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Protein

Exostosin-like 2

Gene

EXTL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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.

Cofactori

Mn2+By similarity

Pathway: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei53 – 542Cleavage
Binding sitei100 – 1001SubstrateBy similarity
Metal bindingi152 – 1521Manganese; catalyticBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Active sitei245 – 2451By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08719-MONOMER.
UniPathwayiUPA00756.

Protein family/group databases

CAZyiGT64. Glycosyltransferase Family 64.

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:EXTL2
Synonyms:EXTR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3516. EXTL2.

Subcellular locationi

Processed exostosin-like 2 :
  • Secreted

  • Note: A soluble form is found in the serum.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei23 – 4321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini44 – 330287LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: BHF-UCL
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27928.

Polymorphism and mutation databases

BioMutaiEXTL2.
DMDMi9296986.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 330Processed exostosin-like 2PRO_0000296227
Chaini1 – 330330Exostosin-like 2PRO_0000149655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)
Disulfide bondi243 ↔ 296By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9UBQ6.
PaxDbiQ9UBQ6.
PRIDEiQ9UBQ6.

PTM databases

PhosphoSiteiQ9UBQ6.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9UBQ6.
CleanExiHS_EXTL2.
ExpressionAtlasiQ9UBQ6. baseline and differential.
GenevisibleiQ9UBQ6. HS.

Organism-specific databases

HPAiCAB020716.

Interactioni

Protein-protein interaction databases

BioGridi108436. 4 interactions.
STRINGi9606.ENSP00000359131.

Structurei

3D structure databases

ProteinModelPortaliQ9UBQ6.
SMRiQ9UBQ6. Positions 63-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1346Substrate bindingBy similarity
Regioni150 – 1523Substrate bindingBy similarity
Regioni241 – 2455Substrate bindingBy similarity
Regioni280 – 29314Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276916.
GeneTreeiENSGT00550000074496.
HOGENOMiHOG000054215.
HOVERGENiHBG051525.
InParanoidiQ9UBQ6.
KOiK02369.
OMAiFPSYANH.
OrthoDBiEOG7SV0VP.
PhylomeDBiQ9UBQ6.
TreeFamiTF314231.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR015338. EXT_C.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UBQ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCCHICKLP GRVMGIRVLR LSLVVILVLL LVAGALTALL PSVKEDKMLM
60 70 80 90 100
LRREIKSQGK STMDSFTLIM QTYNRTDLLL KLLNHYQAVP NLHKVIVVWN
110 120 130 140 150
NIGEKAPDEL WNSLGPHPIP VIFKQQTANR MRNRLQVFPE LETNAVLMVD
160 170 180 190 200
DDTLISTPDL VFAFSVWQQF PDQIVGFVPR KHVSTSSGIY SYGSFEMQAP
210 220 230 240 250
GSGNGDQYSM VLIGASFFNS KYLELFQRQP AAVHALIDDT QNCDDIAMNF
260 270 280 290 300
IIAKHIGKTS GIFVKPVNMD NLEKETNSGY SGMWHRAEHA LQRSYCINKL
310 320 330
VNIYDSMPLR YSNIMISQFG FPYANYKRKI
Length:330
Mass (Da):37,466
Last modified:May 1, 2000 - v1
Checksum:i6976BE7EC6F588C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS775.1.
PIRiJC5935.
RefSeqiNP_001028197.1. NM_001033025.2.
NP_001430.1. NM_001439.3.
XP_005270678.1. XM_005270621.1.
UniGeneiHs.357637.

Genome annotation databases

EnsembliENST00000370113; ENSP00000359131; ENSG00000162694.
ENST00000370114; ENSP00000359132; ENSG00000162694.
GeneIDi2135.
KEGGihsa:2135.
UCSCiuc001dtk.2. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Exostosin-like 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS775.1.
PIRiJC5935.
RefSeqiNP_001028197.1. NM_001033025.2.
NP_001430.1. NM_001439.3.
XP_005270678.1. XM_005270621.1.
UniGeneiHs.357637.

3D structure databases

ProteinModelPortaliQ9UBQ6.
SMRiQ9UBQ6. Positions 63-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108436. 4 interactions.
STRINGi9606.ENSP00000359131.

Protein family/group databases

CAZyiGT64. Glycosyltransferase Family 64.

PTM databases

PhosphoSiteiQ9UBQ6.

Polymorphism and mutation databases

BioMutaiEXTL2.
DMDMi9296986.

Proteomic databases

MaxQBiQ9UBQ6.
PaxDbiQ9UBQ6.
PRIDEiQ9UBQ6.

Protocols and materials databases

DNASUi2135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370113; ENSP00000359131; ENSG00000162694.
ENST00000370114; ENSP00000359132; ENSG00000162694.
GeneIDi2135.
KEGGihsa:2135.
UCSCiuc001dtk.2. human.

Organism-specific databases

CTDi2135.
GeneCardsiGC01M101337.
HGNCiHGNC:3516. EXTL2.
HPAiCAB020716.
MIMi602411. gene.
neXtProtiNX_Q9UBQ6.
PharmGKBiPA27928.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG276916.
GeneTreeiENSGT00550000074496.
HOGENOMiHOG000054215.
HOVERGENiHBG051525.
InParanoidiQ9UBQ6.
KOiK02369.
OMAiFPSYANH.
OrthoDBiEOG7SV0VP.
PhylomeDBiQ9UBQ6.
TreeFamiTF314231.

Enzyme and pathway databases

UniPathwayiUPA00756.
BioCyciMetaCyc:HS08719-MONOMER.

Miscellaneous databases

ChiTaRSiEXTL2. human.
GeneWikiiEXTL2.
GenomeRNAii2135.
NextBioi8627.
PROiQ9UBQ6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBQ6.
CleanExiHS_EXTL2.
ExpressionAtlasiQ9UBQ6. baseline and differential.
GenevisibleiQ9UBQ6. HS.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR015338. EXT_C.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiEXTL2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBQ6
Secondary accession number(s): B2R795, D3DT60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.