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Q49A26

- GLYR1_HUMAN

UniProt

Q49A26 - GLYR1_HUMAN

Protein

Putative oxidoreductase GLYR1

Gene

GLYR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
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    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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei362 – 3621NADBy similarity
    Binding sitei505 – 5051NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi168 – 18013A.T hookAdd
    BLAST
    Nucleotide bindingi271 – 28515NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. methylated histone binding Source: UniProtKB
    3. NAD binding Source: InterPro
    4. phosphogluconate dehydrogenase (decarboxylating) activity Source: InterPro

    GO - Biological processi

    1. pentose-phosphate shunt Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    DNA-binding, NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative oxidoreductase GLYR1 (EC:1.-.-.-)
    Alternative name(s):
    3-hydroxyisobutyrate dehydrogenase-like protein
    Cytokine-like nuclear factor N-PAC
    Glyoxylate reductase 1 homolog
    Nuclear protein NP60
    Nuclear protein of 60 kDa
    Gene namesi
    Name:GLYR1
    Synonyms:HIBDL, NP60
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:24434. GLYR1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. Golgi apparatus Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165450093.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 553553Putative oxidoreductase GLYR1PRO_0000312121Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301Phosphoserine1 Publication
    Modified residuei167 – 1671Phosphoserine2 Publications
    Modified residuei540 – 5401Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ49A26.
    PaxDbiQ49A26.
    PRIDEiQ49A26.

    PTM databases

    PhosphoSiteiQ49A26.

    Expressioni

    Gene expression databases

    ArrayExpressiQ49A26.
    BgeeiQ49A26.
    GenevestigatoriQ49A26.

    Organism-specific databases

    HPAiCAB017022.
    HPA048226.
    HPA050136.

    Interactioni

    Subunit structurei

    Interacts with MAPK14.2 Publications

    Protein-protein interaction databases

    BioGridi124176. 13 interactions.
    IntActiQ49A26. 7 interactions.
    MINTiMINT-3063171.

    Structurei

    Secondary structure

    1
    553
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni215 – 2173
    Helixi220 – 2223
    Beta strandi270 – 2734
    Helixi277 – 28812
    Beta strandi293 – 2964
    Helixi300 – 3034
    Helixi304 – 3085
    Helixi317 – 3237
    Beta strandi325 – 3295
    Helixi334 – 3429
    Helixi347 – 3504
    Beta strandi356 – 3594
    Helixi365 – 37713
    Beta strandi381 – 3844
    Beta strandi387 – 3893
    Helixi391 – 3966
    Beta strandi399 – 4057
    Helixi407 – 4126
    Helixi414 – 4207
    Beta strandi421 – 4266
    Helixi432 – 46029
    Helixi465 – 47410
    Helixi480 – 49112
    Beta strandi497 – 4993
    Helixi500 – 51617
    Helixi522 – 53615
    Helixi544 – 5507

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UYYX-ray2.50A/B/C/D261-553[»]
    4GURX-ray2.51B152-268[»]
    4GUSX-ray2.23B152-268[»]
    4GUTX-ray2.00B152-268[»]
    4GUUX-ray2.30B152-268[»]
    4HSUX-ray1.99B152-268[»]
    ProteinModelPortaliQ49A26.
    SMRiQ49A26. Positions 7-87, 262-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ49A26.

    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.
    The PWWP domain probably mediates the binding to H3K36me3.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG2084.
    InParanoidiQ49A26.
    OMAiTVAGFKW.
    OrthoDBiEOG7992RZ.
    PhylomeDBiQ49A26.
    TreeFamiTF324195.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR006115. 6PGDH_NADP-bd.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR013328. DH_multihelical.
    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]
    SMARTiSM00384. AT_hook. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    PROSITEiPS50812. PWWP. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q49A26-1) [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

    MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE    50
    DHAWIKVEQL KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS 100
    SHNSSDDKNR RNSSEERSRP NSGDEKRKLS LSEGKVKKNM GEGKKRVSSG 150
    SSERGSKSPL KRAQEQSPRK RGRPPKDEKD LTIPESSTVK GMMAGPMAAF 200
    KWQPTASEPV KDADPHFHHF LLSQTEKPAV CYQAITKKLK ICEEETGSTS 250
    IQAADSTAVN GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA 300
    EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG 350
    IRPGKCYVDM STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV 400
    ILAAGDRGLY EDCSSCFQAM GKTSFFLGEV GNAAKMMLIV NMVQGSFMAT 450
    IAEGLTLAHV TGQSQQTLLD ILNQGQLASI FLDQKCQNIL QGNFKPDFYL 500
    KYIQKDLRLA IALGDAVNHP TPMAAAANEV YKRAKALDQS DNDMSAVYRA 550
    YIH 553
    Length:553
    Mass (Da):60,556
    Last modified:November 24, 2009 - v3
    Checksum:i356598A73083203E
    GO
    Isoform 2 (identifier: Q49A26-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         228-244: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:536
    Mass (Da):58,637
    Checksum:i8A8C155A0BFA5CEB
    GO
    Isoform 5 (identifier: Q49A26-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         99-179: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:472
    Mass (Da):51,508
    Checksum:iA7B15666C92A58B3
    GO
    Isoform 3 (identifier: Q49A26-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         303-308: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:547
    Mass (Da):59,837
    Checksum:iD195E1EAEBB338C3
    GO
    Isoform 4 (identifier: Q49A26-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-69: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:484
    Mass (Da):52,559
    Checksum:iCDD318548A80FB06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401K → E in AAH32855. (PubMed:15489334)Curated
    Sequence conflicti419 – 4191A → T in AAH47223. (PubMed:15489334)Curated
    Sequence conflicti463 – 4631Q → R in AAH47223. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031N → D.
    Corresponds to variant rs34176249 [ dbSNP | Ensembl ].
    VAR_037403
    Natural varianti459 – 4591H → Q.6 Publications
    Corresponds to variant rs2085329 [ dbSNP | Ensembl ].
    VAR_037404
    Natural varianti531 – 5311Y → C.
    Corresponds to variant rs17703111 [ dbSNP | Ensembl ].
    VAR_037405

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6969Missing in isoform 4. 1 PublicationVSP_029706Add
    BLAST
    Alternative sequencei99 – 17981Missing in isoform 5. 1 PublicationVSP_038222Add
    BLAST
    Alternative sequencei228 – 24417Missing in isoform 2. 1 PublicationVSP_029707Add
    BLAST
    Alternative sequencei303 – 3086Missing in isoform 3. 1 PublicationVSP_029708

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY352585 mRNA. Translation: AAQ57265.1.
    AF244907 mRNA. Translation: AAQ14242.1.
    AF326966 mRNA. Translation: AAK15524.1.
    AK296842 mRNA. Translation: BAG59409.1.
    AC020663 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85252.1.
    CH471112 Genomic DNA. Translation: EAW85257.1.
    BC003693 mRNA. Translation: AAH03693.1.
    BC032855 mRNA. Translation: AAH32855.1.
    BC047223 mRNA. Translation: AAH47223.1.
    BC064940 mRNA. Translation: AAH64940.1.
    CCDSiCCDS10524.1. [Q49A26-1]
    RefSeqiNP_115958.2. NM_032569.3.
    XP_005255697.2. XM_005255640.2.
    UniGeneiHs.387255.
    Hs.731580.

    Genome annotation databases

    EnsembliENST00000321919; ENSP00000322716; ENSG00000140632. [Q49A26-1]
    ENST00000436648; ENSP00000390276; ENSG00000140632. [Q49A26-5]
    ENST00000591451; ENSP00000468328; ENSG00000140632. [Q49A26-3]
    GeneIDi84656.
    KEGGihsa:84656.
    UCSCiuc002cxx.4. human. [Q49A26-1]
    uc002cxz.1. human. [Q49A26-2]
    uc002cya.2. human. [Q49A26-3]
    uc010uxv.1. human. [Q49A26-5]

    Polymorphism databases

    DMDMi269849681.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY352585 mRNA. Translation: AAQ57265.1 .
    AF244907 mRNA. Translation: AAQ14242.1 .
    AF326966 mRNA. Translation: AAK15524.1 .
    AK296842 mRNA. Translation: BAG59409.1 .
    AC020663 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85252.1 .
    CH471112 Genomic DNA. Translation: EAW85257.1 .
    BC003693 mRNA. Translation: AAH03693.1 .
    BC032855 mRNA. Translation: AAH32855.1 .
    BC047223 mRNA. Translation: AAH47223.1 .
    BC064940 mRNA. Translation: AAH64940.1 .
    CCDSi CCDS10524.1. [Q49A26-1 ]
    RefSeqi NP_115958.2. NM_032569.3.
    XP_005255697.2. XM_005255640.2.
    UniGenei Hs.387255.
    Hs.731580.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UYY X-ray 2.50 A/B/C/D 261-553 [» ]
    4GUR X-ray 2.51 B 152-268 [» ]
    4GUS X-ray 2.23 B 152-268 [» ]
    4GUT X-ray 2.00 B 152-268 [» ]
    4GUU X-ray 2.30 B 152-268 [» ]
    4HSU X-ray 1.99 B 152-268 [» ]
    ProteinModelPortali Q49A26.
    SMRi Q49A26. Positions 7-87, 262-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124176. 13 interactions.
    IntActi Q49A26. 7 interactions.
    MINTi MINT-3063171.

    PTM databases

    PhosphoSitei Q49A26.

    Polymorphism databases

    DMDMi 269849681.

    Proteomic databases

    MaxQBi Q49A26.
    PaxDbi Q49A26.
    PRIDEi Q49A26.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321919 ; ENSP00000322716 ; ENSG00000140632 . [Q49A26-1 ]
    ENST00000436648 ; ENSP00000390276 ; ENSG00000140632 . [Q49A26-5 ]
    ENST00000591451 ; ENSP00000468328 ; ENSG00000140632 . [Q49A26-3 ]
    GeneIDi 84656.
    KEGGi hsa:84656.
    UCSCi uc002cxx.4. human. [Q49A26-1 ]
    uc002cxz.1. human. [Q49A26-2 ]
    uc002cya.2. human. [Q49A26-3 ]
    uc010uxv.1. human. [Q49A26-5 ]

    Organism-specific databases

    CTDi 84656.
    GeneCardsi GC16M004855.
    HGNCi HGNC:24434. GLYR1.
    HPAi CAB017022.
    HPA048226.
    HPA050136.
    MIMi 610660. gene.
    neXtProti NX_Q49A26.
    PharmGKBi PA165450093.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2084.
    InParanoidi Q49A26.
    OMAi TVAGFKW.
    OrthoDBi EOG7992RZ.
    PhylomeDBi Q49A26.
    TreeFami TF324195.

    Miscellaneous databases

    ChiTaRSi GLYR1. human.
    EvolutionaryTracei Q49A26.
    GenomeRNAii 84656.
    NextBioi 74618.
    PROi Q49A26.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q49A26.
    Bgeei Q49A26.
    Genevestigatori Q49A26.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR006115. 6PGDH_NADP-bd.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR013328. DH_multihelical.
    IPR016040. NAD(P)-bd_dom.
    IPR029154. NADP-bd.
    IPR000313. PWWP_dom.
    [Graphical view ]
    Pfami PF14833. NAD_binding_11. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view ]
    SMARTi SM00384. AT_hook. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 1 hit.
    PROSITEi PS50812. PWWP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nuclear protein NP60 regulates p38 MAPK activity."
      Fu J., Yang Z., Wei J., Han J., Gu J.
      J. Cell Sci. 119:115-123(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH MAPK14, VARIANT GLN-459.
    2. "Molecular characterization of a novel human PWWP domain containing protein with homology to 3-hydroxyisobutyrate dehydrogenase."
      Watari Y., Tsujino T., Nonaka H., Shirai Y., Saito N., Yokoyama M.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-459.
    3. "A novel cytokine-like nuclear factor, N-PAC."
      New L., Han J.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT GLN-459.
    4. "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 5), VARIANT GLN-459.
      Tissue: Tongue.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      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.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-459.
    7. "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] (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-553 (ISOFORM 2), VARIANT GLN-459.
      Tissue: Brain, Lymph, Placenta and Testis.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
      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.
      Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN PWWP, FUNCTION.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-167 AND SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The structure of the cytokine-like nuclear factor N-PAC."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 261-553 IN COMPLEX WITH NAD ANALOG.

    Entry informationi

    Entry nameiGLYR1_HUMAN
    AccessioniPrimary (citable) accession number: Q49A26
    Secondary accession number(s): B4DL47
    , C9JJ40, C9JJ60, Q5U632, Q6P1Q2, Q6V3W7, Q9BTI1, Q9BXK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 92 of the entry and version 3 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

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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