Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E2/E3 hybrid ubiquitin-protein ligase UBE2O

Gene

UBE2O

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

Functioni

E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASH1, leading to promote endosomal F-actin assembly (PubMed:23452853).4 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Enzyme regulationi

inhibited by phenylarsine oxide (PAO).1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1040 – 10401Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. ubiquitin conjugating enzyme activity Source: MGI
  5. ubiquitin-like protein transferase activity Source: GO_Central
  6. ubiquitin protein ligase activity Source: MGI
  7. ubiquitin protein ligase binding Source: GO_Central
  8. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. positive regulation of BMP signaling pathway Source: UniProtKB
  2. protein K63-linked ubiquitination Source: UniProtKB
  3. protein monoubiquitination Source: UniProtKB
  4. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transport, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9C0C9.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E2/E3 hybrid ubiquitin-protein ligase UBE2O (EC:6.3.2.-, EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein O
Ubiquitin-conjugating enzyme E2 O
Ubiquitin-conjugating enzyme E2 of 230 kDa
Short name:
Ubiquitin-conjugating enzyme E2-230K
Ubiquitin-protein ligase O
Gene namesi
Name:UBE2O
Synonyms:KIAA1734
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:29554. UBE2O.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

  3. Note: Mainly localizes to the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleoplasm Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1040 – 10401C → S: Loss of function. 2 Publications

Organism-specific databases

PharmGKBiPA142670651.

Polymorphism and mutation databases

BioMutaiUBE2O.
DMDMi209572710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12921292E2/E3 hybrid ubiquitin-protein ligase UBE2OPRO_0000280637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine1 Publication
Modified residuei87 – 871Phosphoserine4 Publications
Modified residuei89 – 891Phosphoserine4 Publications
Modified residuei399 – 3991Phosphoserine1 Publication
Modified residuei401 – 4011Phosphoserine1 Publication
Modified residuei441 – 4411Phosphoserine1 Publication
Modified residuei488 – 4881Phosphothreonine1 Publication
Modified residuei491 – 4911Phosphothreonine1 Publication
Modified residuei836 – 8361Phosphoserine2 Publications
Modified residuei839 – 8391PhosphoserineBy similarity
Modified residuei896 – 8961Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation affects subcellular location.1 Publication
Ubiquitinated: autoubiquitinates, possibly affecting its subcellulat location.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9C0C9.
PaxDbiQ9C0C9.
PRIDEiQ9C0C9.

PTM databases

PhosphoSiteiQ9C0C9.

Expressioni

Tissue specificityi

Predominantly expressed in skeletal muscle and heart.1 Publication

Gene expression databases

BgeeiQ9C0C9.
CleanExiHS_UBE2O.
GenevestigatoriQ9C0C9.

Organism-specific databases

HPAiHPA023605.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL1Q9UKG13EBI-2339946,EBI-741243
Smad6O351824EBI-2339946,EBI-4321242From a different organism.
Smad7O352532EBI-2339946,EBI-5274835From a different organism.

Protein-protein interaction databases

BioGridi121973. 46 interactions.
IntActiQ9C0C9. 27 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9C0C9.
SMRiQ9C0C9. Positions 973-1146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili812 – 88271Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi512 – 53625Nuclear localization signal1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 4342Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110680.
HOVERGENiHBG080116.
InParanoidiQ9C0C9.
KOiK10581.
OMAiGSMAKKV.
OrthoDBiEOG7GN2KX.
PhylomeDBiQ9C0C9.
TreeFamiTF325556.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C0C9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPAAPTPA APAPAQAPAP APEAVPAPAA APVPAPAPAS DSASGPSSDS
60 70 80 90 100
GPEAGSQRLL FSHDLVSGRY RGSVHFGLVR LIHGEDSDSE GEEEGRGSSG
110 120 130 140 150
CSEAGGAGHE EGRASPLRRG YVRVQWYPEG VKQHVKETKL KLEDRSVVPR
160 170 180 190 200
DVVRHMRSTD SQCGTVIDVN IDCAVKLIGT NCIIYPVNSK DLQHIWPFMY
210 220 230 240 250
GDYIAYDCWL GKVYDLKNQI ILKLSNGARC SMNTEDGAKL YDVCPHVSDS
260 270 280 290 300
GLFFDDSYGF YPGQVLIGPA KIFSSVQWLS GVKPVLSTKS KFRVVVEEVQ
310 320 330 340 350
VVELKVTWIT KSFCPGGTDS VSPPPSVITQ ENLGRVKRLG CFDHAQRQLG
360 370 380 390 400
ERCLYVFPAK VEPAKIAWEC PEKNCAQGEG SMAKKVKRLL KKQVVRIMSC
410 420 430 440 450
SPDTQCSRDH SMEDPDKKGE SKTKSEAESA SPEETPDGSA SPVEMQDEGA
460 470 480 490 500
EEPHEAGEQL PPFLLKEGRD DRLHSAEQDA DDEAADDTDD TSSVTSSASS
510 520 530 540 550
TTSSQSGSGT SRKKSIPLSI KNLKRKHKRK KNKITRDFKP GDRVAVEVVT
560 570 580 590 600
TMTSADVMWQ DGSVECNIRS NDLFPVHHLD NNEFCPGDFV VDKRVQSCPD
610 620 630 640 650
PAVYGVVQSG DHIGRTCMVK WFKLRPSGDD VELIGEEEDV SVYDIADHPD
660 670 680 690 700
FRFRTTDIVI RIGNTEDGAP HKEDEPSVGQ VARVDVSSKV EVVWADNSKT
710 720 730 740 750
IILPQHLYNI ESEIEESDYD SVEGSTSGAS SDEWEDDSDS WETDNGLVED
760 770 780 790 800
EHPKIEEPPI PPLEQPVAPE DKGVVISEEA ATAAVQGAVA MAAPMAGLME
810 820 830 840 850
KAGKDGPPKS FRELKEAIKI LESLKNMTVE QLLTGSPTSP TVEPEKPTRE
860 870 880 890 900
KKFLDDIKKL QENLKKTLDN VAIVEEEKME AVPDVERKED KPEGQSPVKA
910 920 930 940 950
EWPSETPVLC QQCGGKPGVT FTSAKGEVFS VLEFAPSNHS FKKIEFQPPE
960 970 980 990 1000
AKKFFSTVRK EMALLATSLP EGIMVKTFED RMDLFSALIK GPTRTPYEDG
1010 1020 1030 1040 1050
LYLFDIQLPN IYPAVPPHFC YLSQCSGRLN PNLYDNGKVC VSLLGTWIGK
1060 1070 1080 1090 1100
GTERWTSKSS LLQVLISIQG LILVNEPYYN EAGFDSDRGL QEGYENSRCY
1110 1120 1130 1140 1150
NEMALIRVVQ SMTQLVRRPP EVFEQEIRQH FSTGGWRLVN RIESWLETHA
1160 1170 1180 1190 1200
LLEKAQALPN GVPKASSSPE PPAVAELSDS GQQEPEDGGP APGEASQGSD
1210 1220 1230 1240 1250
SEGGAQGLAS ASRDHTDQTS ETAPDASVPP SVKPKKRRKS YRSFLPEKSG
1260 1270 1280 1290
YPDIGFPLFP LSKGFIKSIR GVLTQFRAAL LEAGMPECTE DK
Length:1,292
Mass (Da):141,293
Last modified:October 14, 2008 - v3
Checksum:iC9DF6395A32E9AB0
GO

Sequence cautioni

The sequence AAH22237.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH25977.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH36820.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH51868.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14320.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14948.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15313.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB21825.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501S → F in BAB21825 (PubMed:11214970).Curated
Sequence conflicti675 – 6751E → EQ in BAB15313 (PubMed:14702039).Curated
Sequence conflicti1047 – 10471W → C in AAH22237 (PubMed:15489334).Curated
Sequence conflicti1143 – 11431E → D in AAH25977 (PubMed:15489334).Curated
Sequence conflicti1150 – 11501A → T in BAB14320 (PubMed:14702039).Curated
Sequence conflicti1261 – 12611L → P in BAB14320 (PubMed:14702039).Curated
Sequence conflicti1290 – 12901E → G in BAB14948 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1207 – 12071G → S.4 Publications
Corresponds to variant rs3803739 [ dbSNP | Ensembl ].
VAR_031184

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051521 mRNA. Translation: BAB21825.1. Different initiation.
AC090699 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89396.1.
BC004525 mRNA. Translation: AAH04525.2.
BC022237 mRNA. Translation: AAH22237.1. Different initiation.
BC025977 mRNA. Translation: AAH25977.1. Different initiation.
BC036820 mRNA. Translation: AAH36820.1. Different initiation.
BC051868 mRNA. Translation: AAH51868.2. Different initiation.
AL832432 mRNA. Translation: CAH10644.1.
AK022940 mRNA. Translation: BAB14320.1. Different initiation.
AK024657 mRNA. Translation: BAB14948.1. Different initiation.
AK025999 mRNA. Translation: BAB15313.1. Different initiation.
CCDSiCCDS32742.1.
RefSeqiNP_071349.3. NM_022066.3.
UniGeneiHs.16130.

Genome annotation databases

EnsembliENST00000319380; ENSP00000323687; ENSG00000175931.
GeneIDi63893.
KEGGihsa:63893.
UCSCiuc002jrl.4. human.

Polymorphism and mutation databases

BioMutaiUBE2O.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051521 mRNA. Translation: BAB21825.1. Different initiation.
AC090699 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89396.1.
BC004525 mRNA. Translation: AAH04525.2.
BC022237 mRNA. Translation: AAH22237.1. Different initiation.
BC025977 mRNA. Translation: AAH25977.1. Different initiation.
BC036820 mRNA. Translation: AAH36820.1. Different initiation.
BC051868 mRNA. Translation: AAH51868.2. Different initiation.
AL832432 mRNA. Translation: CAH10644.1.
AK022940 mRNA. Translation: BAB14320.1. Different initiation.
AK024657 mRNA. Translation: BAB14948.1. Different initiation.
AK025999 mRNA. Translation: BAB15313.1. Different initiation.
CCDSiCCDS32742.1.
RefSeqiNP_071349.3. NM_022066.3.
UniGeneiHs.16130.

3D structure databases

ProteinModelPortaliQ9C0C9.
SMRiQ9C0C9. Positions 973-1146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121973. 46 interactions.
IntActiQ9C0C9. 27 interactions.

PTM databases

PhosphoSiteiQ9C0C9.

Polymorphism and mutation databases

BioMutaiUBE2O.
DMDMi209572710.

Proteomic databases

MaxQBiQ9C0C9.
PaxDbiQ9C0C9.
PRIDEiQ9C0C9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319380; ENSP00000323687; ENSG00000175931.
GeneIDi63893.
KEGGihsa:63893.
UCSCiuc002jrl.4. human.

Organism-specific databases

CTDi63893.
GeneCardsiGC17M074385.
H-InvDBHIX0020035.
HGNCiHGNC:29554. UBE2O.
HPAiHPA023605.
neXtProtiNX_Q9C0C9.
PharmGKBiPA142670651.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110680.
HOVERGENiHBG080116.
InParanoidiQ9C0C9.
KOiK10581.
OMAiGSMAKKV.
OrthoDBiEOG7GN2KX.
PhylomeDBiQ9C0C9.
TreeFamiTF325556.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9C0C9.

Miscellaneous databases

ChiTaRSiUBE2O. human.
GeneWikiiUBE2O.
GenomeRNAii63893.
NextBioi65578.
PROiQ9C0C9.

Gene expression databases

BgeeiQ9C0C9.
CleanExiHS_UBE2O.
GenevestigatoriQ9C0C9.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-1207.
    Tissue: Brain.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 270-1292, VARIANT SER-1207.
    Tissue: Brain and Skin.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-1292, VARIANT SER-1207.
    Tissue: Melanoma.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-1292, VARIANT SER-1207.
  7. "Identification, tissue expression, and chromosomal position of a novel gene encoding human ubiquitin-conjugating enzyme E2-230k."
    Yokota T., Nagai H., Harada H., Mine N., Terada Y., Fujiwara H., Yabe A., Miyazaki K., Emi M.
    Gene 267:95-100(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-401; SER-441 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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-87; SER-89 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-87 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-87; SER-89 AND SER-896, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Regulation of WASH-dependent actin polymerization and protein trafficking by ubiquitination."
    Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.
    Cell 152:1051-1064(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "UBE2O negatively regulates TRAF6-mediated NF-kappaB activation by inhibiting TRAF6 polyubiquitination."
    Zhang X., Zhang J., Zhang L., van Dam H., ten Dijke P.
    Cell Res. 23:366-377(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Fine-tuning BMP7 signalling in adipogenesis by UBE2O/E2-230K-mediated monoubiquitination of SMAD6."
    Zhang X., Zhang J., Bauer A., Zhang L., Selinger D.W., Lu C.X., Ten Dijke P.
    EMBO J. 32:996-1007(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-1040.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-87; SER-89; THR-488 AND THR-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Autodeubiquitination protects the tumor suppressor BAP1 from cytoplasmic sequestration mediated by the atypical ubiquitin ligase UBE2O."
    Mashtalir N., Daou S., Barbour H., Sen N.N., Gagnon J., Hammond-Martel I., Dar H.H., Therrien M., Affar E.B.
    Mol. Cell 54:392-406(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, PHOSPHORYLATION, UBIQUITINATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF CYS-1040.

Entry informationi

Entry nameiUBE2O_HUMAN
AccessioniPrimary (citable) accession number: Q9C0C9
Secondary accession number(s): A6NDU5
, Q69YP4, Q6PIZ2, Q86UA4, Q8N425, Q8TBN1, Q9BSW1, Q9H6E6, Q9H7E4, Q9H9B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 14, 2008
Last modified: April 29, 2015
This is version 115 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.