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Protein

Glucose 1,6-bisphosphate synthase

Gene

PGM2L1

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

Functioni

Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5-bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities.2 Publications

Catalytic activityi

3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691SubstrateBy similarity
Binding sitei73 – 731SubstrateBy similarity
Active sitei175 – 1751Phosphoserine intermediateBy similarity
Metal bindingi175 – 1751Magnesium; via phosphate groupBy similarity
Metal bindingi332 – 3321MagnesiumBy similarity
Metal bindingi334 – 3341MagnesiumBy similarity
Metal bindingi336 – 3361MagnesiumBy similarity
Binding sitei448 – 4481SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • glucose metabolic process Source: UniProtKB-KW
  • phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1,6-bisphosphate synthase (EC:2.7.1.106)
Alternative name(s):
PMMLP
Phosphoglucomutase-2-like 1
Gene namesi
Name:PGM2L1
Synonyms:BM32A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:20898. PGM2L1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134938366.

Polymorphism and mutation databases

BioMutaiPGM2L1.
DMDMi317373530.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Glucose 1,6-bisphosphate synthasePRO_0000147784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei175 – 1751PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6PCE3.
MaxQBiQ6PCE3.
PaxDbiQ6PCE3.
PRIDEiQ6PCE3.

PTM databases

iPTMnetiQ6PCE3.
PhosphoSiteiQ6PCE3.

Expressioni

Gene expression databases

BgeeiQ6PCE3.
CleanExiHS_PGM2L1.
GenevisibleiQ6PCE3. HS.

Organism-specific databases

HPAiHPA056995.

Interactioni

Protein-protein interaction databases

BioGridi129496. 8 interactions.
IntActiQ6PCE3. 4 interactions.
STRINGi9606.ENSP00000298198.

Structurei

3D structure databases

ProteinModelPortaliQ6PCE3.
SMRiQ6PCE3. Positions 67-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1762Substrate bindingBy similarity
Regioni336 – 3372Substrate bindingBy similarity
Regioni434 – 4363Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ6PCE3.
KOiK11809.
OMAiSVLICEM.
OrthoDBiEOG715Q3R.
PhylomeDBiQ6PCE3.
TreeFamiTF300692.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6PCE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR
60 70 80 90 100
NGMNKELRDR LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE
110 120 130 140 150
RCFSDFKQRG FVVGYDTRGQ VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR
160 170 180 190 200
YVPTPFVPYA VQKLKAVAGV MITASHNRKE DNGYKVYWET GAQITSPHDK
210 220 230 240 250
EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM EDLKKICFYR
260 270 280 290 300
ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST
310 320 330 340 350
VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK
360 370 380 390 400
VFTGNELAAL FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK
410 420 430 440 450
EGFHFEETLP GFKWIGSRII DLLENGKEVL FAFEESIGFL CGTSVLDKDG
460 470 480 490 500
VSAAVVVAEM ASYLETMNIT LKQQLVKVYE KYGYHISKTS YFLCYEPPTI
510 520 530 540 550
KSIFERLRNF DSPKEYPKFC GTFAILHVRD VTTGYDSSQP NKKSVLPVSK
560 570 580 590 600
NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK
610 620
LIDALIENFL QPSKNGLIWR SV
Length:622
Mass (Da):70,442
Last modified:January 11, 2011 - v3
Checksum:i8AE00403B5D973CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691T → A in BAB71227 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141L → P.1 Publication
Corresponds to variant rs12049823 [ dbSNP | Ensembl ].
VAR_028094
Natural varianti531 – 5311V → I.2 Publications
Corresponds to variant rs592644 [ dbSNP | Ensembl ].
VAR_028095
Natural varianti608 – 6081N → I.
Corresponds to variant rs36014178 [ dbSNP | Ensembl ].
VAR_056665

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019210 mRNA. Translation: BAA82756.1.
AK056591 mRNA. Translation: BAB71227.1.
AP001085 Genomic DNA. No translation available.
BC059360 mRNA. Translation: AAH59360.1.
CCDSiCCDS8231.1.
RefSeqiNP_775853.2. NM_173582.4.
UniGeneiHs.26612.

Genome annotation databases

EnsembliENST00000298198; ENSP00000298198; ENSG00000165434.
GeneIDi283209.
KEGGihsa:283209.
UCSCiuc001ovb.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019210 mRNA. Translation: BAA82756.1.
AK056591 mRNA. Translation: BAB71227.1.
AP001085 Genomic DNA. No translation available.
BC059360 mRNA. Translation: AAH59360.1.
CCDSiCCDS8231.1.
RefSeqiNP_775853.2. NM_173582.4.
UniGeneiHs.26612.

3D structure databases

ProteinModelPortaliQ6PCE3.
SMRiQ6PCE3. Positions 67-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129496. 8 interactions.
IntActiQ6PCE3. 4 interactions.
STRINGi9606.ENSP00000298198.

PTM databases

iPTMnetiQ6PCE3.
PhosphoSiteiQ6PCE3.

Polymorphism and mutation databases

BioMutaiPGM2L1.
DMDMi317373530.

Proteomic databases

EPDiQ6PCE3.
MaxQBiQ6PCE3.
PaxDbiQ6PCE3.
PRIDEiQ6PCE3.

Protocols and materials databases

DNASUi283209.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298198; ENSP00000298198; ENSG00000165434.
GeneIDi283209.
KEGGihsa:283209.
UCSCiuc001ovb.2. human.

Organism-specific databases

CTDi283209.
GeneCardsiPGM2L1.
HGNCiHGNC:20898. PGM2L1.
HPAiHPA056995.
MIMi611610. gene.
neXtProtiNX_Q6PCE3.
PharmGKBiPA134938366.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ6PCE3.
KOiK11809.
OMAiSVLICEM.
OrthoDBiEOG715Q3R.
PhylomeDBiQ6PCE3.
TreeFamiTF300692.

Miscellaneous databases

ChiTaRSiPGM2L1. human.
GenomeRNAii283209.
PROiQ6PCE3.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PCE3.
CleanExiHS_PGM2L1.
GenevisibleiQ6PCE3. HS.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Mori K., Miyoshi Y., Nakamura Y.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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], VARIANT ILE-531.
    Tissue: Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS PRO-14 AND ILE-531.
    Tissue: Placenta.
  5. "Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family."
    Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M., Van Schaftingen E.
    J. Biol. Chem. 282:31844-31851(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase."
    Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G., Van Schaftingen E.
    J. Biol. Chem. 283:33988-33993(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPGM2L_HUMAN
AccessioniPrimary (citable) accession number: Q6PCE3
Secondary accession number(s): Q96MQ7, Q9UIK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 11, 2011
Last modified: June 8, 2016
This is version 119 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.