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Q6ZPJ3

- UBE2O_MOUSE

UniProt

Q6ZPJ3 - UBE2O_MOUSE

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Protein

E2/E3 hybrid ubiquitin-protein ligase UBE2O

Gene
Ube2o, Kiaa1734
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity. Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis. 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. 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 By similarity.

Catalytic activityi

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

Enzyme regulationi

Inhibited by inorganic arsenite such as phenylarsenoxides.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1037 – 10371Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. 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

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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 (EC:6.3.2.19)
Ubiquitin-conjugating enzyme E2 of 230 kDa
Short name:
Ubiquitin-conjugating enzyme E2-230K
Ubiquitin-protein ligase O
Gene namesi
Name:Ube2o
Synonyms:Kiaa1734
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2444266. Ube2o.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Mainly localizes to the cytoplasm By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12881288E2/E3 hybrid ubiquitin-protein ligase UBE2OPRO_0000280638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphoserine1 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei394 – 3941Phosphoserine By similarity
Modified residuei436 – 4361Phosphoserine By similarity
Modified residuei833 – 8331Phosphoserine1 Publication
Modified residuei836 – 8361Phosphoserine1 Publication
Modified residuei893 – 8931Phosphoserine By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation affects subcellular location By similarity.
Ubiquitinated: autoubiquitinates, possibly affecting its subcellulat location By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6ZPJ3.
PaxDbiQ6ZPJ3.
PRIDEiQ6ZPJ3.

PTM databases

PhosphoSiteiQ6ZPJ3.

Expressioni

Tissue specificityi

Highly expressed in reticulocytes.1 Publication

Inductioni

By EPO/Erythropoietin which induces erythroid differentiation.2 Publications

Gene expression databases

BgeeiQ6ZPJ3.
CleanExiMM_UBE2O.
GenevestigatoriQ6ZPJ3.

Interactioni

Protein-protein interaction databases

BioGridi229895. 4 interactions.
IntActiQ6ZPJ3. 1 interaction.
MINTiMINT-7034165.

Structurei

3D structure databases

ProteinModelPortaliQ6ZPJ3.
SMRiQ6ZPJ3. Positions 932-1161.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili809 – 87971 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 3837Ala-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110680.
HOGENOMiHOG000231096.
HOVERGENiHBG080116.
InParanoidiA2A7X3.
KOiK10581.
OMAiCAQGEGS.
OrthoDBiEOG7GN2KX.
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.

Q6ZPJ3-1 [UniParc]FASTAAdd to Basket

« Hide

MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG     50
SQRLLFSHDL VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG 100
GAGHEEGRAS PLRRGYVRVQ WYPEGVKQHV KETKLKLEDR SVVPRDVVRH 150
MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY PVNSKDLQHI WPFMYGDYIA 200
YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP HVSDSGLFFD 250
DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK 300
VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY 350
VFPAKVEPAK IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ 400
CPRDHSMEDP DKKGEARAGS EIGSASPEEQ PDGSASPVEM QDEGSEELQE 450
TCEPLPPFLL KEGGDDGLHS AEQDADDEAA DDTDDTSSVT SSASSTTSSQ 500
SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA VEVVTTMTSA 550
DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG 600
VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT 650
TDIVIRIGNT EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ 700
HLYNIESEIE ESDYDSVEGS SSGASSDEWE DDSDSWETDN GLVDDEHPKI 750
EELAAILPAE QPTAPEEDKG VVISEEAATA AIQGAVAMAA PVAGLMEKAG 800
KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE PEKPTREKKF 850
LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP 900
SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK 950
FFSTVRKEMA LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL 1000
FDIQLPNIYP AVPPHFCYLS QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE 1050
RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG FDSDRGLQEG YENSRCYNEM 1100
ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE SWLETHAMQE 1150
RAQVMPNGAL KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG 1200
GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI 1250
GFPLFPLSKG FIKSIRGVLT QFRAALLEAG MPESTEDK 1288
Length:1,288
Mass (Da):140,834
Last modified:July 27, 2011 - v3
Checksum:iD2BCE5F36A687CE1
GO

Sequence cautioni

The sequence AAA69916.1 differs from that shown. Reason: Frameshift at positions 344, 367, 374 and 411.
The sequence AAH59193.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAC32345.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAC98241.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091C → S in AAA69916. 1 Publication
Sequence conflicti317 – 3193SPP → CPR in AAA69916. 1 Publication
Sequence conflicti343 – 3431Q → H in AAA69916. 1 Publication
Sequence conflicti871 – 8711A → G in BAC32345. 1 Publication
Sequence conflicti1160 – 11601L → P in BAC98241. 1 Publication
Sequence conflicti1160 – 11601L → P in AAH59193. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK129431 mRNA. Translation: BAC98241.1. Different initiation.
AL645851, AL607039 Genomic DNA. Translation: CAM17106.1.
AL607039, AL645851 Genomic DNA. Translation: CAM20507.1.
U20780 mRNA. Translation: AAA69916.1. Frameshift.
BC059193 mRNA. Translation: AAH59193.1. Different initiation.
AK045398 mRNA. Translation: BAC32345.1. Different initiation.
CCDSiCCDS25670.1.
PIRiI49264.
RefSeqiNP_776116.2. NM_173755.3.
UniGeneiMm.243950.

Genome annotation databases

EnsembliENSMUST00000082152; ENSMUSP00000080791; ENSMUSG00000020802.
GeneIDi217342.
KEGGimmu:217342.
UCSCiuc007mlm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK129431 mRNA. Translation: BAC98241.1 . Different initiation.
AL645851 , AL607039 Genomic DNA. Translation: CAM17106.1 .
AL607039 , AL645851 Genomic DNA. Translation: CAM20507.1 .
U20780 mRNA. Translation: AAA69916.1 . Frameshift.
BC059193 mRNA. Translation: AAH59193.1 . Different initiation.
AK045398 mRNA. Translation: BAC32345.1 . Different initiation.
CCDSi CCDS25670.1.
PIRi I49264.
RefSeqi NP_776116.2. NM_173755.3.
UniGenei Mm.243950.

3D structure databases

ProteinModelPortali Q6ZPJ3.
SMRi Q6ZPJ3. Positions 932-1161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229895. 4 interactions.
IntActi Q6ZPJ3. 1 interaction.
MINTi MINT-7034165.

PTM databases

PhosphoSitei Q6ZPJ3.

Proteomic databases

MaxQBi Q6ZPJ3.
PaxDbi Q6ZPJ3.
PRIDEi Q6ZPJ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000082152 ; ENSMUSP00000080791 ; ENSMUSG00000020802 .
GeneIDi 217342.
KEGGi mmu:217342.
UCSCi uc007mlm.1. mouse.

Organism-specific databases

CTDi 63893.
MGIi MGI:2444266. Ube2o.
Rougei Search...

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000110680.
HOGENOMi HOG000231096.
HOVERGENi HBG080116.
InParanoidi A2A7X3.
KOi K10581.
OMAi CAQGEGS.
OrthoDBi EOG7GN2KX.
TreeFami TF325556.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi UBE2O. mouse.
NextBioi 375789.
PROi Q6ZPJ3.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZPJ3.
CleanExi MM_UBE2O.
Genevestigatori Q6ZPJ3.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Induction of ubiquitin-conjugating enzymes during terminal erythroid differentiation."
    Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J., Pickart C.M., Finley D.
    Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-628, TISSUE SPECIFICITY, INDUCTION.
    Tissue: Reticulocyte.
  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 123-1288.
    Strain: FVB/N.
    Tissue: Liver.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 867-1288.
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  6. "Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis involving a thiol relay?"
    Berleth E.S., Pickart C.M.
    Biochemistry 35:1664-1671(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiUBE2O_MOUSE
AccessioniPrimary (citable) accession number: Q6ZPJ3
Secondary accession number(s): A2A7X3
, Q60800, Q6PCR9, Q7TPN2, Q8BLE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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