O15294 (OGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
EC=2.4.1.255

Alternative name(s):
O-GlcNAc transferase subunit p110
O-linked N-acetylglucosamine transferase 110 kDa subunit
Short name=OGT

Gene names

Name:

OGT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1046 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. 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. 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. Ref.6 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Isoform 2: the mitochondrial mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line. Ref.6 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24
Catalytic activity	UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine. Ref.12 Ref.18 Ref.23 Ref.24 UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.
Enzyme regulation	Subject to product inhibition by UDP. Ref.24
Pathway	Protein modification; protein glycosylation.
Subunit structure	Heterotrimer; consists of one 78 kDa subunit and two 110 kDa subunits dimerized via TPR repeats 6 and 7. Interacts (via TPR repeats 6 and 7) with ATXN10 By similarity. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, HCFC1, PPP1CC and ACTB. 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. Interacts (via TPR 5-6) with TET1, TET2 and TET3. Ref.6 Ref.7 Ref.12 Ref.13 Ref.15 Ref.18 Ref.19 Ref.21 Ref.22
Subcellular location	Isoform 2: Mitochondrion. Membrane. Note: Associates with the mitochondrial inner membrane. Ref.8 Ref.13 Ref.18 Isoform 3: Cytoplasm. Nucleus Ref.8 Ref.13 Ref.18. Cell membrane. 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 phophatidylinisotide binding. Colocalizes with AKT1 at the plasma membrane. Ref.8 Ref.13 Ref.18 Isoform 4: Cytoplasm. Nucleus Ref.8 Ref.13 Ref.18.
Tissue specificity	Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver. Ref.1
Induction	Induction of the nucleocytoplasmic OGT (ncOGT) isoform in the liver on glucose deprivation is mediated by the decreased hexosamine biosynthesis pathway (HBP) flux. Ref.11 Ref.24
Domain	The TPR repeat domain is required for substrate binding and oligomerization. Ref.23
Post-translational modification	Ubiquitinated, leading to its proteasomal degradation. Ref.18
Involvement in disease	Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum. Ref.10
Sequence similarities	Belongs to the O-GlcNAc transferase family. Contains 13 TPR repeats.
Biophysicochemical properties	Kinetic parameters: KM=1.8 µM for UDP-N-acetyl-D-glucosamine Ref.24

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell membrane Cytoplasm Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat TPR repeat
Ligand	Lipid-binding
Molecular function	Chromatin regulator Glycosyltransferase Transferase
PTM	Acetylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to retinoic acid Inferred from mutant phenotype Ref.12. Source: BHF-UCL histone H3-K4 trimethylation Inferred from mutant phenotype Ref.21. Source: UniProtKB histone H4-K16 acetylation Inferred from direct assay Ref.13. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.13. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.13. Source: UniProtKB induction of apoptosis Inferred from direct assay Ref.16. Source: UniProtKB phosphatidylinositol-mediated signaling Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of granulocyte differentiation Inferred from mutant phenotype Ref.12. Source: BHF-UCL positive regulation of histone H3-K4 methylation Inferred from direct assay Ref.12. Source: BHF-UCL positive regulation of proteolysis Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.22Ref.21. Source: UniProtKB protein O-linked glycosylation Inferred from direct assay Ref.24Ref.18Ref.20Ref.22PubMed 23352454. Source: UniProtKB regulation of Rac protein signal transduction Inferred from direct assay Ref.8. Source: UniProtKB regulation of glycolysis Inferred from direct assay Ref.20. Source: UniProtKB regulation of insulin receptor signaling pathway Inferred from direct assay Ref.8. Source: UniProtKB response to insulin stimulus Inferred from direct assay Ref.8. Source: UniProtKB response to nutrient Traceable author statement Ref.1. Source: ProtInc
Cellular_component	MLL5-L complex Inferred from direct assay Ref.12. Source: UniProtKB centrosome Inferred from direct assay. Source: HPA cytosol Inferred from direct assay Ref.18. Source: UniProtKB histone acetyltransferase complex Inferred from direct assay Ref.13. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	enzyme activator activity Inferred from direct assay Ref.12. Source: BHF-UCL phosphatidylinositol-3,4,5-trisphosphate binding Inferred from direct assay Ref.8. Source: UniProtKB protein N-acetylglucosaminyltransferase activity Inferred from direct assay Ref.12Ref.24Ref.18Ref.20Ref.22PubMed 23352454Ref.21. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCFC1	P51610	9	EBI-539828,EBI-396176
Hoxa1	P09022	3	EBI-539828,EBI-3957603	From a different organism.
MLL5	Q8IZD2	4	EBI-539828,EBI-2689959

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: O15294-1)

Also known as: Nucleocytoplasmic isoform; ncOGT;

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: O15294-2)

Also known as: Mitochondrial isoform; mOGT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: MASSVGNVAD...LKALGRLEEA → MLQGHFWLVR...PSHLLSLTPP

Isoform 1 (identifier: O15294-3)

The sequence of this isoform differs from the canonical sequence as follows:
     13-22: Missing.

Isoform 4 (identifier: O15294-4)

Also known as: Short isoform; sOGT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 1046

1045

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

PRO_0000191772

Regions

Repeat

21 – 54

34

TPR 1

Repeat

89 – 122

34

TPR 2

Repeat

123 – 156

34

TPR 3

Repeat

157 – 190

34

TPR 4

Repeat

191 – 224

34

TPR 5

Repeat

225 – 258

34

TPR 6

Repeat

259 – 292

34

TPR 7

Repeat

293 – 326

34

TPR 8

Repeat

327 – 360

34

TPR 9

Repeat

361 – 394

34

TPR 10

Repeat

395 – 428

34

TPR 11

Repeat

429 – 462

34

TPR 12

Repeat

463 – 473

11

TPR 13; truncated

Nucleotide binding

905 – 908

4

UDP

Nucleotide binding

911 – 914

4

UDP

Nucleotide binding

929 – 931

3

UDP

Region

991 – 1010

20

Required for phosphatidylinositol 3,4,5-triphosphate binding

Motif

487 – 503

17

Nuclear localization signal Potential

Sites

Active site

508

1

Proton acceptor Probable

Binding site

849

1

UDP

Binding site

852

1

UDP

Binding site

935

1

UDP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Natural variations

Alternative sequence

1 – 381

381

Missing in isoform 4.

VSP_040764

Alternative sequence

1 – 176

176

MASSV…RLEEA → MLQGHFWLVREGIMISPSSP PPPNLFFFPLQIFPFPFTSF PSHLLSLTPP in isoform 2.

VSP_006553

Alternative sequence

13 – 22

10

Missing in isoform 1.

VSP_014164

Natural variant

538

1

L → P Found in a renal cell carcinoma sample; somatic mutation.

VAR_064736

Experimental info

Mutagenesis

208

1

W → E: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with D-211. Ref.23

Mutagenesis

211

1

I → D: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208. Ref.23

Mutagenesis

508

1

H → A: Loss of enzyme activity. Ref.24

Mutagenesis

568

1

H → A: Reduces enzyme activity by about 95%. Ref.24

Mutagenesis

911

1

H → A: Reduces enzyme activity by over 90%. Ref.24

Mutagenesis

991 – 992

2

KK → AA: Abolishes phosphatidylinisitol binding, no translocation to the cell membrane, and no effect on phosphorylation of AKT1 nor IRS1.

Mutagenesis

994

1

R → A: No effect on phosphatidylinisitol binding. Ref.8

Mutagenesis

996

1

K → A: Reduced phosphatidylinisitol binding. Ref.8

Mutagenesis

999

1

K → A: Reduced phosphatidylinisitol binding. Ref.8

Mutagenesis

1001

1

R → A: No effect on phosphatidylinisitol binding. Ref.8

Mutagenesis

1010

1

K → A: No effect on phosphatidylinisitol binding. Ref.8

Sequence conflict

308

1

S → Q in CAB62528. Ref.3

Sequence conflict

663

1

L → P in CAD97853. Ref.3

Secondary structure

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1046

Helix Strand Turn

Details...

Helix

27 – 34

8

Helix

37 – 50

14

Helix

55 – 67

13

Helix

71 – 84

14

Helix

89 – 102

14

Helix

105 – 118

14

Helix

123 – 136

14

Helix

141 – 152

12

Helix

158 – 168

11

Helix

173 – 186

14

Helix

191 – 202

12

Turn

203 – 205

3

Helix

207 – 220

14

Helix

225 – 236

12

Turn

237 – 239

3

Helix

243 – 254

12

Helix

259 – 271

13

Helix

275 – 287

13

Helix

293 – 306

14

Helix

309 – 322

14

Helix

325 – 339

15

Helix

343 – 356

14

Helix

361 – 373

13

Helix

377 – 390

14

Helix

395 – 407

13

Helix

411 – 424

14

Helix

429 – 441

13

Helix

445 – 458

14

Helix

463 – 475

13

Helix

482 – 498

17

Helix

509 – 512

4

Helix

517 – 536

20

Turn

537 – 539

3

Beta strand

547 – 549

3

Turn

550 – 554

5

Beta strand

556 – 563

8

Beta strand

565 – 568

4

Helix

569 – 574

6

Helix

577 – 580

4

Turn

583 – 585

3

Beta strand

586 – 594

9

Helix

600 – 608

9

Beta strand

609 – 614

6

Helix

615 – 617

3

Helix

621 – 630

10

Beta strand

634 – 639

6

Beta strand

641 – 643

3

Helix

649 – 652

4

Beta strand

656 – 661

6

Beta strand

676 – 679

4

Turn

681 – 683

3

Helix

686 – 691

6

Beta strand

693 – 698

6

Helix

708 – 711

4

Helix

713 – 715

3

Beta strand

719 – 721

3

Beta strand

731 – 737

7

Helix

741 – 746

6

Beta strand

748 – 750

3

Beta strand

752 – 754

3

Beta strand

774 – 777

4

Helix

781 – 792

12

Beta strand

796 – 799

4

Beta strand

802 – 806

5

Helix

807 – 809

3

Helix

810 – 813

4

Helix

815 – 818

4

Beta strand

820 – 822

3

Beta strand

826 – 831

6

Helix

832 – 835

4

Beta strand

841 – 845

5

Helix

850 – 852

3

Helix

855 – 867

13

Beta strand

869 – 877

9

Helix

880 – 882

3

Helix

883 – 892

10

Helix

897 – 899

3

Beta strand

900 – 904

5

Helix

908 – 914

7

Helix

915 – 917

3

Beta strand

919 – 922

4

Beta strand

925 – 927

3

Helix

931 – 938

8

Beta strand

943 – 945

3

Helix

951 – 953

3

Helix

955 – 963

9

Helix

966 – 968

3

Helix

973 – 985

13

Helix

987 – 1003

17

Helix

1009 – 1028

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 (Nucleocytoplasmic isoform) (ncOGT) [UniParc]. Last modified June 21, 2005. Version 3. Checksum: 852ED68BDDE63363	FASTA	1,046	116,925
	10 20 30 40 50 60 MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL 70 80 90 100 110 120 LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP 130 140 150 160 170 180 DFIDGYINLA AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY 190 200 210 220 230 240 LKAIETQPNF AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI 250 260 270 280 290 300 FDRAVAAYLR ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA 310 320 330 340 350 360 NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF 370 380 390 400 410 420 AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR 430 440 450 460 470 480 AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT 490 500 510 520 530 540 DYDERMKKLV SIVADQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK 550 560 570 580 590 600 PPYEHPKDLK LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN 610 620 630 640 650 660 FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA 670 680 690 700 710 720 MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV 730 740 750 760 770 780 IDFKSNGHIY DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADSSNT ALNMPVIPMN 790 800 810 820 830 840 TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED 850 860 870 880 890 900 AIVYCNFNQL YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI 910 920 930 940 950 960 IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL 970 980 990 1000 1010 1020 TCLGCLELIA KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ RISSPLFNTK QYTMELERLY 1030 1040 LQMWEHYAAG NKPDHMIKPV EVTESA
	Isoform 2 (Mitochondrial isoform) (mOGT) [UniParc]. Checksum: 766BF416ABD547C4	FASTA	920	103,012
	10 20 30 40 50 60 MLQGHFWLVR EGIMISPSSP PPPNLFFFPL QIFPFPFTSF PSHLLSLTPP KACYLKAIET 70 80 90 100 110 120 QPNFAVAWSN LGCVFNAQGE IWLAIHHFEK AVTLDPNFLD AYINLGNVLK EARIFDRAVA 130 140 150 160 170 180 AYLRALSLSP NHAVVHGNLA CVYYEQGLID LAIDTYRRAI ELQPHFPDAY CNLANALKEK 190 200 210 220 230 240 GSVAEAEDCY NTALRLCPTH ADSLNNLANI KREQGNIEEA VRLYRKALEV FPEFAAAHSN 250 260 270 280 290 300 LASVLQQQGK LQEALMHYKE AIRISPTFAD AYSNMGNTLK EMQDVQGALQ CYTRAIQINP 310 320 330 340 350 360 AFADAHSNLA SIHKDSGNIP EAIASYRTAL KLKPDFPDAY CNLAHCLQIV CDWTDYDERM 370 380 390 400 410 420 KKLVSIVADQ LEKNRLPSVH PHHSMLYPLS HGFRKAIAER HGNLCLDKIN VLHKPPYEHP 430 440 450 460 470 480 KDLKLSDGRL RVGYVSSDFG NHPTSHLMQS IPGMHNPDKF EVFCYALSPD DGTNFRVKVM 490 500 510 520 530 540 AEANHFIDLS QIPCNGKAAD RIHQDGIHIL VNMNGYTKGA RNELFALRPA PIQAMWLGYP 550 560 570 580 590 600 GTSGALFMDY IITDQETSPA EVAEQYSEKL AYMPHTFFIG DHANMFPHLK KKAVIDFKSN 610 620 630 640 650 660 GHIYDNRIVL NGIDLKAFLD SLPDVKIVKM KCPDGGDNAD SSNTALNMPV IPMNTIAEAV 670 680 690 700 710 720 IEMINRGQIQ ITINGFSISN GLATTQINNK AATGEEVPRT IIVTTRSQYG LPEDAIVYCN 730 740 750 760 770 780 FNQLYKIDPS TLQMWANILK RVPNSVLWLL RFPAVGEPNI QQYAQNMGLP QNRIIFSPVA 790 800 810 820 830 840 PKEEHVRRGQ LADVCLDTPL CNGHTTGMDV LWAGTPMVTM PGETLASRVA ASQLTCLGCL 850 860 870 880 890 900 ELIAKNRQEY EDIAVKLGTD LEYLKKVRGK VWKQRISSPL FNTKQYTMEL ERLYLQMWEH 910 920 YAAGNKPDHM IKPVEVTESA
	Isoform 1 [UniParc]. Checksum: C3BD67340925A2C2	FASTA	1,036	115,706
	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 SIVADQLEKN 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 GGDNADSSNT ALNMPVIPMN TIAEAVIEMI 790 800 810 820 830 840 NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL 850 860 870 880 890 900 YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI IFSPVAPKEE 910 920 930 940 950 960 HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL TCLGCLELIA 970 980 990 1000 1010 1020 KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ RISSPLFNTK QYTMELERLY LQMWEHYAAG 1030 NKPDHMIKPV EVTESA
	Isoform 4 (Short isoform) (sOGT) [UniParc]. Checksum: 181B846A6B09E63A	FASTA	665	74,536
	10 20 30 40 50 60 MHYKEAIRIS PTFADAYSNM GNTLKEMQDV QGALQCYTRA IQINPAFADA HSNLASIHKD 70 80 90 100 110 120 SGNIPEAIAS YRTALKLKPD FPDAYCNLAH CLQIVCDWTD YDERMKKLVS IVADQLEKNR 130 140 150 160 170 180 LPSVHPHHSM LYPLSHGFRK AIAERHGNLC LDKINVLHKP PYEHPKDLKL SDGRLRVGYV 190 200 210 220 230 240 SSDFGNHPTS HLMQSIPGMH NPDKFEVFCY ALSPDDGTNF RVKVMAEANH FIDLSQIPCN 250 260 270 280 290 300 GKAADRIHQD GIHILVNMNG YTKGARNELF ALRPAPIQAM WLGYPGTSGA LFMDYIITDQ 310 320 330 340 350 360 ETSPAEVAEQ YSEKLAYMPH TFFIGDHANM FPHLKKKAVI DFKSNGHIYD NRIVLNGIDL 370 380 390 400 410 420 KAFLDSLPDV KIVKMKCPDG GDNADSSNTA LNMPVIPMNT IAEAVIEMIN RGQIQITING 430 440 450 460 470 480 FSISNGLATT QINNKAATGE EVPRTIIVTT RSQYGLPEDA IVYCNFNQLY KIDPSTLQMW 490 500 510 520 530 540 ANILKRVPNS VLWLLRFPAV GEPNIQQYAQ NMGLPQNRII FSPVAPKEEH VRRGQLADVC 550 560 570 580 590 600 LDTPLCNGHT TGMDVLWAGT PMVTMPGETL ASRVAASQLT CLGCLELIAK NRQEYEDIAV 610 620 630 640 650 660 KLGTDLEYLK KVRGKVWKQR ISSPLFNTKQ YTMELERLYL QMWEHYAAGN KPDHMIKPVE VTESA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats." Lubas W.A., Frank D.W., Krause M., Hanover J.A. J. Biol. Chem. 272:9316-9324(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 227-236 AND 955-971, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1." Nolte D., Muller U. Mamm. Genome 13:62-64(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]	"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] (ISOFORMS 1 AND 4). Tissue: Endometrium, Fetal brain and Spinal cord.
[4]	"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] (ISOFORMS 1 AND 3). Tissue: Colon and Pancreas.
[5]	Bienvenut W.V., Dhillon A.S., Kolch W. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17; 31-42; 161-168; 244-250; 339-348; 734-752; 868-877 AND 1002-1010, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Hepatoma.
[6]	"Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression." Yang X., Zhang F., Kudlow J.E. Cell 110:69-80(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIN3A, FUNCTION.
[7]	"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCFC1.
[8]	"Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance." Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V., Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M. Nature 451:964-969(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, PHOSPHATIDYLINOSITOL-BINDING, MUTAGENESIS OF 991-LYS-LYS-992; ARG-994; LYS-996; LYS-999; ARG-1001 AND LYS-1010.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease." Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.X. Brain 132:1820-1832(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH ALZHEIMER DISEASE.
[11]	"Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux." Taylor R.P., Geisler T.S., Chambers J.H., McClain D.A. J. Biol. Chem. 284:3425-3432(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[12]	"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis." Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S. Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MLL5-L COMPLEX.
[13]	"Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex." Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C. J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
[14]	"Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes." Whelan S.A., Dias W.B., Thiruneelakantapillai L., Lane M.D., Hart G.W. J. Biol. Chem. 285:5204-5211(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, POSSIBLE ASSOCIATION WITH DIABETES.
[15]	"The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias." Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B., Kristie T.M., Girard J.P. J. Biol. Chem. 285:13364-13371(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX, INTERACTION WITH HCFC1; THAP1 AND THAP3, FUNCTION.
[16]	"Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis." Shin S.H., Love D.C., Hanover J.A. Amino Acids 40:885-893(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ISOFORM 2.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway." Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G., Vogel J.L., Kristie T.M., Affar E.B. Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH HCFC1.
[19]	"GlcNAcylation of histone H2B facilitates its monoubiquitination." Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S., Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F., Kitagawa H., Roeder R.G., Brown M., Kato S. Nature 480:557-560(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH H2B.
[20]	"Phosphofructokinase 1 glycosylation regulates cell growth and metabolism." Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III, Peters E.C., Driggers E.M., Hsieh-Wilson L.C. Science 337:975-980(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS." Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N., Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., Levine R.L., Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., Fuks F. EMBO J. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HCFC1; TET2 AND TET3.
[22]	"TET2 promotes histone O-GlcNAcylation during gene transcription." Chen Q., Chen Y., Bian C., Fujiki R., Yu X. Nature 493:561-564(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TET2 AND TET3.
[23]	"The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha." Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A., Conti E. Nat. Struct. Mol. Biol. 11:1001-1007(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF TRP-208 AND ILE-211.
[24]	"Structure of human O-GlcNAc transferase and its complex with a peptide substrate." Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S. Nature 469:564-567(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 323-1041 IN COMPLEXES WITH UDP AND PEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF HIS-508; HIS-568 AND HIS-911.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110kDa subunit

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U77413 mRNA. Translation: AAB63466.1.
AJ315767 Genomic DNA. Translation: CAC86127.1.
AJ315767 Genomic DNA. Translation: CAC86128.1.
AJ315767 Genomic DNA. Translation: CAC86129.1.
AL050366 mRNA. Translation: CAB62528.1.
AL833085 mRNA. Translation: CAD89970.1.
BX537844 mRNA. Translation: CAD97853.1.
BC014434 mRNA. Translation: AAH14434.1.
BC038180 mRNA. Translation: AAH38180.1.

IPI

IPI00005780.
IPI00219856.
IPI00607723.
IPI01008950.

RefSeq

NP_858058.1. NM_181672.2.
NP_858059.1. NM_181673.2.

UniGene

Hs.405410.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W3B	X-ray	2.85	A/B	26-400	[»]
3PE3	X-ray	2.78	A/B/C/D	323-1041	[»]
3PE4	X-ray	1.95	A/C	323-1041	[»]
3TAX	X-ray	1.88	A/C	323-1041	[»]
4AY5	X-ray	3.15	A/B/C/D	323-1041	[»]
4AY6	X-ray	3.30	A/B/C/D	323-1041	[»]
4GYW	X-ray	1.70	A/C	323-1041	[»]
4GYY	X-ray	1.85	A/C	323-1041	[»]
4GZ3	X-ray	1.90	A/C	323-1041	[»]
4GZ5	X-ray	3.08	A/B/C/D	323-1041	[»]
4GZ6	X-ray	2.98	A/B/C/D	323-1041	[»]

ProteinModelPortal

O15294.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33491N.

IntAct

O15294. 19 interactions.

MINT

MINT-2998811.

STRING

9606.ENSP00000362824.

Protein family/group databases

CAZy

GT41. Glycosyltransferase Family 41.

PTM databases

PhosphoSite

O15294.

Proteomic databases

PaxDb

O15294.

PRIDE

O15294.

Protocols and materials databases

DNASU

8473.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373701; ENSP00000362805; ENSG00000147162.
ENST00000373719; ENSP00000362824; ENSG00000147162.

GeneID

8473.

KEGG

hsa:8473.

UCSC

uc004eaa.2. human.
uc004eab.2. human.

Organism-specific databases

CTD

8473.

GeneCards

GC0XP070752.

HGNC

HGNC:8127. OGT.

HPA

CAB034099.
HPA030751.
HPA030752.

MIM

300255. gene.

neXtProt

NX_O15294.

PharmGKB

PA31914.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3914.

HOGENOM

HOG000003765.

HOVERGEN

HBG000351.

InParanoid

O15294.

KO

K09667.

OMA

LAYMPNT.

OrthoDB

EOG4HQDHJ.

PhylomeDB

O15294.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000147162-MONOMER.

SABIO-RK

O15294.

UniPathway

UPA00378.

Gene expression databases

ArrayExpress

O15294.

Bgee

O15294.

CleanEx

HS_OGT.

Genevestigator

O15294.

GermOnline

ENSG00000147162. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 5 hits.

InterPro

IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF00515. TPR_1. 9 hits.
[Graphical view]

SMART

SM00028. TPR. 12 hits.
[Graphical view]

PROSITE

PS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O15294.

ChEMBL

CHEMBL5955.

EvolutionaryTrace

O15294.

GenomeRNAi

8473.

NextBio

31706.

SOURCE

Search...

Entry information

Entry name

OGT1_HUMAN

Accession

Primary (citable) accession number: O15294
Secondary accession number(s): Q7Z3K0 , Q8WWM8, Q96CC1, Q9UG57

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 21, 2005
Last modified:	May 1, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.