Q6PCE3 (PGM2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucose 1,6-bisphosphate synthase
EC=2.7.1.106

Alternative name(s):
PMMLP
Phosphoglucomutase-2-like 1

Gene names

Name:	PGM2L1
Synonyms:	BM32A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	622 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.6 Ref.8
Catalytic activity	3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Coding sequence diversity	Polymorphism
Molecular function	Isomerase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	glucose-1,6-bisphosphate synthase activity Inferred from electronic annotation. Source: EC phosphoglucomutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 622	622	Glucose 1,6-bisphosphate synthase		PRO_0000147784
Sites
	Active site	175	1	Phosphoserine intermediate By similarity
Amino acid modifications
	Modified residue	175	1	Phosphoserine Ref.5 Ref.7 Ref.9 Ref.10 Ref.11
Natural variations
	Natural variant	14	1	L → P. Ref.4 Corresponds to variant rs12049823 [ dbSNP | Ensembl ].		VAR_028094
	Natural variant	531	1	V → I. Ref.2 Ref.4 Corresponds to variant rs592644 [ dbSNP | Ensembl ].		VAR_028095
	Natural variant	608	1	N → I. Corresponds to variant rs36014178 [ dbSNP | Ensembl ].		VAR_056665
Experimental info
	Sequence conflict	69	1	T → A in BAB71227. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6PCE3 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 8AE00403B5D973CA	FASTA	622	70,442
	10 20 30 40 50 60 MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR 70 80 90 100 110 120 LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ 130 140 150 160 170 180 VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR YVPTPFVPYA VQKLKAVAGV MITASHNRKE 190 200 210 220 230 240 DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM 250 260 270 280 290 300 EDLKKICFYR ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST 310 320 330 340 350 360 VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK VFTGNELAAL 370 380 390 400 410 420 FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK EGFHFEETLP GFKWIGSRII 430 440 450 460 470 480 DLLENGKEVL FAFEESIGFL CGTSVLDKDG VSAAVVVAEM ASYLETMNIT LKQQLVKVYE 490 500 510 520 530 540 KYGYHISKTS YFLCYEPPTI KSIFERLRNF DSPKEYPKFC GTFAILHVRD VTTGYDSSQP 550 560 570 580 590 600 NKKSVLPVSK NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK 610 620 LIDALIENFL QPSKNGLIWR SV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-531. Tissue: Tongue.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PRO-14 AND ILE-531. Tissue: Placenta.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: FUNCTION.
[7]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 18927083] [Abstract] Cited for: FUNCTION.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB019210 mRNA. Translation: BAA82756.1. AK056591 mRNA. Translation: BAB71227.1. AP001085 Genomic DNA. No translation available. BC059360 mRNA. Translation: AAH59360.1.
IPI	IPI00173346.
RefSeq	NP_775853.2. NM_173582.3.
UniGene	Hs.26612.
3D structure databases
ProteinModelPortal	Q6PCE3.
SMR	Q6PCE3. Positions 559-606.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6PCE3.
PTM databases
PhosphoSite	Q6PCE3.
Polymorphism databases
DMDM	71153044.
Proteomic databases
PRIDE	Q6PCE3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298198; ENSP00000298198; ENSG00000165434.
GeneID	283209.
KEGG	hsa:283209.
UCSC	uc001ovb.1. human.
Organism-specific databases
CTD	283209.
GeneCards	GC11M074041.
HGNC	HGNC:20898. PGM2L1.
MIM	611610. gene.
neXtProt	NX_Q6PCE3.
PharmGKB	PA134938366.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17864.
GeneTree	ENSGT00390000017247.
HOGENOM	HBG571743.
HOVERGEN	HBG056917.
InParanoid	Q6PCE3.
OMA	IYKEFGY.
OrthoDB	EOG4BRWKK.
PhylomeDB	Q6PCE3.
Gene expression databases
ArrayExpress	Q6PCE3.
Bgee	Q6PCE3.
CleanEx	HS_PGM2L1.
Genevestigator	Q6PCE3.
GermOnline	ENSG00000165434. Homo sapiens.
Family and domain databases
InterPro	IPR005844. 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]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K11809.
Pfam	PF02878. 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]
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	93718.
SOURCE	Search...

Entry information

Entry name

PGM2L_HUMAN

Accession

Primary (citable) accession number: Q6PCE3
Secondary accession number(s): Q96MQ7, Q9UIK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 77 of the entry and version 3 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.