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P63280

- UBC9_MOUSE

UniProt

P63280 - UBC9_MOUSE

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Protein

SUMO-conjugating enzyme UBC9

Gene

Ube2i

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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'.By similarity3 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei4 – 41Interaction with RANBP2By similarity
Sitei25 – 251Interaction with RANBP2By similarity
Sitei57 – 571Interaction with RANBP2By similarity
Active sitei93 – 931Glycyl thioester intermediate
Sitei100 – 1012Substrate bindingBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. HLH domain binding Source: UniProtKB
  3. poly(A) RNA binding Source: Ensembl
  4. SUMO ligase activity Source: Ensembl
  5. ubiquitin-protein transferase activity Source: Ensembl

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. chromosome segregation Source: UniProtKB-KW
  3. mitotic nuclear division Source: UniProtKB-KW
  4. multicellular organismal development Source: UniProtKB-KW
  5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  6. positive regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
  7. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  9. protein sumoylation Source: UniProtKB-UniPathway
  10. regulation of receptor activity Source: Ensembl
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ligase

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198626. Meiotic synapsis.
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_75800. Meiotic Synapsis.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ube2i
Synonyms:Ubc9, Ubce2i, Ubce9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:107365. Ube2i.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. dendrite Source: Ensembl
  3. fibrillar center Source: Ensembl
  4. nuclear body Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. PML body Source: Ensembl
  7. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death prior to E7.5 due to major defects in nuclear organization.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 158157SUMO-conjugating enzyme UBC9PRO_0000082456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei65 – 651N6-acetyllysineBy similarity
Modified residuei71 – 711Phosphoserine; by CDK1By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP63280.
PaxDbiP63280.
PRIDEiP63280.

PTM databases

PhosphoSiteiP63280.

Expressioni

Tissue specificityi

Present in spleen, kidney, lung, brain, heart and testis (at protein level).1 Publication

Gene expression databases

BgeeiP63280.
CleanExiMM_UBE2I.
ExpressionAtlasiP63280. baseline and differential.
GenevestigatoriP63280.

Interactioni

Subunit structurei

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. Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Egr2P081522EBI-80180,EBI-7070449

Protein-protein interaction databases

BioGridi204408. 26 interactions.
DIPiDIP-29276N.
IntActiP63280. 8 interactions.
MINTiMINT-1526807.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Beta strandi25 – 306Combined sources
Beta strandi36 – 4611Combined sources
Turni52 – 554Combined sources
Beta strandi57 – 637Combined sources
Turni66 – 694Combined sources
Beta strandi74 – 796Combined sources
Beta strandi90 – 923Combined sources
Helixi95 – 973Combined sources
Turni99 – 1024Combined sources
Helixi109 – 12113Combined sources
Helixi131 – 1399Combined sources
Helixi141 – 15414Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U9AX-ray2.00A1-158[»]
1U9BX-ray2.00A1-158[»]
2UYZX-ray1.40A1-158[»]
2VRRX-ray2.22A1-158[»]
ProteinModelPortaliP63280.
SMRiP63280. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63280.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 186Interaction with SUMO1By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63280.
KOiK10577.
OMAiWEGGVYK.
OrthoDBiEOG7B8S5F.
PhylomeDBiP63280.
TreeFamiTF101122.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PANTHERiPTHR24067:SF51. PTHR24067:SF51. 1 hit.
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63280 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG
60 70 80 90 100
TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED
110 120 130 140 150
KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA

QAKKFAPS
Length:158
Mass (Da):18,007
Last modified:October 11, 2004 - v1
Checksum:iE2C826E9C8D0683D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28513.1.
RefSeqiNP_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.
UniGeneiMm.240044.
Mm.384234.
Mm.442797.

Genome annotation databases

EnsembliENSMUST00000049911; ENSMUSP00000055714; ENSMUSG00000015120.
ENSMUST00000172618; ENSMUSP00000134169; ENSMUSG00000015120.
ENSMUST00000173084; ENSMUSP00000134261; ENSMUSG00000015120.
ENSMUST00000173713; ENSMUSP00000134491; ENSMUSG00000015120.
ENSMUST00000174001; ENSMUSP00000134450; ENSMUSG00000015120.
ENSMUST00000174031; ENSMUSP00000134350; ENSMUSG00000015120.
GeneIDi102641751.
22196.
KEGGimmu:102641751.
mmu:22196.
UCSCiuc008bai.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28513.1.
RefSeqi NP_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.
UniGenei Mm.240044.
Mm.384234.
Mm.442797.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U9A X-ray 2.00 A 1-158 [» ]
1U9B X-ray 2.00 A 1-158 [» ]
2UYZ X-ray 1.40 A 1-158 [» ]
2VRR X-ray 2.22 A 1-158 [» ]
ProteinModelPortali P63280.
SMRi P63280. Positions 1-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204408. 26 interactions.
DIPi DIP-29276N.
IntActi P63280. 8 interactions.
MINTi MINT-1526807.

Chemistry

BindingDBi P63280.

PTM databases

PhosphoSitei P63280.

Proteomic databases

MaxQBi P63280.
PaxDbi P63280.
PRIDEi P63280.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049911 ; ENSMUSP00000055714 ; ENSMUSG00000015120 .
ENSMUST00000172618 ; ENSMUSP00000134169 ; ENSMUSG00000015120 .
ENSMUST00000173084 ; ENSMUSP00000134261 ; ENSMUSG00000015120 .
ENSMUST00000173713 ; ENSMUSP00000134491 ; ENSMUSG00000015120 .
ENSMUST00000174001 ; ENSMUSP00000134450 ; ENSMUSG00000015120 .
ENSMUST00000174031 ; ENSMUSP00000134350 ; ENSMUSG00000015120 .
GeneIDi 102641751.
22196.
KEGGi mmu:102641751.
mmu:22196.
UCSCi uc008bai.2. mouse.

Organism-specific databases

CTDi 7329.
MGIi MGI:107365. Ube2i.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00550000075088.
HOGENOMi HOG000233454.
HOVERGENi HBG063308.
InParanoidi P63280.
KOi K10577.
OMAi WEGGVYK.
OrthoDBi EOG7B8S5F.
PhylomeDBi P63280.
TreeFami TF101122.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_198626. Meiotic synapsis.
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

ChiTaRSi UBE2I. mouse.
EvolutionaryTracei P63280.
NextBioi 302181.
PROi P63280.
SOURCEi Search...

Gene expression databases

Bgeei P63280.
CleanExi MM_UBE2I.
ExpressionAtlasi P63280. baseline and differential.
Genevestigatori P63280.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
PANTHERi PTHR24067:SF51. PTHR24067:SF51. 1 hit.
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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).

Entry informationi

Entry nameiUBC9_MOUSE
AccessioniPrimary (citable) accession number: P63280
Secondary accession number(s): P50550
, Q15698, Q6RUT3, Q86VB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3