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Q08257

- QOR_HUMAN

UniProt

Q08257 - QOR_HUMAN

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Protein

Quinone oxidoreductase

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

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 – 531NADP
Binding sitei181 – 1811NADP; via amide nitrogen
Binding sitei200 – 2001NADP
Binding sitei229 – 2291NADP

Regions

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

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
Complete GO annotation...

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
Complete GO annotation...

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-succinyllysine By 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.1 Publication

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.

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

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. VSP_042927
Alternative sequencei6 – 142137Missing in isoform 2. VSP_042928Add
BLAST
Alternative sequencei211 – 24434Missing in isoform 3. VSP_046425Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051E → G in AK314813. 1 Publication

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. Dicumarol.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 136 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

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