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Q8T079 (GLYR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative oxidoreductase GLYR1 homolog
EC=1.-.-.-
Alternative name(s):
Glyoxylate reductase 1 homolog
Nuclear protein NP60 homolog
Gene names
ORF Names:CG4747
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have oxidoreductase activity By similarity.

Miscellaneous

The conserved NAD-binding sites suggest that this protein may have oxidoreductase activity.

Sequence similarities

Belongs to the 3-hydroxyisobutyrate dehydrogenase family. NP60 subfamily.

Contains 1 PWWP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG14860-RAQ9VFE81EBI-160222,EBI-138433
CG14932Q9VKF41EBI-160222,EBI-82420
CG3099Q9W3251EBI-160222,EBI-173625
CG6999Q9W3931EBI-160222,EBI-187457

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602Putative oxidoreductase GLYR1 homolog
PRO_0000312130

Regions

Domain22 – 8160PWWP
Nucleotide binding319 – 33315NAD Potential

Sites

Binding site4111NAD Potential
Binding site5541NAD Potential

Amino acid modifications

Modified residue81Phosphoserine Ref.4
Modified residue101Phosphoserine Ref.4
Modified residue2241Phosphoserine Ref.4
Modified residue2281Phosphoserine Ref.4
Modified residue2431Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8T079 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E004EEC610C23625

FASTA60265,252
        10         20         30         40         50         60 
MSKNKKLSLS GGDTTEKFIY KPKDLIWAKM KGFTPWPGMI VDPPLDLLSQ QRRANTKCVF 

        70         80         90        100        110        120 
FFGSRNFAWI EENNIKPFEG PWKEELAKVS KPAAFRHAMT DIEKYIDDPA EVDEQVNKSC 

       130        140        150        160        170        180 
GAPNHATEAD FDKIRDGLDS EEIVGEEATA DGNNGVVAHV VGSPDEGDGL DVEINADSSA 

       190        200        210        220        230        240 
SPVTSPAVTT KAAGKRTPKA KSVAATSVKS TKGSAKSAQK RRTSAQQSPS GPSNAKRGKR 

       250        260        270        280        290        300 
DVSGEALQDA DEASSTPTGR RRVETDALLA SIAAKRAPNA IALLDRPVVT RPEAQVIDMS 

       310        320        330        340        350        360 
SRSNTLADRD IVPSEQTFGF LGLGMMGSTI VKDLIYTGHK VVVWNRTIDK CQPFAEAGAE 

       370        380        390        400        410        420 
VKDTPMDVVE AADVIFCCVS DPKGAKDLVF GNCGVLQLKD LNNKAYVEMS TIDPDTSLDI 

       430        440        450        460        470        480 
GEGIKQCNGR YLEAQIHGSR QEAAEGMLII LAGGDRSVFE ECHSCFKTIA KNTFFLGNIG 

       490        500        510        520        530        540 
NACKVNLILQ TILGVSLVGL AEALALADRF SISLNDIIDI FDLTSMKSPM LLAKGKEMAK 

       550        560        570        580        590        600 
GDFNPQQPLS HMQRDLRLVL NMAENLDQSM PVTSITNEVF KHTKRLGYSE HDSSAVFVRS 


RF

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-10; SER-224; SER-228 AND SER-243, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014134 Genomic DNA. Translation: AAF52846.3.
AY069497 mRNA. Translation: AAL39642.1.
RefSeqNP_609336.3. NM_135492.4.

3D structure databases

HSSPHSSP built from PDB template 1RI0 based on UniProtKB P51858.
ProteinModelPortalQ8T079.
SMRQ8T079. Positions 19-107, 311-597.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8T079. 4 interactions.
MINTMINT-320537.
STRINGQ8T079.

Proteomic databases

PRIDEQ8T079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079930; FBpp0079520; FBgn0043456.
GeneID192507.
KEGGdme:Dmel_CG4747.
NMPDRfig|7227.3.peg.1699.
UCSCCG4747-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0043456. CG4747.

Phylogenomic databases

eggNOGinNOG09173.
GeneTreeEMGT00050000006794.
InParanoidQ8T079.
OMANHATEAD.
OrthoDBEOG42BVQQ.
PhylomeDBQ8T079.

Gene expression databases

ArrayExpressQ8T079.
BgeeQ8T079.

Family and domain databases

InterProIPR015815. 3hydroxyacid_DH/Rdtase.
IPR008927. 6-PGluconate_DH_C-like.
IPR006115. 6PGDH_NADP-bd.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
IPR000313. PWWP.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KOK00020.
PANTHERPTHR22981. 3hydroxy_acid_DH. 1 hit.
PfamPF03446. NAD_binding_2. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
PROSITEPS00895. 3_HYDROXYISOBUT_DH. False negative.
PS50812. PWWP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio842223.

Entry information

Entry nameGLYR1_DROME
AccessionPrimary (citable) accession number: Q8T079
Secondary accession number(s): Q9VL51
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: June 1, 2002
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents