Q49A26 (GLYR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GLYR1
Synonyms:	HIBDL, NP60

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.1 Ref.12
Subunit structure	Interacts with MAPK14. Ref.1
Subcellular location	Nucleus Ref.1.
Domain	The A.T hook DNA-binding domain is required for the interaction with MAPK14. Ref.1 Ref.12 The PWWP domain probably mediates the binding to H3K36me3. Ref.1 Ref.12
Miscellaneous	The conserved NAD-binding sites and sequence similarity to plant dehydrogenases suggest that this protein may have oxidoreductase activity.
Sequence similarities	Belongs to the 3-hydroxyisobutyrate dehydrogenase family. NP60 subfamily. Contains 1 A.T hook DNA-binding domain. Contains 1 PWWP domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW coenzyme binding Inferred from electronic annotation. Source: InterPro methylated histone residue binding Inferred from direct assay Ref.12. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q49A26-1)

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.

Isoform 2 (identifier: Q49A26-2)

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

Note: No experimental confirmation available.

Isoform 5 (identifier: Q49A26-5)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q49A26-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: Q49A26-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 553

553

Putative oxidoreductase GLYR1

PRO_0000312121

Regions

Domain

8 – 66

59

PWWP

DNA binding

168 – 180

13

A.T hook

Nucleotide binding

271 – 285

15

NAD By similarity

Sites

Binding site

362

1

NAD By similarity

Binding site

505

1

NAD By similarity

Amino acid modifications

Modified residue

25

1

N6-acetyllysine Ref.11

Modified residue

130

1

Phosphoserine Ref.8 Ref.9

Modified residue

132

1

Phosphoserine Ref.8 Ref.9

Modified residue

167

1

Phosphoserine Ref.8

Modified residue

540

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

1 – 69

69

Missing in isoform 4.

VSP_029706

Alternative sequence

99 – 179

81

Missing in isoform 5.

VSP_038222

Alternative sequence

228 – 244

17

Missing in isoform 2.

VSP_029707

Alternative sequence

303 – 308

6

Missing in isoform 3.

VSP_029708

Natural variant

103

1

N → D.
Corresponds to variant rs34176249 [ dbSNP | Ensembl ].

VAR_037403

Natural variant

459

1

H → Q. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7
Corresponds to variant rs2085329 [ dbSNP | Ensembl ].

VAR_037404

Natural variant

531

1

Y → C.
Corresponds to variant rs17703111 [ dbSNP | Ensembl ].

VAR_037405

Experimental info

Sequence conflict

40

1

K → E in AAH32855. Ref.7

Sequence conflict

419

1

A → T in AAH47223. Ref.7

Sequence conflict

463

1

Q → R in AAH47223. Ref.7

Secondary structure

1

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553

Helix Strand Turn

Details...

Helix

283 – 288

6

Helix

300 – 303

4

Helix

304 – 308

5

Helix

317 – 323

7

Beta strand

325 – 329

5

Helix

334 – 341

8

Beta strand

356 – 359

4

Helix

365 – 377

13

Beta strand

382 – 384

3

Helix

391 – 395

5

Beta strand

399 – 404

6

Turn

410 – 413

4

Helix

414 – 419

6

Beta strand

422 – 426

5

Helix

433 – 443

11

Helix

447 – 452

6

Helix

456 – 460

5

Helix

465 – 473

9

Helix

480 – 490

11

Beta strand

497 – 499

3

Helix

500 – 512

13

Helix

522 – 536

15

Helix

544 – 550

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 24, 2009. Version 3. Checksum: 356598A73083203E	FASTA	553	60,556
	10 20 30 40 50 60 MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL 70 80 90 100 110 120 KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS SHNSSDDKNR RNSSEERSRP 130 140 150 160 170 180 NSGDEKRKLS LSEGKVKKNM GEGKKRVSSG SSERGSKSPL KRAQEQSPRK RGRPPKDEKD 190 200 210 220 230 240 LTIPESSTVK GMMAGPMAAF KWQPTASEPV KDADPHFHHF LLSQTEKPAV CYQAITKKLK 250 260 270 280 290 300 ICEEETGSTS IQAADSTAVN GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA 310 320 330 340 350 360 EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG IRPGKCYVDM 370 380 390 400 410 420 STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV ILAAGDRGLY EDCSSCFQAM 430 440 450 460 470 480 GKTSFFLGEV GNAAKMMLIV NMVQGSFMAT IAEGLTLAHV TGQSQQTLLD ILNQGQLASI 490 500 510 520 530 540 FLDQKCQNIL QGNFKPDFYL KYIQKDLRLA IALGDAVNHP TPMAAAANEV YKRAKALDQS 550 DNDMSAVYRA YIH
	Isoform 2 [UniParc]. Checksum: 8A8C155A0BFA5CEB	FASTA	536	58,637
	10 20 30 40 50 60 MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL 70 80 90 100 110 120 KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS SHNSSDDKNR RNSSEERSRP 130 140 150 160 170 180 NSGDEKRKLS LSEGKVKKNM GEGKKRVSSG SSERGSKSPL KRAQEQSPRK RGRPPKDEKD 190 200 210 220 230 240 LTIPESSTVK GMMAGPMAAF KWQPTASEPV KDADPHFHHF LLSQTEKETG STSIQAADST 250 260 270 280 290 300 AVNGSITPTD KKIGFLGLGL MGSGIVSNLL KMGHTVTVWN RTAEKCDLFI QEGARLGRTP 310 320 330 340 350 360 AEVVSTCDIT FACVSDPKAA KDLVLGPSGV LQGIRPGKCY VDMSTVDADT VTELAQVIVS 370 380 390 400 410 420 RGGRFLEAPV SGNQQLSNDG MLVILAAGDR GLYEDCSSCF QAMGKTSFFL GEVGNAAKMM 430 440 450 460 470 480 LIVNMVQGSF MATIAEGLTL AHVTGQSQQT LLDILNQGQL ASIFLDQKCQ NILQGNFKPD 490 500 510 520 530 FYLKYIQKDL RLAIALGDAV NHPTPMAAAA NEVYKRAKAL DQSDNDMSAV YRAYIH
	Isoform 5 [UniParc]. Checksum: A7B15666C92A58B3	FASTA	472	51,508
	10 20 30 40 50 60 MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL 70 80 90 100 110 120 KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQDL TIPESSTVKG MMAGPMAAFK 130 140 150 160 170 180 WQPTASEPVK DADPHFHHFL LSQTEKPAVC YQAITKKLKI CEEETGSTSI QAADSTAVNG 190 200 210 220 230 240 SITPTDKKIG FLGLGLMGSG IVSNLLKMGH TVTVWNRTAE KCDLFIQEGA RLGRTPAEVV 250 260 270 280 290 300 STCDITFACV SDPKAAKDLV LGPSGVLQGI RPGKCYVDMS TVDADTVTEL AQVIVSRGGR 310 320 330 340 350 360 FLEAPVSGNQ QLSNDGMLVI LAAGDRGLYE DCSSCFQAMG KTSFFLGEVG NAAKMMLIVN 370 380 390 400 410 420 MVQGSFMATI AEGLTLAHVT GQSQQTLLDI LNQGQLASIF LDQKCQNILQ GNFKPDFYLK 430 440 450 460 470 YIQKDLRLAI ALGDAVNHPT PMAAAANEVY KRAKALDQSD NDMSAVYRAY IH
	Isoform 3 [UniParc]. Checksum: D195E1EAEBB338C3	FASTA	547	59,837
	10 20 30 40 50 60 MAAVSLRLGD LVWGKLGRYP PWPGKIVNPP KDLKKPRGKK CFFVKFFGTE DHAWIKVEQL 70 80 90 100 110 120 KPYHAHKEEM IKINKGKRFQ QAVDAVEEFL RRAKGKDQTS SHNSSDDKNR RNSSEERSRP 130 140 150 160 170 180 NSGDEKRKLS LSEGKVKKNM GEGKKRVSSG SSERGSKSPL KRAQEQSPRK RGRPPKDEKD 190 200 210 220 230 240 LTIPESSTVK GMMAGPMAAF KWQPTASEPV KDADPHFHHF LLSQTEKPAV CYQAITKKLK 250 260 270 280 290 300 ICEEETGSTS IQAADSTAVN GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA 310 320 330 340 350 360 EKEGARLGRT PAEVVSTCDI TFACVSDPKA AKDLVLGPSG VLQGIRPGKC YVDMSTVDAD 370 380 390 400 410 420 TVTELAQVIV SRGGRFLEAP VSGNQQLSND GMLVILAAGD RGLYEDCSSC FQAMGKTSFF 430 440 450 460 470 480 LGEVGNAAKM MLIVNMVQGS FMATIAEGLT LAHVTGQSQQ TLLDILNQGQ LASIFLDQKC 490 500 510 520 530 540 QNILQGNFKP DFYLKYIQKD LRLAIALGDA VNHPTPMAAA ANEVYKRAKA LDQSDNDMSA VYRAYIH
	Isoform 4 [UniParc]. Checksum: CDD318548A80FB06	FASTA	484	52,559
	10 20 30 40 50 60 MIKINKGKRF QQAVDAVEEF LRRAKGKDQT SSHNSSDDKN RRNSSEERSR PNSGDEKRKL 70 80 90 100 110 120 SLSEGKVKKN MGEGKKRVSS GSSERGSKSP LKRAQEQSPR KRGRPPKDEK DLTIPESSTV 130 140 150 160 170 180 KGMMAGPMAA FKWQPTASEP VKDADPHFHH FLLSQTEKPA VCYQAITKKL KICEEETGST 190 200 210 220 230 240 SIQAADSTAV NGSITPTDKK IGFLGLGLMG SGIVSNLLKM GHTVTVWNRT AEKCDLFIQE 250 260 270 280 290 300 GARLGRTPAE VVSTCDITFA CVSDPKAAKD LVLGPSGVLQ GIRPGKCYVD MSTVDADTVT 310 320 330 340 350 360 ELAQVIVSRG GRFLEAPVSG NQQLSNDGML VILAAGDRGL YEDCSSCFQA MGKTSFFLGE 370 380 390 400 410 420 VGNAAKMMLI VNMVQGSFMA TIAEGLTLAH VTGQSQQTLL DILNQGQLAS IFLDQKCQNI 430 440 450 460 470 480 LQGNFKPDFY LKYIQKDLRL AIALGDAVNH PTPMAAAANE VYKRAKALDQ SDNDMSAVYR AYIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16352664] [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: 14702039] [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: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 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: 15489334] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-132 AND SER-167, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, MASS SPECTROMETRY.
[12]	"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: 20850016] [Abstract] Cited for: DOMAIN PWWP, FUNCTION.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00000155.
IPI00644210.
IPI00647134.
IPI00647648.
IPI00910934.

RefSeq

NP_115958.2. NM_032569.3.

UniGene

Hs.387255.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UYY	X-ray	2.50	A/B/C/D	261-553	[»]

ProteinModelPortal

Q49A26.

SMR

Q49A26. Positions 4-91, 262-553.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q49A26. 4 interactions.

MINT

MINT-3063171.

STRING

Q49A26.

PTM databases

PhosphoSite

Q49A26.

Polymorphism databases

DMDM

269849681.

Proteomic databases

PRIDE

Q49A26.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321919; ENSP00000322716; ENSG00000140632.
ENST00000436648; ENSP00000390276; ENSG00000140632.

GeneID

84656.

KEGG

hsa:84656.

UCSC

uc002cxx.2. human.
uc002cxz.1. human.
uc002cya.2. human.

Organism-specific databases

CTD

84656.

GeneCards

GC16M004794.

H-InvDB

HIX0023256.

HGNC

HGNC:24434. GLYR1.

HPA

CAB017022.

MIM

610660. gene.

neXtProt

NX_Q49A26.

PharmGKB

PA165450093.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06496.

GeneTree

ENSGT00530000063270.

HOGENOM

HBG729179.

InParanoid

Q49A26.

OMA

HTSADDK.

OrthoDB

EOG45B1F6.

PhylomeDB

Q49A26.

Gene expression databases

ArrayExpress

Q49A26.

Bgee

Q49A26.

Genevestigator

Q49A26.

Family and domain databases

InterPro

IPR015815. 3hydroxyacid_DH/Rdtase.
IPR008927. 6-PGluconate_DH_C-like.
IPR006115. 6PGDH_NADP-bd.
IPR017956. AT_hook_DNA-bd_motif.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
IPR000313. PWWP.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.

PANTHER

PTHR22981. 3hydroxy_acid_DH. 1 hit.

Pfam

PF03446. NAD_binding_2. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]

SMART

SM00384. AT_hook. 1 hit.
[Graphical view]

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.

PROSITE

PS00895. 3_HYDROXYISOBUT_DH. False negative.
PS50812. PWWP. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

74618.

SOURCE

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Entry information

Entry name

GLYR1_HUMAN

Accession

Primary (citable) accession number: Q49A26
Secondary accession number(s): B4DL47 , C9JJ40, C9JJ60, Q5U632, Q6P1Q2, Q6V3W7, Q9BTI1, Q9BXK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	November 24, 2009
Last modified:	December 14, 2011
This is version 65 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.