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Q9UBQ6 (EXTL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exostosin-like 2

EC=2.4.1.223
Alternative name(s):
Alpha-1,4-N-acetylhexosaminyltransferase EXTL2
Alpha-GalNAcT EXTL2
EXT-related protein 2
Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase

Cleaved into the following chain:

  1. Processed exostosin-like 2
Gene names
Name:EXTL2
Synonyms:EXTR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains. Ref.4

Catalytic activity

UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan.

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity Ref.3.

Processed exostosin-like 2: Secreted. Note: A soluble form is found in the serum. Ref.3

Tissue specificity

Ubiquitous.

Post-translational modification

The soluble form derives from the membrane form by proteolytic processing.

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Exostosin-like 2
PRO_0000149655
Chain? – 330Processed exostosin-like 2PRO_0000296227

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain44 – 330287Lumenal Potential

Sites

Metal binding1521Manganese; catalytic By similarity
Site53 – 542Cleavage

Amino acid modifications

Glycosylation741N-linked (GlcNAc...)
Disulfide bond243 ↔ 296 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UBQ6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6976BE7EC6F588C8

FASTA33037,466
        10         20         30         40         50         60 
MRCCHICKLP GRVMGIRVLR LSLVVILVLL LVAGALTALL PSVKEDKMLM LRREIKSQGK 

        70         80         90        100        110        120 
STMDSFTLIM QTYNRTDLLL KLLNHYQAVP NLHKVIVVWN NIGEKAPDEL WNSLGPHPIP 

       130        140        150        160        170        180 
VIFKQQTANR MRNRLQVFPE LETNAVLMVD DDTLISTPDL VFAFSVWQQF PDQIVGFVPR 

       190        200        210        220        230        240 
KHVSTSSGIY SYGSFEMQAP GSGNGDQYSM VLIGASFFNS KYLELFQRQP AAVHALIDDT 

       250        260        270        280        290        300 
QNCDDIAMNF IIAKHIGKTS GIFVKPVNMD NLEKETNSGY SGMWHRAEHA LQRSYCINKL 

       310        320        330 
VNIYDSMPLR YSNIMISQFG FPYANYKRKI 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel member of the EXT gene family, EXTL2."
Wuyts W., Van Hul W., Hendrickx J., Speleman F., Wauters J., De Boulle K., Van Roy N., Van Agtmael T., Bossuyt P., Willems P.J.
Eur. J. Hum. Genet. 5:382-389(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family."
Saito T., Seki N., Yamauchi M., Tsuji S., Hayashi A., Kozuma S., Hori T.-A.
Biochem. Biophys. Res. Commun. 243:61-66(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: SUBCELLULAR LOCATION.
[4]"The tumor suppressor EXT-like gene EXTL2 encodes an alpha1, 4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate."
Kitagawa H., Shimakawa H., Sugahara K.
J. Biol. Chem. 274:13933-13937(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROTEIN SEQUENCE OF 54-83.
[5]"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. expand/collapse author list , 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].
Tissue: Amygdala.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Exostosin-like 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF000416 mRNA. Translation: AAC02898.1.
AB009284 mRNA. Translation: BAA24081.1.
AK312895 mRNA. Translation: BAG35742.1.
CH471097 Genomic DNA. Translation: EAW72946.1.
CH471097 Genomic DNA. Translation: EAW72948.1.
CCDSCCDS775.1.
PIRJC5935.
RefSeqNP_001028197.1. NM_001033025.2.
NP_001430.1. NM_001439.3.
XP_005270678.1. XM_005270621.1.
UniGeneHs.357637.

3D structure databases

ProteinModelPortalQ9UBQ6.
SMRQ9UBQ6. Positions 63-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000359131.

Protein family/group databases

CAZyGT64. Glycosyltransferase Family 64.

PTM databases

PhosphoSiteQ9UBQ6.

Polymorphism databases

DMDM9296986.

Proteomic databases

MaxQBQ9UBQ6.
PaxDbQ9UBQ6.
PRIDEQ9UBQ6.

Protocols and materials databases

DNASU2135.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370113; ENSP00000359131; ENSG00000162694.
ENST00000370114; ENSP00000359132; ENSG00000162694.
GeneID2135.
KEGGhsa:2135.
UCSCuc001dtk.2. human.

Organism-specific databases

CTD2135.
GeneCardsGC01M101337.
HGNCHGNC:3516. EXTL2.
HPACAB020716.
MIM602411. gene.
neXtProtNX_Q9UBQ6.
PharmGKBPA27928.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276916.
HOGENOMHOG000054215.
HOVERGENHBG051525.
InParanoidQ9UBQ6.
KOK02369.
OMAHICKLPG.
OrthoDBEOG7SV0VP.
PhylomeDBQ9UBQ6.
TreeFamTF314231.

Enzyme and pathway databases

BioCycMetaCyc:HS08719-MONOMER.
UniPathwayUPA00756.

Gene expression databases

ArrayExpressQ9UBQ6.
BgeeQ9UBQ6.
CleanExHS_EXTL2.
GenevestigatorQ9UBQ6.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR004263. Exostosin.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR11062. PTHR11062. 1 hit.
PfamPF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEXTL2. human.
GeneWikiEXTL2.
GenomeRNAi2135.
NextBio8627.
PROQ9UBQ6.
SOURCESearch...

Entry information

Entry nameEXTL2_HUMAN
AccessionPrimary (citable) accession number: Q9UBQ6
Secondary accession number(s): B2R795, D3DT60
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM