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Protein

Putative oxidoreductase GLYR1

Gene

Glyr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei355 – 3551NADBy similarity
Binding sitei498 – 4981NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi167 – 17913A.T hookAdd
BLAST
Nucleotide bindingi270 – 28415NADBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

DNA-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Putative oxidoreductase GLYR1 (EC:1.-.-.-)
Alternative name(s):
Glyoxylate reductase 1 homolog
Nuclear protein NP60
Gene namesi
Name:Glyr1
Synonyms:Np60
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1921272. Glyr1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Putative oxidoreductase GLYR1PRO_0000312122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301PhosphoserineBy similarity
Cross-linki135 – 135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei166 – 1661PhosphoserineBy similarity
Cross-linki226 – 226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki236 – 236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki268 – 268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei533 – 5331PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ922P9.
MaxQBiQ922P9.
PaxDbiQ922P9.
PRIDEiQ922P9.

PTM databases

iPTMnetiQ922P9.
PhosphoSiteiQ922P9.

Expressioni

Gene expression databases

BgeeiQ922P9.
CleanExiMM_3930401K13RIK.
ExpressionAtlasiQ922P9. baseline and differential.
GenevisibleiQ922P9. MM.

Interactioni

Subunit structurei

Interacts with MAPK14.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ922P9. 3 interactions.
MINTiMINT-4125995.
STRINGi10090.ENSMUSP00000111510.

Structurei

3D structure databases

ProteinModelPortaliQ922P9.
SMRiQ922P9. Positions 7-87, 261-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 6659PWWPPROSITE-ProRule annotationAdd
BLAST

Domaini

The A.T hook DNA-binding domain is required for the interaction with MAPK14.By similarity
The PWWP domain probably mediates the binding to H3K36me3.By similarity

Sequence similaritiesi

Contains 1 A.T hook DNA-binding domain.Curated
Contains 1 PWWP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0409. Eukaryota.
KOG1904. Eukaryota.
COG2084. LUCA.
GeneTreeiENSGT00530000063270.
HOGENOMiHOG000219609.
InParanoidiQ922P9.
OrthoDBiEOG7992RZ.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
IPR000313. PWWP_dom.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS50812. PWWP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q922P9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE
60 70 80 90 100
DHAWIKVEQL KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS
110 120 130 140 150
SHTSADDKNR RNSSEERSRP NSGDEKRKLS LSEGKVKKNM GEGKKRVTSG
160 170 180 190 200
SADRGSKCLK RAQEQSPRKR GRPPKDEKDL TIPESSTVKG MMAGPMAAFK
210 220 230 240 250
WQPTATEPVK DADPHFHHFL LSQTEKPAVC YQAITKKLKI CEEETGSTSI
260 270 280 290 300
QAADSTAVNG SITPTDKKIG FLGLGLMGSG IVSNLLKMGH TVTVWNRTAE
310 320 330 340 350
KEGARLGRTP AEVVSTCDIT FACVSDPKAA KDLVLGPSGV LQGIRPGKCY
360 370 380 390 400
VDMSTVDADT VTELAQVIVS RGGRFLEAPV SGNQQLSNDG MLVILAAGDR
410 420 430 440 450
GLYEDCSSCF QAMGKTSFFL GEVGNAAKMM LIVNMVQGSF MATIAEGLTL
460 470 480 490 500
AQVTGQSQQT LLDILNQGQL ASIFLDQKCQ NILQGNFKPD FYLKYIQKDL
510 520 530 540
RLAIALGDAV NHPTPMAAAA NEVYKRAKAL DQSDNDMSAV YRAYIH
Length:546
Mass (Da):59,716
Last modified:December 1, 2001 - v1
Checksum:iF5D2090DE1F64723
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 512ED → KN in BAB29363 (PubMed:16141072).Curated
Sequence conflicti109 – 1102NR → DW in BAB29363 (PubMed:16141072).Curated
Sequence conflicti296 – 2961N → S in BAE35114 (PubMed:16141072).Curated
Sequence conflicti535 – 5351N → S in BAE35114 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014456 mRNA. Translation: BAB29363.1.
AK150349 mRNA. Translation: BAE29486.1.
AK152887 mRNA. Translation: BAE31570.1.
AK159476 mRNA. Translation: BAE35114.1.
BC006893 mRNA. Translation: AAH06893.1.
CCDSiCCDS27930.1.
RefSeqiNP_082996.2. NM_028720.2.
UniGeneiMm.21652.

Genome annotation databases

EnsembliENSMUST00000023189; ENSMUSP00000023189; ENSMUSG00000022536.
GeneIDi74022.
KEGGimmu:74022.
UCSCiuc007ybm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014456 mRNA. Translation: BAB29363.1.
AK150349 mRNA. Translation: BAE29486.1.
AK152887 mRNA. Translation: BAE31570.1.
AK159476 mRNA. Translation: BAE35114.1.
BC006893 mRNA. Translation: AAH06893.1.
CCDSiCCDS27930.1.
RefSeqiNP_082996.2. NM_028720.2.
UniGeneiMm.21652.

3D structure databases

ProteinModelPortaliQ922P9.
SMRiQ922P9. Positions 7-87, 261-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ922P9. 3 interactions.
MINTiMINT-4125995.
STRINGi10090.ENSMUSP00000111510.

PTM databases

iPTMnetiQ922P9.
PhosphoSiteiQ922P9.

Proteomic databases

EPDiQ922P9.
MaxQBiQ922P9.
PaxDbiQ922P9.
PRIDEiQ922P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023189; ENSMUSP00000023189; ENSMUSG00000022536.
GeneIDi74022.
KEGGimmu:74022.
UCSCiuc007ybm.1. mouse.

Organism-specific databases

CTDi84656.
MGIiMGI:1921272. Glyr1.

Phylogenomic databases

eggNOGiKOG0409. Eukaryota.
KOG1904. Eukaryota.
COG2084. LUCA.
GeneTreeiENSGT00530000063270.
HOGENOMiHOG000219609.
InParanoidiQ922P9.
OrthoDBiEOG7992RZ.

Miscellaneous databases

ChiTaRSiGlyr1. mouse.
NextBioi339560.
PROiQ922P9.
SOURCEiSearch...

Gene expression databases

BgeeiQ922P9.
CleanExiMM_3930401K13RIK.
ExpressionAtlasiQ922P9. baseline and differential.
GenevisibleiQ922P9. MM.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
IPR000313. PWWP_dom.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS50812. PWWP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Embryo.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGLYR1_MOUSE
AccessioniPrimary (citable) accession number: Q922P9
Secondary accession number(s): Q3TX02, Q9CYQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The conserved NAD-binding sites and sequence similarity to plant dehydrogenases suggest that this protein may have oxidoreductase activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.