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.-

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

Gene names

Name:

OGT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	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. Ref.9 Ref.10 Ref.11 Ref.13
Catalytic activity	UDP-N-acetyl-D-glucosamine + peptide = UDP + N-acetyl-beta-D-glucosaminyl-peptide. Ref.9 Ref.10 Ref.11 Ref.13
Enzyme regulation	Subject to product inhibition by UDP. Ref.13
Pathway	Protein modification; protein glycosylation.
Subunit structure	Heterotrimer of two 110 kDa and one 70 kDa subunits. It is not known if the 70 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 By similarity. Interacts with ATXN10 By similarity. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts directly with HCFC1. Ref.6 Ref.10
Subcellular location	Cytoplasm. Nucleus. Note: Mostly in the nucleus. Ref.10
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.
Domain	The TPR repeat domain mediates recognition of protein substrates. Ref.11
Post-translational modification	Ubiquitinated, leading to its proteasomal degradation. 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.13

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat TPR repeat
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular response to retinoic acid Inferred from mutant phenotype Ref.9. Source: BHF-UCL positive regulation of granulocyte differentiation Inferred from mutant phenotype Ref.9. Source: BHF-UCL positive regulation of histone H3-K4 methylation Inferred from direct assay Ref.9. Source: BHF-UCL positive regulation of proteolysis Inferred from direct assay Ref.10. Source: UniProtKB protein O-linked glycosylation Inferred from direct assay Ref.13Ref.10. Source: UniProtKB signal transduction Traceable author statement. Source: ProtInc
Cellular component	MLL5-L complex Inferred from direct assay Ref.9. Source: UniProtKB centrosome Inferred from direct assay. Source: HPA cytosol Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	enzyme activator activity Inferred from direct assay Ref.9. Source: BHF-UCL protein N-acetylglucosaminyltransferase activity Inferred from direct assay Ref.9Ref.13Ref.10. Source: UniProtKB protein binding Inferred from physical interaction Ref.6Ref.9Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCFC1	P51610	9	EBI-539828,EBI-396176
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)

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)

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)

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

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 Ref.8

Modified residue

20

1

Phosphoserine Ref.7

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.11

Mutagenesis

211

1

I → D: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208. Ref.11

Mutagenesis

508

1

H → A: Loss of enzyme activity. Ref.13

Mutagenesis

568

1

H → A: Reduces enzyme activity by about 95%. Ref.13

Mutagenesis

911

1

H → A: Reduces enzyme activity by over 90%. Ref.13

Sequence conflict

308

1

S → Q in CAB62528. Ref.3

Sequence conflict

663

1

L → P in CAD97853. Ref.3

Secondary structure

1

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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

327 – 338

12

Turn

339 – 341

3

Helix

343 – 353

11

Helix

361 – 372

12

Turn

373 – 375

3

Helix

378 – 388

11

Helix

395 – 407

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [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 [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 [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: 9083068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 227-236 AND 955-971. 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: 11773972] [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: 17974005] [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: 15489334] [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]	"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: 12670868] [Abstract] Cited for: INTERACTION WITH HCFC1.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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: 19377461] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MLL5-L COMPLEX.
[10]	"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: 21285374] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH HCFC1.
[11]	"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: 15361863] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF TRP-208 AND ILE-211.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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: 21240259] [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, 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	[»]

ProteinModelPortal

O15294.

SMR

O15294. Positions 23-1038.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15294. 18 interactions.

MINT

MINT-2998811.

STRING

O15294.

Protein family/group databases

CAZy

GT41. Glycosyltransferase Family 41.

PTM databases

PhosphoSite

O15294.

Proteomic databases

PRIDE

O15294.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373719; ENSP00000362824; ENSG00000147162.

GeneID

8473.

KEGG

hsa:8473.

NMPDR

fig|9606.3.peg.32971.

UCSC

uc004eaa.1. human.
uc004eab.1. human.

Organism-specific databases

CTD

8473.

GeneCards

GC0XP070752.

H-InvDB

HIX0016863.

HGNC

HGNC:8127. OGT.

HPA

CAB034099.
HPA030751.
HPA030752.

MIM

300255. gene.

neXtProt

NX_O15294.

PharmGKB

PA31914.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG19154.

GeneTree

ENSGT00550000074327.

HOGENOM

HBG317910.

HOVERGEN

HBG000351.

InParanoid

O15294.

OMA

NFPDAYC.

OrthoDB

EOG4HQDHJ.

PhylomeDB

O15294.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000147162-MONOMER.

Gene expression databases

ArrayExpress

O15294.

Bgee

O15294.

CleanEx

HS_OGT.

Genevestigator

O15294.

GermOnline

ENSG00000147162. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 2 hits.

KO

K09667.

Pfam

PF00515. TPR_1. 10 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

NextBio

31706.

SOURCE

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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:	January 25, 2012
This is version 134 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.