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P56558 (OGT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

EC=2.4.1.-
Alternative name(s):
O-GlcNAc transferase subunit p110
O-linked N-acetylglucosamine transferase 110 kDa subunit
Gene names
Name:Ogt
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1036 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Mediates the O-glycosylation of MLL5 and HCFC1. Promotes proteolytic maturation of HCFC1 By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + peptide = UDP + N-acetyl-beta-D-glucosaminyl-peptide.

Enzyme regulation

By tyrosine phosphorylation and O-GlcNAc modifications.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts directly with HCFC1. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT By similarity. Heterotrimer of two 110 kDa and one 78 kDa subunits. It is not known if the 78 kDa subunit is encoded by a separate gene or is the product of either of a proteolytic degradation or an alternative initiation of the 110 kDa subunit. Interacts with ATXN10. Ref.2

Subcellular location

Cytoplasm. Nucleus By similarity. Note: Mostly in the nucleus By similarity. Ref.2

Tissue specificity

Appears to be present in all tissues examined except kidney.

Domain

The TPR repeat domain mediates recognition of protein substrates By similarity.

Post-translational modification

O-glycosylated; contains O-GlcNAc.

Ubiquitinated, leading to its proteasomal degradation By similarity.

Sequence similarities

Belongs to the O-GlcNAc transferase family.

Contains 13 TPR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10361035UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
PRO_0000191774

Regions

Repeat11 – 4434TPR 1
Repeat79 – 11234TPR 2
Repeat113 – 14634TPR 3
Repeat147 – 18034TPR 4
Repeat181 – 21434TPR 5
Repeat215 – 24834TPR 6
Repeat249 – 28234TPR 7
Repeat283 – 31634TPR 8
Repeat317 – 35034TPR 9
Repeat351 – 38434TPR 10
Repeat385 – 41834TPR 11
Repeat419 – 45234TPR 12
Repeat453 – 46311TPR 13; truncated
Nucleotide binding895 – 8984UDP By similarity
Nucleotide binding901 – 9044UDP By similarity
Nucleotide binding919 – 9213UDP By similarity
Motif478 – 49316Nuclear localization signal Potential

Sites

Active site4981Proton acceptor By similarity
Binding site8391UDP By similarity
Binding site8421UDP By similarity
Binding site9251UDP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue9791Phosphotyrosine Probable

Sequences

Sequence LengthMass (Da)Tools
P56558 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: 3F057CABDD019BD6

FASTA1,036115,606
        10         20         30         40         50         60 
MASSVGNVAD STGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL LSSIHFQCRR 

        70         80         90        100        110        120 
LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP DFIDGYINLA 

       130        140        150        160        170        180 
AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF 

       190        200        210        220        230        240 
AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR 

       250        260        270        280        290        300 
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA NALKEKGSVA 

       310        320        330        340        350        360 
EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF AAAHSNLASV 

       370        380        390        400        410        420 
LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR AIQINPAFAD 

       430        440        450        460        470        480 
AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV 

       490        500        510        520        530        540 
SIVAEQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK 

       550        560        570        580        590        600 
LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN FRVKVMAEAN 

       610        620        630        640        650        660 
HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA MWLGYPGTSG 

       670        680        690        700        710        720 
ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY 

       730        740        750        760        770        780 
DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADTTNT ALNMPVIPMN TIAEAVIEMI 

       790        800        810        820        830        840 
NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL 

       850        860        870        880        890        900 
YKIDPSTLQM GANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI IFSPVAPKEE 

       910        920        930        940        950        960 
HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL TCLGCLELIA 

       970        980        990       1000       1010       1020 
KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY LQMWEHYAAG 

      1030 
NKPDHMIKPV EVTESA 

« Hide

References

[1]"Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats."
Kreppel L.K., Blomberg M.A., Hart G.W.
J. Biol. Chem. 272:9308-9315(1997) [PubMed: 9083067] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain."
Maerz P., Stetefeld J., Bendfeldt K., Nitsch C., Reinstein J., Shoeman R.L., Dimitriades-Schmutz B., Schwager M., Leiser D., Ozcan S., Otten U., Ozbek S.
J. Biol. Chem. 281:20263-20270(2006) [PubMed: 16714295] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ATXN10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76557 mRNA. Translation: AAC53121.1.
IPIIPI00231503.
PIRT31673.
RefSeqNP_058803.2. NM_017107.2.
UniGeneRn.82705.

3D structure databases

ProteinModelPortalP56558.
SMRP56558. Positions 13-400.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56558.

Protein family/group databases

CAZyGT41. Glycosyltransferase Family 41.

PTM databases

PhosphoSiteP56558.

Proteomic databases

PRIDEP56558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID26295.
KEGGrno:26295.
UCSCNM_017107. rat.

Organism-specific databases

CTD8473.
RGD62060. Ogt.

Phylogenomic databases

eggNOGroNOG07233.
GeneTreeENSGT00550000074327.
HOVERGENHBG000351.
InParanoidP56558.
OrthoDBEOG4HQDHJ.
PhylomeDBP56558.

Enzyme and pathway databases

BRENDA2.4.1.94. 5301.

Gene expression databases

ArrayExpressP56558.
GenevestigatorP56558.
GermOnlineENSRNOG00000003359. Rattus norvegicus.

Family and domain databases

InterProIPR001440. TPR-1.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 2 hits.
KOK09667.
PfamPF00515. TPR_1. 10 hits.
[Graphical view]
SMARTSM00028. TPR. 11 hits.
[Graphical view]
PROSITEPS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608004.

Entry information

Entry nameOGT1_RAT
AccessionPrimary (citable) accession number: P56558
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 16, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families