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O60502

- NCOAT_HUMAN

UniProt

O60502 - NCOAT_HUMAN

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Protein

Bifunctional protein NCOAT

Gene

MGEA5

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

Functioni

Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase activity. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3.2 Publications

Catalytic activityi

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.
[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.
Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Enzyme regulationi

Inhibited by N-acetylglucosamine and not N-acetylgalactosamine.1 Publication

Kineticsi

  1. KM=1.1 mM for pNP-GlcNAc2 Publications

Vmax=652 µmol/min/mg enzyme with pNP-GLcNAc as substrate2 Publications

pH dependencei

Optimum pH is 5.7-7.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei175 – 1751Nucleophile; for O-GlcNAcase activityBy similarity
Active sitei177 – 1771Proton donor; for O-GlcNAcase activityBy similarity

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB-EC
  2. hyalurononglucosaminidase activity Source: ProtInc

GO - Biological processi

  1. aging Source: Ensembl
  2. dATP metabolic process Source: Ensembl
  3. glycoprotein catabolic process Source: ProtInc
  4. N-acetylglucosamine metabolic process Source: Ensembl
  5. necrotic cell death Source: Ensembl
  6. negative regulation of cardiac muscle adaptation Source: Ensembl
  7. negative regulation of protein glycosylation Source: Ensembl
  8. positive regulation of calcium ion transport into cytosol Source: Ensembl
  9. positive regulation of cell killing Source: Ensembl
  10. positive regulation of DNA metabolic process Source: Ensembl
  11. positive regulation of glucose import Source: Ensembl
  12. positive regulation of growth hormone secretion Source: Ensembl
  13. positive regulation of insulin secretion Source: Ensembl
  14. positive regulation of mitochondrial depolarization Source: Ensembl
  15. positive regulation of protein complex disassembly Source: Ensembl
  16. positive regulation of proteolysis Source: Ensembl
  17. protein targeting to membrane Source: Ensembl
  18. response to steroid hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Glycosidase, Hydrolase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS03036-MONOMER.
BRENDAi3.2.1.35. 2681.

Protein family/group databases

CAZyiGH84. Glycoside Hydrolase Family 84.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein NCOAT
Alternative name(s):
Meningioma-expressed antigen 5
Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
Including the following 2 domains:
Protein O-GlcNAcase (EC:3.2.1.169)
Alternative name(s):
Glycoside hydrolase O-GlcNAcase
Hexosaminidase C
N-acetyl-beta-D-glucosaminidase
N-acetyl-beta-glucosaminidase
O-GlcNAcase
Short name:
OGA
Histone acetyltransferase (EC:2.3.1.48)
Short name:
HAT
Gene namesi
Name:MGEA5
Synonyms:HEXC, KIAA0679, MEA5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:7056. MGEA5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30787.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916Bifunctional protein NCOATPRO_0000252118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei364 – 3641Phosphoserine4 Publications
Disulfide bondi777 ↔ 793By similarity

Post-translational modificationi

Proteolytically cleaved by caspase-3.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO60502.
PaxDbiO60502.
PRIDEiO60502.

PTM databases

PhosphoSiteiO60502.

Miscellaneous databases

PMAP-CutDBO60502.

Expressioni

Tissue specificityi

Ubiquitous. Shows highest expression in the brain, placenta and pancreas.2 Publications

Gene expression databases

BgeeiO60502.
CleanExiHS_MGEA5.
ExpressionAtlasiO60502. baseline and differential.
GenevestigatoriO60502.

Organism-specific databases

HPAiHPA036141.

Interactioni

Subunit structurei

Monomer. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding. Interacts with CLOCK (By similarity).By similarity

Protein-protein interaction databases

BioGridi115948. 28 interactions.
IntActiO60502. 17 interactions.
STRINGi9606.ENSP00000354850.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YDQX-ray2.60T402-408[»]
ProteinModelPortaliO60502.
SMRiO60502. Positions 61-331, 717-916.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni583 – 916334Histone acetyltransferase activityBy similarityAdd
BLAST
Regioni695 – 814120Required for histone H4 bindingBy similarityAdd
BLAST

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00390000007726.
HOVERGENiHBG053044.
InParanoidiO60502.
KOiK15719.
OMAiLIKVDIH.
OrthoDBiEOG7P02H7.
PhylomeDBiO60502.
TreeFamiTF313732.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR011496. Beta-N-acetylglucosaminidase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07555. NAGidase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55729. SSF55729. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60502-1) [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
MVQKESQATL EERESELSSN PAASAGASLE PPAAPAPGED NPAGAGGAAV
60 70 80 90 100
AGAAGGARRF LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD
110 120 130 140 150
YKHRMFWREM YSVEEAEQLM TLISAAREYE IEFIYAISPG LDITFSNPKE
160 170 180 190 200
VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM CAADKEVFSS FAHAQVSITN
210 220 230 240 250
EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK LLPGIEVLWT
260 270 280 290 300
GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
310 320 330 340 350
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED
360 370 380 390 400
STVSIQIKLE NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR
410 420 430 440 450
QVAHSGAKAS VVDGTPLVAA PSLNATTVVT TVYQEPIMSQ GAALSGEPTT
460 470 480 490 500
LTKEEEKKQP DEEPMDMVVE KQEETDHKND NQILSEIVEA KMAEELKPMD
510 520 530 540 550
TDKESIAESK SPEMSMQEDC ISDIAPMQTD EQTNKEQFVP GPNEKPLYTA
560 570 580 590 600
EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
610 620 630 640 650
SEKIEEWRSR AAKFEEMCGL VMGMFTRLSN CANRTILYDM YSYVWDIKSI
660 670 680 690 700
MSMVKSFVQW LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND
710 720 730 740 750
LFFQPPPLTP TSKVYTIRPY FPKDEASVYK ICREMYDDGV GLPFQSQPDL
760 770 780 790 800
IGDKLVGGLL SLSLDYCFVL EDEDGICGYA LGTVDVTPFI KKCKISWIPF
810 820 830 840 850
MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP SLIKMDIHKK
860 870 880 890 900
VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
910
KMEGFPKDVV ILGRSL
Length:916
Mass (Da):102,915
Last modified:March 1, 2001 - v2
Checksum:i01F8A64A9B1475C6
GO
Isoform 2 (identifier: O60502-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     346-398: Missing.
     691-704: Missing.

Show »
Length:849
Mass (Da):95,331
Checksum:iA65EFD64BE0AD17C
GO
Isoform 3 (identifier: O60502-3) [UniParc]FASTAAdd to Basket

Also known as: MGEA5s

The sequence of this isoform differs from the canonical sequence as follows:
     663-677: CRSHSSAQFLIGDQE → RCTRNNLFSSNILSL
     678-916: Missing.

Show »
Length:677
Mass (Da):76,193
Checksum:iBF83DEF3ABDE4AA8
GO
Isoform 4 (identifier: O60502-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     346-398: Missing.

Show »
Length:863
Mass (Da):96,932
Checksum:iD6AB77EE6830F570
GO

Sequence cautioni

The sequence AAH47877.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAA31654.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461G → E.
Corresponds to variant rs3740421 [ dbSNP | Ensembl ].
VAR_027761
Natural varianti602 – 6021E → K.1 Publication
Corresponds to variant rs17853930 [ dbSNP | Ensembl ].
VAR_027762

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei346 – 39853Missing in isoform 2 and isoform 4. CuratedVSP_020866Add
BLAST
Alternative sequencei663 – 67715CRSHS…IGDQE → RCTRNNLFSSNILSL in isoform 3. 1 PublicationVSP_020867Add
BLAST
Alternative sequencei678 – 916239Missing in isoform 3. 1 PublicationVSP_020868Add
BLAST
Alternative sequencei691 – 70414Missing in isoform 2. CuratedVSP_020869Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF036144 mRNA. Translation: AAD05385.2.
AF307332 mRNA. Translation: AAG21428.1.
AB014579 mRNA. Translation: BAA31654.2. Different initiation.
AC010789 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49744.1.
CH471066 Genomic DNA. Translation: EAW49741.1.
CH471066 Genomic DNA. Translation: EAW49742.1.
BC001343 mRNA. Translation: AAH01343.1.
BC039583 mRNA. Translation: AAH39583.2.
BC047877 mRNA. Translation: AAH47877.1. Sequence problems.
CCDSiCCDS44471.1. [O60502-4]
CCDS7520.1. [O60502-1]
PIRiT00360.
RefSeqiNP_001135906.1. NM_001142434.1. [O60502-4]
NP_036347.1. NM_012215.3. [O60502-1]
UniGeneiHs.500842.

Genome annotation databases

EnsembliENST00000357797; ENSP00000350445; ENSG00000198408. [O60502-2]
ENST00000361464; ENSP00000354850; ENSG00000198408. [O60502-1]
ENST00000370094; ENSP00000359112; ENSG00000198408. [O60502-3]
ENST00000439817; ENSP00000409973; ENSG00000198408. [O60502-4]
GeneIDi10724.
KEGGihsa:10724.
UCSCiuc001ktv.2. human. [O60502-1]
uc001ktw.2. human. [O60502-3]
uc009xws.2. human. [O60502-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF036144 mRNA. Translation: AAD05385.2 .
AF307332 mRNA. Translation: AAG21428.1 .
AB014579 mRNA. Translation: BAA31654.2 . Different initiation.
AC010789 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW49744.1 .
CH471066 Genomic DNA. Translation: EAW49741.1 .
CH471066 Genomic DNA. Translation: EAW49742.1 .
BC001343 mRNA. Translation: AAH01343.1 .
BC039583 mRNA. Translation: AAH39583.2 .
BC047877 mRNA. Translation: AAH47877.1 . Sequence problems.
CCDSi CCDS44471.1. [O60502-4 ]
CCDS7520.1. [O60502-1 ]
PIRi T00360.
RefSeqi NP_001135906.1. NM_001142434.1. [O60502-4 ]
NP_036347.1. NM_012215.3. [O60502-1 ]
UniGenei Hs.500842.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YDQ X-ray 2.60 T 402-408 [» ]
ProteinModelPortali O60502.
SMRi O60502. Positions 61-331, 717-916.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115948. 28 interactions.
IntActi O60502. 17 interactions.
STRINGi 9606.ENSP00000354850.

Chemistry

BindingDBi O60502.
ChEMBLi CHEMBL5921.

Protein family/group databases

CAZyi GH84. Glycoside Hydrolase Family 84.

PTM databases

PhosphoSitei O60502.

Proteomic databases

MaxQBi O60502.
PaxDbi O60502.
PRIDEi O60502.

Protocols and materials databases

DNASUi 10724.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357797 ; ENSP00000350445 ; ENSG00000198408 . [O60502-2 ]
ENST00000361464 ; ENSP00000354850 ; ENSG00000198408 . [O60502-1 ]
ENST00000370094 ; ENSP00000359112 ; ENSG00000198408 . [O60502-3 ]
ENST00000439817 ; ENSP00000409973 ; ENSG00000198408 . [O60502-4 ]
GeneIDi 10724.
KEGGi hsa:10724.
UCSCi uc001ktv.2. human. [O60502-1 ]
uc001ktw.2. human. [O60502-3 ]
uc009xws.2. human. [O60502-2 ]

Organism-specific databases

CTDi 10724.
GeneCardsi GC10M103534.
HGNCi HGNC:7056. MGEA5.
HPAi HPA036141.
MIMi 604039. gene.
neXtProti NX_O60502.
PharmGKBi PA30787.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0454.
GeneTreei ENSGT00390000007726.
HOVERGENi HBG053044.
InParanoidi O60502.
KOi K15719.
OMAi LIKVDIH.
OrthoDBi EOG7P02H7.
PhylomeDBi O60502.
TreeFami TF313732.

Enzyme and pathway databases

BioCyci MetaCyc:HS03036-MONOMER.
BRENDAi 3.2.1.35. 2681.

Miscellaneous databases

ChiTaRSi MGEA5. human.
GeneWikii MGEA5.
GenomeRNAii 10724.
NextBioi 40709.
PMAP-CutDB O60502.
PROi O60502.
SOURCEi Search...

Gene expression databases

Bgeei O60502.
CleanExi HS_MGEA5.
ExpressionAtlasi O60502. baseline and differential.
Genevestigatori O60502.

Family and domain databases

Gene3Di 3.40.630.30. 2 hits.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR011496. Beta-N-acetylglucosaminidase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF07555. NAGidase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Novel immunogenic antigen homologous to hyaluronidase in meningioma."
    Heckel D., Comtesse N., Brass N., Blin N., Zang K.D., Meese E.
    Hum. Mol. Genet. 7:1859-1872(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    Tissue: Meningioma.
  2. "Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase."
    Comtesse N., Maldener E., Meese E.
    Biochem. Biophys. Res. Commun. 283:634-640(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain."
    Gao Y., Wells L., Comer F.I., Parker G.J., Hart G.W.
    J. Biol. Chem. 276:9838-9845(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain.
  4. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1), VARIANT LYS-602.
    Tissue: Cervix, Eye and Skin.
  9. "Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase."
    Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A., Hart G.W.
    J. Biol. Chem. 277:1755-1761(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PTM, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNCOAT_HUMAN
AccessioniPrimary (citable) accession number: O60502
Secondary accession number(s): B7WPB9
, D3DR79, E9PGF9, O75166, Q86WV0, Q8IV98, Q9BVA5, Q9HAR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 113 of the entry and version 2 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

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3