Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5NDL2 (EOGT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EGF domain-specific O-linked N-acetylglucosamine transferase

EC=2.4.1.255
Alternative name(s):
Extracellular O-linked N-acetylglucosamine transferase
Gene names
Name:EOGT
Synonyms:AER61, C3orf64, EOGT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains. Ref.1

Catalytic activity

UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine.

UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Involvement in disease

Adams-Oliver syndrome 4 (AOS4) [MIM:615297]: A form of Adams-Oliver syndrome, a disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 61 family.

Sequence caution

The sequence BAF83045.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG57436.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein O-linked glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein N-acetylglucosaminyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5NDL2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5NDL2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: F → C
     209-527: Missing.
Isoform 3 (identifier: Q5NDL2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     278-361: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 527510EGF domain-specific O-linked N-acetylglucosamine transferase
PRO_0000301970

Regions

Motif295 – 2973Required for optimal activity
Motif524 – 5274Prevents secretion from ER Potential

Amino acid modifications

Glycosylation3541N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence2081F → C in isoform 2.
VSP_027897
Alternative sequence209 – 527319Missing in isoform 2.
VSP_027898
Alternative sequence278 – 36184Missing in isoform 3.
VSP_027899
Natural variant2071W → S in AOS4. Ref.7
VAR_070090
Natural variant3771R → Q in AOS4. Ref.7
VAR_070091

Experimental info

Mutagenesis295 – 2973DYD → AYA: Partial loss of activity. Ref.1
Sequence conflict1991Q → R in BAC86479. Ref.3
Sequence conflict2471Y → C in CAE45897. Ref.6
Sequence conflict2871S → F in BAG57436. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: C34D267187BFDDA9

FASTA52762,011
        10         20         30         40         50         60 
MLMLFVFGVL LHEVSLSGQN EAPPNTHSIP GEPLYNYASI RLPEEHIPFF LHNNRHIATV 

        70         80         90        100        110        120 
CRKDSLCPYK KHLEKLKYCW GYEKSCKPEF RFGYPVCSYV DMGWTDTLES AEDIFWKQAD 

       130        140        150        160        170        180 
FGYARERLEE MHVLCQPKET SDSSLVCSRY LQYCRATNLY LDLRNIKRNH DRFKEDFFQS 

       190        200        210        220        230        240 
GEIGGHCKLD IRTLTSEGQR KSPLQSWFAE LQSYTQLNFR PIEDAKCDIV IEKPTYFMKL 

       250        260        270        280        290        300 
DAGVNMYHHF CDFINLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW NAFTDYDVIH 

       310        320        330        340        350        360 
LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFAQHVL HRLNITQEGP 

       370        380        390        400        410        420 
KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV DYKYRELGFL DQLRITHNTD 

       430        440        450        460        470        480 
IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG 

       490        500        510        520 
HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKHDEL 

« Hide

Isoform 2 [UniParc].

Checksum: 387DDF61D5A96C3A
Show »

FASTA20824,403
Isoform 3 [UniParc].

Checksum: EB338AE6E854889F
Show »

FASTA44352,297

References

« Hide 'large scale' references
[1]"The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with Notch signaling and pyrimidine metabolism pathways in Drosophila."
Muller R., Jenny A., Stanley P.
PLoS ONE 8:E62835-E62835(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF 295-ASP--ASP-297.
Tissue: Embryonic kidney.
[2]"Phylogeny of xylosyltransferases."
Kiefer-Meyer M.C., Pagny S., Durambure G., Faye L., Gomord V., Mollicone R., Oriol R.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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] (ISOFORM 2).
Tissue: Brain cortex, Thymus and Tongue.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 102-527.
[5]"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] (ISOFORM 3).
Tissue: Placenta.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-527 (ISOFORM 1).
Tissue: Esophageal carcinoma.
[7]"Mutations in EOGT confirm the genetic heterogeneity of autosomal-recessive Adams-Oliver syndrome."
Shaheen R., Aglan M., Keppler-Noreuil K., Faqeih E., Ansari S., Horton K., Ashour A., Zaki M.S., Al-Zahrani F., Cueto-Gonzalez A.M., Abdel-Salam G., Temtamy S., Alkuraya F.S.
Am. J. Hum. Genet. 92:598-604(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AOS4 SER-207 AND GLN-377.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
KC347596 mRNA. Translation: AGC92970.1.
AJ868234 mRNA. Translation: CAI30569.1.
AK126187 mRNA. Translation: BAC86479.1.
AK290356 mRNA. Translation: BAF83045.1. Different initiation.
AK294101 mRNA. Translation: BAG57436.1. Different initiation.
AC109587 Genomic DNA. No translation available.
BC060887 mRNA. Translation: AAH60887.1.
BX640821 mRNA. Translation: CAE45897.2.
CCDSCCDS2908.1. [Q5NDL2-3]
CCDS63684.1. [Q5NDL2-1]
RefSeqNP_001265618.1. NM_001278689.1. [Q5NDL2-1]
NP_775925.1. NM_173654.2. [Q5NDL2-3]
XP_005264800.1. XM_005264743.1. [Q5NDL2-1]
XP_005264801.1. XM_005264744.1. [Q5NDL2-1]
XP_006713174.1. XM_006713111.1. [Q5NDL2-1]
UniGeneHs.518059.

3D structure databases

ProteinModelPortalQ5NDL2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130045. 1 interaction.
STRING9606.ENSP00000295571.

Protein family/group databases

CAZyGT61. Glycosyltransferase Family 61.

PTM databases

PhosphoSiteQ5NDL2.

Polymorphism databases

DMDM74708096.

Proteomic databases

MaxQBQ5NDL2.
PaxDbQ5NDL2.
PRIDEQ5NDL2.

Protocols and materials databases

DNASU285203.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295571; ENSP00000295571; ENSG00000163378. [Q5NDL2-3]
ENST00000383701; ENSP00000373206; ENSG00000163378. [Q5NDL2-1]
ENST00000540764; ENSP00000443780; ENSG00000163378.
GeneID285203.
KEGGhsa:285203.
UCSCuc003dnk.3. human. [Q5NDL2-3]
uc003dnl.3. human. [Q5NDL2-1]

Organism-specific databases

CTD285203.
GeneCardsGC03M069025.
HGNCHGNC:28526. EOGT.
HPAHPA019460.
MIM614789. gene.
615297. phenotype.
neXtProtNX_Q5NDL2.
Orphanet974. Adams-Oliver syndrome.
PharmGKBPA143485338.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320328.
HOGENOMHOG000033829.
HOVERGENHBG056678.
InParanoidQ5NDL2.
KOK18134.
OMADSKRVCF.
OrthoDBEOG7D2FDQ.
PhylomeDBQ5NDL2.
TreeFamTF313716.

Gene expression databases

ArrayExpressQ5NDL2.
BgeeQ5NDL2.
CleanExHS_C3orf64.
GenevestigatorQ5NDL2.

Family and domain databases

InterProIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi285203.
NextBio35463951.
PROQ5NDL2.
SOURCESearch...

Entry information

Entry nameEOGT_HUMAN
AccessionPrimary (citable) accession number: Q5NDL2
Secondary accession number(s): A8K2U1 expand/collapse secondary AC list , B4DFH5, L7X1M5, Q6MZY0, Q6P985, Q6ZTV0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 1, 2005
Last modified: July 9, 2014
This is version 74 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM