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Protein

NADPH:adrenodoxin oxidoreductase, mitochondrial

Gene

FDXR

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

Functioni

Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.

Catalytic activityi

2 reduced adrenodoxin + NADP+ = 2 oxidized adrenodoxin + NADPH.

Cofactori

Pathway: cholesterol metabolism

This protein is involved in the pathway cholesterol metabolism, which is part of Steroid metabolism.
View all proteins of this organism that are known to be involved in the pathway cholesterol metabolism and in Steroid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491FAD; via amide nitrogenBy similarity
Binding sitei69 – 691FADBy similarity
Binding sitei77 – 771FAD; via amide nitrogenBy similarity
Binding sitei113 – 1131FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei240 – 2401NADPBy similarity
Binding sitei398 – 3981FAD; via amide nitrogenBy similarity
Binding sitei405 – 4051NADP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1874NADPBy similarity
Nucleotide bindingi228 – 2292NADPBy similarity
Nucleotide bindingi405 – 4073FADBy similarity

GO - Molecular functioni

  • ferredoxin-NADP+ reductase activity Source: ProtInc
  • NADPH-adrenodoxin reductase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cholesterol metabolism, Electron transport, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS08587-MONOMER.
ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
REACT_150128. Electron transport from NADPH to Ferredoxin.
REACT_268767. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).
UniPathwayiUPA00296.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH:adrenodoxin oxidoreductase, mitochondrial (EC:1.18.1.6)
Short name:
AR
Short name:
Adrenodoxin reductase
Alternative name(s):
Ferredoxin--NADP(+) reductase
Short name:
Ferredoxin reductase
Gene namesi
Name:FDXR
Synonyms:ADXR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3642. FDXR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28086.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Polymorphism and mutation databases

BioMutaiFDXR.
DMDMi85681283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionAdd
BLAST
Chaini33 – 491459NADPH:adrenodoxin oxidoreductase, mitochondrialPRO_0000019420Add
BLAST

Proteomic databases

MaxQBiP22570.
PaxDbiP22570.
PeptideAtlasiP22570.
PRIDEiP22570.

2D gel databases

REPRODUCTION-2DPAGEIPI00026958.

PTM databases

PhosphoSiteiP22570.

Expressioni

Gene expression databases

BgeeiP22570.
CleanExiHS_FDXR.
ExpressionAtlasiP22570. baseline and differential.
GenevisibleiP22570. HS.

Organism-specific databases

HPAiHPA044393.
HPA053673.

Interactioni

Subunit structurei

Monomer. Interacts directly with FDX1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FHITP497894EBI-1751533,EBI-741760

Protein-protein interaction databases

BioGridi108523. 9 interactions.
IntActiP22570. 2 interactions.
STRINGi9606.ENSP00000462972.

Structurei

3D structure databases

ProteinModelPortaliP22570.
SMRiP22570. Positions 38-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0493.
GeneTreeiENSGT00390000013574.
HOGENOMiHOG000249250.
HOVERGENiHBG002132.
InParanoidiP22570.
KOiK18914.
OMAiFTTKEFR.
PhylomeDBiP22570.
TreeFamiTF314193.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR021163. Ferredox_Rdtase_adrenod.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000362. FNR. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Short (identifier: P22570-1) [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
MASRCWRWWG WSAWPRTRLP PAGSTPSFCH HFSTQEKTPQ ICVVGSGPAG
60 70 80 90 100
FYTAQHLLKH PQAHVDIYEK QPVPFGLVRF GVAPDHPEVK NVINTFTQTA
110 120 130 140 150
HSGRCAFWGN VEVGRDVTVP ELREAYHAVV LSYGAEDHRA LEIPGEELPG
160 170 180 190 200
VCSARAFVGW YNGLPENQEL EPDLSCDTAV ILGQGNVALD VARILLTPPE
210 220 230 240 250
HLERTDITKA ALGVLRQSRV KTVWLVGRRG PLQVAFTIKE LREMIQLPGA
260 270 280 290 300
RPILDPVDFL GLQDKIKEVP RPRKRLTELL LRTATEKPGP AEAARQASAS
310 320 330 340 350
RAWGLRFFRS PQQVLPSPDG RRAAGVRLAV TRLEGVDEAT RAVPTGDMED
360 370 380 390 400
LPCGLVLSSI GYKSRPVDPS VPFDSKLGVI PNVEGRVMDV PGLYCSGWVK
410 420 430 440 450
RGPTGVIATT MTDSFLTGQM LLQDLKAGLL PSGPRPGYAA IQALLSSRGV
460 470 480 490
RPVSFSDWEK LDAEEVARGQ GTGKPREKLV DPQEMLRLLG H
Length:491
Mass (Da):53,837
Last modified:January 24, 2006 - v3
Checksum:i15D07E714F592C9D
GO
Isoform Long (identifier: P22570-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     203-203: E → EALLLCQ

Note: Represents 10-20% of all adrenodoxin reductase mRNAs and seems to be inactive.
Show »
Length:497
Mass (Da):54,479
Checksum:i08C3D3F2C86564DA
GO
Isoform 3 (identifier: P22570-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-59: K → KRVEALCSQPRVLNSPALSGEGEDLGASQPLSLDPTSCHPVPQQ

Show »
Length:534
Mass (Da):58,304
Checksum:i755B0612AAD29612
GO
Isoform 4 (identifier: P22570-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLK → MEDKDRE

Show »
Length:439
Mass (Da):48,056
Checksum:i20D88F1A91909900
GO
Isoform 5 (identifier: P22570-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     91-98: Missing.

Show »
Length:483
Mass (Da):52,919
Checksum:i8AD11CAC35C3E4C1
GO
Isoform 6 (identifier: P22570-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-59: K → KQ
     91-131: Missing.

Note: No experimental confirmation available.
Show »
Length:451
Mass (Da):49,425
Checksum:i367CE00CA673D9E2
GO
Isoform 7 (identifier: P22570-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-34: SFCHHFST → TFGGSDEVRDPANAKALRNKRRRMQVRVKLGKFQLLLDI

Note: No experimental confirmation available.
Show »
Length:522
Mass (Da):57,370
Checksum:i1D82107E5C08C814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231V → G in BAG56748 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71R → L.1 Publication
Corresponds to variant rs28365947 [ dbSNP | Ensembl ].
VAR_025192
Natural varianti123 – 1231R → Q.3 Publications
Corresponds to variant rs690514 [ dbSNP | Ensembl ].
VAR_004624
Natural varianti213 – 2131G → V.1 Publication
Corresponds to variant rs35692345 [ dbSNP | Ensembl ].
VAR_025193
Natural varianti248 – 2481P → L.1 Publication
Corresponds to variant rs35072974 [ dbSNP | Ensembl ].
VAR_025194
Natural varianti251 – 2511R → W.1 Publication
Corresponds to variant rs34038065 [ dbSNP | Ensembl ].
VAR_025195
Natural varianti301 – 3011R → C.1 Publication
Corresponds to variant rs34118765 [ dbSNP | Ensembl ].
VAR_025196
Natural varianti345 – 3451T → M.1 Publication
Corresponds to variant rs35660143 [ dbSNP | Ensembl ].
VAR_025197
Natural varianti352 – 3521P → S.1 Publication
Corresponds to variant rs35696549 [ dbSNP | Ensembl ].
VAR_025198
Natural varianti472 – 4721T → A.1 Publication
Corresponds to variant rs35769464 [ dbSNP | Ensembl ].
VAR_025199

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5959MASRC…QHLLK → MEDKDRE in isoform 4. 1 PublicationVSP_046669Add
BLAST
Alternative sequencei27 – 348SFCHHFST → TFGGSDEVRDPANAKALRNK RRRMQVRVKLGKFQLLLDI in isoform 7. 1 PublicationVSP_046670
Alternative sequencei59 – 591K → KRVEALCSQPRVLNSPALSG EGEDLGASQPLSLDPTSCHP VPQQ in isoform 3. 1 PublicationVSP_045135
Alternative sequencei59 – 591K → KQ in isoform 6. 1 PublicationVSP_046671
Alternative sequencei91 – 13141Missing in isoform 6. 1 PublicationVSP_046672Add
BLAST
Alternative sequencei91 – 988Missing in isoform 5. 1 PublicationVSP_046673
Alternative sequencei203 – 2031E → EALLLCQ in isoform Long. 1 PublicationVSP_003416

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03826 mRNA. Translation: AAB59498.1.
J03826 mRNA. Translation: AAB59497.1.
M58509, M58508 Genomic DNA. Translation: AAA51668.1.
M58509, M58508 Genomic DNA. Translation: AAA51669.1.
DQ085780 Genomic DNA. Translation: AAY68215.1.
AK293208 mRNA. Translation: BAG56748.1.
AK295307 mRNA. Translation: BAG58287.1.
AK298908 mRNA. Translation: BAG61016.1.
AK301779 mRNA. Translation: BAG63236.1.
AK301977 mRNA. Translation: BAH13598.1.
AC068874 Genomic DNA. No translation available.
BC002960 mRNA. Translation: AAH02960.1.
CCDSiCCDS11707.1. [P22570-2]
CCDS58591.1. [P22570-4]
CCDS58592.1. [P22570-5]
CCDS58593.1. [P22570-1]
CCDS58594.1. [P22570-6]
CCDS58595.1. [P22570-3]
CCDS58596.1. [P22570-7]
PIRiA40487.
RefSeqiNP_001244941.2. NM_001258012.3.
NP_001244942.2. NM_001258013.3.
NP_001244943.2. NM_001258014.3.
NP_001244944.1. NM_001258015.2. [P22570-6]
NP_001244945.2. NM_001258016.3.
NP_004101.3. NM_004110.5.
NP_077728.3. NM_024417.4.
UniGeneiHs.69745.

Genome annotation databases

EnsembliENST00000420580; ENSP00000414172; ENSG00000161513. [P22570-6]
GeneIDi2232.
KEGGihsa:2232.
UCSCiuc002jlx.3. human. [P22570-2]
uc002jly.3. human. [P22570-1]
uc002jlz.3. human.
uc010wri.2. human.
uc010wrk.2. human.
uc010wrl.2. human.
uc010wrm.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03826 mRNA. Translation: AAB59498.1.
J03826 mRNA. Translation: AAB59497.1.
M58509, M58508 Genomic DNA. Translation: AAA51668.1.
M58509, M58508 Genomic DNA. Translation: AAA51669.1.
DQ085780 Genomic DNA. Translation: AAY68215.1.
AK293208 mRNA. Translation: BAG56748.1.
AK295307 mRNA. Translation: BAG58287.1.
AK298908 mRNA. Translation: BAG61016.1.
AK301779 mRNA. Translation: BAG63236.1.
AK301977 mRNA. Translation: BAH13598.1.
AC068874 Genomic DNA. No translation available.
BC002960 mRNA. Translation: AAH02960.1.
CCDSiCCDS11707.1. [P22570-2]
CCDS58591.1. [P22570-4]
CCDS58592.1. [P22570-5]
CCDS58593.1. [P22570-1]
CCDS58594.1. [P22570-6]
CCDS58595.1. [P22570-3]
CCDS58596.1. [P22570-7]
PIRiA40487.
RefSeqiNP_001244941.2. NM_001258012.3.
NP_001244942.2. NM_001258013.3.
NP_001244943.2. NM_001258014.3.
NP_001244944.1. NM_001258015.2. [P22570-6]
NP_001244945.2. NM_001258016.3.
NP_004101.3. NM_004110.5.
NP_077728.3. NM_024417.4.
UniGeneiHs.69745.

3D structure databases

ProteinModelPortaliP22570.
SMRiP22570. Positions 38-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108523. 9 interactions.
IntActiP22570. 2 interactions.
STRINGi9606.ENSP00000462972.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSiteiP22570.

Polymorphism and mutation databases

BioMutaiFDXR.
DMDMi85681283.

2D gel databases

REPRODUCTION-2DPAGEIPI00026958.

Proteomic databases

MaxQBiP22570.
PaxDbiP22570.
PeptideAtlasiP22570.
PRIDEiP22570.

Protocols and materials databases

DNASUi2232.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000420580; ENSP00000414172; ENSG00000161513. [P22570-6]
GeneIDi2232.
KEGGihsa:2232.
UCSCiuc002jlx.3. human. [P22570-2]
uc002jly.3. human. [P22570-1]
uc002jlz.3. human.
uc010wri.2. human.
uc010wrk.2. human.
uc010wrl.2. human.
uc010wrm.2. human.

Organism-specific databases

CTDi2232.
GeneCardsiGC17M072858.
HGNCiHGNC:3642. FDXR.
HPAiHPA044393.
HPA053673.
MIMi103270. gene.
neXtProtiNX_P22570.
PharmGKBiPA28086.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0493.
GeneTreeiENSGT00390000013574.
HOGENOMiHOG000249250.
HOVERGENiHBG002132.
InParanoidiP22570.
KOiK18914.
OMAiFTTKEFR.
PhylomeDBiP22570.
TreeFamiTF314193.

Enzyme and pathway databases

UniPathwayiUPA00296.
BioCyciMetaCyc:HS08587-MONOMER.
ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
REACT_150128. Electron transport from NADPH to Ferredoxin.
REACT_268767. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).

Miscellaneous databases

GeneWikiiAdrenodoxin_reductase.
GenomeRNAii2232.
NextBioi9037.
PROiP22570.
SOURCEiSearch...

Gene expression databases

BgeeiP22570.
CleanExiHS_FDXR.
ExpressionAtlasiP22570. baseline and differential.
GenevisibleiP22570. HS.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR021163. Ferredox_Rdtase_adrenod.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000362. FNR. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human adrenodoxin reductase: two mRNAs encoded by a single gene on chromosome 17cen-->q25 are expressed in steroidogenic tissues."
    Solish S.B., Picado-Leonard J., Morel Y., Kuhn R.W., Mohandas T.K., Hanukoglu I., Miller W.L.
    Proc. Natl. Acad. Sci. U.S.A. 85:7104-7108(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), VARIANT GLN-123.
  2. "Cloning and sequence of the human adrenodoxin reductase gene."
    Lin D., Shi Y., Miller W.L.
    Proc. Natl. Acad. Sci. U.S.A. 87:8516-8520(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. NIEHS SNPs program
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-7; GLN-123; VAL-213; LEU-248; TRP-251; CYS-301; MET-345; SER-352 AND ALA-472.
  4. "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 3; 4; 5; 6 AND 7), VARIANT GLN-123.
    Tissue: Adrenal gland, Caudate nucleus and Testis.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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 SHORT).
    Tissue: Lung.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiADRO_HUMAN
AccessioniPrimary (citable) accession number: P22570
Secondary accession number(s): B4DDI7
, B4DHX5, B4DQQ4, B4DX24, B7Z7G2, E7EQC1, Q13716, Q4PJI0, Q9BU12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 24, 2006
Last modified: June 24, 2015
This is version 158 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

Dasty 3

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 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.