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Q8CAA7 (PGM2L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose 1,6-bisphosphate synthase
EC=2.7.1.106
Alternative name(s):
Phosphoglucomutase-2-like 1
Gene names
Name:Pgm2l1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Tissue specificity

Expressed at highest levels in the brain and testis, at intermediate levels in thymus, spleen, lung and skeletal muscle, and at lowest levels in kidney, liver and heart. Ref.4

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621Glucose 1,6-bisphosphate synthase
PRO_0000147785

Sites

Active site1751Phosphoserine intermediate By similarity

Amino acid modifications

Modified residue1751Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CAA7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 976F86C1FECD52CA

FASTA62170,279
        10         20         30         40         50         60 
MAENADDDLN SNLLHAPYLT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR 

        70         80         90        100        110        120 
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ 

       130        140        150        160        170        180 
VTSSCSSQRL AKLTAAVLLA KDIPVYLFSR YVPTPFVPYA VQELKAVAGV MITASHNRKE 

       190        200        210        220        230        240 
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNDSWNDN LVDTSPLKKD PLQDICKKYM 

       250        260        270        280        290        300 
EDLKKICFYR DLNSKTTLKF VHTSFHGVGH DYVQLAFQVF GFKPPIPVPE QKDPDPDFST 

       310        320        330        340        350        360 
VKCPNPEEGE SVLELSLRLA EKENARIVLA TDPDADRLAV AELQENGRWK VFTGNELAAL 

       370        380        390        400        410        420 
FGWWMFDCWK KNKPNADVKN VYMLATTVSS KILKAIALKE GFHFEETLPG FKWIGSRIKD 

       430        440        450        460        470        480 
LLGNGKEVLF AFEESIGFLC GTSVLDKDGV SAAAVVAEMA SFLDTRKVTL MEQLTKVYEI 

       490        500        510        520        530        540 
YGYHMSKTSY FLCYDPPTIK TIFERIRNFE SPKEYPKFCG AFAILHVRDI TTGYDSSQPN 

       550        560        570        580        590        600 
KKSVLPVSKN SQMITFTFQN GCVATLRTSG TEPKIKYYAE MCASPGQSDT TFLEEELKKL 

       610        620 
IDALIENFLE PSKNALVWRS V

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Hypothalamus.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 142-150 AND 600-613, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"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: 17804405] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK039189 mRNA. Translation: BAC30270.1.
BC076571 mRNA. Translation: AAH76571.1.
IPIIPI00228059.
RefSeqNP_081905.1. NM_027629.3.
UniGeneMm.440524.

3D structure databases

ProteinModelPortalQ8CAA7.
SMRQ8CAA7. Positions 557-605.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8CAA7. 1 interaction.
STRINGQ8CAA7.

PTM databases

PhosphoSiteQ8CAA7.

Proteomic databases

PRIDEQ8CAA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054436; ENSMUSP00000054782; ENSMUSG00000030729.
ENSMUST00000084935; ENSMUSP00000081998; ENSMUSG00000030729.
GeneID70974.
KEGGmmu:70974.
UCSCuc012fqa.1. mouse.

Organism-specific databases

CTD283209.
MGIMGI:1918224. Pgm2l1.

Phylogenomic databases

eggNOGroNOG10554.
GeneTreeENSGT00390000017247.
HOGENOMHBG571743.
HOVERGENHBG056917.
InParanoidQ8CAA7.
OMAIGEDVDM.
OrthoDBEOG4BRWKK.
PhylomeDBQ8CAA7.

Gene expression databases

ArrayExpressQ8CAA7.
BgeeQ8CAA7.
CleanExMM_PGM2L1.
GenevestigatorQ8CAA7.
GermOnlineENSMUSG00000030729. Mus musculus.

Family and domain databases

InterProIPR005844. 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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK11809.
PfamPF02878. 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]
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITEPS00710. PGM_PMM. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio332727.
SOURCESearch...

Entry information

Entry namePGM2L_MOUSE
AccessionPrimary (citable) accession number: Q8CAA7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents