Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q08257

- QOR_HUMAN

UniProt

Q08257 - QOR_HUMAN

Protein

Quinone oxidoreductase

Gene

CRYZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.2 Publications

    Catalytic activityi

    NADPH + 2 quinone = NADP+ + 2 semiquinone.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531NADP1 Publication
    Binding sitei181 – 1811NADP; via amide nitrogen1 Publication
    Binding sitei200 – 2001NADP1 Publication
    Binding sitei229 – 2291NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 1614NADP1 Publication
    Nucleotide bindingi246 – 2494NADP1 Publication
    Nucleotide bindingi269 – 2713NADP1 Publication

    GO - Molecular functioni

    1. mRNA 3'-UTR binding Source: UniProtKB
    2. NADPH:quinone reductase activity Source: UniProtKB
    3. NADPH binding Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein homotetramerization Source: UniProtKB
    2. visual perception Source: ProtInc
    3. xenobiotic catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinone oxidoreductase (EC:1.6.5.5)
    Alternative name(s):
    NADPH:quinone reductase
    Zeta-crystallin
    Gene namesi
    Name:CRYZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2419. CRYZ.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: HPA
    5. intracellular membrane-bounded organelle Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26925.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 329328Quinone oxidoreductasePRO_0000160906Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei23 – 231N6-acetyllysine1 Publication
    Modified residuei248 – 2481Phosphoserine1 Publication
    Modified residuei296 – 2961N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ08257.
    PaxDbiQ08257.
    PRIDEiQ08257.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00000792.

    PTM databases

    PhosphoSiteiQ08257.

    Expressioni

    Tissue specificityi

    Only very low amounts in the lens.

    Gene expression databases

    ArrayExpressiQ08257.
    BgeeiQ08257.
    CleanExiHS_CRYZ.
    GenevestigatoriQ08257.

    Organism-specific databases

    HPAiHPA021921.
    HPA023290.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi107816. 10 interactions.
    IntActiQ08257. 1 interaction.
    MINTiMINT-5002754.
    STRINGi9606.ENSP00000339399.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 159
    Helixi19 – 213
    Beta strandi22 – 298
    Beta strandi37 – 4610
    Helixi49 – 557
    Beta strandi65 – 673
    Beta strandi73 – 808
    Beta strandi92 – 965
    Beta strandi102 – 1109
    Helixi111 – 1133
    Beta strandi114 – 1163
    Helixi123 – 1264
    Turni127 – 1293
    Helixi130 – 14112
    Beta strandi151 – 1566
    Helixi160 – 17112
    Beta strandi175 – 1828
    Helixi183 – 1919
    Beta strandi195 – 1995
    Helixi205 – 2139
    Beta strandi218 – 2247
    Helixi226 – 23611
    Beta strandi237 – 2459
    Beta strandi252 – 2543
    Helixi257 – 2604
    Turni261 – 2633
    Beta strandi265 – 2684
    Helixi271 – 2733
    Helixi276 – 29217
    Beta strandi299 – 3046
    Helixi305 – 3073
    Helixi308 – 31710
    Beta strandi322 – 3287

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YB5X-ray1.85A/B1-329[»]
    ProteinModelPortaliQ08257.
    SMRiQ08257. Positions 6-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08257.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0604.
    HOGENOMiHOG000294672.
    HOVERGENiHBG002466.
    InParanoidiQ08257.
    KOiK00344.
    OMAiPSANINW.
    OrthoDBiEOG7BGHM8.
    PhylomeDBiQ08257.
    TreeFamiTF314255.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. 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]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    PROSITEiPS01162. QOR_ZETA_CRYSTAL. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08257-1) [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

    MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV    50
    ETYIRSGTYS RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS 100
    GGYAEYALAA DHTVYKLPEK LDFKQGAAIG IPYFTAYRAL IHSACVKAGE 150
    SVLVHGASGG VGLAACQIAR AYGLKILGTA GTEEGQKIVL QNGAHEVFNH 200
    REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG GRVIVVGSRG 250
    TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG 300
    SQYPLEKVAE AHENIIHGSG ATGKMILLL 329
    Length:329
    Mass (Da):35,207
    Last modified:October 1, 1994 - v1
    Checksum:i68C1828911486D4E
    GO
    Isoform 2 (identifier: Q08257-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MATGQ → MHLLS
         6-142: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:192
    Mass (Da):20,421
    Checksum:iCA6C67D141CDD8B5
    GO
    Isoform 3 (identifier: Q08257-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         211-244: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:295
    Mass (Da):31,528
    Checksum:i6062614A6DCB2A9E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051E → G in AK314813. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661P → S.1 Publication
    Corresponds to variant rs11551729 [ dbSNP | Ensembl ].
    VAR_022913
    Natural varianti176 – 1761I → V.1 Publication
    Corresponds to variant rs3819946 [ dbSNP | Ensembl ].
    VAR_022914
    Natural varianti183 – 1831E → K.
    Corresponds to variant rs17095822 [ dbSNP | Ensembl ].
    VAR_048200

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 55MATGQ → MHLLS in isoform 2. 1 PublicationVSP_042927
    Alternative sequencei6 – 142137Missing in isoform 2. 1 PublicationVSP_042928Add
    BLAST
    Alternative sequencei211 – 24434Missing in isoform 3. 1 PublicationVSP_046425Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13278 mRNA. Translation: AAA36536.1.
    L31526
    , 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.
    CCDSiCCDS44162.1. [Q08257-3]
    CCDS44163.1. [Q08257-2]
    CCDS665.1. [Q08257-1]
    PIRiPN0448.
    RefSeqiNP_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]
    UniGeneiHs.83114.

    Genome annotation databases

    EnsembliENST00000340866; ENSP00000339399; ENSG00000116791. [Q08257-1]
    ENST00000370871; ENSP00000359908; ENSG00000116791. [Q08257-3]
    ENST00000370872; ENSP00000359909; ENSG00000116791. [Q08257-2]
    ENST00000417775; ENSP00000399805; ENSG00000116791. [Q08257-1]
    GeneIDi1429.
    KEGGihsa:1429.
    UCSCiuc001dgj.3. human. [Q08257-1]
    uc001dgm.3. human. [Q08257-2]

    Polymorphism databases

    DMDMi585013.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13278 mRNA. Translation: AAA36536.1 .
    L31526
    , 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 .
    CCDSi CCDS44162.1. [Q08257-3 ]
    CCDS44163.1. [Q08257-2 ]
    CCDS665.1. [Q08257-1 ]
    PIRi PN0448.
    RefSeqi NP_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 ]
    UniGenei Hs.83114.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YB5 X-ray 1.85 A/B 1-329 [» ]
    ProteinModelPortali Q08257.
    SMRi Q08257. Positions 6-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107816. 10 interactions.
    IntActi Q08257. 1 interaction.
    MINTi MINT-5002754.
    STRINGi 9606.ENSP00000339399.

    Chemistry

    ChEMBLi CHEMBL6118.
    DrugBanki DB00266. Dicoumarol.

    PTM databases

    PhosphoSitei Q08257.

    Polymorphism databases

    DMDMi 585013.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00000792.

    Proteomic databases

    MaxQBi Q08257.
    PaxDbi Q08257.
    PRIDEi Q08257.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340866 ; ENSP00000339399 ; ENSG00000116791 . [Q08257-1 ]
    ENST00000370871 ; ENSP00000359908 ; ENSG00000116791 . [Q08257-3 ]
    ENST00000370872 ; ENSP00000359909 ; ENSG00000116791 . [Q08257-2 ]
    ENST00000417775 ; ENSP00000399805 ; ENSG00000116791 . [Q08257-1 ]
    GeneIDi 1429.
    KEGGi hsa:1429.
    UCSCi uc001dgj.3. human. [Q08257-1 ]
    uc001dgm.3. human. [Q08257-2 ]

    Organism-specific databases

    CTDi 1429.
    GeneCardsi GC01M075171.
    HGNCi HGNC:2419. CRYZ.
    HPAi HPA021921.
    HPA023290.
    MIMi 123691. gene.
    neXtProti NX_Q08257.
    PharmGKBi PA26925.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0604.
    HOGENOMi HOG000294672.
    HOVERGENi HBG002466.
    InParanoidi Q08257.
    KOi K00344.
    OMAi PSANINW.
    OrthoDBi EOG7BGHM8.
    PhylomeDBi Q08257.
    TreeFami TF314255.

    Miscellaneous databases

    EvolutionaryTracei Q08257.
    GeneWikii CRYZ.
    GenomeRNAii 1429.
    NextBioi 5829.
    PROi Q08257.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08257.
    Bgeei Q08257.
    CleanExi HS_CRYZ.
    Genevestigatori Q08257.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. 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 ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 1 hit.
    PROSITEi PS01162. QOR_ZETA_CRYSTAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiQOR_HUMAN
    AccessioniPrimary (citable) accession number: Q08257
    Secondary accession number(s): A6NN60
    , D3DQ76, Q53FT0, Q59EU7, Q5HYE7, Q6NSK9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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