P46926 (GNPI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucosamine-6-phosphate isomerase 1
EC=3.5.99.6

Alternative name(s):
Glucosamine-6-phosphate deaminase 1
Short name=GNPDA 1
Short name=GlcN6P deaminase 1
Oscillin

Gene names

Name:	GNPDA1
Synonyms:	GNPI, HLN, KIAA0060

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo By similarity.
Catalytic activity	D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3.
Subunit structure	Homohexamer. Ref.10
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the glucosamine/galactosamine-6-phosphate isomerase family.
Sequence caution	The sequence BAA06544.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: InterPro carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW generation of precursor metabolites and energy Inferred from mutant phenotype Ref.1. Source: UniProtKB glucosamine catabolic process Inferred from mutant phenotype Ref.1. Source: UniProtKB single fertilization Traceable author statement Ref.2. Source: ProtInc
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	glucosamine-6-phosphate deaminase activity Inferred from mutant phenotype Ref.1. Source: UniProtKB hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 289

289

Glucosamine-6-phosphate isomerase 1

PRO_0000160122

Sites

Active site

72

1

Proton acceptor; for enolization step By similarity

Active site

141

1

For ring-opening step By similarity

Active site

143

1

Proton acceptor; for ring-opening step By similarity

Active site

148

1

For ring-opening step By similarity

Amino acid modifications

Modified residue

64

1

N6-acetyllysine Ref.8

Secondary structure

1

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289

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

9 – 27

19

Beta strand

35 – 39

5

Helix

43 – 57

15

Beta strand

66 – 74

9

Helix

85 – 92

8

Helix

94 – 96

3

Helix

101 – 103

3

Helix

114 – 127

14

Beta strand

132 – 136

5

Beta strand

157 – 161

5

Helix

164 – 170

7

Helix

171 – 173

3

Turn

174 – 176

3

Helix

178 – 180

3

Beta strand

183 – 187

5

Helix

190 – 194

5

Beta strand

199 – 203

5

Helix

206 – 208

3

Helix

209 – 216

8

Helix

225 – 231

7

Beta strand

233 – 240

8

Helix

241 – 244

4

Helix

249 – 257

9

Helix

259 – 262

4

Helix

263 – 265

3

Sequences

	Sequence		Length	Mass (Da)
	P46926 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4111F655D574F74F	FASTA	289	32,669
	10 20 30 40 50 60 MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK KLIEYYKNGD 70 80 90 100 110 120 LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AVDLQAECDA 130 140 150 160 170 180 FEEKIKAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGELTK 190 200 210 220 230 240 VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD 250 260 270 280 EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity." Wolosker H., Kline D., Bian Y., Blackshaw S., Cameron A.M., Fralich T.J., Schnaar R.L., Snyder S.H. FASEB J. 12:91-99(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization." Shevchenko V., Hogben M., Ekong R., Parrington J., Lai F.A. Gene 216:31-38(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[3]	Hirata S., Koh T., Hoshi K. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Testis.
[4]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [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].
[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]. Tissue: Ovary and Skin.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, MASS SPECTROMETRY.
[9]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study." Arreola R., Valderrama B., Morante M.L., Horjales E. FEBS Lett. 551:63-70(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF048826 mRNA. Translation: AAC05123.1.
AJ002231 mRNA. Translation: CAA05259.1.
AF029914 mRNA. Translation: AAB84217.1.
AF035809 , AF035804, AF035805, AF035806, AF035807, AF035808 Genomic DNA. Translation: AAB88748.1.
D31766 mRNA. Translation: BAA06544.2. Different initiation.
AC005740 Genomic DNA. Translation: AAC62119.1.
CH471062 Genomic DNA. Translation: EAW61890.1.
CH471062 Genomic DNA. Translation: EAW61891.1.
CH471062 Genomic DNA. Translation: EAW61892.1.
CH471062 Genomic DNA. Translation: EAW61893.1.
BC012853 mRNA. Translation: AAH12853.1.
BC020769 mRNA. Translation: AAH20769.1.
BC022322 mRNA. Translation: AAH22322.1.

IPI

IPI00009305.

RefSeq

NP_005462.1. NM_005471.4.

UniGene

Hs.633853.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NE7	X-ray	1.75	A/B/C/D/E/F	1-289	[»]

ProteinModelPortal

P46926.

ModBase

Search...

Protein-protein interaction databases

IntAct

P46926. 1 interaction.

STRING

9606.ENSP00000311876.

PTM databases

PhosphoSite

P46926.

Polymorphism databases

DMDM

1171639.

Proteomic databases

PaxDb

P46926.

PeptideAtlas

P46926.

PRIDE

P46926.

Protocols and materials databases

DNASU

10007.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311337; ENSP00000311876; ENSG00000113552.
ENST00000500692; ENSP00000424275; ENSG00000113552.
ENST00000503794; ENSP00000423485; ENSG00000113552.
ENST00000508177; ENSP00000423674; ENSG00000113552.

GeneID

10007.

KEGG

hsa:10007.

UCSC

uc003lmf.4. human.

Organism-specific databases

CTD

10007.

GeneCards

GC05M141360.

HGNC

HGNC:4417. GNPDA1.

HPA

HPA000499.

MIM

601798. gene.

neXtProt

NX_P46926.

PharmGKB

PA28796.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0363.

HOGENOM

HOG000064979.

HOVERGEN

HBG002546.

InParanoid

P46926.

KO

K02564.

OrthoDB

EOG4F1X3Q.

PhylomeDB

P46926.

Enzyme and pathway databases

SABIO-RK

P46926.

Gene expression databases

ArrayExpress

P46926.

Bgee

P46926.

CleanEx

HS_GNPDA1.

Genevestigator

P46926.

GermOnline

ENSG00000113552. Homo sapiens.

Family and domain databases

InterPro

IPR006148. Glc/Gal-6P_isomerase.
IPR004547. Glucosamine6P_isomerase.
IPR018321. Glucosamine6P_isomerase_CS.
[Graphical view]

PANTHER

PTHR11280. PTHR11280. 1 hit.

Pfam

PF01182. Glucosamine_iso. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00502. nagB. 1 hit.

PROSITE

PS01161. GLC_GALNAC_ISOMERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P46926.

GenomeRNAi

10007.

NextBio

37805.

SOURCE

Search...

Entry information

Entry name

GNPI1_HUMAN

Accession

Primary (citable) accession number: P46926
Secondary accession number(s): D3DQE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 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.