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P17516

- AK1C4_HUMAN

UniProt

P17516 - AK1C4_HUMAN

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Protein

Aldo-keto reductase family 1 member C4

Gene

AKR1C4

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

Functioni

Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route.

Catalytic activityi

Chlordecone alcohol + NADP+ = chlordecone + NADPH.
A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501NADP1 Publication
Sitei54 – 541Important for substrate specificityBy similarity
Active sitei55 – 551Proton donorBy similarity
Sitei84 – 841Lowers pKa of active site TyrBy similarity
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei190 – 1901NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 245NADP1 Publication
Nucleotide bindingi166 – 1672NADP1 Publication
Nucleotide bindingi216 – 2216NADP1 Publication
Nucleotide bindingi270 – 28011NADP1 PublicationAdd
BLAST

GO - Molecular functioni

  1. aldo-keto reductase (NADP) activity Source: ProtInc
  2. androsterone dehydrogenase activity Source: UniProtKB
  3. bile acid transmembrane transporter activity Source: ProtInc
  4. chlordecone reductase activity Source: UniProtKB-EC
  5. electron carrier activity Source: UniProtKB
  6. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
  7. retinal dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. androgen metabolic process Source: ProtInc
  2. bile acid and bile salt transport Source: ProtInc
  3. bile acid biosynthetic process Source: Reactome
  4. bile acid metabolic process Source: Reactome
  5. cellular response to jasmonic acid stimulus Source: UniProtKB
  6. daunorubicin metabolic process Source: UniProtKB
  7. doxorubicin metabolic process Source: UniProtKB
  8. phototransduction, visible light Source: Reactome
  9. retinoid metabolic process Source: Reactome
  10. small molecule metabolic process Source: Reactome
  11. steroid metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_24968. Retinoid metabolism and transport.
SABIO-RKP17516.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldo-keto reductase family 1 member C4 (EC:1.1.1.-)
Alternative name(s):
3-alpha-HSD1
3-alpha-hydroxysteroid dehydrogenase type I (EC:1.1.1.357)
Chlordecone reductase (EC:1.1.1.225)
Short name:
CDR
Dihydrodiol dehydrogenase 4
Short name:
DD-4
Short name:
DD4
HAKRA
Gene namesi
Name:AKR1C4
Synonyms:CHDR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:387. AKR1C4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.1 Publication
Note: The gene represented in this entry may act as a disease modifier. A splicing mutation resulting in loss of AKR1C4 exon 2 has been found in affected individuals carrying a causative mutation in AKR1C2 (PubMed:21802064). These patients manifest a more severe disease phenotype than individuals only carrying mutations in AKR1C2.1 Publication

Organism-specific databases

MIMi614279. phenotype.
Orphaneti90796. 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
PharmGKBiPA24680.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Aldo-keto reductase family 1 member C4PRO_0000124640Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiP17516.
PaxDbiP17516.
PRIDEiP17516.

PTM databases

PhosphoSiteiP17516.

Expressioni

Tissue specificityi

Liver specific.2 Publications

Gene expression databases

BgeeiP17516.
CleanExiHS_AKR1C4.
ExpressionAtlasiP17516. baseline and differential.
GenevestigatoriP17516.

Organism-specific databases

HPAiHPA044720.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi107534. 5 interactions.
STRINGi9606.ENSP00000263126.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53
Beta strandi7 – 93
Beta strandi15 – 228
Helixi33 – 4412
Beta strandi48 – 503
Helixi53 – 553
Helixi58 – 7114
Helixi76 – 783
Beta strandi80 – 856
Helixi87 – 893
Helixi92 – 10615
Beta strandi111 – 1177
Beta strandi124 – 1263
Helixi144 – 15613
Beta strandi159 – 1679
Helixi170 – 1778
Beta strandi187 – 1926
Helixi200 – 2089
Beta strandi212 – 2176
Turni225 – 2273
Helixi235 – 2373
Helixi239 – 2479
Helixi252 – 26211
Beta strandi266 – 2705
Helixi274 – 2807
Helixi281 – 2855
Helixi290 – 2978
Helixi309 – 3113
Beta strandi318 – 3214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FVLX-ray2.40A/B/C1-323[»]
ProteinModelPortaliP17516.
SMRiP17516. Positions 1-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17516.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP17516.
KOiK00037.
K00089.
K00092.
K00212.
OMAiLLHFPMA.
OrthoDBiEOG70KGQF.
PhylomeDBiP17516.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17516-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID
60 70 80 90 100
SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE
110 120 130 140 150
SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV
160 170 180 190 200
MEKCKDAGLA KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS
210 220 230 240 250
KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKQ
260 270 280 290 300
TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN
310 320
RNYRYVVMDF LMDHPDYPFS DEY
Length:323
Mass (Da):37,067
Last modified:October 5, 2010 - v3
Checksum:iE728CE4B420E8C58
GO

Sequence cautioni

The sequence AAA35658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Polymorphismi

The allele with Cys-145/Val-311 shows a three- to five-fold decrease in catalytic efficiency for xenobiotic and steroidal substrates compared to the Ser-145/Leu-311 allele.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351G → E.
Corresponds to variant rs11253043 [ dbSNP | Ensembl ].
VAR_028240
Natural varianti145 – 1451S → C.1 Publication
Corresponds to variant rs3829125 [ dbSNP | Ensembl ].
VAR_013290
Natural varianti170 – 1701C → Y.1 Publication
Corresponds to variant rs17851824 [ dbSNP | Ensembl ].
VAR_028241
Natural varianti250 – 2501Q → R.9 Publications
Corresponds to variant rs4880718 [ dbSNP | Ensembl ].
VAR_028242
Natural varianti311 – 3111L → V.1 Publication
Corresponds to variant rs17134592 [ dbSNP | Ensembl ].
VAR_013291

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S68287 mRNA. Translation: AAD14010.1.
AB045829 mRNA. Translation: BAA99542.1.
AB031085 mRNA. Translation: BAA92885.1.
AB032163 Genomic DNA. Translation: BAA92893.1.
AL355303 Genomic DNA. No translation available.
BC020744 mRNA. Translation: AAH20744.1.
M33375 mRNA. Translation: AAA35658.1. Different initiation.
D26125 mRNA. Translation: BAA05122.1.
CCDSiCCDS7064.1.
PIRiA57407.
S59620.
RefSeqiNP_001809.3. NM_001818.3.
UniGeneiHs.567245.

Genome annotation databases

EnsembliENST00000263126; ENSP00000263126; ENSG00000198610.
ENST00000380448; ENSP00000369814; ENSG00000198610.
GeneIDi1109.
KEGGihsa:1109.
UCSCiuc001ihw.2. human.

Polymorphism databases

DMDMi308153631.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S68287 mRNA. Translation: AAD14010.1 .
AB045829 mRNA. Translation: BAA99542.1 .
AB031085 mRNA. Translation: BAA92885.1 .
AB032163 Genomic DNA. Translation: BAA92893.1 .
AL355303 Genomic DNA. No translation available.
BC020744 mRNA. Translation: AAH20744.1 .
M33375 mRNA. Translation: AAA35658.1 . Different initiation.
D26125 mRNA. Translation: BAA05122.1 .
CCDSi CCDS7064.1.
PIRi A57407.
S59620.
RefSeqi NP_001809.3. NM_001818.3.
UniGenei Hs.567245.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FVL X-ray 2.40 A/B/C 1-323 [» ]
ProteinModelPortali P17516.
SMRi P17516. Positions 1-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107534. 5 interactions.
STRINGi 9606.ENSP00000263126.

Chemistry

BindingDBi P17516.
ChEMBLi CHEMBL4999.

PTM databases

PhosphoSitei P17516.

Polymorphism databases

DMDMi 308153631.

Proteomic databases

MaxQBi P17516.
PaxDbi P17516.
PRIDEi P17516.

Protocols and materials databases

DNASUi 1109.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263126 ; ENSP00000263126 ; ENSG00000198610 .
ENST00000380448 ; ENSP00000369814 ; ENSG00000198610 .
GeneIDi 1109.
KEGGi hsa:1109.
UCSCi uc001ihw.2. human.

Organism-specific databases

CTDi 1109.
GeneCardsi GC10P005228.
HGNCi HGNC:387. AKR1C4.
HPAi HPA044720.
MIMi 600451. gene.
614279. phenotype.
neXtProti NX_P17516.
Orphaneti 90796. 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
PharmGKBi PA24680.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
GeneTreei ENSGT00760000119041.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi P17516.
KOi K00037.
K00089.
K00092.
K00212.
OMAi LLHFPMA.
OrthoDBi EOG70KGQF.
PhylomeDBi P17516.
TreeFami TF106492.

Enzyme and pathway databases

Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_24968. Retinoid metabolism and transport.
SABIO-RK P17516.

Miscellaneous databases

EvolutionaryTracei P17516.
GeneWikii 3-alpha-HSD.
GenomeRNAii 1109.
NextBioi 4602.
PROi P17516.
SOURCEi Search...

Gene expression databases

Bgeei P17516.
CleanExi HS_AKR1C4.
ExpressionAtlasi P17516. baseline and differential.
Genevestigatori P17516.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase."
    Qin K.-N., New M.I., Cheng K.-C.
    J. Steroid Biochem. Mol. Biol. 46:673-679(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-250.
    Tissue: Liver.
  2. "Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases."
    Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.
    J. Biol. Chem. 270:20162-20168(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, VARIANT ARG-250.
  3. "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans."
    Khanna M., Qin K.-N., Cheng K.-C.
    J. Steroid Biochem. Mol. Biol. 53:41-46(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-250.
  4. "Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver."
    Kume T., Iwasa H., Shiraishi H., Yokoi T., Nagashima K., Otsuka M., Terada T., Takagi T., Hara A., Kamataki T.
    Pharmacogenetics 9:763-771(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CYS-145; ARG-250 AND VAL-311.
    Tissue: Liver.
  5. "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes."
    Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S.
    Genes Cells 5:111-125(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ARG-250.
    Tissue: Liver.
  6. "Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution."
    Dufort I., Labrie F., Luu-The V.
    J. Clin. Endocrinol. Metab. 86:841-846(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION OF 3-ALPHA-HSD ACTIVITY, TISSUE SPECIFICITY, VARIANT ARG-250.
    Tissue: Liver.
  7. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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], VARIANTS TYR-170 AND ARG-250.
    Tissue: Liver.
  9. "Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase."
    Winters C.J., Molowa D.T., Guzelian P.S.
    Biochemistry 29:1080-1087(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-323, VARIANT ARG-250.
    Tissue: Liver.
  10. "Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder."
    Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y., Sato K., Hara A.
    Biochem. J. 299:545-552(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-323, PROTEIN SEQUENCE OF 5-29; 76-131; 184-201 AND 271-294, VARIANT ARG-250.
    Tissue: Liver.
  11. "Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase."
    Binstock J.M., Iyer R.B., Hamby C.V., Fried V.A., Schwartz I.S., Weinstein B.I., Southren A.L.
    Biochem. Biophys. Res. Commun. 187:760-766(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-54; 105-121; 162-175; 184-196; 277-291 AND 307-321, CHARACTERIZATION AS 3-ALPHA-HSD.
  12. "Why boys will be boys: two pathways of fetal testicular androgen biosynthesis are needed for male sexual differentiation."
    Fluck C.E., Meyer-Boni M., Pandey A.V., Kempna P., Miller W.L., Schoenle E.J., Biason-Lauber A.
    Am. J. Hum. Genet. 89:201-218(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SRXY8.
  13. "Crystal structure of human 3-alpha hydroxysteroid/dihydrodiol dehydrogenase (AKR1C4) complexed with NADP+."
    Structural genomics consortium (SGC)
    Submitted (FEB-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.

Entry informationi

Entry nameiAK1C4_HUMAN
AccessioniPrimary (citable) accession number: P17516
Secondary accession number(s): Q5T6A3, Q8WW84, Q9NS54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 165 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3