UniProtKB - Q8CGY8 (OGT1_MOUSE)
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Ogt
Functioni
Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:29465778).
Glycosylates a large and diverse number of proteins including histone H2B, AKT1, ATG4B, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination (By similarity).
Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling (By similarity).
Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (By similarity).
Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2 (PubMed:23337503, PubMed:23395176).
O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (By similarity).
Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity).
Glycosylates HOXA1 (PubMed:29465778).
O-glycosylates FNIP1 (By similarity).
Promotes autophagy by mediating O-glycosylation of ATG4B (By similarity).
By similarity3 PublicationsCatalytic activityi
- L-seryl-[protein] + UDP-N-acetyl-α-D-glucosamine = 3-O-(N-acetyl-β-D-glucosaminyl)-L-seryl-[protein] + H+ + UDPBy similarityEC:2.4.1.255By similarity
- L-threonyl-[protein] + UDP-N-acetyl-α-D-glucosamine = 3-O-(N-acetyl-β-D-glucosaminyl)-L-threonyl-[protein] + H+ + UDPBy similarityEC:2.4.1.255By similarity
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 PublicationView all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 508 | Proton acceptorBy similarity | 1 | |
Binding sitei | 849 | UDPBy similarity | 1 | |
Binding sitei | 852 | UDPBy similarity | 1 | |
Binding sitei | 935 | UDPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 906 – 908 | UDPBy similarity | 3 | |
Nucleotide bindingi | 911 – 914 | UDPBy similarity | 4 | |
Nucleotide bindingi | 930 – 932 | UDPBy similarity | 3 |
GO - Molecular functioni
- catalytic activity Source: MGI
- identical protein binding Source: MGI
- monosaccharide binding Source: MGI
- N-acetyltransferase activity Source: MGI
- peptide binding Source: MGI
- phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
- protein-containing complex binding Source: MGI
- protein domain specific binding Source: MGI
- protein N-acetylglucosaminyltransferase activity Source: UniProtKB
- protein O-GlcNAc transferase activity Source: MGI
GO - Biological processi
- apoptotic process Source: UniProtKB
- cellular response to glucose stimulus Source: MGI
- cellular response to lipopolysaccharide Source: MGI
- chromatin organization Source: UniProtKB-KW
- circadian regulation of gene expression Source: UniProtKB
- glucosamine metabolic process Source: MGI
- histone H3-K4 trimethylation Source: MGI
- histone H4-K16 acetylation Source: UniProtKB
- histone H4-K5 acetylation Source: UniProtKB
- histone H4-K8 acetylation Source: UniProtKB
- intracellular distribution of mitochondria Source: MGI
- negative regulation of cell death Source: MGI
- negative regulation of cellular response to hypoxia Source: MGI
- negative regulation of peptidyl-serine phosphorylation Source: MGI
- negative regulation of peptidyl-threonine phosphorylation Source: MGI
- negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
- negative regulation of protein phosphorylation Source: MGI
- negative regulation of protein targeting to membrane Source: MGI
- negative regulation of protein ubiquitination Source: UniProtKB
- phosphatidylinositol-mediated signaling Source: UniProtKB
- positive regulation of cell size Source: MGI
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- positive regulation of gene expression Source: MGI
- positive regulation of histone H3-K27 methylation Source: UniProtKB
- positive regulation of histone H3-K4 methylation Source: Ensembl
- positive regulation of protein localization to nucleus Source: MGI
- positive regulation of protein phosphorylation Source: MGI
- positive regulation of proteolysis Source: UniProtKB
- positive regulation of reactive oxygen species biosynthetic process Source: MGI
- positive regulation of transcription by RNA polymerase II Source: MGI
- protein O-linked glycosylation Source: MGI
- protein processing Source: UniProtKB
- regulation of dosage compensation by inactivation of X chromosome Source: ComplexPortal
- regulation of gluconeogenesis Source: UniProtKB
- regulation of glycolytic process Source: UniProtKB
- regulation of insulin receptor signaling pathway Source: MGI
- regulation of Rac protein signal transduction Source: MGI
- regulation of transcription by RNA polymerase II Source: MGI
- response to insulin Source: MGI
Keywordsi
Molecular function | Chromatin regulator, Glycosyltransferase, Transferase |
Biological process | Biological rhythms |
Ligand | Lipid-binding |
Enzyme and pathway databases
BRENDAi | 2.4.1.255, 3474 |
Reactomei | R-MMU-3214847, HATs acetylate histones R-MMU-5675482, Regulation of necroptotic cell death R-MMU-5689603, UCH proteinases |
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | GT41, Glycosyltransferase Family 41 |
Names & Taxonomyi
Protein namesi | Recommended name: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC:2.4.1.2551 Publication)Alternative name(s): O-GlcNAc transferase subunit p110 O-linked N-acetylglucosamine transferase 110 kDa subunit Short name: OGT |
Gene namesi | Name:Ogt |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1339639, Ogt |
VEuPathDBi | HostDB:ENSMUSG00000034160 |
Subcellular locationi
Mitochondrion
- Mitochondrion membrane By similarity
Cytoplasm and Cytosol
- Cytoplasm By similarity
Plasma membrane
- Cell membrane By similarity
Nucleus
- Nucleus 1 Publication
Other locations
- Cell projection By similarity
Note: Mostly in the nucleus. Retained in the nucleus via interaction with HCFC1. After insulin induction, translocated from the nucleus to the cell membrane via phosphatidylinositide binding. Colocalizes with AKT1 at the plasma membrane (By similarity). TRAK1 recruits this protein to mitochondria. In the absence of TRAK1, localizes in cytosol and nucleus (By similarity).By similarity
Cytosol
- cytosol Source: UniProtKB
Mitochondrion
- mitochondrial membrane Source: UniProtKB-SubCell
- mitochondrion Source: MGI
Nucleus
- histone acetyltransferase complex Source: UniProtKB
- NSL complex Source: Ensembl
- nucleoplasm Source: MGI
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: UniProtKB
Other locations
- cytoplasm Source: MGI
- euchromatin Source: MGI
- neuron projection Source: MGI
- neuronal cell body Source: MGI
- protein N-acetylglucosaminyltransferase complex Source: MGI
- protein-containing complex Source: MGI
- zymogen granule Source: MGI
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Membrane, Mitochondrion, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 – 473 | Missing : Loss of interaction with HOXA1. Loss of glycosylation of HOXA1. 1 PublicationAdd BLAST | 472 | |
Mutagenesisi | 474 – 1046 | Missing : Interacts with HOXA1. Interaction is localized to the nucleus. 1 PublicationAdd BLAST | 573 | |
Mutagenesisi | 504 – 1046 | Missing : Interacts with HOXA1. Interaction is localized to the nucleus. 1 PublicationAdd BLAST | 543 | |
Mutagenesisi | 991 – 1046 | Missing : Impaired interaction with HOXA1. Loss of glycosylation of HOXA1. 1 PublicationAdd BLAST | 56 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000285216 | 2 – 1046 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitAdd BLAST | 1045 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 3 | Phosphoserine; by GSK3-beta; alternate1 Publication | 1 | |
Glycosylationi | 3 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
Modified residuei | 4 | Phosphoserine; by GSK3-beta; alternate1 Publication | 1 | |
Glycosylationi | 4 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
Modified residuei | 20 | PhosphoserineCombined sources | 1 | |
Modified residuei | 989 | PhosphotyrosineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q8CGY8 |
MaxQBi | Q8CGY8 |
PaxDbi | Q8CGY8 |
PeptideAtlasi | Q8CGY8 |
PRIDEi | Q8CGY8 |
ProteomicsDBi | 293497 [Q8CGY8-1] 293498 [Q8CGY8-2] |
PTM databases
GlyGeni | Q8CGY8, 2 sites |
iPTMneti | Q8CGY8 |
PhosphoSitePlusi | Q8CGY8 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000034160, Expressed in female gonad and 332 other tissues |
Genevisiblei | Q8CGY8, MM |
Interactioni
Subunit structurei
Homotrimer, oligomerizes via TPR repeats 6 and 7. Trimerization is not necessary for activity in vitro, however it increases affinity for UDP-GlcNAc (By similarity).
Component of a THAP1/THAP3-HCFC1-OGT complex.
Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
Interacts directly with HCFC1; the interaction O-glycosylates HCFC1, regulates its proteolytic processing and transcriptional activity and, in turn, stabilizes OGT in the nucleus.
Interacts (via TPRs 1-6) with SIN3A; the interaction mediates transcriptional repression in parallel with histone deacetylase (By similarity).
Interacts (via TPR 5-6) with TET1, TET2 and TET3 (PubMed:23352454).
Interacts (via TPR repeats 6 and 7) with ATXN10 (PubMed:16182253).
Interacts with histone H2B (By similarity).
Interacts with ARNTL/BMAL1 (PubMed:23337503).
Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894).
Interacts with SINHCAF (PubMed:28554894).
Component of a complex composed of KMT2E/MLL5, OGT and USP7; the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and proteosomal-mediated degradation.
Interacts (via TRP repeats) with KMT2E/MLL5 (via N-terminus).
Interacts with USP7 (By similarity).
Interacts with TRAK1; this interaction is not required for glycosylation of TRAK1 by this protein.
Found in a complex with KIF5B, RHOT1, RHOT2 and TRAK1 (By similarity).
Interacts (via TPR repeats domain) with HOXA1; the interaction takes place mainly in the nucleus (PubMed:29465778).
Interacts with NSD2 (PubMed:19483677).
By similarity6 PublicationsBinary interactionsi
Q8CGY8
With | #Exp. | IntAct |
---|---|---|
Tet2 [Q4JK59] | 2 | EBI-928496,EBI-4291768 |
GO - Molecular functioni
- identical protein binding Source: MGI
- protein domain specific binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 223870, 29 interactors |
ComplexPortali | CPX-3441, SIN3A histone deacetylase complex, ES cell-specific variant CPX-875, NSL histone acetyltransferase complex |
DIPi | DIP-35700N |
IntActi | Q8CGY8, 8 interactors |
STRINGi | 10090.ENSMUSP00000045409 |
Miscellaneous databases
RNActi | Q8CGY8, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 21 – 54 | TPR 1Add BLAST | 34 | |
Repeati | 89 – 122 | TPR 2Add BLAST | 34 | |
Repeati | 123 – 156 | TPR 3Add BLAST | 34 | |
Repeati | 157 – 190 | TPR 4Add BLAST | 34 | |
Repeati | 191 – 224 | TPR 5Add BLAST | 34 | |
Repeati | 225 – 258 | TPR 6Add BLAST | 34 | |
Repeati | 259 – 292 | TPR 7Add BLAST | 34 | |
Repeati | 293 – 326 | TPR 8Add BLAST | 34 | |
Repeati | 327 – 360 | TPR 9Add BLAST | 34 | |
Repeati | 361 – 394 | TPR 10Add BLAST | 34 | |
Repeati | 395 – 428 | TPR 11Add BLAST | 34 | |
Repeati | 429 – 462 | TPR 12Add BLAST | 34 | |
Repeati | 463 – 473 | TPR 13; truncatedAdd BLAST | 11 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 991 – 1010 | Required for phosphatidylinositol 3,4,5-triphosphate bindingAdd BLAST | 20 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 487 – 503 | Nuclear localization signalSequence analysisAdd BLAST | 17 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, TPR repeatPhylogenomic databases
eggNOGi | KOG1124, Eukaryota KOG4626, Eukaryota |
GeneTreei | ENSGT00940000155085 |
HOGENOMi | CLU_001721_1_0_1 |
InParanoidi | Q8CGY8 |
OMAi | YNQQCIR |
OrthoDBi | 142546at2759 |
PhylomeDBi | Q8CGY8 |
TreeFami | TF105785 |
Family and domain databases
Gene3Di | 1.25.40.10, 2 hits |
InterProi | View protein in InterPro IPR037919, OGT IPR029489, OGT/SEC/SPY_C IPR011990, TPR-like_helical_dom_sf IPR001440, TPR_1 IPR019734, TPR_repeat |
PANTHERi | PTHR44366, PTHR44366, 1 hit |
Pfami | View protein in Pfam PF13844, Glyco_transf_41, 1 hit PF00515, TPR_1, 2 hits PF13181, TPR_8, 2 hits |
SMARTi | View protein in SMART SM00028, TPR, 12 hits |
SUPFAMi | SSF48452, SSF48452, 3 hits |
PROSITEi | View protein in PROSITE PS50005, TPR, 12 hits PS50293, TPR_REGION, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ
60 70 80 90 100
EPDNTGVLLL LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK
110 120 130 140 150
ERGQLQEAIE HYRHALRLKP DFIDGYINLA AALVAAGDME GAVQAYVSAL
160 170 180 190 200
QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF AVAWSNLGCV
210 220 230 240 250
FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR
260 270 280 290 300
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
310 320 330 340 350
NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY
360 370 380 390 400
RKALEVFPEF AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN
410 420 430 440 450
MGNTLKEMQD VQGALQCYTR AIQINPAFAD AHSNLASIHK DSGNIPEAIA
460 470 480 490 500
SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV SIVAEQLEKN
510 520 530 540 550
RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK
560 570 580 590 600
LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN
610 620 630 640 650
FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL
660 670 680 690 700
FALRPAPIQA MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP
710 720 730 740 750
HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY DNRIVLNGID LKAFLDSLPD
760 770 780 790 800
VKIVKMKCPD GGDNPDSSNT ALNMPVIPMN TIAEAVIEMI NRGQIQITIN
810 820 830 840 850
GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL
860 870 880 890 900
YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
910 920 930 940 950
IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET
960 970 980 990 1000
LASRVAASQL TCLGCLELIA KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ
1010 1020 1030 1040
RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 57 | V → A in AAO17363 (PubMed:12504895).Curated | 1 | |
Sequence conflicti | 992 | K → R in AAK39123 (Ref. 2) Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_024844 | 13 – 22 | Missing in isoform 2. Curated | 10 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF539527 Genomic DNA Translation: AAO17363.1 AF363030 mRNA Translation: AAK39123.1 AL805980 Genomic DNA No translation available. AL806534 Genomic DNA No translation available. BC057319 mRNA Translation: AAH57319.1 AK047095 mRNA Translation: BAC32961.1 |
CCDSi | CCDS30318.1 [Q8CGY8-1] CCDS72415.1 [Q8CGY8-2] |
RefSeqi | NP_001277464.1, NM_001290535.1 [Q8CGY8-2] NP_631883.2, NM_139144.4 [Q8CGY8-1] XP_006527799.1, XM_006527736.3 [Q8CGY8-1] XP_011245805.1, XM_011247503.2 [Q8CGY8-2] |
Genome annotation databases
Ensembli | ENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160 [Q8CGY8-1] ENSMUST00000119299; ENSMUSP00000113454; ENSMUSG00000034160 [Q8CGY8-2] |
GeneIDi | 108155 |
KEGGi | mmu:108155 |
UCSCi | uc009tyc.3, mouse [Q8CGY8-1] uc057ask.1, mouse [Q8CGY8-2] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF539527 Genomic DNA Translation: AAO17363.1 AF363030 mRNA Translation: AAK39123.1 AL805980 Genomic DNA No translation available. AL806534 Genomic DNA No translation available. BC057319 mRNA Translation: AAH57319.1 AK047095 mRNA Translation: BAC32961.1 |
CCDSi | CCDS30318.1 [Q8CGY8-1] CCDS72415.1 [Q8CGY8-2] |
RefSeqi | NP_001277464.1, NM_001290535.1 [Q8CGY8-2] NP_631883.2, NM_139144.4 [Q8CGY8-1] XP_006527799.1, XM_006527736.3 [Q8CGY8-1] XP_011245805.1, XM_011247503.2 [Q8CGY8-2] |
3D structure databases
SMRi | Q8CGY8 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 223870, 29 interactors |
ComplexPortali | CPX-3441, SIN3A histone deacetylase complex, ES cell-specific variant CPX-875, NSL histone acetyltransferase complex |
DIPi | DIP-35700N |
IntActi | Q8CGY8, 8 interactors |
STRINGi | 10090.ENSMUSP00000045409 |
Protein family/group databases
CAZyi | GT41, Glycosyltransferase Family 41 |
PTM databases
GlyGeni | Q8CGY8, 2 sites |
iPTMneti | Q8CGY8 |
PhosphoSitePlusi | Q8CGY8 |
Proteomic databases
EPDi | Q8CGY8 |
MaxQBi | Q8CGY8 |
PaxDbi | Q8CGY8 |
PeptideAtlasi | Q8CGY8 |
PRIDEi | Q8CGY8 |
ProteomicsDBi | 293497 [Q8CGY8-1] 293498 [Q8CGY8-2] |
Protocols and materials databases
Antibodypediai | 27791, 457 antibodies from 45 providers |
DNASUi | 108155 |
Genome annotation databases
Ensembli | ENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160 [Q8CGY8-1] ENSMUST00000119299; ENSMUSP00000113454; ENSMUSG00000034160 [Q8CGY8-2] |
GeneIDi | 108155 |
KEGGi | mmu:108155 |
UCSCi | uc009tyc.3, mouse [Q8CGY8-1] uc057ask.1, mouse [Q8CGY8-2] |
Organism-specific databases
CTDi | 8473 |
MGIi | MGI:1339639, Ogt |
VEuPathDBi | HostDB:ENSMUSG00000034160 |
Phylogenomic databases
eggNOGi | KOG1124, Eukaryota KOG4626, Eukaryota |
GeneTreei | ENSGT00940000155085 |
HOGENOMi | CLU_001721_1_0_1 |
InParanoidi | Q8CGY8 |
OMAi | YNQQCIR |
OrthoDBi | 142546at2759 |
PhylomeDBi | Q8CGY8 |
TreeFami | TF105785 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
BRENDAi | 2.4.1.255, 3474 |
Reactomei | R-MMU-3214847, HATs acetylate histones R-MMU-5675482, Regulation of necroptotic cell death R-MMU-5689603, UCH proteinases |
Miscellaneous databases
BioGRID-ORCSi | 108155, 25 hits in 66 CRISPR screens |
ChiTaRSi | Ogt, mouse |
PROi | PR:Q8CGY8 |
RNActi | Q8CGY8, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000034160, Expressed in female gonad and 332 other tissues |
Genevisiblei | Q8CGY8, MM |
Family and domain databases
Gene3Di | 1.25.40.10, 2 hits |
InterProi | View protein in InterPro IPR037919, OGT IPR029489, OGT/SEC/SPY_C IPR011990, TPR-like_helical_dom_sf IPR001440, TPR_1 IPR019734, TPR_repeat |
PANTHERi | PTHR44366, PTHR44366, 1 hit |
Pfami | View protein in Pfam PF13844, Glyco_transf_41, 1 hit PF00515, TPR_1, 2 hits PF13181, TPR_8, 2 hits |
SMARTi | View protein in SMART SM00028, TPR, 12 hits |
SUPFAMi | SSF48452, SSF48452, 3 hits |
PROSITEi | View protein in PROSITE PS50005, TPR, 12 hits PS50293, TPR_REGION, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | OGT1_MOUSE | |
Accessioni | Q8CGY8Primary (citable) accession number: Q8CGY8 Secondary accession number(s): A2ALY1 Q91Y38 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 2007 |
Last sequence update: | May 1, 2007 | |
Last modified: | February 23, 2022 | |
This is version 159 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families