Q91WG8 (GLCNE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Alternative name(s):
UDP-GlcNAc-2-epimerase/ManAc kinase

Including the following 2 domains:

1. UDP-N-acetylglucosamine 2-epimerase
   EC=5.1.3.14
   Alternative name(s):
   UDP-GlcNAc-2-epimerase
   Uridine diphosphate-N-acetylglucosamine-2-epimerase
2. N-acetylmannosamine kinase
   EC=2.7.1.60
   Alternative name(s):
   ManAc kinase

Gene names

Name:	Gne
Synonyms:	Glcne, Uae1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	722 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Required for normal sialylation in hematopoietic cells By similarity. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development. Ref.5
Catalytic activity	UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine. ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate.
Enzyme regulation	Allosterically regulated; feedback inhibited by cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac), the end product of neuraminic acid biosynthesis. Activity is dependent on oligomerization. The monomer is inactive, whereas the dimer catalyzes only the phosphorylation of N-acetylmannosamine; the hexamer is fully active for both enzyme activities By similarity. Up-regulated after PKC-dependent phosphorylation.
Pathway	Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
Subunit structure	Homodimer and homohexamer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Widely expressed. Highest expression in liver. Also found at high levels in lung, brain and kidney. Ref.1
Developmental stage	In the embryo, expressed at day E7, E11 and E15. Ref.1
Post-translational modification	Phosphorylated by PKC. Ref.4
Sequence similarities	In the N-terminal section; belongs to the UDP-N-acetylglucosamine 2-epimerase family. In the C-terminal section; belongs to the ROK (nagC/xylR) family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Isomerase Kinase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	N-acetylneuraminate metabolic process Traceable author statement Ref.1. Source: MGI UDP-N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: InterPro lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acylmannosamine kinase activity Inferred from electronic annotation. Source: EC UDP-N-acetylglucosamine 2-epimerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 722	722	Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase		PRO_0000095717
Regions
	Nucleotide binding	411 – 418	8	ATP Potential
	Nucleotide binding	545 – 552	8	ATP Potential
	Region	1 – ?		UDP-N-acetylglucosamine 2-epimerase
	Region	406 – 722	317	N-acetylmannosamine kinase By similarity
Experimental info
	Sequence conflict	566 – 567	2	EL → DV in CAB36908. Ref.1
	Sequence conflict	623	1	G → V in CAB36908. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q91WG8 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0DFDD681BFD17984	FASTA	722	79,199
	10 20 30 40 50 60 MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPAFFE LDVVVLGSHL IDDYGNTYRM 70 80 90 100 110 120 IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA 130 140 150 160 170 180 TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL 190 200 210 220 230 240 AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK CKDYIVALQH PVTTDIKHSI KMFELTLDAL 250 260 270 280 290 300 ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN 310 320 330 340 350 360 SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI 370 380 390 400 410 420 YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR 430 440 450 460 470 480 VAIVSMKGEI VKKYTQFNPK TYEERISLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP 490 500 510 520 530 540 QEGVVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AAMAERKFGQ GKGQENFVTL 550 560 570 580 590 600 ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA 610 620 630 640 650 660 KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNVKAQS ILRTAGTALG LGVVNILHTM 670 680 690 700 710 720 NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR IH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tissue expression and amino acid sequence of murine UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase." Horstkorte R., Noehring S., Wiechens N., Schwarzkopf M., Danker K., Reutter W., Lucka L. Eur. J. Biochem. 260:923-927(1999) [PubMed: 10103025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: BALB/c. Tissue: Liver.
[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: FVB/N. Tissue: Colon.
[3]	"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. , 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] OF 572-722. Strain: C57BL/6J. Tissue: Colon.
[4]	"Protein kinase C phosphorylates and regulates UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase." Horstkorte R., Noehring S., Danker K., Effertz K., Reutter W., Lucka L. FEBS Lett. 470:315-318(2000) [PubMed: 10745088] [Abstract] Cited for: PHOSPHORYLATION.
[5]	"Sialylation is essential for early development in mice." Schwarzkopf M., Knobeloch K.-P., Rohde E., Hinderlich S., Wiechens N., Lucka L., Horak I., Reutter W., Horstkorte R. Proc. Natl. Acad. Sci. U.S.A. 99:5267-5270(2002) [PubMed: 11929971] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132236 mRNA. Translation: CAB36908.1. BC015277 mRNA. Translation: AAH15277.1. BC051254 mRNA. Translation: AAH51254.1. AK033507 mRNA. Translation: BAC28328.1. AK033691 mRNA. Translation: BAC28432.1.
IPI	IPI00874876.
RefSeq	NP_001177343.1. NM_001190414.1. NP_056643.3. NM_015828.3.
UniGene	Mm.256718.
3D structure databases
ProteinModelPortal	Q91WG8.
SMR	Q91WG8. Positions 10-717.
ModBase	Search...
Protein-protein interaction databases
STRING	Q91WG8.
PTM databases
PhosphoSite	Q91WG8.
Proteomic databases
PRIDE	Q91WG8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000102936; ENSMUSP00000100000; ENSMUSG00000028479. ENSMUST00000102937; ENSMUSP00000100001; ENSMUSG00000028479.
GeneID	50798.
KEGG	mmu:50798.
NMPDR	fig|10090.3.peg.9502.
Organism-specific databases
CTD	10020.
MGI	MGI:1354951. Gne.
Phylogenomic databases
GeneTree	ENSGT00390000017246.
HOVERGEN	HBG051733.
InParanoid	Q91WG8.
OrthoDB	EOG4QFWCN.
PhylomeDB	Q91WG8.
Gene expression databases
ArrayExpress	Q91WG8.
Bgee	Q91WG8.
CleanEx	MM_GNE.
Genevestigator	Q91WG8.
GermOnline	ENSMUSG00000028479. Mus musculus.
Family and domain databases
InterPro	IPR001312. Hexokinase. IPR000600. ROK. IPR020004. UDP-GlcNAc_Epase. IPR003331. UDP_GlcNAc_Epimerase_2. [Graphical view]
KO	K12409.
Pfam	PF02350. Epimerase_2. 1 hit. PF00480. ROK. 1 hit. [Graphical view]
PRINTS	PR00475. HEXOKINASE.
TIGRFAMs	TIGR03568. NeuC_NnaA. 1 hit.
PROSITE	PS01125. ROK. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	307809.
SOURCE	Search...

Entry information

Entry name

GLCNE_MOUSE

Accession

Primary (citable) accession number: Q91WG8
Secondary accession number(s): Q8CC83, Q8CCB0, Q9Z0P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program