P70428 (EXT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exostosin-2
EC=2.4.1.224
EC=2.4.1.225

Alternative name(s):
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Multiple exostoses protein 2 homolog

Gene names

Name:

Ext2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor.
Catalytic activity	UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan. UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with GALNT5 By similarity. Forms a homo/hetero-oligomeric complex with EXT1.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Note: The EXT1/EXT2 complex is localized in the Golgi apparatus.
Tissue specificity	Heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.
Developmental stage	Expressed in early stages of embryonic development.
Sequence similarities	Belongs to the glycosyltransferase 47 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from mutant phenotype PubMed 16236767. Source: MGI glycosaminoglycan biosynthetic process Inferred from electronic annotation. Source: Compara heparan sulfate proteoglycan biosynthetic process Inferred from mutant phenotype PubMed 16236767. Source: MGI heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Inferred from electronic annotation. Source: Compara mesoderm formation Inferred from mutant phenotype PubMed 16236767. Source: MGI ossification Inferred from electronic annotation. Source: Compara protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred by curator Ref.7. Source: BHF-UCL endoplasmic reticulum membrane Inferred by curator Ref.7. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Inferred by curator Ref.7. Source: BHF-UCL glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Inferred by curator Ref.7. Source: BHF-UCL heparan sulfate N-acetylglucosaminyltransferase activity Inferred by curator Ref.7. Source: BHF-UCL protein homodimerization activity Inferred from direct assay Ref.7. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 718	718	Exostosin-2		PRO_0000149652
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Transmembrane	26 – 46	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	47 – 718	672	Lumenal Potential
Amino acid modifications
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	637	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	62	1	S → T in AAC53143. Ref.2
	Sequence conflict	160	1	L → V in AAC53143. Ref.2
	Sequence conflict	323	1	G → R in AAC53143. Ref.2
	Sequence conflict	355	1	V → I in AAC53143. Ref.2
	Sequence conflict	360	1	R → K in AAC53143. Ref.2
	Sequence conflict	389	1	Q → H in AAC53143. Ref.2
	Sequence conflict	622	1	T → A in AAC53143. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P70428 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 45D947BF6678378B	FASTA	718	82,064
	10 20 30 40 50 60 MCASVKSNIR GPALIPRMKT KHRIYYVTLF SIVLLGLIAT GMFQFWPHSI ESSSDGGVEK 70 80 90 100 110 120 RSIREVPVVR LPTDSPIPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYP LKKYVDDAGV 130 140 150 160 170 180 PVSSAISREY NELLTAISDS DYYTDDINRA CLFVPSIDVL NQNPLRIKET AQALAQLSRW 190 200 210 220 230 240 DRGTNHLLFN MLPGAPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVFSPLSAEM 250 260 270 280 290 300 ALPEKAPGPR RYFLLSSQMA IHPEYREELE ALQAKHQESV LVLDKCTNLS EGVLSVRKRC 310 320 330 340 350 360 HQHQVFDYPQ VLQEATFCTV LRGARLGQAV LSDVLQAGCV PVVIADSYIL PFSEVLDWKR 370 380 390 400 410 420 ASVVVPEEKM SDVYSILQNI PQRQIEEMQR QARWFWEAYF QSIKAIALAT LQIINDRIYP 430 440 450 460 470 480 YAAISYEEWN DPPAVKWASV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF RVITEVSKVP 490 500 510 520 530 540 SLSKLLVVWN NQNKNPPEES LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD 550 560 570 580 590 600 IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY 610 620 630 640 650 660 HKYFNYLYTY KMPGDIKNWV DTHMNCEDIA MNFLVANVTG KAVIKVTPRK KFKCPECTAI 670 680 690 700 710 DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the murine homolog of the human EXT2 multiple exostoses gene." Stickens D.J., Evans G.A. Biochem. Mol. Med. 61:16-21(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The structure of the human multiple exostoses 2 gene and characterization of homologs in mouse and Caenorhabditis elegans." Clines G.A., Ashley J.A., Shah S., Lovett M. Genome Res. 7:359-367(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spinal ganglion.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Mammary gland.
[7]	"The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate." McCormick C., Duncan G., Goutsos K.T., Tufaro F. Proc. Natl. Acad. Sci. U.S.A. 97:668-673(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U72141 mRNA. Translation: AAB17006.1. U67837 mRNA. Translation: AAC53143.1. AK164342 mRNA. Translation: BAE37749.1. AL732493, AL732472 Genomic DNA. Translation: CAM22097.1. AL732472, AL732493 Genomic DNA. Translation: CAM23881.1. CH466519 Genomic DNA. Translation: EDL27629.1. BC006597 mRNA. Translation: AAH06597.1.
IPI	IPI00308075.
RefSeq	NP_034293.2. NM_010163.3.
UniGene	Mm.4336.
3D structure databases
ProteinModelPortal	P70428.
SMR	P70428. Positions 456-690.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29858N.
Protein family/group databases
CAZy	GT47. Glycosyltransferase Family 47. GT64. Glycosyltransferase Family 64.
PTM databases
PhosphoSite	P70428.
Proteomic databases
PaxDb	P70428.
PRIDE	P70428.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028623; ENSMUSP00000028623; ENSMUSG00000027198.
GeneID	14043.
KEGG	mmu:14043.
Organism-specific databases
CTD	2132.
MGI	MGI:108050. Ext2.
Phylogenomic databases
eggNOG	NOG272619.
GeneTree	ENSGT00550000074496.
HOVERGEN	HBG101211.
InParanoid	Q3TPI7.
KO	K02367.
OMA	QFGYEVW.
OrthoDB	EOG41VK2B.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	P70428.
Bgee	P70428.
CleanEx	MM_EXT2.
Genevestigator	P70428.
GermOnline	ENSMUSG00000027198. Mus musculus.
Family and domain databases
InterPro	IPR004263. Exostosin. IPR015338. HexNAc_Trfase_a. [Graphical view]
Pfam	PF03016. Exostosin. 1 hit. PF09258. Glyco_transf_64. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EXT2. mouse.
NextBio	284982.
SOURCE	Search...

Entry information

Entry name

EXT2_MOUSE

Accession

Primary (citable) accession number: P70428
Secondary accession number(s): P70395, Q3TPI7, Q923D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program