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P63280 (UBC9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SUMO-conjugating enzyme UBC9

EC=6.3.2.-
Alternative name(s):
SUMO-protein ligase
Ubiquitin carrier protein 9
Short name=mUBC9
Ubiquitin carrier protein I
Ubiquitin-conjugating enzyme E2 I
Ubiquitin-protein ligase I
Gene names
Name:Ube2i
Synonyms:Ubc9, Ubce2i, Ubce9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 By similarity. Sumoylates p53/TP53 at 'Lys-386'. Ref.10 Ref.13 Ref.15

Catalytic activity

ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.

Pathway

Protein modification; protein sumoylation.

Subunit structure

Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RASD2. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with DNM1L (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in the B domain By similarity. Interacts with HIPK1, HIPK2, PPM1J and TCF3. Interacts with Moloney murine leukemia virus CA and adenovirus type 5 and type 12 E1A. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT By similarity. Interacts with PRKRA and p53/TP53. Interacts with UHRF2 By similarity. Ref.2 Ref.4 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

Nucleus. Cytoplasm. Note: Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body. Ref.3 Ref.5 Ref.14

Tissue specificity

Present in spleen, kidney, lung, brain, heart and testis (at protein level). Ref.4

Post-translational modification

Phosphorylation at Ser-71 significantly enhances SUMOylation activity By similarity.

Disruption phenotype

Death prior to E7.5 due to major defects in nuclear organization. Ref.10

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Host-virus interaction
Mitosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Ligase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein modification process

Traceable author statement PubMed 10806190. Source: ProtInc

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 16127449. Source: BHF-UCL

positive regulation of intracellular steroid hormone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein sumoylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from electronic annotation. Source: Ensembl

fibrillar center

Inferred from electronic annotation. Source: Ensembl

nuclear body

Inferred from direct assay Ref.14. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

HLH domain binding

Inferred from physical interaction Ref.4. Source: UniProtKB

SUMO ligase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 21836637. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Egr2P081522EBI-80180,EBI-7070449

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 158157SUMO-conjugating enzyme UBC9
PRO_0000082456

Regions

Region13 – 186Interaction with SUMO1 By similarity

Sites

Active site931Glycyl thioester intermediate
Site41Interaction with RANBP2 By similarity
Site251Interaction with RANBP2 By similarity
Site571Interaction with RANBP2 By similarity
Site100 – 1012Substrate binding By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue651N6-acetyllysine By similarity
Modified residue711Phosphoserine; by CDK1 By similarity
Cross-link18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

........................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63280 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E2C826E9C8D0683D

FASTA15818,007
        10         20         30         40         50         60 
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL 

        70         80         90        100        110        120 
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL 

       130        140        150 
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS 

« Hide

References

« Hide 'large scale' references
[1]"E3, a hematopoietic-specific transcript directly regulated by the retinoic acid receptor alpha."
Scott L.M., Mueller L., Collins S.J.
Blood 88:2517-2530(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: MDF1.
Tissue: Promyelocytic leukemia.
[2]"mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect."
Hateboer G., Hijmans E.M., Nooij J.B.D., Schlenker S., Jentsch S., Bernards R.
J. Biol. Chem. 271:25906-25911(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADENOVIRUS TYPE 5 AND TYPE 12 E1A.
[3]"Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes."
Kovalenko O.V., Plug A.W., Haaf T., Gonda D.K., Ashley T., Ward D.C., Radding C.M., Golub E.I.
Proc. Natl. Acad. Sci. U.S.A. 93:2958-2963(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[4]"The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors."
Loveys D.A., Streiff M.B., Schaefer T.S., Kato G.J.
Gene 201:169-177(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH TCF3.
Strain: BALB/c.
Tissue: Fibroblast.
[5]"Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IkappaBalpha."
Tashiro K., Pando M.P., Kanegae Y., Wamsley P.M., Inoue S., Verma I.M.
Proc. Natl. Acad. Sci. U.S.A. 94:7862-7867(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: B-cell lymphoma.
[6]Weber B.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: PJS1.
[7]"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].
Strain: BALB/c, C57BL/6J and NOD.
Tissue: Bone marrow, Head, Heart, Kidney, Liver, Lung and Thymus.
[8]"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.
[9]"Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1."
Kim Y.H., Choi C.Y., Kim Y.
Proc. Natl. Acad. Sci. U.S.A. 96:12350-12355(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK1 AND HIPK2.
[10]"The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice."
Nacerddine K., Lehembre F., Bhaumik M., Artus J., Cohen-Tannoudji M., Babinet C., Pandolfi P.P., Dejean A.
Dev. Cell 9:769-779(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"A novel protein phosphatase 2C family member (PP2Czeta) is able to associate with ubiquitin conjugating enzyme 9."
Kashiwaba M., Katsura K., Ohnishi M., Sasaki M., Tanaka H., Nishimune Y., Kobayashi T., Tamura S.
FEBS Lett. 538:197-202(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPM1J.
[12]"Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection."
Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., Pu S.-Y., Goff S.P.
J. Virol. 80:342-352(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MOMLV CA.
[13]"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1, FUNCTION IN NR2C1 SUMOYLATION.
[14]"BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body."
Kuwata T., Nakamura T.
Genes Cells 13:931-940(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest."
Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.
Cell Cycle 11:407-417(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKRA AND TP53.
[16]"Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system."
Tong H., Hateboer G., Perrakis A., Bernards R., Sixma T.K.
J. Biol. Chem. 272:21381-21387(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94402 mRNA. Translation: AAB52424.1.
X99739 mRNA. Translation: CAA68072.1.
U31934 mRNA. Translation: AAB02182.1.
U76416 mRNA. Translation: AAB18790.1.
U82627 mRNA. Translation: AAB48446.1.
X97575 mRNA. Translation: CAA66188.1.
AK003141 mRNA. Translation: BAB22599.1.
AK005058 mRNA. Translation: BAB23783.1.
AK011239 mRNA. Translation: BAB27487.1.
AK012282 mRNA. Translation: BAB28140.1.
AK088508 mRNA. Translation: BAC40395.1.
AK150575 mRNA. Translation: BAE29670.1.
AK160014 mRNA. Translation: BAE35560.1.
AK160988 mRNA. Translation: BAE36134.1.
AK165606 mRNA. Translation: BAE38290.1.
AK165615 mRNA. Translation: BAE38295.1.
AK166016 mRNA. Translation: BAE38521.1.
AK166657 mRNA. Translation: BAE38922.1.
AK166930 mRNA. Translation: BAE39124.1.
AK167162 mRNA. Translation: BAE39303.1.
AK168212 mRNA. Translation: BAE40170.1.
AK168706 mRNA. Translation: BAE40548.1.
AK168766 mRNA. Translation: BAE40602.1.
AY491413 Genomic DNA. Translation: AAS21651.1.
CCDSCCDS28513.1.
RefSeqNP_001171080.1. NM_001177609.1.
NP_001171081.1. NM_001177610.1.
NP_035795.1. NM_011665.4.
XP_006524111.1. XM_006524048.1.
XP_006524112.1. XM_006524049.1.
XP_006524113.1. XM_006524050.1.
XP_006524114.1. XM_006524051.1.
XP_006543476.1. XM_006543413.1.
UniGeneMm.240044.
Mm.384234.
Mm.442797.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U9AX-ray2.00A1-158[»]
1U9BX-ray2.00A1-158[»]
2UYZX-ray1.40A1-158[»]
2VRRX-ray2.22A1-158[»]
ProteinModelPortalP63280.
SMRP63280. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204408. 26 interactions.
DIPDIP-29276N.
IntActP63280. 8 interactions.
MINTMINT-1526807.

Chemistry

BindingDBP63280.

PTM databases

PhosphoSiteP63280.

Proteomic databases

MaxQBP63280.
PaxDbP63280.
PRIDEP63280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049911; ENSMUSP00000055714; ENSMUSG00000015120.
ENSMUST00000172618; ENSMUSP00000134169; ENSMUSG00000015120.
ENSMUST00000173084; ENSMUSP00000134261; ENSMUSG00000015120.
ENSMUST00000173713; ENSMUSP00000134491; ENSMUSG00000015120.
ENSMUST00000174001; ENSMUSP00000134450; ENSMUSG00000015120.
ENSMUST00000174031; ENSMUSP00000134350; ENSMUSG00000015120.
GeneID102641751.
22196.
KEGGmmu:102641751.
mmu:22196.
UCSCuc008bai.2. mouse.

Organism-specific databases

CTD7329.
MGIMGI:107365. Ube2i.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00550000075088.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidP63280.
KOK10577.
OMAWEGGVYK.
OrthoDBEOG7B8S5F.
PhylomeDBP63280.
TreeFamTF101122.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressP63280.
BgeeP63280.
CleanExMM_UBE2I.
GenevestigatorP63280.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PANTHERPTHR24067:SF51. PTHR24067:SF51. 1 hit.
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2I. mouse.
EvolutionaryTraceP63280.
NextBio302181.
PROP63280.
SOURCESearch...

Entry information

Entry nameUBC9_MOUSE
AccessionPrimary (citable) accession number: P63280
Secondary accession number(s): P50550 expand/collapse secondary AC list , Q15698, Q6RUT3, Q86VB3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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