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Q08257 (QOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Quinone oxidoreductase

EC=1.6.5.5
Alternative name(s):
NADPH:quinone reductase
Zeta-crystallin
Gene names
Name:CRYZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding. Ref.9 Ref.11

Catalytic activity

NADPH + 2 quinone = NADP+ + 2 semiquinone. Ref.9

Subunit structure

Homotetramer. Ref.9

Subcellular location

Cytoplasm Ref.11.

Tissue specificity

Only very low amounts in the lens.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08257-1)

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: Q08257-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MATGQ → MHLLS
     6-142: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q08257-3)

The sequence of this isoform differs from the canonical sequence as follows:
     211-244: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 329328Quinone oxidoreductase
PRO_0000160906

Regions

Nucleotide binding158 – 1614NADP
Nucleotide binding246 – 2494NADP
Nucleotide binding269 – 2713NADP

Sites

Binding site531NADP
Binding site1811NADP; via amide nitrogen
Binding site2001NADP
Binding site2291NADP

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue231N6-acetyllysine Ref.10
Modified residue2481Phosphoserine Ref.13
Modified residue2961N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 55MATGQ → MHLLS in isoform 2.
VSP_042927
Alternative sequence6 – 142137Missing in isoform 2.
VSP_042928
Alternative sequence211 – 24434Missing in isoform 3.
VSP_046425
Natural variant661P → S. Ref.8
Corresponds to variant rs11551729 [ dbSNP | Ensembl ].
VAR_022913
Natural variant1761I → V. Ref.4
Corresponds to variant rs3819946 [ dbSNP | Ensembl ].
VAR_022914
Natural variant1831E → K.
Corresponds to variant rs17095822 [ dbSNP | Ensembl ].
VAR_048200

Experimental info

Sequence conflict1051E → G in AK314813. Ref.3

Secondary structure

......................................................... 329
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1994. Version 1.
Checksum: 68C1828911486D4E

FASTA32935,207
        10         20         30         40         50         60 
MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS 

        70         80         90        100        110        120 
RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK 

       130        140        150        160        170        180 
LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA 

       190        200        210        220        230        240 
GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG 

       250        260        270        280        290        300 
GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG 

       310        320 
SQYPLEKVAE AHENIIHGSG ATGKMILLL 

« Hide

Isoform 2 [UniParc].

Checksum: CA6C67D141CDD8B5
Show »

FASTA19220,421
Isoform 3 [UniParc].

Checksum: 6062614A6DCB2A9E
Show »

FASTA29531,528

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver."
Gonzalez P., Rao P.V., Zigler J.S. Jr.
Biochem. Biophys. Res. Commun. 191:902-907(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Organization of the human zeta-crystallin/quinone reductase gene (CRYZ)."
Gonzalez P., Rao P.V., Zigler J.S. Jr.
Genomics 21:317-324(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. 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] (ISOFORM 3).
Tissue: Thalamus.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-176.
Tissue: Brain, Kidney proximal tubule and Lung.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal kidney.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1), VARIANT SER-66.
Tissue: Testis.
[9]"Human and yeast zeta-crystallins bind AU-rich elements in RNA."
Fernandez M.R., Porte S., Crosas E., Barbera N., Farres J., Biosca J.A., Pares X.
Cell. Mol. Life Sci. 64:1419-1427(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2 overexpression in T-cell acute lymphocytic leukemia."
Lapucci A., Lulli M., Amedei A., Papucci L., Witort E., Di Gesualdo F., Bertolini F., Brewer G., Nicolin A., Bevilacqua A., Schiavone N., Morello D., Donnini M., Capaccioli S.
FASEB J. 24:1852-1865(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Crystal structure of human zeta-crystallin at 1.85 A."
Structural genomics consortium (SGC)
Submitted (MAR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH NADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13278 mRNA. Translation: AAA36536.1.
L31526 expand/collapse EMBL AC list , L31521, L31522, L31523, L31524, L31525 Genomic DNA. Translation: AAK40311.1.
AB209714 mRNA. Translation: BAD92951.1.
AK223150 mRNA. Translation: BAD96870.1.
AK223201 mRNA. Translation: BAD96921.1.
BX647883 mRNA. Translation: CAI46072.1.
AK314813 mRNA. No translation available.
AC091611 Genomic DNA. No translation available.
AC135803 Genomic DNA. No translation available.
CH471059 Genomic DNA. Translation: EAX06409.1.
CH471059 Genomic DNA. Translation: EAX06410.1.
CH471059 Genomic DNA. Translation: EAX06411.1.
CH471059 Genomic DNA. Translation: EAX06412.1.
BC039578 mRNA. Translation: AAH39578.1.
BC070058 mRNA. Translation: AAH70058.1.
CCDSCCDS44162.1. [Q08257-3]
CCDS44163.1. [Q08257-2]
CCDS665.1. [Q08257-1]
PIRPN0448.
RefSeqNP_001123514.1. NM_001130042.1. [Q08257-1]
NP_001123515.1. NM_001130043.1. [Q08257-3]
NP_001128231.1. NM_001134759.1. [Q08257-2]
NP_001880.2. NM_001889.3. [Q08257-1]
XP_005270548.1. XM_005270491.2. [Q08257-2]
UniGeneHs.83114.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YB5X-ray1.85A/B1-329[»]
ProteinModelPortalQ08257.
SMRQ08257. Positions 6-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107816. 10 interactions.
IntActQ08257. 1 interaction.
MINTMINT-5002754.
STRING9606.ENSP00000339399.

Chemistry

ChEMBLCHEMBL6118.
DrugBankDB00266. Dicumarol.

PTM databases

PhosphoSiteQ08257.

Polymorphism databases

DMDM585013.

2D gel databases

REPRODUCTION-2DPAGEIPI00000792.

Proteomic databases

MaxQBQ08257.
PaxDbQ08257.
PRIDEQ08257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340866; ENSP00000339399; ENSG00000116791. [Q08257-1]
ENST00000370871; ENSP00000359908; ENSG00000116791. [Q08257-3]
ENST00000370872; ENSP00000359909; ENSG00000116791. [Q08257-2]
ENST00000417775; ENSP00000399805; ENSG00000116791. [Q08257-1]
GeneID1429.
KEGGhsa:1429.
UCSCuc001dgj.3. human. [Q08257-1]
uc001dgm.3. human. [Q08257-2]

Organism-specific databases

CTD1429.
GeneCardsGC01M075171.
HGNCHGNC:2419. CRYZ.
HPAHPA021921.
HPA023290.
MIM123691. gene.
neXtProtNX_Q08257.
PharmGKBPA26925.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0604.
HOGENOMHOG000294672.
HOVERGENHBG002466.
InParanoidQ08257.
KOK00344.
OMAPSANINW.
OrthoDBEOG7BGHM8.
PhylomeDBQ08257.
TreeFamTF314255.

Gene expression databases

ArrayExpressQ08257.
BgeeQ08257.
CleanExHS_CRYZ.
GenevestigatorQ08257.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
PROSITEPS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ08257.
GeneWikiCRYZ.
GenomeRNAi1429.
NextBio5829.
PROQ08257.
SOURCESearch...

Entry information

Entry nameQOR_HUMAN
AccessionPrimary (citable) accession number: Q08257
Secondary accession number(s): A6NN60 expand/collapse secondary AC list , D3DQ76, Q53FT0, Q59EU7, Q5HYE7, Q6NSK9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 136 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM