ref.22 Ref.36 Ref.56
Corresponds to variant rs6476 [ dbSNP | Ensembl ].
VAR_001290
Natural variant2611L → P in AH3. Ref.43
VAR_026065
Natural variant2681S → T in allele CYP21A2*5. Ref.3 Ref.21 Ref.38 Ref.40
Corresponds to variant rs6472 [ dbSNP | Ensembl ].
VAR_001291
Natural variant2811V → G in AH3; salt wasting form. Ref.42
VAR_026066
Natural variant2811V → L in AH3; non-classic form; 50% activity; most common variant; normal KM but 20% reduced Vmax. Ref.4 Ref.14 Ref.15 Ref.18 Ref.22 Ref.26 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.40 Ref.42 Ref.44 Ref.45 Ref.47 Ref.50 Ref.51 Ref.52 Ref.55 Ref.56 Ref.61
Corresponds to variant rs6471 [ dbSNP | Ensembl ].
VAR_001292
Natural variant2831M → L in AH3. Ref.47
VAR_026067
Natural variant2911G → C in AH3. Ref.33
VAR_026068
Natural variant2911G → R in AH3. Ref.52
VAR_018365
Natural variant2911G → S in AH3; salt wasting form; less then 1% activity. Ref.24 Ref.31 Ref.35 Ref.45 Ref.56 Ref.61
VAR_001293
Natural variant2921G → D in AH3; salt wasting form; less then 1% activity. Ref.61
VAR_065676
Natural variant3001L → F in AH3; salt wasting form. Ref.42
VAR_026069
Natural variant3011S → Y in AH3. Ref.52
VAR_018366
Natural variant3041V → M in hyperandrogenism; due to 21-hydroxylase deficiency; non-classic type; residual activity of 46% for conversion of 17-hydroxyprogesterone and 26% for conversion of progesterone compared with the normal enzyme. Ref.48
VAR_026070
Natural variant3171L → M in AH3. Ref.44
VAR_026071
Natural variant3201E → K in AH3; simple virilizing form; 4% activity. Ref.61
VAR_065677
Natural variant3391R → H in AH3; non-classic form; 50% activity. Ref.5
VAR_001294
Natural variant3411R → P in AH3; simple virilizing form. Ref.51 Ref.52 Ref.61
VAR_018367
Natural variant3411R → W in AH3; non-classic form; mild.
VAR_001295
Natural variant3541R → C in AH3; salt wasting form. Ref.42
VAR_026072
Natural variant3541R → H in AH3; salt wasting form. Ref.33 Ref.61
VAR_026073
Natural variant3561R → P in AH3; salt wasting form; 0.15% activity. Ref.28
VAR_001296
Natural variant3561R → Q in AH3; simple virilizing form; mild; 0.65% activity. Ref.28 Ref.34 Ref.56
VAR_001297
Natural variant3561R → W in AH3; salt wasting form. Ref.19 Ref.22 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47 Ref.51 Ref.52 Ref.53 Ref.56 Ref.57 Ref.58 Ref.59 Ref.61
VAR_001298
Natural variant3621A → V in AH3; no activity. Ref.35
VAR_007924
Natural variant3631L → W in AH3. Ref.46
VAR_026074
Natural variant3651H → Y in AH3. Ref.56
VAR_026075
Natural variant3691R → W in AH3. Ref.61
VAR_065678
Natural variant3751G → S in hyperandrogenism; due to 21-hydroxylase deficiency; almost completely abolished enzyme activity. Ref.48
VAR_026076
Natural variant3801E → D in AH3; salt wasting form. Ref.27
VAR_001299
Natural variant4081R → C in AH3; very low residual activity. Ref.49 Ref.59 Ref.61
VAR_026077
Natural variant4241G → S in AH3; very low activity. Ref.37 Ref.45 Ref.49 Ref.61
VAR_026078
Natural variant4261R → H in AH3; exhibit only low enzyme activity toward 17-hydroxyprogesterone. Ref.45 Ref.61
VAR_026079
Natural variant4351R → C in AH3. Ref.44
VAR_026080
Natural variant4531P → S in AH3; non-classic form; simple virilizing form when associated with L-62; 50% of activity; almost completely abolished enzyme activity when associated with S-375. Ref.5 Ref.23 Ref.24 Ref.29 Ref.33 Ref.40 Ref.42 Ref.44 Ref.45 Ref.47 Ref.48 Ref.50 Ref.51 Ref.56 Ref.58 Ref.59 Ref.60 Ref.61
Corresponds to variant rs6445 [ dbSNP | Ensembl ].
VAR_001300
Natural variant4791R → L in AH3. Ref.56
VAR_026081
Natural variant4821P → S in AH3; reduced enzyme activity to 70% of normal. Ref.55
VAR_026082
Natural variant4831R → P in AH3; moderate; 1-2% of activity. Ref.25 Ref.26 Ref.31 Ref.43 Ref.45 Ref.51 Ref.56
VAR_001301
Natural variant4831R → Q in AH3. Ref.52
VAR_018368
Natural variant4831R → W in AH3; salt wasting form. Ref.53
VAR_026083
Natural variant4931N → S in allele CYP21A2*6. Ref.3 Ref.5 Ref.10 Ref.26 Ref.38 Ref.40
Corresponds to variant rs6473 [ dbSNP | Ensembl ].
VAR_001302

Experimental info

Mutagenesis2681S → C, M or T: No loss of function. Ref.15
Mutagenesis2811V → I: Normal KM but 50% reduced Vmax.
Mutagenesis2811V → T: Normal KM but 10% reduced Vmax.
Mutagenesis4281C → M, S or T: Loss of activity and loss of P450 absorption. Ref.15
Sequence conflict1551G → D in BAB70774. Ref.7
Sequence conflict2421R → G in BAB70774. Ref.7
Sequence conflict2771L → Q in BAB70774. Ref.7
Sequence conflict3041V → A in BAB70774. Ref.7
Sequence conflict3111P → L in AAA59985. Ref.14
Sequence conflict3461N → I in AAA59985. Ref.14
Sequence conflict4261R → P in AAB59440. Ref.1
Sequence conflict4371E → D in AAB59440. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 7E1FF83B59FBA136

FASTA49455,887
        10         20         30         40         50         60 
MLLLGLLLLP LLAGARLLWN WWKLRSLHLP PLAPGFLHLL QPDLPIYLLG LTQKFGPIYR 

        70         80         90        100        110        120 
LHLGLQDVVV LNSKRTIEEA MVKKWADFAG RPEPLTYKLV SKNYPDLSLG DYSLLWKAHK 

       130        140        150        160        170        180 
KLTRSALLLG IRDSMEPVVE QLTQEFCERM RAQPGTPVAI EEEFSLLTCS IICYLTFGDK 

       190        200        210        220        230        240 
IKDDNLMPAY YKCIQEVLKT WSHWSIQIVD VIPFLRFFPN PGLRRLKQAI EKRDHIVEMQ 

       250        260        270        280        290        300 
LRQHKESLVA GQWRDMMDYM LQGVAQPSME EGSGQLLEGH VHMAAVDLLI GGTETTANTL 

       310        320        330        340        350        360 
SWAVVFLLHH PEIQQRLQEE LDHELGPGAS SSRVPYKDRA RLPLLNATIA EVLRLRPVVP 

       370        380        390        400        410        420 
LALPHRTTRP SSISGYDIPE GTVIIPNLQG AHLDETVWER PHEFWPDRFL EPGKNSRALA 

       430        440        450        460        470        480 
FGCGARVCLG EPLARLELFV VLTRLLQAFT LLPSGDALPS LQPLPHCSVI LKMQPFQVRL 

       490 
QPRGMGAHSP GQNQ

« Hide

Isoform 2 [UniParc].

Checksum: 467E740266FFCE89
Show »

FASTA46552,597

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of two steroid 21-hydroxylase genes tandemly arranged in human chromosome: a pseudogene and a genuine gene."
Higashi Y., Yoshioka H., Yamane M., Gotoh O., Fujii-Kuriyama Y.
Proc. Natl. Acad. Sci. U.S.A. 83:2841-2845(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CYP21A2*1A).
[2]"Structure of human steroid 21-hydroxylase genes."
White P.C., New M.I., Dupont B.
Proc. Natl. Acad. Sci. U.S.A. 83:5111-5115(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE CYP21A2*1B) (ISOFORM 1).
[3]"Molecular characterization of the HLA-linked steroid 21-hydroxylase B gene from an individual with congenital adrenal hyperplasia."
Rodrigues N.R., Dunham I., Yu C.Y., Carroll M.C., Porter R.R., Campbell R.D.
EMBO J. 6:1653-1661(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AH3 THR-268, VARIANTS LEU-9 INS; ARG-102 AND SER-493.
[4]"Nonsense mutation causing steroid 21-hydroxylase deficiency."
Globerman H., Amor M., Parker K.L., New M.I., White P.C.
J. Clin. Invest. 82:139-144(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AH3 LEU-281, VARIANT LEU-9 INS.
[5]"R339H and P453S: CYP21 mutations associated with nonclassic steroid 21-hydroxylase deficiency that are not apparent gene conversions."
Helmberg A., Tusie-Luna M.-T., Tabarelli M., Kofler R., White P.C.
Mol. Endocrinol. 6:1318-1322(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-9 INS; ARG-102 AND SER-493, VARIANTS AH3 HIS-339 AND SER-453.
Tissue: Peripheral blood.
[6]"Linkage analysis of the C4A/C4B copy number variation and polymorphisms of the adjacent steroid 21-hydroxylase gene in a healthy population."
Blasko B., Banlaki Z., Gyapay G., Pozsonyi E., Sasvari-Szekely M., Rajczy K., Fust G., Szilagyi A.
Mol. Immunol. 46:2623-2629(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. expand/collapse author list , 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] (ALLELE CYP21A2*6) (ISOFORM 2).
Tissue: Adrenal gland.
[8]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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), VARIANT SER-493.
[11]"A de novo pathological point mutation at the 21-hydroxylase locus: implications for gene conversion in the human genome."
Collier S., Tassabehji M., Sinnott P., Strachan T.
Nat. Genet. 3:260-265(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-185, VARIANT ASN-172.
[12]"Mapping of steroid 21-hydroxylase genes adjacent to complement component C4 genes in HLA, the major histocompatibility complex in man."
Carroll M.C., Campbell R.D., Porter R.R.
Proc. Natl. Acad. Sci. U.S.A. 82:521-525(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-182, VARIANT AH3 ASN-172.
[13]"Mutation in the CYP21B gene (Ile-172-->Asn) causes steroid 21-hydroxylase deficiency."
Amor M., Parker K.L., Globerman H., New M.I., White P.C.
Proc. Natl. Acad. Sci. U.S.A. 85:1600-1604(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-182, VARIANT AH3 ASN-172.
[14]"P450XXI (steroid 21-hydroxylase) gene deletions are not found in family studies of congenital adrenal hyperplasia."
Matteson K.J., Phillips J.A. III, Miller W.L., Chung B.C., Orlando P.J., Frisch H., Ferrandez A., Burr I.M.
Proc. Natl. Acad. Sci. U.S.A. 84:5858-5862(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 265-494 (ISOFORM 1), VARIANT AH3 LEU-281.
[15]"Mutations of P450c21 (steroid 21-hydroxylase) at Cys428, Val281, and Ser268 result in complete, partial, or no loss of enzymatic activity, respectively."
Wu D.-A., Chung B.-C.
J. Clin. Invest. 88:519-523(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT AH3 LEU-281, MUTAGENESIS OF SER-268 AND CYS-428.
[16]"Molecular genetics of 21-hydroxylase deficient late-onset adrenal hyperplasia."
Gunn S.K., Sherman L.D., Therrell B.L., Owerbach D.I.
Semin. Reprod. Endocrinol. 11:347-352(1993)
Cited for: REVIEW ON AH3 VARIANTS.
[17]"Mutations in steroid 21-hydroxylase (CYP21)."
White P.C., Tusie-Luna M.-T., New M.I., Speiser P.W.
Hum. Mutat. 3:373-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON AH3 VARIANTS, GENE CONVERSION.
[18]"Molecular genetic analysis of nonclassic steroid 21-hydroxylase deficiency associated with HLA-B14,DR1."
Speiser P.W., New M.I., White P.C.
N. Engl. J. Med. 319:19-23(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-211 AND LEU-281.
[19]"A missense mutation at Ile172-->Asn or Arg356-->Trp causes steroid 21-hydroxylase deficiency."
Chiou S.-H., Hu M.-C., Chung B.-C.
J. Biol. Chem. 265:3549-3552(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 ASN-172 AND TRP-356, VARIANT LEU-9 INS.
[20]"Substitution of Ile-172 to Asn in the steroid 21-hydroxylase B (P450c21B) gene in a Finnish patient with the simple virilizing form of congenital adrenal hyperplasia."
Partanen J., Campbell R.D.
Hum. Genet. 87:716-720(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 ASN-172.
[21]"A mutation (Pro-30 to Leu) in CYP21 represents a potential nonclassic steroid 21-hydroxylase deficiency allele."
Tusie-Luna M.T., Speiser P.W., Dumic M., New M.I., White P.C.
Mol. Endocrinol. 5:685-692(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 LEU-30, VARIANT THR-268.
[22]"Disease expression and molecular genotype in congenital adrenal hyperplasia due to 21-hydroxylase deficiency."
Speiser P.W., Dupont J., Zhu D., Serrat J., Buegeleisen M., Tusie-Luna M.-T., Lesser M., New M.I., White P.C.
J. Clin. Invest. 90:584-595(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281 AND TRP-356.
[23]"Pro-453 to Ser mutation in CYP21 is associated with nonclassic steroid 21-hydroxylase deficiency."
Owerbach D., Sherman L., Ballard A.L., Azziz R.
Mol. Endocrinol. 6:1211-1215(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 SER-453.
[24]"Steroid 21-hydroxylase deficiency: three additional mutated alleles and establishment of phenotype-genotype relationships of common mutations."
Wedell A., Ritzen E.M., Haglund-Stengler B., Luthman H.
Proc. Natl. Acad. Sci. U.S.A. 89:7232-7236(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-105; SER-291 AND SER-453.
[25]"Steroid 21-hydroxylase (P450c21): a new allele and spread of mutations through the pseudogene."
Wedell A., Luthman H.
Hum. Genet. 91:236-240(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 PRO-483.
[26]"Screening of CYP21 gene mutations in 129 French patients affected by steroid 21-hydroxylase deficiency."
Barbat B., Bogyo A., Raux-Demay M.-C., Kuttenn F., Boue J., Simon-Bouy B., Serre J.-L., Boue A., Mornet E.
Hum. Mutat. 5:126-130(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 ASN-172; ASN-236; LEU-281 AND PRO-483, VARIANT SER-493.
[27]"E380D: a novel point mutation of CYP21 in an HLA-homozygous patient with salt-losing congenital adrenal hyperplasia due to 21-hydroxylase deficiency."
Kirby-Keyser L., Porter C.C., Donohoue P.A.
Hum. Mutat. 9:181-182(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 ASP-380.
[28]"A cluster of missense mutations at Arg356 of human steroid 21-hydroxylase may impair redox partner interaction."
Lajic S., Levo A., Nikoshkov A., Lundberg Y., Partanen J., Wedell A.
Hum. Genet. 99:704-709(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 PRO-356 AND GLN-356.
[29]"Synergistic effect of partially inactivating mutations in steroid 21-hydroxylase deficiency."
Nikoshkov A., Lajic S., Holst M., Wedell A., Luthman H.
J. Clin. Endocrinol. Metab. 82:194-199(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-105 AND SER-453.
[30]"Molecular genetic analysis of patients carrying steroid 21-hydroxylase deficiency in the Mexican population: identification of possible new mutations and high prevalence of apparent germ-line mutations."
Ordonez-Sanchez M.L., Ramirez-Jimenez S., Lopez-Gutierrez A.U., Riba L., Gamboa-Cardiel S., Cerrillo-Hinojosa M., Altamirano-Bustamante N., Calzada-Leon R., Robles-Valdes C., Mendoza-Morfin F., Tusie-Luna M.T.
Hum. Genet. 102:170-177(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3, VARIANTS.
[31]"Naturally occurring mutants of human steroid 21-hydroxylase (P450c21) pinpoint residues important for enzyme activity and stability."
Nikoshkov A., Lajic S., Vlamis-Gardikas A., Tranebjaerg L., Holst M., Wedell A., Luthman H.
J. Biol. Chem. 273:6163-6165(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 GLU-196 DEL; SER-291 AND PRO-483.
[32]"Effects of missense mutations and deletions on membrane anchoring and enzyme function of human steroid 21-hydroxylase (P450c21)."
Lajic S., Nikoshkov A., Holst M., Wedell A.
Biochem. Biophys. Res. Commun. 257:384-390(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 GLN-30, CHARACTERIZATION OF VARIANT AH3 GLN-30.
[33]"Mutation analysis in patients with congenital adrenal hyperplasia in the Spanish population: identification of putative novel steroid 21-hydroxylase deficiency alleles associated with the classic form of the disease."
Lobato M.N., Ordonez-Sanchez M.L., Tusie-Luna M.T., Meseguer A.
Hum. Hered. 49:169-175(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; VAL-90; ASN-172; ALA-178; LEU-281; CYS-291; HIS-354; TRP-356 AND SER-453.
[34]"Identification of CYP21 mutations, one novel, by single strand conformational polymorphism (SSCP) analysis."
Witchel S.F., Smith R., Suda-Hartman M.
Hum. Mutat. 13:172-172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 TYR-169; LEU-281 AND GLN-356.
[35]"Steroid 21-hydroxylase deficiency: mutational spectrum in Denmark, three novel mutations, and in vitro expression analysis."
Ohlsson G., Mueller J., Skakkebaek N.E., Schwartz M.
Hum. Mutat. 13:482-486(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; GLU-64; ASN-172; ASN-236; LEU-281; SER-291; TRP-356 AND VAL-362.
[36]"A rapid screening for steroid 21-hydroxylase mutations in patients with congenital adrenal hyperplasia."
Kapelari K., Ghanaati Z., Wollmann H., Ventz M., Ranke M.B., Kofler R., Peters H.
Hum. Mutat. 13:505-505(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281 AND TRP-356.
[37]"A novel missense mutation, GLY424SER, in Brazilian patients with 21-hydroxylase deficiency."
Billerbeck A.E.C., Bachega T.A.S.S., Frazatto E.T., Nishi M.Y., Goldberg A.C., Marin M.L.C., Madureira G., Monte O., Arnhold I.J.P., Mendonca B.B.
J. Clin. Endocrinol. Metab. 84:2870-2872(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-281; TRP-356 AND SER-424.
[38]"Molecular analysis of Japanese patients with steroid 21-hydroxylase deficiency."
Asanuma A., Ohura T., Ogawa E., Sato S., Igarashi Y., Matsubara Y., Iinuma K.
J. Hum. Genet. 44:312-317(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; LEU-281; TRP-356 AND SER-493, VARIANT THR-268.
[39]"Mutation screening in British 21-hydroxylase deficiency families and development of novel microsatellite based approaches to prenatal diagnosis."
Lako M., Ramsden S., Campbell R.D., Strachan T.
J. Med. Genet. 36:119-124(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 ASN-172 AND TRP-356.
[40]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-281 AND SER-453, VARIANTS THR-268 AND SER-493.
[41]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[42]"Predicting phenotype in steroid 21-hydroxylase deficiency? Comprehensive genotyping in 155 unrelated, well defined patients from southern Germany."
Krone N., Braun A., Roscher A.A., Knorr D., Schwarz H.P.
J. Clin. Endocrinol. Metab. 85:1059-1065(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; LEU-281; GLY-281; PHE-300; CYS-354; TRP-356 AND SER-453.
[43]"Molecular analysis of CYP-21 mutations for congenital adrenal hyperplasia in Singapore."
Loke K.Y., Lee Y.S., Lee W.W.R., Poh L.K.S.
Horm. Res. 55:179-184(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; PRO-261; TRP-356 AND PRO-483.
[44]"Phenotype-genotype correlation in 56 women with nonclassical congenital adrenal hyperplasia due to 21-hydroxylase deficiency."
Deneux C., Tardy V., Dib A., Mornet E., Billaud L., Charron D., Morel Y., Kuttenn F.
J. Clin. Endocrinol. Metab. 86:207-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; LEU-281; MET-317; TRP-356; CYS-435 AND SER-453.
[45]"Mutational spectrum of the steroid 21-hydroxylase gene in Austria: identification of a novel missense mutation."
Baumgartner-Parzer S.M., Schulze E., Waldhaeusl W., Pauschenwein S., Rondot S., Nowotny P., Meyer K., Frisch H., Waldhauser F., Vierhapper H.
J. Clin. Endocrinol. Metab. 86:4771-4775(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; LEU-281; SER-291; TRP-356; SER-424; HIS-426; SER-453 AND PRO-483, CHARACTERIZATION OF VARIANT AH3 HIS-426.
[46]"Novel mutations in the human CYP21 gene."
Levo A., Partanen J.
Prenat. Diagn. 21:885-889(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 TRP-363.
[47]"Non-classical 21-hydroxylase deficiency in children: association of adrenocorticotropic hormone-stimulated 17-hydroxyprogesterone with the risk of compound heterozygosity with severe mutations."
Ezquieta B., Cueva E., Varela J., Oliver A., Fernandez J., Jariego C.
Acta Paediatr. 91:892-898(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; LEU-281; LEU-283; TRP-356 AND SER-453.
[48]"Novel mutations in CYP21 detected in individuals with hyperandrogenism."
Lajic S., Clauin S., Robins T., Vexiau P., Blanche H., Bellanne-Chantelot C., Wedell A.
J. Clin. Endocrinol. Metab. 87:2824-2829(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPERANDROGENISM MET-304; SER-375 AND SER-453, CHARACTERIZATION OF VARIANTS HYPERANDROGENISM MET-304; SER-375 AND SER-453.
[49]"Three novel mutations in CYP21 gene in Brazilian patients with the classical form of 21-hydroxylase deficiency due to a founder effect."
Billerbeck A.E.C., Mendonca B.B., Pinto E.M., Madureira G., Arnhold I.J.P., Bachega T.A.S.S.
J. Clin. Endocrinol. Metab. 87:4314-4317(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 CYS-408 AND SER-424.
[50]"Mutational spectrum of congenital adrenal hyperplasia in Slovenian patients: a novel Ala15Thr mutation and Pro30Leu within a larger gene conversion associated with a severe form of the disease."
Dolzan V., Stopar-Obreza M., Zerjav-Tansek M., Breskvar K., Krzisnik C., Battelino T.
Eur. J. Endocrinol. 149:137-144(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 THR-15; LEU-30; ASN-172; LEU-281 AND SER-453.
[51]"Follow-up of 68 children with congenital adrenal hyperplasia due to 21-hydroxylase deficiency: relevance of genotype for management."
Pinto G., Tardy V., Trivin C., Thalassinos C., Lortat-Jacob S., Nihoul-Fekete C., Morel Y., Brauner R.
J. Clin. Endocrinol. Metab. 88:2624-2633(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; LEU-62; ASN-172; LEU-281; PRO-341; TRP-356; SER-453 AND PRO-483.
[52]"CYP21 gene mutation analysis in 198 patients with 21-hydroxylase deficiency in The Netherlands: six novel mutations and a specific cluster of four mutations."
Stikkelbroeck N.M., Hoefsloot L.H., de Wijs I.J., Otten B.J., Hermus A.R., Sistermans E.A.
J. Clin. Endocrinol. Metab. 88:3852-3859(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 ASN-172; LEU-281; ARG-291; TYR-301; PRO-341; TRP-356 AND GLN-483.
[53]"Molecular genetic analysis of Tunisian patients with a classic form of 21-hydroxylase deficiency: identification of four novel mutations and high prevalence of Q318X mutation."
Kharrat M., Tardy V., M'Rad R., Maazoul F., Jemaa L.B., Refai M., Morel Y., Chaabouni H.
J. Clin. Endocrinol. Metab. 89:368-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 ASN-172; TRP-356 AND TRP-483.
[54]"Three novel mutations in Japanese patients with 21-hydroxylase deficiency."
Usui T., Nishisho K., Kaji M., Ikuno N., Yorifuji T., Yasuda T., Kuzuya H., Shimatsu A.
Horm. Res. 61:126-132(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH3 HIS-124.
[55]"Functional analysis of two recurrent amino acid substitutions in the CYP21 gene from Italian patients with congenital adrenal hyperplasia."
Barbaro M., Lajic S., Baldazzi L., Balsamo A., Pirazzoli P., Cicognani A., Wedell A., Cacciari E.
J. Clin. Endocrinol. Metab. 89:2402-2407(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 THR-15; LEU-30; LEU-281 AND SER-482, CHARACTERIZATION OF VARIANTS AH3 THR-15 AND SER-482.
[56]"Detection and assignment of CYP21 mutations using peptide mass signature genotyping."
Zeng X., Witchel S.F., Dobrowolski S.F., Moulder P.V., Jarvik J.W., Telmer C.A.
Mol. Genet. Metab. 82:38-47(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281; SER-291; GLN-356; TRP-356; TYR-365; SER-453; LEU-479 AND PRO-483, VARIANT ARG-102.
[57]"21-Hydroxylase and 11beta-hydroxylase mutations in Romanian patients with classic congenital adrenal hyperplasia."
Grigorescu Sido A., Weber M.M., Grigorescu Sido P., Clausmeyer S., Heinrich U., Schulze E.
J. Clin. Endocrinol. Metab. 90:5769-5773(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; ASN-172 AND TRP-356.
[58]"p.H62L, a rare mutation of the CYP21 gene identified in two forms of 21-hydroxylase deficiency."
Menassa R., Tardy V., Despert F., Bouvattier-Morel C., Brossier J.P., Cartigny M., Morel Y.
J. Clin. Endocrinol. Metab. 93:1901-1908(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 LEU-30; LEU-62; ASN-172; TRP-356 AND SER-453, CHARACTERIZATION OF VARIANTS AH3 LEU-62 AND SER-453.
[59]"Inhibition of CYP21A2 enzyme activity caused by novel missense mutations identified in Brazilian and Scandinavian patients."
Soardi F.C., Barbaro M., Lau I.F., Lemos-Marini S.H., Baptista M.T., Guerra-Junior G., Wedell A., Lajic S., de Mello M.P.
J. Clin. Endocrinol. Metab. 93:2416-2420(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 ARG-56; LEU-62; ARG-107; PRO-142; ASN-172; TRP-356; CYS-408 AND SER-453, CHARACTERIZATION OF VARIANTS AH3 ARG-56; LEU-62; ARG-107; PRO-142; CYS-408 AND SER-453.
[60]"Functional and structural consequences of a novel point mutation in the CYP21A2 gene causing congenital adrenal hyperplasia: potential relevance of helix C for P450 oxidoreductase-21-hydroxylase interaction."
Riepe F.G., Hiort O., Grotzinger J., Sippell W.G., Krone N., Holterhus P.M.
J. Clin. Endocrinol. Metab. 93:2891-2895(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 GLN-121 AND SER-453, CHARACTERIZATION OF VARIANT AH3 GLN-121.
[61]"Phenotype-genotype correlations of 13 rare CYP21A2 mutations detected in 46 patients affected with 21-hydroxylase deficiency and in one carrier."
Tardy V., Menassa R., Sulmont V., Lienhardt-Roussie A., Lecointre C., Brauner R., David M., Morel Y.
J. Clin. Endocrinol. Metab. 95:1288-1300(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH3 THR-77; PRO-167; ASN-172; THR-230; LYS-233; LEU-281; SER-291; ASP-292; LYS-320; PRO-341; HIS-354; TRP-356; TRP-369; CYS-408; SER-424; HIS-426 AND SER-453, CHARACTERIZATION OF VARIANTS AH3 PRO-167; ASN-172; LEU-281; ASP-292; LYS-320; TRP-369 AND SER-424.
+Additional computationally mapped references.

Web resources

Cytochrome P450 Allele Nomenclature Committee

CYP21A2 alleles

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12792 Genomic DNA. Translation: AAB59440.1.
M13936 Genomic DNA. Translation: AAA59695.1.
M26856 Genomic DNA. Translation: AAA52064.1.
X58906 Genomic DNA. Translation: CAA41709.1.
GQ222286 Genomic DNA. Translation: ACT35412.1.
GQ222296 Genomic DNA. Translation: ACT35422.1.
GQ222301 Genomic DNA. Translation: ACT35427.1.
AK054616 mRNA. Translation: BAB70774.1.
AL645922 Genomic DNA. No translation available.
AL662828 Genomic DNA. No translation available.
AL662849 Genomic DNA. No translation available.
AL844853 Genomic DNA. No translation available.
AL929593 Genomic DNA. No translation available.
BX679671 Genomic DNA. Translation: CAM26070.1.
CR753845 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03570.1.
CR936924 Genomic DNA. Translation: CAQ07659.1.
BC125182 mRNA. Translation: AAI25183.1.
K02771 Genomic DNA. Translation: AAA59706.1.
M19711 Genomic DNA. Translation: AAA83248.1.
M17252 mRNA. Translation: AAA59985.1.
IPIIPI00332799.
IPI00894349.
PIRO4HUC2. A25446.
RefSeqNP_000491.4. NM_000500.7.
NP_001122062.3. NM_001128590.3.
UniGeneHs.654479.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GEGmodel-C27-494[»]
ProteinModelPortalP08686.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364304.

PTM databases

PhosphoSiteP08686.

Polymorphism databases

DMDM117275.

Proteomic databases

PaxDbP08686.
PRIDEP08686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383321; ENSP00000372811; ENSG00000206338.
ENST00000436607; ENSP00000403721; ENSG00000235134.
ENST00000448314; ENSP00000398594; ENSG00000198457.
GeneID1589.
KEGGhsa:1589.
UCSCuc021zxa.1. human.

Organism-specific databases

CTD1589.
GeneCardsGC06P032077.
H-InvDBHIX0057724.
HIX0166983.
HGNCHGNC:2600. CYP21A2.
HPAHPA048979.
MIM201910. phenotype.
613815. gene.
neXtProtNX_P08686.
Orphanet90794. Congenital adrenal hyperplasia due to 21-hydroxylase deficiency, classic form.
95698. Nonclassic congenital adrenal hyperplasia due to 21-hydroxylase deficiency.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOVERGENHBG106944.
InParanoidP08686.
KOK00513.
OrthoDBEOG4TB4B5.

Enzyme and pathway databases

BioCycMetaCyc:HS09769-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.

Gene expression databases

ArrayExpressP08686.
CleanExHS_CYP21A2.
GenevestigatorP08686.
GermOnlineENSG00000198457. Homo sapiens.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP08686.
ChEMBLCHEMBL2759.
GenomeRNAi1589.
NextBio6532.
SOURCESearch...

Entry information

Entry nameCP21A_HUMAN
AccessionPrimary (citable) accession number: P08686
Secondary accession number(s): A2BHY6 expand/collapse secondary AC list , P04033, Q01204, Q08AG8, Q16749, Q16806, Q5ST44, Q96NU8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 1, 1988
Last modified: May 1, 2013
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents