P63280 (UBC9_MOUSE) 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
Short name=mUBC9
Ubiquitin carrier protein I
Ubiquitin-conjugating enzyme E2 I
Ubiquitin-protein ligase I

Gene names

Name:	Ube2i
Synonyms:	Ubc9, Ubce2i, Ubce9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 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. Ref.10 Ref.13
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. Ref.2 Ref.4 Ref.9 Ref.11 Ref.12 Ref.13
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
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 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	Developmental protein 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 cellular protein modification process Traceable author statement PubMed 10806190. Source: ProtInc chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW mitosis 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: 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 electronic annotation. Source: UniProtKB-UniPathway regulation of receptor activity Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from electronic annotation. Source: Compara fibrillar center Inferred from electronic annotation. Source: Compara nuclear body Inferred from direct assay Ref.14. Source: UniProtKB synapse Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO ligase activity Inferred from electronic annotation. Source: Compara ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 158

158

SUMO-conjugating enzyme UBC9

PRO_0000082456

Regions

Region

13 – 18

6

Interaction with SUMO1 By similarity

Sites

Active site

93

1

Glycyl thioester intermediate

Site

4

1

Interaction with RANBP2 By similarity

Site

25

1

Interaction with RANBP2 By similarity

Site

57

1

Interaction with RANBP2 By similarity

Site

100 – 101

2

Substrate binding By similarity

Amino acid modifications

Modified residue

65

1

N6-acetyllysine By similarity

Cross-link

18

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1

.

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158

Helix Strand Turn

Details...

Helix

4 – 18

15

Beta strand

25 – 30

6

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)
	P63280 [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]	"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]	"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. , 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]	"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.

IPI

IPI00119227.

RefSeq

NP_001171080.1. NM_001177609.1.
NP_001171081.1. NM_001177610.1.
NP_035795.1. NM_011665.4.
XP_003946066.1. XM_003946017.1.

UniGene

Mm.240044.
Mm.384234.
Mm.442797.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P63280.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29276N.

IntAct

P63280. 6 interactions.

MINT

MINT-1526807.

PTM databases

PhosphoSite

P63280.

Proteomic databases

PaxDb

P63280.

PRIDE

P63280.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000049911; ENSMUSP00000055714; ENSMUSG00000015120.
ENSMUST00000172618; ENSMUSP00000134169; ENSMUSG00000015120.
ENSMUST00000173084; ENSMUSP00000134261; ENSMUSG00000015120.
ENSMUST00000173713; ENSMUSP00000134491; ENSMUSG00000015120.
ENSMUST00000174001; ENSMUSP00000134450; ENSMUSG00000015120.
ENSMUST00000174031; ENSMUSP00000134350; ENSMUSG00000015120.

GeneID

100044900.
22196.

KEGG

mmu:100044900.
mmu:22196.

UCSC

uc008bai.2. mouse.

Organism-specific databases

CTD

7329.

MGI

MGI:107365. Ube2i.

Phylogenomic databases

eggNOG

COG5078.

GeneTree

ENSGT00550000075088.

HOGENOM

HOG000233454.

HOVERGEN

HBG063308.

InParanoid

P63280.

KO

K10577.

OMA

PFGFYAK.

OrthoDB

EOG4RXZ19.

Enzyme and pathway databases

Reactome

REACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_75800. Meiotic Synapsis (mouse).

UniPathway

UPA00886.

Gene expression databases

ArrayExpress

P63280.

Bgee

P63280.

CleanEx

MM_UBE2I.

Genevestigator

P63280.

GermOnline

ENSMUSG00000015120. Mus musculus.

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

P63280.

ChiTaRS

UBE2I. mouse.

EvolutionaryTrace

P63280.

NextBio

302181.

SOURCE

Search...

Entry information

Entry name

UBC9_MOUSE

Accession

Primary (citable) accession number: P63280
Secondary accession number(s): P50550 , Q15698, Q6RUT3, 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 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program