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Q6ZNW5

- GDPP1_HUMAN

UniProt

Q6ZNW5 - GDPP1_HUMAN

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Protein

GDP-D-glucose phosphorylase 1

Gene

GDPGP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.1 Publication

Catalytic activityi

GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + GDP.1 Publication

Kineticsi

kcat is 26 s(-1) at 31 degrees Celsius. The catalytic efficiency for GDP-D-glucose is 35-fold higher than for GDP-L-galactose.

  1. KM=2 µM for GDP-D-glucose (at 31 degrees Celsius)1 Publication
  2. KM=12 µM for GDP-L-galactose (at 31 degrees Celsius)1 Publication
  3. KM=42 µM for GDP-D-mannose (at 31 degrees Celsius)1 Publication
  4. KM=2.9 mM for inorganic phosphate (at 31 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei218 – 2181Tele-GMP-histidine intermediateBy similarity

GO - Molecular functioni

  1. GDP-D-glucose phosphorylase activity Source: UniProtKB
  2. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
  3. hydrolase activity Source: UniProtKB-KW
  4. nucleotide binding Source: UniProtKB-KW
  5. nucleotidyltransferase activity Source: UniProtKB-KW

GO - Biological processi

  1. glucose metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor, Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:G66-31756-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-D-glucose phosphorylase 1 (EC:2.7.7.78)
Gene namesi
Name:GDPGP1
Synonyms:C15orf58
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:34360. GDPGP1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162378247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385GDP-D-glucose phosphorylase 1PRO_0000336750Add
BLAST

Proteomic databases

MaxQBiQ6ZNW5.
PaxDbiQ6ZNW5.
PRIDEiQ6ZNW5.

Expressioni

Gene expression databases

BgeeiQ6ZNW5.
CleanExiHS_C15orf58.
ExpressionAtlasiQ6ZNW5. baseline and differential.
GenevestigatoriQ6ZNW5.

Organism-specific databases

HPAiHPA048189.

Interactioni

Protein-protein interaction databases

BioGridi133642. 3 interactions.
STRINGi9606.ENSP00000368405.

Structurei

3D structure databases

ProteinModelPortaliQ6ZNW5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GDPGP1 family.Curated

Phylogenomic databases

eggNOGiNOG307761.
GeneTreeiENSGT00390000016718.
HOVERGENiHBG106673.
InParanoidiQ6ZNW5.
KOiK15630.
OMAiGIQWPRN.
OrthoDBiEOG7M98H0.
PhylomeDBiQ6ZNW5.
TreeFamiTF313615.

Family and domain databases

InterProiIPR026506. GDPGP.
[Graphical view]
PANTHERiPTHR20884. PTHR20884. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6ZNW5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALPHDSNET SYLLPPNNED WGRQTIPDFV YGQKDLMAEG IQWPRNAPGI
60 70 80 90 100
PDALPQSPFD AALCSAWKQR VELGLFRYRL RELQTQILPG AVGFVAQLNV
110 120 130 140 150
ERGVQRRPPQ TIKSVRQAFD PVQFNFNKIR PGEVLFRLHR EPDLPGTLLQ
160 170 180 190 200
EDILVVINVS PLEWGHVLLV PEPARQLPQR LLPGALRAGI EAVLLSLHPG
210 220 230 240 250
FRVGFNSLGG LASVNHLHLH GYYLAHRLPV EQAPSEPLDP GGHLHLLQDL
260 270 280 290 300
PAPGFLFYTR GPGPDLESLI SRVCRATDYL TDHEIAHNLF VTRGAPPGKT
310 320 330 340 350
SPSSALTGVR VILWARKSSF GIKDGEAFNV ALCELAGHLP VKTSQDFSSL
360 370 380
TEAAAVALIQ DCRLPPSQAE DVQAALVALM SQEEQ
Length:385
Mass (Da):42,362
Last modified:May 18, 2010 - v2
Checksum:i921A656C721876EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231R → G in BAC85370. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371M → T.1 Publication
Corresponds to variant rs7171194 [ dbSNP | Ensembl ].
VAR_043555
Natural varianti264 – 2641P → T.1 Publication
Corresponds to variant rs10152994 [ dbSNP | Ensembl ].
VAR_043556
Natural varianti307 – 3071T → I.1 Publication
Corresponds to variant rs10153004 [ dbSNP | Ensembl ].
VAR_043557

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK130527 mRNA. Translation: BAC85370.1.
AC091167 Genomic DNA. No translation available.
CCDSiCCDS32327.1.
RefSeqiNP_001013679.2. NM_001013657.2.
UniGeneiHs.304673.

Genome annotation databases

EnsembliENST00000329600; ENSP00000368405; ENSG00000183208.
ENST00000558017; ENSP00000452793; ENSG00000183208.
GeneIDi390637.
KEGGihsa:390637.
UCSCiuc002bpc.3. human.

Polymorphism databases

DMDMi296434456.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK130527 mRNA. Translation: BAC85370.1 .
AC091167 Genomic DNA. No translation available.
CCDSi CCDS32327.1.
RefSeqi NP_001013679.2. NM_001013657.2.
UniGenei Hs.304673.

3D structure databases

ProteinModelPortali Q6ZNW5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 133642. 3 interactions.
STRINGi 9606.ENSP00000368405.

Polymorphism databases

DMDMi 296434456.

Proteomic databases

MaxQBi Q6ZNW5.
PaxDbi Q6ZNW5.
PRIDEi Q6ZNW5.

Protocols and materials databases

DNASUi 390637.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329600 ; ENSP00000368405 ; ENSG00000183208 .
ENST00000558017 ; ENSP00000452793 ; ENSG00000183208 .
GeneIDi 390637.
KEGGi hsa:390637.
UCSCi uc002bpc.3. human.

Organism-specific databases

CTDi 390637.
GeneCardsi GC15P090778.
HGNCi HGNC:34360. GDPGP1.
HPAi HPA048189.
neXtProti NX_Q6ZNW5.
PharmGKBi PA162378247.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307761.
GeneTreei ENSGT00390000016718.
HOVERGENi HBG106673.
InParanoidi Q6ZNW5.
KOi K15630.
OMAi GIQWPRN.
OrthoDBi EOG7M98H0.
PhylomeDBi Q6ZNW5.
TreeFami TF313615.

Enzyme and pathway databases

BioCyci MetaCyc:G66-31756-MONOMER.

Miscellaneous databases

GenomeRNAii 390637.
NextBioi 103948.
PROi Q6ZNW5.

Gene expression databases

Bgeei Q6ZNW5.
CleanExi HS_C15orf58.
ExpressionAtlasi Q6ZNW5. baseline and differential.
Genevestigatori Q6ZNW5.

Family and domain databases

InterProi IPR026506. GDPGP.
[Graphical view ]
PANTHERi PTHR20884. PTHR20884. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANTS THR-37; THR-264 AND ILE-307.
    Tissue: Salivary gland.
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "A novel GDP-D-glucose phosphorylase involved in quality control of the nucleoside diphosphate sugar pool in Caenorhabditis elegans and mammals."
    Adler L.N., Gomez T.A., Clarke S.G., Linster C.L.
    J. Biol. Chem. 286:21511-21523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.

Entry informationi

Entry nameiGDPP1_HUMAN
AccessioniPrimary (citable) accession number: Q6ZNW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 69 of the entry and version 2 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 orthologs in A.thaliana are GDP-L-galactose phosphorylases catalyzing the first reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families
  5. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

External Data

Dasty 3