Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Putative oxidoreductase GLYR1 (EC 1.-.-.-) (3-hydroxyisobutyrate dehydrogenase-like protein) (Cytokine-like nuclear factor N-PAC) (Glyoxylate reductase 1 homolog) (Nuclear protein NP60) (Nuclear protein of 60 kDa)

 GLYR1_HUMAN             Reviewed;         553 AA.
Q49A26; B4DL47; C9JJ40; C9JJ60; Q5U632; Q6P1Q2; Q6V3W7; Q9BTI1;
Q9BXK2;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 3.
22-NOV-2017, entry version 123.
RecName: Full=Putative oxidoreductase GLYR1;
EC=1.-.-.-;
AltName: Full=3-hydroxyisobutyrate dehydrogenase-like protein;
AltName: Full=Cytokine-like nuclear factor N-PAC;
AltName: Full=Glyoxylate reductase 1 homolog;
AltName: Full=Nuclear protein NP60;
AltName: Full=Nuclear protein of 60 kDa;
Name=GLYR1; Synonyms=HIBDL, NP60;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, DOMAIN, INTERACTION WITH MAPK14, AND VARIANT GLN-459.
PubMed=16352664; DOI=10.1242/jcs.02699;
Fu J., Yang Z., Wei J., Han J., Gu J.;
"Nuclear protein NP60 regulates p38 MAPK activity.";
J. Cell Sci. 119:115-123(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-459.
Watari Y., Tsujino T., Nonaka H., Shirai Y., Saito N., Yokoyama M.;
"Molecular characterization of a novel human PWWP domain containing
protein with homology to 3-hydroxyisobutyrate dehydrogenase.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT GLN-459.
New L., Han J.;
"A novel cytokine-like nuclear factor, N-PAC.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
GLN-459.
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-459.
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 14-553 (ISOFORM 2), AND VARIANT
GLN-459.
TISSUE=Brain, Lymph, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
DOMAIN PWWP, AND FUNCTION.
PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
Mann M.;
"Quantitative interaction proteomics and genome-wide profiling of
epigenetic histone marks and their readers.";
Cell 142:967-980(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-540, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-540, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-540, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-269, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-227; LYS-237 AND
LYS-269, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-176; LYS-179;
LYS-201; LYS-211; LYS-227; LYS-237; LYS-240; LYS-269 AND LYS-302, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 261-553 IN COMPLEX WITH NAD
ANALOG.
Tickle J., Pilka E.S., Bunkoczi G., Berridge G., Smee C.,
Kavanagh K.L., Hozjan V., Niesen F.H., Papagrigoriou E., Pike A.C.W.,
Turnbull A., Arrowsmith C.H., Edwards A., Sundstrom M., Weigelt J.,
Von Delft F., Oppermann U.;
"The structure of the cytokine-like nuclear factor N-PAC.";
Submitted (APR-2007) to the PDB data bank.
[19]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 152-268.
PubMed=23357850; DOI=10.1038/cr.2013.17;
Chen F., Yang H., Dong Z., Fang J., Wang P., Zhu T., Gong W., Fang R.,
Shi Y.G., Li Z., Xu Y.;
"Structural insight into substrate recognition by histone demethylase
LSD2/KDM1b.";
Cell Res. 23:306-309(2013).
[20]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 152-268 IN COMPLEX WITH
KDM1B AND HISTONE H3 PEPTIDE, FUNCTION, INTERACTION WITH KDM1B, AND
MUTAGENESIS OF ASP-214; HIS-216; PHE-217; HIS-219; 220-PHE--LEU-222
AND SER-223.
PubMed=23260659; DOI=10.1016/j.molcel.2012.11.019;
Fang R., Chen F., Dong Z., Hu D., Barbera A.J., Clark E.A., Fang J.,
Yang Y., Mei P., Rutenberg M., Li Z., Zhang Y., Xu Y., Yang H.,
Wang P., Simon M.D., Zhou Q., Li J., Marynick M.P., Li X., Lu H.,
Kaiser U.B., Kingston R.E., Xu Y., Shi Y.G.;
"LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and
molecular model for regulation of H3K4 demethylation.";
Mol. Cell 49:558-570(2013).
-!- FUNCTION: Putative oxidoreductase that is recruited on chromatin
and promotes KDM1B demethylase activity (PubMed:23260659).
Recognizes and binds trimethylated 'Lys-36' of histone H3
(H3K36me3) (PubMed:20850016). Regulates p38 MAP kinase activity by
mediating stress activation of p38alpha/MAPK14 and specifically
regulating MAPK14 signaling (PubMed:16352664). Indirectly promotes
phosphorylation of MAPK14 and activation of ATF2
(PubMed:16352664). The phosphorylation of MAPK14 requires upstream
activity of MAP2K4 and MAP2K6 (PubMed:16352664).
{ECO:0000269|PubMed:16352664, ECO:0000269|PubMed:20850016,
ECO:0000269|PubMed:23260659}.
-!- SUBUNIT: Interacts with MAPK14 (PubMed:16352664, Ref.18).
Interacts with KDM1B at nucleosomes; this interaction stimulates
H3K4me1 and H3K4me2 demethylation (PubMed:23260659).
{ECO:0000269|PubMed:16352664, ECO:0000269|PubMed:23260659,
ECO:0000269|Ref.18}.
-!- INTERACTION:
Q8IZP9-4:ADGRG2; NbExp=4; IntAct=EBI-12143817, EBI-13048936;
Q9H3H3-3:C11orf68; NbExp=4; IntAct=EBI-12143817, EBI-12002214;
P24863:CCNC; NbExp=3; IntAct=EBI-2804292, EBI-395261;
P55273:CDKN2D; NbExp=4; IntAct=EBI-12143817, EBI-745859;
Q8IYR0:CFAP206; NbExp=3; IntAct=EBI-2804292, EBI-749051;
Q8N9N8:EIF1AD; NbExp=3; IntAct=EBI-2804292, EBI-750700;
Q9Y3B2:EXOSC1; NbExp=4; IntAct=EBI-12143817, EBI-371892;
Q969U6:FBXW5; NbExp=4; IntAct=EBI-12143817, EBI-741068;
Q14192:FHL2; NbExp=3; IntAct=EBI-2804292, EBI-701903;
Q15345:LRRC41; NbExp=4; IntAct=EBI-12143817, EBI-721408;
Q8N4Z0:RAB42; NbExp=4; IntAct=EBI-12143817, EBI-12878310;
P60866:RPS20; NbExp=4; IntAct=EBI-12143817, EBI-353105;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16352664}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q49A26-1; Sequence=Displayed;
Name=2;
IsoId=Q49A26-2; Sequence=VSP_029707;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q49A26-5; Sequence=VSP_038222;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q49A26-3; Sequence=VSP_029708;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q49A26-4; Sequence=VSP_029706;
Note=No experimental confirmation available.;
-!- DOMAIN: The A.T hook DNA-binding domain is required for the
interaction with MAPK14. {ECO:0000305}.
-!- DOMAIN: The PWWP domain probably mediates the binding to H3K36me3.
{ECO:0000305|PubMed:20850016}.
-!- MISCELLANEOUS: The conserved NAD-binding sites and sequence
similarity to plant dehydrogenases suggest that this protein may
have oxidoreductase activity. {ECO:0000305}.
-!- SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase
family. NP60 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY352585; AAQ57265.1; -; mRNA.
EMBL; AF244907; AAQ14242.1; -; mRNA.
EMBL; AF326966; AAK15524.1; -; mRNA.
EMBL; AK296842; BAG59409.1; -; mRNA.
EMBL; AC020663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85252.1; -; Genomic_DNA.
EMBL; CH471112; EAW85257.1; -; Genomic_DNA.
EMBL; BC003693; AAH03693.1; -; mRNA.
EMBL; BC032855; AAH32855.1; -; mRNA.
EMBL; BC047223; AAH47223.1; -; mRNA.
EMBL; BC064940; AAH64940.1; -; mRNA.
CCDS; CCDS10524.1; -. [Q49A26-1]
CCDS; CCDS81945.1; -. [Q49A26-3]
RefSeq; NP_001295025.1; NM_001308096.1.
RefSeq; NP_115958.2; NM_032569.3.
RefSeq; XP_011521019.1; XM_011522717.1.
UniGene; Hs.387255; -.
UniGene; Hs.731580; -.
PDB; 2UYY; X-ray; 2.50 A; A/B/C/D=261-553.
PDB; 4GUR; X-ray; 2.51 A; B=152-268.
PDB; 4GUS; X-ray; 2.23 A; B=152-268.
PDB; 4GUT; X-ray; 2.00 A; B=152-268.
PDB; 4GUU; X-ray; 2.30 A; B=152-268.
PDB; 4HSU; X-ray; 1.99 A; B=152-268.
PDBsum; 2UYY; -.
PDBsum; 4GUR; -.
PDBsum; 4GUS; -.
PDBsum; 4GUT; -.
PDBsum; 4GUU; -.
PDBsum; 4HSU; -.
ProteinModelPortal; Q49A26; -.
SMR; Q49A26; -.
BioGrid; 124176; 80.
IntAct; Q49A26; 267.
MINT; MINT-3063171; -.
STRING; 9606.ENSP00000322716; -.
iPTMnet; Q49A26; -.
PhosphoSitePlus; Q49A26; -.
BioMuta; GLYR1; -.
DMDM; 269849681; -.
EPD; Q49A26; -.
MaxQB; Q49A26; -.
PaxDb; Q49A26; -.
PeptideAtlas; Q49A26; -.
PRIDE; Q49A26; -.
TopDownProteomics; Q49A26-2; -. [Q49A26-2]
Ensembl; ENST00000321919; ENSP00000322716; ENSG00000140632.
Ensembl; ENST00000436648; ENSP00000390276; ENSG00000140632.
Ensembl; ENST00000591451; ENSP00000468328; ENSG00000140632.
GeneID; 84656; -.
KEGG; hsa:84656; -.
UCSC; uc002cxx.5; human. [Q49A26-1]
CTD; 84656; -.
DisGeNET; 84656; -.
EuPathDB; HostDB:ENSG00000140632.16; -.
GeneCards; GLYR1; -.
HGNC; HGNC:24434; GLYR1.
HPA; CAB017022; -.
HPA; HPA048226; -.
HPA; HPA050136; -.
MIM; 610660; gene.
neXtProt; NX_Q49A26; -.
PharmGKB; PA165450093; -.
eggNOG; KOG0409; Eukaryota.
eggNOG; KOG1904; Eukaryota.
eggNOG; COG2084; LUCA.
InParanoid; Q49A26; -.
OrthoDB; EOG091G0MNC; -.
PhylomeDB; Q49A26; -.
TreeFam; TF324195; -.
ChiTaRS; GLYR1; human.
EvolutionaryTrace; Q49A26; -.
GenomeRNAi; 84656; -.
PRO; PR:Q49A26; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140632; -.
ExpressionAtlas; Q49A26; baseline and differential.
Genevisible; Q49A26; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro.
CDD; cd05836; N_Pac_NP60; 1.
Gene3D; 1.10.1040.10; -; 1.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR013328; 6PGD_dom2.
InterPro; IPR006115; 6PGDH_NADP-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR029154; NADP-bd.
InterPro; IPR035501; NP60_PWWP.
InterPro; IPR000313; PWWP_dom.
Pfam; PF14833; NAD_binding_11; 1.
Pfam; PF03446; NAD_binding_2; 1.
Pfam; PF00855; PWWP; 1.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS50812; PWWP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA-binding;
Isopeptide bond; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 553 Putative oxidoreductase GLYR1.
/FTId=PRO_0000312121.
DOMAIN 8 66 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DNA_BIND 168 180 A.T hook. {ECO:0000305}.
NP_BIND 271 285 NAD. {ECO:0000244|PDB:2UYY,
ECO:0000269|Ref.18}.
REGION 214 217 Interaction with histone H3.
{ECO:0000269|PubMed:23260659}.
REGION 216 225 Interaction with KDM1B.
{ECO:0000244|PDB:4GUR,
ECO:0000244|PDB:4GUS,
ECO:0000244|PDB:4GUT,
ECO:0000244|PDB:4GUU,
ECO:0000269|PubMed:23260659}.
BINDING 362 362 NAD. {ECO:0000244|PDB:2UYY,
ECO:0000269|Ref.18}.
BINDING 505 505 NAD. {ECO:0000244|PDB:2UYY,
ECO:0000269|Ref.18}.
SITE 217 217 Required to promote KDM1B demethylase
activity toward histone H3K4me1 and
H3K4me2. {ECO:0000269|PubMed:23260659}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 135 135 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 201 201 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 227 227 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 302 302 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 69 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029706.
VAR_SEQ 99 179 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038222.
VAR_SEQ 228 244 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029707.
VAR_SEQ 303 308 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_029708.
VARIANT 103 103 N -> D (in dbSNP:rs34176249).
/FTId=VAR_037403.
VARIANT 459 459 H -> Q (in dbSNP:rs2085329).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16352664,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.6}.
/FTId=VAR_037404.
VARIANT 531 531 Y -> C (in dbSNP:rs17703111).
/FTId=VAR_037405.
MUTAGEN 214 214 D->A: Slightly reduced stimulation of
KDM1B demethylase activity, but normal
KDM1B-binding.
{ECO:0000269|PubMed:23260659}.
MUTAGEN 216 216 H->A: Slightly reduced stimulation of
KDM1B demethylase activity, but normal
KDM1B-binding.
{ECO:0000269|PubMed:23260659}.
MUTAGEN 217 217 F->A: Abolished stimulation of KDM1B
demethylase activity, reduced affinity
for histone H3 of the dimer with KDM1B,
but normal KDM1B-binding.
{ECO:0000269|PubMed:23260659}.
MUTAGEN 219 219 H->A: Impaired KDM1B-binding and
abolished stimulation of KDM1B
demethylase activity; when associated
with A-223.
{ECO:0000269|PubMed:23260659}.
MUTAGEN 220 222 FLL->AAA: Impaired KDM1B-binding and
abolished stimulation of KDM1B
demethylase activity.
{ECO:0000269|PubMed:23260659}.
MUTAGEN 223 223 S->A: Impaired KDM1B-binding and
abolished stimulation of KDM1B
demethylase activity; when associated
with A-219.
{ECO:0000269|PubMed:23260659}.
CONFLICT 40 40 K -> E (in Ref. 7; AAH32855).
{ECO:0000305}.
CONFLICT 419 419 A -> T (in Ref. 7; AAH47223).
{ECO:0000305}.
CONFLICT 463 463 Q -> R (in Ref. 7; AAH47223).
{ECO:0000305}.
TURN 215 217 {ECO:0000244|PDB:4HSU}.
HELIX 220 222 {ECO:0000244|PDB:4HSU}.
STRAND 270 273 {ECO:0000244|PDB:2UYY}.
HELIX 277 288 {ECO:0000244|PDB:2UYY}.
STRAND 293 296 {ECO:0000244|PDB:2UYY}.
HELIX 300 303 {ECO:0000244|PDB:2UYY}.
HELIX 304 308 {ECO:0000244|PDB:2UYY}.
HELIX 317 323 {ECO:0000244|PDB:2UYY}.
STRAND 325 329 {ECO:0000244|PDB:2UYY}.
HELIX 334 342 {ECO:0000244|PDB:2UYY}.
HELIX 347 350 {ECO:0000244|PDB:2UYY}.
STRAND 356 359 {ECO:0000244|PDB:2UYY}.
HELIX 365 377 {ECO:0000244|PDB:2UYY}.
STRAND 381 384 {ECO:0000244|PDB:2UYY}.
STRAND 387 389 {ECO:0000244|PDB:2UYY}.
HELIX 391 396 {ECO:0000244|PDB:2UYY}.
STRAND 399 405 {ECO:0000244|PDB:2UYY}.
HELIX 407 412 {ECO:0000244|PDB:2UYY}.
HELIX 414 420 {ECO:0000244|PDB:2UYY}.
STRAND 421 426 {ECO:0000244|PDB:2UYY}.
HELIX 432 460 {ECO:0000244|PDB:2UYY}.
HELIX 465 474 {ECO:0000244|PDB:2UYY}.
HELIX 480 491 {ECO:0000244|PDB:2UYY}.
STRAND 497 499 {ECO:0000244|PDB:2UYY}.
HELIX 500 516 {ECO:0000244|PDB:2UYY}.
HELIX 522 536 {ECO:0000244|PDB:2UYY}.
HELIX 544 550 {ECO:0000244|PDB:2UYY}.
SEQUENCE 553 AA; 60556 MW; 356598A73083203E CRC64;
MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL
KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS SHNSSDDKNR RNSSEERSRP
NSGDEKRKLS LSEGKVKKNM GEGKKRVSSG SSERGSKSPL KRAQEQSPRK RGRPPKDEKD
LTIPESSTVK GMMAGPMAAF KWQPTASEPV KDADPHFHHF LLSQTEKPAV CYQAITKKLK
ICEEETGSTS IQAADSTAVN GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA
EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG IRPGKCYVDM
STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV ILAAGDRGLY EDCSSCFQAM
GKTSFFLGEV GNAAKMMLIV NMVQGSFMAT IAEGLTLAHV TGQSQQTLLD ILNQGQLASI
FLDQKCQNIL QGNFKPDFYL KYIQKDLRLA IALGDAVNHP TPMAAAANEV YKRAKALDQS
DNDMSAVYRA YIH


Related products :

Catalog number Product name Quantity
30-558 UNC84A is a a nuclear nuclear envelope protein with an Unc84 (SUN) domain. The protein is involved in nuclear anchorage and migration.This gene is a member of the unc-84 homolog family and encodes a n 0.05 mg
18-661-15150 Putative HLA-DR-associated protein I - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associ 0.1 mg
18-661-15153 Putative HLA-DR-associated protein I - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associ 0.1 mg
18-661-15152 Putative HLA-DR-associated protein - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associat 0.1 mg
18-661-15154 Putative HLA-DR-associated protein I - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associ 0.1 mg
EIAAB05063 Antigen nuclear dot 52 kDa protein,Calcium-binding and coiled-coil domain-containing protein 2,CALCOCO2,Homo sapiens,Human,NDP52,Nuclear domain 10 protein 52,Nuclear domain 10 protein NDP52,Nuclear do
EIAAB27055 CCAAT-box-binding transcription factor,CTF,Homo sapiens,Human,KIAA1439,NF1-A,NF-I_A,NFIA,NFI-A,Nuclear factor 1 A-type,Nuclear factor 1_A,Nuclear factor I_A,TGGCA-binding protein
EIAAB27058 CCAAT-box-binding transcription factor,CTF,Homo sapiens,Human,NF1-B,NF-I_B,NFIB,NFI-B,Nuclear factor 1 B-type,Nuclear factor 1_B,Nuclear factor I_B,TGGCA-binding protein
EIAAB27061 CCAAT-box-binding transcription factor,CTF,Homo sapiens,Human,NF1-C,NFI,NF-I_C,NFIC,NFI-C,Nuclear factor 1 C-type,Nuclear factor 1_C,Nuclear factor I_C,TGGCA-binding protein
EIAAB27075 CCAAT-box-binding transcription factor,CTF,Homo sapiens,Human,NF1-X,NF-I_X,NFIX,NFI-X,Nuclear factor 1 X-type,Nuclear factor 1_X,Nuclear factor I_X,TGGCA-binding protein
EIAAB27054 CCAAT-box-binding transcription factor,CTF,NF1-A,Nf1l21,NF-I_A,Nfia,NFI-A,Nuclear factor 1 A-type,Nuclear factor 1_A,Nuclear factor I_A,Rat,Rattus norvegicus,TGGCA-binding protein
18-003-42302 Nuclear body protein SP140 - Nuclear autoantigen Sp-140; Speckled 140 kDa; LYSp100 protein; Lymphoid-restricted homolog of Sp100 Polyclonal 0.1 mg Protein A
EIAAB27052 CCAAT-box-binding transcription factor,CTF,Mouse,Mus musculus,NF1-A,NF-I_A,Nfia,NFI-A,Nuclear factor 1 A-type,Nuclear factor 1_A,Nuclear factor I_A,TGGCA-binding protein
EIAAB27076 CCAAT-box-binding transcription factor,CTF,Mouse,Mus musculus,NF1-X,NF-I_X,Nfix,NFI-X,Nuclear factor 1 X-type,Nuclear factor 1_X,Nuclear factor I_X,TGGCA-binding protein
EIAAB27057 CCAAT-box-binding transcription factor,CTF,Mouse,Mus musculus,NF1-B,NF-I_B,Nfib,NFI-B,Nuclear factor 1 B-type,Nuclear factor 1_B,Nuclear factor I_B,TGGCA-binding protein
EIAAB27063 CCAAT-box-binding transcription factor,CTF,Mouse,Mus musculus,NF1-C,NF-I_C,Nfic,NFI-C,Nuclear factor 1 C-type,Nuclear factor 1_C,Nuclear factor I_C,TGGCA-binding protein
EIAAB27062 CCAAT-box-binding transcription factor,CTF,NF1-C,NFI,NF-I_C,NFIC,NFI-C,Nuclear factor 1 C-type,Nuclear factor 1_C,Nuclear factor I_C,Pig,Sus scrofa,TGGCA-binding protein
EIAAB28231 Mouse,Mus musculus,Nuclear distribution protein C homolog,Nuclear migration protein nudC,Nudc,SIG-92,Silica-induced gene 92 protein
EIAAB40793 C6orf98,Enaptin,Homo sapiens,Human,KIAA0796,KIAA1262,KIAA1756,MYNE1,Myne-1,Myocyte nuclear envelope protein 1,Nesprin-1,Nuclear envelope spectrin repeat protein 1,Synaptic nuclear envelope protein 1,S
EIAAB40794 Enaptin,Mouse,Mus musculus,Myne-1,Myocyte nuclear envelope protein 1,Nesprin-1,Nuclear envelope spectrin repeat protein 1,Synaptic nuclear envelope protein 1,Syne1,Syne-1
18-373-88001 Nesprin-1 - Nuclear envelope spectrin repeat protein 1; Synaptic nuclear envelope protein 1; Syne-1; Myocyte nuclear envelope protein 1; Myne-1; Enaptin Polyclonal 0.1 ml
EIAAB27810 Gfrp,Hmr,Mouse,Mus musculus,N10,Nr4a1,Nuclear hormone receptor NUR_77,Nuclear protein N10,Nuclear receptor subfamily 4 group A member 1,Nur77,Orphan nuclear receptor HMR
EIAAB33742 Androgen receptor-associated protein 24,ARA24,GTPase Ran,GTP-binding nuclear protein Ran,Homo sapiens,Human,OK_SW-cl.81,RAN,Ras-like protein TC4,Ras-related nuclear protein
EIAAB27060 CCAAT-box-binding transcription factor,Chicken,CTF,Gallus gallus,NF1-C,NF-I_C,NFIC,NFI-C,NFI-C,Nuclear factor 1 C-type,Nuclear factor 1_C,Nuclear factor I_C,TGGCA-binding protein
EIAAB27077 CCAAT-box-binding transcription factor,Chicken,CTF,Gallus gallus,NF1-X,NF-I_X,NFIX,NFI-X,NFI-X,Nuclear factor 1 X-type,Nuclear factor 1_X,Nuclear factor I_X,TGGCA-binding protein


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur