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O01705

- EXT2_CAEEL

UniProt

O01705 - EXT2_CAEEL

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Protein

Exostosin-2

Gene

rib-2

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Probable alpha1,4-N-acetylglucosaminyltransferase required for the biosynthesis of heparan-sulfate.By similarity

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.
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.

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei595 – 5951SubstrateBy similarity
Metal bindingi643 – 6431Manganese; catalyticBy similarity
Binding sitei671 – 6711SubstrateBy similarity
Active sitei728 – 7281By similarity

GO - Molecular functioni

  1. acetylglucosaminyltransferase activity Source: WormBase
  2. enzyme binding Source: WormBase
  3. glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  4. glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  5. heparan sulfate N-acetylglucosaminyltransferase activity Source: WormBase

GO - Biological processi

  1. embryonic morphogenesis Source: WormBase
  2. heparan sulfate proteoglycan biosynthetic process Source: WormBase
  3. pharynx development Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_197732. XBP1(S) activates chaperone genes.
UniPathwayiUPA00756.

Protein family/group databases

CAZyiGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Names & Taxonomyi

Protein namesi
Recommended name:
Exostosin-2 (EC:2.4.1.223, EC:2.4.1.224)
Alternative name(s):
Glucuronyl-galactosyl-proteoglycan/Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Multiple exostoses homolog 2
Gene namesi
Name:rib-2
ORF Names:K01G5.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome III

Organism-specific databases

WormBaseiK01G5.6; CE16196; WBGene00004361; rib-2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei15 – 3521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 814779LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. intrinsic component of endoplasmic reticulum membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 814814Exostosin-2PRO_0000149663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi726 ↔ 774By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO01705.

Interactioni

Protein-protein interaction databases

BioGridi41689. 1 interaction.
STRINGi6239.K01G5.6.

Structurei

3D structure databases

ProteinModelPortaliO01705.
SMRiO01705. Positions 559-790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni620 – 6256Substrate bindingBy similarity
Regioni641 – 6433Substrate bindingBy similarity
Regioni724 – 7285Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG243446.
GeneTreeiENSGT00550000074496.
HOGENOMiHOG000007975.
InParanoidiO01705.
KOiK02370.
OMAiWDRIETE.
OrthoDBiEOG7PZRWK.
PhylomeDBiO01705.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027674. EXO3/EXOL3.
IPR004263. Exostosin.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF57. PTHR11062:SF57. 1 hit.
PfamiPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

O01705-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAIKLNGSSR SFVPSLRVSA FLIFIFFVIT YIIIYNVSFS EPSWITQDAL
60 70 80 90 100
KQNIENLDDY DASCSGYSIG RILREQKRIL ASVRLELTES QVKIEEIRTV
110 120 130 140 150
QEELQRLIPQ KQLELSALEG EIEAAQRQLE ELRETQNVKV FLPFSPLQIP
160 170 180 190 200
RELEQPSQIS PNQLDDIIDY SRCSISSFMP VYVDIITSGQ SEKEWLNVFQ
210 220 230 240 250
EVIPNLVETP DKACIKIHIS NGIASPNTTF NSILFNVGSP IINFQSKSIH
260 270 280 290 300
VQASKIRSFD FPVDVNHIAV EKVDLTPLLP FQRENLISLI VDNTELNFSA
310 320 330 340 350
FSSLSAEPSR RPIVIVKCSQ ENCSLERRRQ LIGSSTFCFL LPSEMFFQDF
360 370 380 390 400
LSSLQLGCIP IILSNSQLLP FQDLIDWRRA TYRLPLARLP EAHFIVQSFE
410 420 430 440 450
ISDIIEMRRV GRLFYETYLA DRHLLARSLL AALRYKLQIP TREVRRNQAI
460 470 480 490 500
PLFNSSFTAP KGSVVNVQAN FDDEYLLGPL ESRVESTSYA YNFTEFQLYS
510 520 530 540 550
YDFWNIIMSP HYTKEFLVNA AELPTEAEFF EDTKIGFRPI EPGSGAEFSK
560 570 580 590 600
ALGGNRQREQ FTVVLLTYER DAVLTGALER LHQLPYLNKI IVVWNNVNRD
610 620 630 640 650
PPDTWPSLHI PVEFIRVAEN NLNNRFVPWD RIETEAVLSL DDDIDLMQQE
660 670 680 690 700
IILAFRVWRE NRDRIVGFPA RHHARYGDSM FYNSNHTCQM SMILTGAAFI
710 720 730 740 750
HKNYLTAYTY EMPAEIREHV NSIKNCEDIA MNYLVSHLTR KPPIKTTSRW
760 770 780 790 800
TLKCPTCTES LYKEGTHFEK RHECMRLFTK IYGYNPLKFS QFRADSILFK
810
TRLPQNHQKC FKYV
Length:814
Mass (Da):94,197
Last modified:March 27, 2002 - v2
Checksum:i38FA58C5EB17DB16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti604 – 6041T → S in AAC47510. (PubMed:9110175)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94835 mRNA. Translation: AAC47510.1.
AB077851 mRNA. Translation: BAB83878.1.
Z92803 Genomic DNA. Translation: CAB07245.1.
PIRiT23200.
RefSeqiNP_499368.1. NM_066967.6.
UniGeneiCel.17904.

Genome annotation databases

EnsemblMetazoaiK01G5.6; K01G5.6; WBGene00004361.
GeneIDi176502.
KEGGicel:CELE_K01G5.6.
UCSCiK01G5.6. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94835 mRNA. Translation: AAC47510.1 .
AB077851 mRNA. Translation: BAB83878.1 .
Z92803 Genomic DNA. Translation: CAB07245.1 .
PIRi T23200.
RefSeqi NP_499368.1. NM_066967.6.
UniGenei Cel.17904.

3D structure databases

ProteinModelPortali O01705.
SMRi O01705. Positions 559-790.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 41689. 1 interaction.
STRINGi 6239.K01G5.6.

Protein family/group databases

CAZyi GT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Proteomic databases

PRIDEi O01705.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai K01G5.6 ; K01G5.6 ; WBGene00004361 .
GeneIDi 176502.
KEGGi cel:CELE_K01G5.6.
UCSCi K01G5.6. c. elegans.

Organism-specific databases

CTDi 176502.
WormBasei K01G5.6 ; CE16196 ; WBGene00004361 ; rib-2.

Phylogenomic databases

eggNOGi NOG243446.
GeneTreei ENSGT00550000074496.
HOGENOMi HOG000007975.
InParanoidi O01705.
KOi K02370.
OMAi WDRIETE.
OrthoDBi EOG7PZRWK.
PhylomeDBi O01705.

Enzyme and pathway databases

UniPathwayi UPA00756 .
Reactomei REACT_197732. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi 892848.
PROi O01705.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027674. EXO3/EXOL3.
IPR004263. Exostosin.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR11062. PTHR11062. 1 hit.
PTHR11062:SF57. PTHR11062:SF57. 1 hit.
Pfami PF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel alpha1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate."
    Kitagawa H., Egusa N., Tamura J., Kusche-Gullberg M., Lindahl U., Sugahara K.
    J. Biol. Chem. 276:4834-4838(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiEXT2_CAEEL
AccessioniPrimary (citable) accession number: O01705
Secondary accession number(s): O17920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 27, 2002
Last modified: November 26, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3