SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P46926

- GNPI1_HUMAN

UniProt

P46926 - GNPI1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucosamine-6-phosphate isomerase 1

Gene
GNPDA1, GNPI, HLN, KIAA0060
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

Alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Proton acceptor; for enolization step By similarity
Active sitei141 – 1411For ring-opening step By similarity
Active sitei143 – 1431Proton acceptor; for ring-opening step By similarity
Active sitei148 – 1481For ring-opening step By similarity

GO - Molecular functioni

  1. glucosamine-6-phosphate deaminase activity Source: UniProtKB
  2. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. generation of precursor metabolites and energy Source: UniProtKB
  3. glucosamine catabolic process Source: UniProtKB
  4. N-acetylglucosamine metabolic process Source: InterPro
  5. single fertilization Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

SABIO-RKP46926.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GNPDA1
Synonyms:GNPI, HLN, KIAA0060
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4417. GNPDA1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Glucosamine-6-phosphate isomerase 1UniRule annotationPRO_0000160122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP46926.
PaxDbiP46926.
PeptideAtlasiP46926.
PRIDEiP46926.

PTM databases

PhosphoSiteiP46926.

Expressioni

Gene expression databases

ArrayExpressiP46926.
BgeeiP46926.
CleanExiHS_GNPDA1.
GenevestigatoriP46926.

Organism-specific databases

HPAiHPA000499.
HPA046891.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

BioGridi115325. 25 interactions.
IntActiP46926. 1 interaction.
STRINGi9606.ENSP00000311876.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87
Helixi9 – 2719
Beta strandi35 – 395
Helixi43 – 5715
Beta strandi66 – 749
Helixi85 – 928
Helixi94 – 963
Helixi101 – 1033
Helixi114 – 12714
Beta strandi132 – 1365
Beta strandi157 – 1615
Helixi164 – 1707
Helixi171 – 1733
Turni174 – 1763
Helixi178 – 1803
Beta strandi183 – 1875
Helixi190 – 1945
Beta strandi199 – 2035
Helixi206 – 2083
Helixi209 – 2168
Helixi225 – 2317
Beta strandi233 – 2408
Helixi241 – 2444
Helixi249 – 2579
Helixi259 – 2624
Helixi263 – 2653

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NE7X-ray1.75A/B/C/D/E/F1-289[»]
ProteinModelPortaliP46926.
SMRiP46926. Positions 1-281.

Miscellaneous databases

EvolutionaryTraceiP46926.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0363.
HOGENOMiHOG000064979.
HOVERGENiHBG002546.
InParanoidiP46926.
KOiK02564.
PhylomeDBiP46926.
TreeFamiTF300841.

Family and domain databases

HAMAPiMF_01241. GlcN6P_deamin.
InterProiIPR006148. Glc/Gal-6P_isomerase.
IPR004547. Glucosamine6P_isomerase.
IPR018321. Glucosamine6P_isomerase_CS.
[Graphical view]
PANTHERiPTHR11280. PTHR11280. 1 hit.
PfamiPF01182. Glucosamine_iso. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00502. nagB. 1 hit.
PROSITEiPS01161. GLC_GALNAC_ISOMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46926-1 [UniParc]FASTAAdd to Basket

« Hide

MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK    50
KLIEYYKNGD LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH 100
PENTHILDGN AVDLQAECDA FEEKIKAAGG IELFVGGIGP DGHIAFNEPG 150
SSLVSRTRVK TLAMDTILAN ARFFDGELTK VPTMALTVGV GTVMDAREVM 200
ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD EDATLELKVK 250
TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD 289
Length:289
Mass (Da):32,669
Last modified:November 1, 1995 - v1
Checksum:i4111F655D574F74F
GO

Sequence cautioni

The sequence BAA06544.2 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4272.1.
RefSeqiNP_005462.1. NM_005471.4.
XP_006714810.1. XM_006714747.1.
UniGeneiHs.633853.

Genome annotation databases

EnsembliENST00000311337; ENSP00000311876; ENSG00000113552.
ENST00000500692; ENSP00000424275; ENSG00000113552.
ENST00000503794; ENSP00000423485; ENSG00000113552.
ENST00000508177; ENSP00000423674; ENSG00000113552.
GeneIDi10007.
KEGGihsa:10007.
UCSCiuc003lmf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4272.1.
RefSeqi NP_005462.1. NM_005471.4.
XP_006714810.1. XM_006714747.1.
UniGenei Hs.633853.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NE7 X-ray 1.75 A/B/C/D/E/F 1-289 [» ]
ProteinModelPortali P46926.
SMRi P46926. Positions 1-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115325. 25 interactions.
IntActi P46926. 1 interaction.
STRINGi 9606.ENSP00000311876.

PTM databases

PhosphoSitei P46926.

Proteomic databases

MaxQBi P46926.
PaxDbi P46926.
PeptideAtlasi P46926.
PRIDEi P46926.

Protocols and materials databases

DNASUi 10007.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311337 ; ENSP00000311876 ; ENSG00000113552 .
ENST00000500692 ; ENSP00000424275 ; ENSG00000113552 .
ENST00000503794 ; ENSP00000423485 ; ENSG00000113552 .
ENST00000508177 ; ENSP00000423674 ; ENSG00000113552 .
GeneIDi 10007.
KEGGi hsa:10007.
UCSCi uc003lmf.4. human.

Organism-specific databases

CTDi 10007.
GeneCardsi GC05M141360.
HGNCi HGNC:4417. GNPDA1.
HPAi HPA000499.
HPA046891.
MIMi 601798. gene.
neXtProti NX_P46926.
PharmGKBi PA28796.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0363.
HOGENOMi HOG000064979.
HOVERGENi HBG002546.
InParanoidi P46926.
KOi K02564.
PhylomeDBi P46926.
TreeFami TF300841.

Enzyme and pathway databases

SABIO-RK P46926.

Miscellaneous databases

EvolutionaryTracei P46926.
GeneWikii GNPDA1.
GenomeRNAii 10007.
NextBioi 37805.
PROi P46926.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46926.
Bgeei P46926.
CleanExi HS_GNPDA1.
Genevestigatori P46926.

Family and domain databases

HAMAPi MF_01241. GlcN6P_deamin.
InterProi IPR006148. Glc/Gal-6P_isomerase.
IPR004547. Glucosamine6P_isomerase.
IPR018321. Glucosamine6P_isomerase_CS.
[Graphical view ]
PANTHERi PTHR11280. PTHR11280. 1 hit.
Pfami PF01182. Glucosamine_iso. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00502. nagB. 1 hit.
PROSITEi PS01161. GLC_GALNAC_ISOMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. 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.

Entry informationi

Entry nameiGNPI1_HUMAN
AccessioniPrimary (citable) accession number: P46926
Secondary accession number(s): D3DQE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 138 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi