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Q49A26

- GLYR1_HUMAN

UniProt

Q49A26 - GLYR1_HUMAN

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Protein

Putative oxidoreductase GLYR1

Gene

GLYR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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).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
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):
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
Complete GO annotation...

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

BgeeiQ49A26.
ExpressionAtlasiQ49A26. baseline and differential.
GenevestigatoriQ49A26.

Organism-specific databases

HPAiCAB017022.
HPA048226.
HPA050136.

Interactioni

Subunit structurei

Interacts with MAPK14.2 Publications

Protein-protein interaction databases

BioGridi124176. 27 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.
GeneTreeiENSGT00530000063270.
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

        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
SHNSSDDKNR RNSSEERSRP NSGDEKRKLS LSEGKVKKNM GEGKKRVSSG
160 170 180 190 200
SSERGSKSPL KRAQEQSPRK RGRPPKDEKD LTIPESSTVK GMMAGPMAAF
210 220 230 240 250
KWQPTASEPV KDADPHFHHF LLSQTEKPAV CYQAITKKLK ICEEETGSTS
260 270 280 290 300
IQAADSTAVN GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA
310 320 330 340 350
EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG
360 370 380 390 400
IRPGKCYVDM STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV
410 420 430 440 450
ILAAGDRGLY EDCSSCFQAM GKTSFFLGEV GNAAKMMLIV NMVQGSFMAT
460 470 480 490 500
IAEGLTLAHV TGQSQQTLLD ILNQGQLASI FLDQKCQNIL QGNFKPDFYL
510 520 530 540 550
KYIQKDLRLA IALGDAVNHP TPMAAAANEV YKRAKALDQS DNDMSAVYRA

YIH
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.
ENST00000436648; ENSP00000390276; ENSG00000140632.
ENST00000591451; ENSP00000468328; ENSG00000140632.
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. 27 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 .
ENST00000436648 ; ENSP00000390276 ; ENSG00000140632 .
ENST00000591451 ; ENSP00000468328 ; ENSG00000140632 .
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.
GeneTreei ENSGT00530000063270.
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

Bgeei Q49A26.
ExpressionAtlasi Q49A26. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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