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P63279 (UBC9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
Ubiquitin carrier protein I
Ubiquitin-conjugating enzyme E2 I
Ubiquitin-protein ligase I
p18
Gene names
Name:UBE2I
Synonyms:UBC9, UBCE9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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, SUMO3 and SUMO4 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. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Ref.1 Ref.20 Ref.25 Ref.34 Ref.35 Ref.47 Ref.48

Catalytic activity

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

Pathway

Protein modification; protein sumoylation.

Subunit structure

Interacts with HIPK1, HIPK2, PPM1J, RASD2 and TCF3 Interacts with NR2C1; the interaction promotes its sumoylation By similarity. 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 RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with DNMT1. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with human herpesvirus 6 IE2. Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation Probable. Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML-RARA oncoprotein. Interacts with IPO13. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT. Interacts with PRKRA and p53/TP53 By similarity. Interacts with UHRF2. Ref.4 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35 Ref.37 Ref.42 Ref.47 Ref.48

Subcellular location

Nucleus. Cytoplasm. Note: Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body By similarity. Ref.28 Ref.34 Ref.39

Tissue specificity

Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. Ref.5

Post-translational modification

Phosphorylation at Ser-71 significantly enhances SUMOylation activity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAH51289.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAD92225.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Traceable author statement. Source: Reactome

cellular protein modification process

Traceable author statement Ref.7. Source: ProtInc

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19955185. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.28. 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

post-translational protein modification

Traceable author statement. Source: Reactome

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein sumoylation

Inferred from direct assay PubMed 19955185. Source: BHF-UCL

regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.3. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from direct assay PubMed 9885291. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

dendrite

Inferred from electronic annotation. Source: Ensembl

fibrillar center

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 14752048. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: Ensembl

synaptonemal complex

Traceable author statement Ref.5. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RING-like zinc finger domain binding

Inferred from physical interaction PubMed 19407830. Source: UniProtKB

SUMO ligase activity

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction PubMed 17087506. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.34. Source: UniProtKB

ubiquitin-protein ligase activity

Traceable author statement PubMed 19955185. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.32
Chain2 – 158157SUMO-conjugating enzyme UBC9
PRO_0000082454

Regions

Region13 – 186Interaction with SUMO1

Sites

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

Amino acid modifications

Modified residue21N-acetylserine Ref.32 Ref.41
Modified residue651N6-acetyllysine Ref.36
Modified residue711Phosphoserine; by CDK1 Ref.40
Cross-link18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Mutagenesis13 – 142RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.22 Ref.23
Mutagenesis17 – 182RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.22 Ref.23
Mutagenesis221F → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis251V → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis271V → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis421E → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis481K → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis541E → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis571L → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis591K → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis611R → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26
Mutagenesis851N → Q: Impairs catalytic activity. Ref.22 Ref.23 Ref.46
Mutagenesis871Y → A: Impairs catalytic activity. Ref.22 Ref.23 Ref.46
Mutagenesis931C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. Ref.22 Ref.23
Mutagenesis100 – 1012DK → AA: Impairs catalytic activity. Ref.22 Ref.23
Mutagenesis1271D → A: Impairs catalytic activity. Ref.22 Ref.23 Ref.46
Mutagenesis1271D → S: No effect on catalytic activity. Ref.22 Ref.23 Ref.46
Sequence conflict181K → P in AAC50603. Ref.6
Sequence conflict86 – 894VYPS → GVPF in AAC50603. Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P63279 [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]"Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9."
Yasugi T., Howley P.M.
Nucleic Acids Res. 24:2005-2010(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization."
Tachibana M., Iwata N., Watanabe A., Nobukuni Y., Ploplis B., Kajigaya S.
Cytogenet. Cell Genet. 75:222-223(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning, expression, and mapping of UBE2I, a novel gene encoding a human homologue of yeast ubiquitin-conjugating enzymes which are critical for regulating the cell cycle."
Watanabe T.K., Fujiwara T., Kawai A., Shimizu F., Takami S., Hirano H., Okuno S., Ozaki K., Takeda S., Shimada Y., Nagata M., Takaichi A., Takahashi E., Nakamura Y., Shin S.
Cytogenet. Cell Genet. 72:86-89(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[4]"Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9."
Masson M., Menissier-de Murcia J., Mattei M.-G., de Murcia G.M., Niedergang C.P.
Gene 190:287-296(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PARP.
[5]"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], TISSUE SPECIFICITY.
[6]"Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae."
Jiang W., Koltin Y.
Mol. Gen. Genet. 251:153-160(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9."
Wang Z.-Y., Qiu Q., Seufert W., Taguchi T., Testa J.R., Whitmore S.A., Callen D.F., Welsh D., Shenk T., Deuel T.F.
J. Biol. Chem. 271:24811-24816(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[8]Shen Z.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[9]"Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme."
Hahn S.L., Criqui-Filipe P., Wasylyk B.
Oncogene 15:1489-1495(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[10]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[12]"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]"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].
Tissue: Lung.
[16]"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: INTERACTION WITH ADENOVIRUS E1A.
[17]"Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway."
Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.
Genes Dev. 11:2701-2714(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1.
[18]"Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription."
Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.
J. Biol. Chem. 274:19441-19446(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AR.
[19]"Association of FHIT (fragile histidine triad), a candidate tumour suppressor gene, with the ubiquitin-conjugating enzyme hUBC9."
Shi Y., Zou M., Farid N.R., Paterson M.C.
Biochem. J. 352:443-448(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FHIT.
[20]"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo."
Eloranta J.J., Hurst H.C.
J. Biol. Chem. 277:30798-30804(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
[22]"Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex."
Tatham M.H., Chen Y., Hay R.T.
Biochemistry 42:3168-3179(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 100-ASP-LYS-101.
[23]"Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation."
Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.
Biochemistry 42:9959-9969(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUMO1; SUMO2; SUMO3 AND THE UBLE1A-UBLE1B E1 COMPLEX, MUTAGENESIS OF 13-ARG-LYS-14 AND 17-ARG-LYS-18.
[24]"The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type."
Pichler A., Knipscheer P., Saitoh H., Sixma T.K., Melchior F.
Nat. Struct. Mol. Biol. 11:984-991(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP2.
[25]"Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation."
Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.
Biochem. Biophys. Res. Commun. 330:746-754(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE PML-RARALPHA ONCOPROTEIN, FUNCTION.
[26]"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection."
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.
Nat. Struct. Mol. Biol. 12:67-74(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP2, MUTAGENESIS OF PHE-22; VAL-25; VAL-27; GLU-42; LYS-48; GLU-54; LEU-57; LYS-59 AND ARG-61.
[27]"A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."
Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H., Chock P.B.
Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[28]"Ubc9 interacts with SOX4 and represses its transcriptional activity."
Pan X., Li H., Zhang P., Jin B., Man J., Tian L., Su G., Zhao J., Li W., Liu H., Gong W., Zhou T., Zhang X.
Biochem. Biophys. Res. Commun. 344:727-734(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SOX4.
[29]"Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation."
Tomoiu A., Gravel A., Tanguay R.M., Flamand L.
J. Virol. 80:10218-10228(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HERPESVIRUS 6 IE2.
[30]"RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia."
Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M., Silberstein S., Stalla G.K., Holsboer F., Arzt E.
Cell 131:309-323(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RWDD3.
[31]"Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response."
Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z., Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S., Wu Q., Reddy S.E. expand/collapse author list , Hu R., Huang H., Jin C., Yao X.
Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
[32]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[33]"SUMOylation enhances DNA methyltransferase 1 activity."
Lee B., Muller M.T.
Biochem. J. 421:449-461(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNMT1.
[34]"Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the Steroidogenic Acute Regulatory gene."
Kuo F.T., Bentsi-Barnes I.K., Barlow G.M., Bae J., Pisarska M.D.
Cell. Signal. 21:1935-1944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FOXL2, ROLE IN FOXL2 SUMOYLATION, SUBCELLULAR LOCATION.
[35]"SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle."
Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R., Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.
FASEB J. 23:3917-3927(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNM1L, FUNCTION IN DNM1L SUMOYLATION.
[36]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation."
Yousef A.F., Fonseca G.J., Pelka P., Ablack J.N., Walsh C., Dick F.A., Bazett-Jones D.P., Shaw G.S., Mymryk J.S.
Oncogene 29:4693-4704(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
[38]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"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: SUBCELLULAR LOCATION.
[40]"Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity."
Su Y.F., Yang T., Huang H., Liu L.F., Hwang J.
PLoS ONE 7:E34250-E34250(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-71.
[41]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131."
Oh Y., Chung K.C.
J. Biol. Chem. 288:9102-9111(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UHRF2.
[43]"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).
[44]"Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1."
Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.
Cell 108:345-356(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH RANGAP1.
[45]"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
Reverter D., Lima C.D.
Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SUMO1; RANGAP1 AND RANBP2.
[46]"Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway."
Yunus A.A., Lima C.D.
Nat. Struct. Mol. Biol. 13:491-499(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH RANGAP1, MUTAGENESIS OF ASN-85; TYR-87 AND ASP-127.
[47]"Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction."
Capili A.D., Lima C.D.
J. Mol. Biol. 369:608-618(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUMO1, INTERACTION WITH SUMO1; SUMO2 AND SUMO3, FUNCTION.
[48]"Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45."
Sekiyama N., Arita K., Ikeda Y., Hashiguchi K., Ariyoshi M., Tochio H., Saitoh H., Shirakawa M.
Proteins 78:1491-1502(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NFATC2IP/NIP45, INTERACTION WITH NFATC2IP, FUNCTION.
[49]"Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation."
Grunwald M., Bono F.
EMBO J. 30:427-438(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH IPO13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96427 mRNA. Translation: CAA65287.1.
U45328 mRNA. Translation: AAA86662.1.
D45050 mRNA. Translation: BAA08091.1.
U29092 mRNA. Translation: AAC51361.1.
U31933 mRNA. Translation: AAB02181.1.
U31882 mRNA. Translation: AAC50603.1.
U66867 mRNA. Translation: AAC50716.1.
U66818 mRNA. Translation: AAC50715.1.
U38785 mRNA. Translation: AAB09410.1.
AJ002385 mRNA. Translation: CAA05359.1.
BT006932 mRNA. Translation: AAP35578.1.
AB208988 mRNA. Translation: BAD92225.1. Different initiation.
AE006466 Genomic DNA. Translation: AAK61274.1.
AL031714 Genomic DNA. Translation: CAB45853.1.
CH471112 Genomic DNA. Translation: EAW85673.1.
CH471112 Genomic DNA. Translation: EAW85676.1.
CH471112 Genomic DNA. Translation: EAW85677.1.
CH471112 Genomic DNA. Translation: EAW85678.1.
CH471112 Genomic DNA. Translation: EAW85679.1.
BC000427 mRNA. Translation: AAH00427.1.
BC004429 mRNA. Translation: AAH04429.1.
BC051289 mRNA. Translation: AAH51289.3. Different initiation.
PIRJC6056.
RefSeqNP_003336.1. NM_003345.4.
NP_919235.1. NM_194259.2.
NP_919236.1. NM_194260.2.
NP_919237.1. NM_194261.2.
UniGeneHs.302903.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3SX-ray2.80A1-158[»]
1KPSX-ray2.50A/C1-158[»]
1Z5Qmodel-A1-158[»]
1Z5SX-ray3.01A1-158[»]
2GRNX-ray1.80A1-158[»]
2GROX-ray1.70A1-158[»]
2GRPX-ray2.05A1-158[»]
2GRQX-ray1.70A1-158[»]
2GRRX-ray1.30A1-158[»]
2O25X-ray2.60C/D1-158[»]
2PE6X-ray2.40A1-158[»]
2PX9NMR-B1-158[»]
2XWUX-ray2.80A1-158[»]
3A4SX-ray2.70A/B1-158[»]
3UINX-ray2.60A1-158[»]
3UIOX-ray2.60A1-158[»]
3UIPX-ray2.29A1-158[»]
ProteinModelPortalP63279.
SMRP63279. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113177. 282 interactions.
DIPDIP-29078N.
IntActP63279. 138 interactions.
MINTMINT-137807.
STRING9606.ENSP00000324897.

Chemistry

BindingDBP63279.

Protein family/group databases

TCDB3.A.20.1.1. the peroxisomal protein importer (ppi) family.

PTM databases

PhosphoSiteP63279.

Polymorphism databases

DMDM54039791.

Proteomic databases

PaxDbP63279.
PeptideAtlasP63279.
PRIDEP63279.

Protocols and materials databases

DNASU7329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325437; ENSP00000324897; ENSG00000103275.
ENST00000355803; ENSP00000348056; ENSG00000103275.
ENST00000397514; ENSP00000380649; ENSG00000103275.
ENST00000397515; ENSP00000380650; ENSG00000103275.
ENST00000403747; ENSP00000385009; ENSG00000103275.
ENST00000406620; ENSP00000384568; ENSG00000103275.
ENST00000566587; ENSP00000457064; ENSG00000103275.
GeneID7329.
KEGGhsa:7329.
UCSCuc002clc.2. human.

Organism-specific databases

CTD7329.
GeneCardsGC16P001359.
HGNCHGNC:12485. UBE2I.
HPACAB009021.
HPA003909.
MIM601661. gene.
neXtProtNX_P63279.
PharmGKBPA37134.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
HOVERGENHBG063308.
KOK10577.
OMAWEGGVYK.
OrthoDBEOG7B8S5F.
PhylomeDBP63279.
TreeFamTF101122.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
SignaLinkP63279.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressP63279.
BgeeP63279.
CleanExHS_UBE2I.
GenevestigatorP63279.

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. human.
EvolutionaryTraceP63279.
GeneWikiUBE2I.
GenomeRNAi7329.
NextBio28682.
PROP63279.
SOURCESearch...

Entry information

Entry nameUBC9_HUMAN
AccessionPrimary (citable) accession number: P63279
Secondary accession number(s): D3DU69 expand/collapse secondary AC list , P50550, Q15698, Q59GX1, Q86VB3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM