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Protein

EGF domain-specific O-linked N-acetylglucosamine transferase

Gene

EOGT

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

Functioni

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.1 Publication

Catalytic activityi

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGT61. Glycosyltransferase Family 61.

Names & Taxonomyi

Protein namesi
Recommended name:
EGF domain-specific O-linked N-acetylglucosamine transferase (EC:2.4.1.255)
Alternative name(s):
Extracellular O-linked N-acetylglucosamine transferase
Gene namesi
Name:EOGT
Synonyms:AER61, C3orf64, EOGT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:28526. EOGT.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Adams-Oliver syndrome 4 (AOS4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:615297
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071W → S in AOS4. 1 Publication
VAR_070090
Natural varianti377 – 3771R → Q in AOS4. 1 Publication
VAR_070091

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi295 – 2973DYD → AYA: Partial loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615297. phenotype.
Orphaneti974. Adams-Oliver syndrome.
PharmGKBiPA143485338.

Polymorphism and mutation databases

BioMutaiEOGT.
DMDMi74708096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 527510EGF domain-specific O-linked N-acetylglucosamine transferasePRO_0000301970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ5NDL2.
PaxDbiQ5NDL2.
PRIDEiQ5NDL2.

PTM databases

PhosphoSiteiQ5NDL2.

Expressioni

Gene expression databases

BgeeiQ5NDL2.
CleanExiHS_C3orf64.
ExpressionAtlasiQ5NDL2. baseline and differential.
GenevestigatoriQ5NDL2.

Organism-specific databases

HPAiHPA019460.

Interactioni

Protein-protein interaction databases

BioGridi130045. 8 interactions.
IntActiQ5NDL2. 1 interaction.
STRINGi9606.ENSP00000295571.

Structurei

3D structure databases

ProteinModelPortaliQ5NDL2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi295 – 2973Required for optimal activity
Motifi524 – 5274Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyltransferase 61 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG320328.
GeneTreeiENSGT00770000120599.
HOGENOMiHOG000033829.
HOVERGENiHBG056678.
InParanoidiQ5NDL2.
KOiK18134.
OMAiDSKRVCF.
OrthoDBiEOG7D2FDQ.
PhylomeDBiQ5NDL2.
TreeFamiTF313716.

Family and domain databases

InterProiIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamiPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5NDL2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLMLFVFGVL LHEVSLSGQN EAPPNTHSIP GEPLYNYASI RLPEEHIPFF
60 70 80 90 100
LHNNRHIATV CRKDSLCPYK KHLEKLKYCW GYEKSCKPEF RFGYPVCSYV
110 120 130 140 150
DMGWTDTLES AEDIFWKQAD FGYARERLEE MHVLCQPKET SDSSLVCSRY
160 170 180 190 200
LQYCRATNLY LDLRNIKRNH DRFKEDFFQS GEIGGHCKLD IRTLTSEGQR
210 220 230 240 250
KSPLQSWFAE LQSYTQLNFR PIEDAKCDIV IEKPTYFMKL DAGVNMYHHF
260 270 280 290 300
CDFINLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW NAFTDYDVIH
310 320 330 340 350
LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFAQHVL
360 370 380 390 400
HRLNITQEGP KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV
410 420 430 440 450
DYKYRELGFL DQLRITHNTD IFIGMHGAGL THLLFLPDWA AVFELYNCED
460 470 480 490 500
ERCYLDLARL RGVHYITWRR QNKVFPQDKG HHPTLGEHPK FTNYSFDVEE
510 520
FMYLVLQAAD HVLQHPKWPF KKKHDEL
Length:527
Mass (Da):62,011
Last modified:February 1, 2005 - v1
Checksum:iC34D267187BFDDA9
GO
Isoform 2 (identifier: Q5NDL2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: F → C
     209-527: Missing.

Show »
Length:208
Mass (Da):24,403
Checksum:i387DDF61D5A96C3A
GO
Isoform 3 (identifier: Q5NDL2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-361: Missing.

Note: No experimental confirmation available.

Show »
Length:443
Mass (Da):52,297
Checksum:iEB338AE6E854889F
GO

Sequence cautioni

The sequence BAF83045.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG57436.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991Q → R in BAC86479 (PubMed:14702039).Curated
Sequence conflicti247 – 2471Y → C in CAE45897 (PubMed:17974005).Curated
Sequence conflicti287 – 2871S → F in BAG57436 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071W → S in AOS4. 1 Publication
VAR_070090
Natural varianti377 – 3771R → Q in AOS4. 1 Publication
VAR_070091

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei208 – 2081F → C in isoform 2. 1 PublicationVSP_027897
Alternative sequencei209 – 527319Missing in isoform 2. 1 PublicationVSP_027898Add
BLAST
Alternative sequencei278 – 36184Missing in isoform 3. 1 PublicationVSP_027899Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2908.1. [Q5NDL2-3]
CCDS63684.1. [Q5NDL2-1]
RefSeqiNP_001265618.1. NM_001278689.1. [Q5NDL2-1]
NP_775925.1. NM_173654.2. [Q5NDL2-3]
XP_005264800.1. XM_005264743.2. [Q5NDL2-1]
UniGeneiHs.518059.

Genome annotation databases

EnsembliENST00000295571; ENSP00000295571; ENSG00000163378. [Q5NDL2-3]
ENST00000383701; ENSP00000373206; ENSG00000163378. [Q5NDL2-1]
ENST00000540764; ENSP00000443780; ENSG00000163378. [Q5NDL2-1]
ENST00000540955; ENSP00000444264; ENSG00000163378. [Q5NDL2-3]
GeneIDi285203.
KEGGihsa:285203.
UCSCiuc003dnk.3. human. [Q5NDL2-3]
uc003dnl.3. human. [Q5NDL2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2908.1. [Q5NDL2-3]
CCDS63684.1. [Q5NDL2-1]
RefSeqiNP_001265618.1. NM_001278689.1. [Q5NDL2-1]
NP_775925.1. NM_173654.2. [Q5NDL2-3]
XP_005264800.1. XM_005264743.2. [Q5NDL2-1]
UniGeneiHs.518059.

3D structure databases

ProteinModelPortaliQ5NDL2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130045. 8 interactions.
IntActiQ5NDL2. 1 interaction.
STRINGi9606.ENSP00000295571.

Protein family/group databases

CAZyiGT61. Glycosyltransferase Family 61.

PTM databases

PhosphoSiteiQ5NDL2.

Polymorphism and mutation databases

BioMutaiEOGT.
DMDMi74708096.

Proteomic databases

MaxQBiQ5NDL2.
PaxDbiQ5NDL2.
PRIDEiQ5NDL2.

Protocols and materials databases

DNASUi285203.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295571; ENSP00000295571; ENSG00000163378. [Q5NDL2-3]
ENST00000383701; ENSP00000373206; ENSG00000163378. [Q5NDL2-1]
ENST00000540764; ENSP00000443780; ENSG00000163378. [Q5NDL2-1]
ENST00000540955; ENSP00000444264; ENSG00000163378. [Q5NDL2-3]
GeneIDi285203.
KEGGihsa:285203.
UCSCiuc003dnk.3. human. [Q5NDL2-3]
uc003dnl.3. human. [Q5NDL2-1]

Organism-specific databases

CTDi285203.
GeneCardsiGC03M069025.
HGNCiHGNC:28526. EOGT.
HPAiHPA019460.
MIMi614789. gene.
615297. phenotype.
neXtProtiNX_Q5NDL2.
Orphaneti974. Adams-Oliver syndrome.
PharmGKBiPA143485338.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG320328.
GeneTreeiENSGT00770000120599.
HOGENOMiHOG000033829.
HOVERGENiHBG056678.
InParanoidiQ5NDL2.
KOiK18134.
OMAiDSKRVCF.
OrthoDBiEOG7D2FDQ.
PhylomeDBiQ5NDL2.
TreeFamiTF313716.

Miscellaneous databases

GenomeRNAii285203.
NextBioi35463951.
PROiQ5NDL2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5NDL2.
CleanExiHS_C3orf64.
ExpressionAtlasiQ5NDL2. baseline and differential.
GenevestigatoriQ5NDL2.

Family and domain databases

InterProiIPR007657. Glycosyltransferase_AER61.
[Graphical view]
PfamiPF04577. DUF563. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-527 (ISOFORM 1).
    Tissue: Esophageal carcinoma.
  7. Cited for: VARIANTS AOS4 SER-207 AND GLN-377.

Entry informationi

Entry nameiEOGT_HUMAN
AccessioniPrimary (citable) accession number: Q5NDL2
Secondary accession number(s): A8K2U1
, B4DFH5, L7X1M5, Q6MZY0, Q6P985, Q6ZTV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 1, 2005
Last modified: April 29, 2015
This is version 80 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.