P63279 (UBC9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.20 Ref.25 Ref.34 Ref.35 Ref.43 Ref.44
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. 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.43 Ref.44
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
Tissue specificity	Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. Ref.5
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 process	Cell cycle Cell division Chromosome partition Host-virus interaction Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW 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 positive regulation of intracellular steroid hormone receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara protein sumoylation Inferred from direct assay PubMed 19955185. Source: BHF-UCL regulation of receptor activity Inferred from electronic annotation. Source: Compara ubiquitin-dependent protein catabolic process Traceable author statement Ref.3. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from direct assay PubMed 9885291. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from electronic annotation. Source: Compara fibrillar center Inferred from electronic annotation. Source: Compara synapse Inferred from electronic annotation. Source: Compara synaptonemal complex Traceable author statement Ref.5. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO ligase activity Inferred from electronic annotation. Source: Compara ubiquitin-protein ligase activity Traceable author statement PubMed 19955185. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BHLHE40	O14503	3	EBI-80168,EBI-711810
DNMT3B	Q9UBC3	3	EBI-80168,EBI-80125
HDAC4	P56524	3	EBI-80168,EBI-308629
PIAS2	O75928	5	EBI-80168,EBI-348555
RWDD3	Q9Y3V2	5	EBI-80168,EBI-1549885
SMAD4	Q13485	3	EBI-80168,EBI-347263
TFAP2C	Q92754	3	EBI-80168,EBI-937309
UBA1	P22314	2	EBI-80168,EBI-709688

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 158

158

SUMO-conjugating enzyme UBC9

PRO_0000082454

Regions

Region

13 – 18

6

Interaction with SUMO1

Sites

Active site

93

1

Glycyl thioester intermediate

Site

4

1

Interaction with RANBP2

Site

25

1

Interaction with RANBP2

Site

57

1

Interaction with RANBP2

Site

100 – 101

2

Substrate binding

Amino acid modifications

Modified residue

65

1

N6-acetyllysine Ref.36

Cross-link

18

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.31

Experimental info

Mutagenesis

13 – 14

2

RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.22 Ref.23

Mutagenesis

17 – 18

2

RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.22 Ref.23

Mutagenesis

22

1

F → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

25

1

V → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

27

1

V → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

42

1

E → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

48

1

K → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

54

1

E → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

57

1

L → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

59

1

K → A: Impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

61

1

R → A: Slightly impairs binding to RANBP2. Ref.22 Ref.23 Ref.26

Mutagenesis

85

1

N → Q: Impairs catalytic activity. Ref.22 Ref.23 Ref.42

Mutagenesis

87

1

Y → A: Impairs catalytic activity. Ref.22 Ref.23 Ref.42

Mutagenesis

93

1

C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. Ref.22 Ref.23

Mutagenesis

100 – 101

2

DK → AA: Impairs catalytic activity. Ref.22 Ref.23

Mutagenesis

127

1

D → A: Impairs catalytic activity. Ref.22 Ref.23 Ref.42

Mutagenesis

127

1

D → S: No effect on catalytic activity. Ref.22 Ref.23 Ref.42

Sequence conflict

18

1

K → P in AAC50603. Ref.6

Sequence conflict

86 – 89

4

VYPS → GVPF in AAC50603. Ref.6

Secondary structure

1

.

.

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.

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158

Helix Strand Turn

Details...

Helix

3 – 18

16

Beta strand

25 – 30

6

Beta strand

32 – 34

3

Beta strand

36 – 46

11

Turn

52 – 55

4

Beta strand

57 – 63

7

Turn

66 – 69

4

Beta strand

74 – 79

6

Beta strand

90 – 92

3

Helix

95 – 97

3

Turn

99 – 102

4

Helix

109 – 121

13

Helix

131 – 139

9

Helix

141 – 154

14

Sequences

	Sequence		Length	Mass (Da)
	P63279 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: E2C826E9C8D0683D	FASTA	158	18,007
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-18, MASS SPECTROMETRY.
[32]	"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. , 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.
[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, MASS SPECTROMETRY.
[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]	"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).
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.

IPI

IPI00032957.

PIR

JC6056.

RefSeq

NP_003336.1. NM_003345.4.
NP_919235.1. NM_194259.2.
NP_919236.1. NM_194260.2.
NP_919237.1. NM_194261.2.

UniGene

Hs.302903.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3S	X-ray	2.80	A	1-158	[»]
1KPS	X-ray	2.50	A/C	1-158	[»]
1Z5Q	model	-	A	1-158	[»]
1Z5S	X-ray	3.01	A	1-158	[»]
2GRN	X-ray	1.80	A	1-158	[»]
2GRO	X-ray	1.70	A	1-158	[»]
2GRP	X-ray	2.05	A	1-158	[»]
2GRQ	X-ray	1.70	A	1-158	[»]
2GRR	X-ray	1.30	A	1-158	[»]
2O25	X-ray	2.60	C/D	1-158	[»]
2PE6	X-ray	2.40	A	1-158	[»]
2PX9	NMR	-	B	1-158	[»]
2XWU	X-ray	2.80	A	1-158	[»]
3A4S	X-ray	2.70	A/B	1-158	[»]
3UIN	X-ray	2.60	A	1-158	[»]
3UIO	X-ray	2.60	A	1-158	[»]
3UIP	X-ray	2.29	A	1-158	[»]

ProteinModelPortal

P63279.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29078N.

IntAct

P63279. 119 interactions.

MINT

MINT-137807.

STRING

9606.ENSP00000324897.

PTM databases

PhosphoSite

P63279.

Polymorphism databases

DMDM

54039791.

Proteomic databases

PaxDb

P63279.

PeptideAtlas

P63279.

PRIDE

P63279.

Protocols and materials databases

DNASU

7329.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000325437; ENSP00000324897; ENSG00000103275.
ENST00000355803; ENSP00000348056; ENSG00000103275.
ENST00000397514; ENSP00000380649; ENSG00000103275.
ENST00000397515; ENSP00000380650; ENSG00000103275.
ENST00000403747; ENSP00000385009; ENSG00000103275.
ENST00000406620; ENSP00000384568; ENSG00000103275.
ENST00000566587; ENSP00000457064; ENSG00000103275.

GeneID

7329.

KEGG

hsa:7329.

UCSC

uc002clc.2. human.

Organism-specific databases

CTD

7329.

GeneCards

GC16P001359.

HGNC

HGNC:12485. UBE2I.

HPA

CAB009021.
HPA003909.

MIM

601661. gene.

neXtProt

NX_P63279.

PharmGKB

PA37134.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233454.

HOVERGEN

HBG063308.

KO

K10577.

OMA

PFGFYAK.

OrthoDB

EOG4RXZ19.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.

UniPathway

UPA00886.

Gene expression databases

ArrayExpress

P63279.

Bgee

P63279.

CleanEx

HS_UBE2I.

Genevestigator

P63279.

GermOnline

ENSG00000103275. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

PANTHER

PTHR24067:SF51. PTHR24067:SF51. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P63279.

ChEMBL

CHEMBL1741191.

ChiTaRS

UBE2I. human.

EvolutionaryTrace

P63279.

GenomeRNAi

7329.

NextBio

28682.

SOURCE

Search...

Entry information

Entry name

UBC9_HUMAN

Accession

Primary (citable) accession number: P63279
Secondary accession number(s): D3DU69 , P50550, Q15698, Q59GX1, Q86VB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.