Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6ZPJ3 (UBE2O_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 O
EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein O
Ubiquitin-conjugating enzyme E2 of 230 kDa
Short name=Ubiquitin-conjugating enzyme E2-230K
Ubiquitin-protein ligase O
Gene names
Name:Ube2o
Synonyms:Kiaa1734
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins By similarity.

Catalytic activity

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

Enzyme regulation

Inhibited by inorganic arsenite such as phenylarsenoxides. Ref.6

Pathway

Protein modification; protein ubiquitination.

Tissue specificity

Highly expressed in reticulocytes. Ref.3

Induction

By EPO/Erythropoietin which induces erythroid differentiation. Ref.3 Ref.6

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

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.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12881288Ubiquitin-conjugating enzyme E2 O
PRO_0000280638

Regions

Coiled coil809 – 87971 Potential
Compositional bias2 – 3837Ala-rich

Sites

Active site10371Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue821Phosphoserine Ref.7 Ref.8
Modified residue841Phosphoserine Ref.7 Ref.8
Modified residue3941Phosphoserine By similarity
Modified residue4361Phosphoserine By similarity
Modified residue8331Phosphoserine Ref.7
Modified residue8361Phosphoserine Ref.7
Modified residue8931Phosphoserine Ref.8

Experimental info

Sequence conflict3091C → S in AAA69916. Ref.3
Sequence conflict317 – 3193SPP → CPR in AAA69916. Ref.3
Sequence conflict3431Q → H in AAA69916. Ref.3
Sequence conflict8711A → G in BAC32345. Ref.4
Sequence conflict11601L → P in BAC98241. Ref.1
Sequence conflict11601L → P in AAH59193. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q6ZPJ3 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: D2BCE5F36A687CE1

FASTA1,288140,834
        10         20         30         40         50         60 
MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG SQRLLFSHDL 

        70         80         90        100        110        120 
VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG GAGHEEGRAS PLRRGYVRVQ 

       130        140        150        160        170        180 
WYPEGVKQHV KETKLKLEDR SVVPRDVVRH MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY 

       190        200        210        220        230        240 
PVNSKDLQHI WPFMYGDYIA YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP 

       250        260        270        280        290        300 
HVSDSGLFFD DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK 

       310        320        330        340        350        360 
VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY VFPAKVEPAK 

       370        380        390        400        410        420 
IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ CPRDHSMEDP DKKGEARAGS 

       430        440        450        460        470        480 
EIGSASPEEQ PDGSASPVEM QDEGSEELQE TCEPLPPFLL KEGGDDGLHS AEQDADDEAA 

       490        500        510        520        530        540 
DDTDDTSSVT SSASSTTSSQ SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA 

       550        560        570        580        590        600 
VEVVTTMTSA DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG 

       610        620        630        640        650        660 
VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT TDIVIRIGNT 

       670        680        690        700        710        720 
EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ HLYNIESEIE ESDYDSVEGS 

       730        740        750        760        770        780 
SSGASSDEWE DDSDSWETDN GLVDDEHPKI EELAAILPAE QPTAPEEDKG VVISEEAATA 

       790        800        810        820        830        840 
AIQGAVAMAA PVAGLMEKAG KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE 

       850        860        870        880        890        900 
PEKPTREKKF LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP 

       910        920        930        940        950        960 
SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK FFSTVRKEMA 

       970        980        990       1000       1010       1020 
LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL FDIQLPNIYP AVPPHFCYLS 

      1030       1040       1050       1060       1070       1080 
QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG 

      1090       1100       1110       1120       1130       1140 
FDSDRGLQEG YENSRCYNEM ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE 

      1150       1160       1170       1180       1190       1200 
SWLETHAMQE RAQVMPNGAL KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG 

      1210       1220       1230       1240       1250       1260 
GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI GFPLFPLSKG 

      1270       1280 
FIKSIRGVLT QFRAALLEAG MPESTEDK

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND SER-836, MASS SPECTROMETRY.
Tissue: Liver.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84 AND SER-893, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00453803.
PIRI49264.
RefSeqNP_776116.2. NM_173755.3.
UniGeneMm.243950.

3D structure databases

HSSPHSSP built from PDB template 1ZDN based on UniProtKB Q16763.
ProteinModelPortalQ6ZPJ3.
SMRQ6ZPJ3. Positions 932-1161.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-7034165.

PTM databases

PhosphoSiteQ6ZPJ3.

Proteomic databases

PaxDbQ6ZPJ3.
PRIDEQ6ZPJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000082152; ENSMUSP00000080791; ENSMUSG00000020802.
GeneID217342.
KEGGmmu:217342.

Organism-specific databases

CTD63893.
MGIMGI:2444266. Ube2o.
RougeSearch...

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00680000099547.
HOGENOMHOG000231096.
HOVERGENHBG080116.
InParanoidA2A7X3.
KOK10581.
OMACFDHAQR.
OrthoDBEOG45DWP7.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ6ZPJ3.
CleanExMM_UBE2O.
GenevestigatorQ6ZPJ3.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2O. mouse.
NextBio375789.
SOURCESearch...

Entry information

Entry nameUBE2O_MOUSE
AccessionPrimary (citable) accession number: Q6ZPJ3
Secondary accession number(s): A2A7X3 expand/collapse secondary AC list , Q60800, Q6PCR9, Q7TPN2, Q8BLE8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents