UBE2I

Functionⁱ

Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. 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'.9 Publications

Pathwayⁱ: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	93	Glycyl thioester intermediate		1
Siteⁱ	100 – 101	Substrate binding		2

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
bHLH transcription factor binding Source: Ensembl
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17087506
HLH domain binding Source: Ensembl
protein C-terminus binding Source: Ensembl
RING-like zinc finger domain binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19407830
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
small protein activating enzyme binding
Source: CAFA
Inferred from physical interactionⁱ
- 15660128
SUMO conjugating enzyme activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 19955185
SUMO transferase activity
Source: Reactome
Inferred from experimentⁱ
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19744555
ubiquitin-protein transferase activity Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell cycle Source: UniProtKB-KW
cell division Source: UniProtKB-KW
cellular protein modification process
Source: ProtInc
Traceable author statementⁱ
- 8798754
chromosome segregation Source: UniProtKB-KW
negative regulation of transcription, DNA-templated
Source: BHF-UCL
Inferred from direct assayⁱ
- 16631117
negative regulation of transcription by RNA polymerase II
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19955185
positive regulation of DNA-binding transcription factor activity Source: Ensembl
positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
positive regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
positive regulation of SUMO transferase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 19955185
proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
protein sumoylation
Source: UniProtKB
Inferred from direct assayⁱ
- 21968017
regulation of signaling receptor activity Source: Ensembl
ubiquitin-dependent protein catabolic process
Source: ProtInc
Traceable author statementⁱ
- 8565643
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Cell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1221632 Meiotic synapsis R-HSA-196791 Vitamin D (calciferol) metabolism R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9) R-HSA-3108214 SUMOylation of DNA damage response and repair proteins R-HSA-3232118 SUMOylation of transcription factors R-HSA-3232142 SUMOylation of ubiquitinylation proteins R-HSA-3899300 SUMOylation of transcription cofactors R-HSA-4085377 SUMOylation of SUMOylation proteins R-HSA-4090294 SUMOylation of intracellular receptors R-HSA-4551638 SUMOylation of chromatin organization proteins R-HSA-4570464 SUMOylation of RNA binding proteins R-HSA-4615885 SUMOylation of DNA replication proteins R-HSA-4655427 SUMOylation of DNA methylation proteins R-HSA-4755510 SUMOylation of immune response proteins R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-HSA-5693607 Processing of DNA double-strand break ends R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors
SignaLinkⁱ	P63279
SIGNORⁱ	P63279
UniPathwayⁱ	UPA00886

Protein family/group databases

MoonDBⁱ	P63279 Predicted
TCDBⁱ	3.A.20.1.1 the peroxisomal protein importer (ppi) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: SUMO-conjugating enzyme UBC9 (EC:2.3.2.-1 Publication) Alternative name(s): RING-type E3 SUMO transferase UBC9 SUMO-protein ligase Ubiquitin carrier protein 9 Ubiquitin carrier protein I Ubiquitin-conjugating enzyme E2 I Ubiquitin-protein ligase I p18
Gene namesⁱ	Name:UBE2I Synonyms:UBC9, UBCE9
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 16

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000103275.18
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:12485 UBE2I
MIMⁱ	601661 gene
neXtProtⁱ	NX_P63279

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	13 – 14	RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication	2
Mutagenesisⁱ	17 – 18	RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication	2
Mutagenesisⁱ	22	F → A: Impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	25	V → A: Impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	27	V → A: Impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	42	E → A: Slightly impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	48	K → A: Slightly impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	54	E → A: Slightly impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	57	L → A: Impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	59	K → A: Impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	61	R → A: Slightly impairs binding to RANBP2. 1 Publication	1
Mutagenesisⁱ	85	N → Q: Impairs catalytic activity. 1 Publication	1
Mutagenesisⁱ	87	Y → A: Impairs catalytic activity. 1 Publication	1
Mutagenesisⁱ	93	C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels.	1
Mutagenesisⁱ	100 – 101	DK → AA: Impairs catalytic activity. 1 Publication	2
Mutagenesisⁱ	127	D → A: Impairs catalytic activity. 1 Publication	1
Mutagenesisⁱ	127	D → S: No effect on catalytic activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	7329
Open Targets More...OpenTargetsⁱ	ENSG00000103275
PharmGKBⁱ	PA37134

Chemistry databases

ChEMBLⁱ	CHEMBL1741191

ChEMBLⁱ

CHEMBL1741191

Polymorphism and mutation databases

BioMutaⁱ	UBE2I
DMDMⁱ	54039791

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000082454	2 – 158	SUMO-conjugating enzyme UBC9Add BLAST		157

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineCombined sources	1
Cross-linkⁱ	18	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linkⁱ	18	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-linkⁱ	48	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	49	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linkⁱ	49	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	65	N6-acetyllysineCombined sources	1
Modified residueⁱ	71	Phosphoserine; by CDK1Combined sources1 Publication	1
Cross-linkⁱ	101	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationⁱ

Phosphorylation at Ser-71 significantly enhances SUMOylation activity.1 Publication

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P63279
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P63279
PaxDbⁱ	P63279
PeptideAtlas More...PeptideAtlasⁱ	P63279
PRIDEⁱ	P63279
ProteomicsDBⁱ	12715 57517
TopDownProteomicsⁱ	P63279

PTM databases

iPTMnetⁱ	P63279
PhosphoSitePlusⁱ	P63279
SwissPalmⁱ	P63279

Expressionⁱ

Tissue specificityⁱ

Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000103275 Expressed in 235 organ(s), highest expression level in oocyte
CleanExⁱ	HS_UBE2I
ExpressionAtlasⁱ	P63279 baseline and differential
Genevisibleⁱ	P63279 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB009021 HPA003909

HPAⁱ

CAB009021
HPA003909

Interactionⁱ

Subunit structureⁱ

Interacts with SETX (PubMed:24105744). 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 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. Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1. Interacts with ZNF451. Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of the same UBE2I molecule. Interacts with CPEB3 (By similarity). Interacts with SUMO1P1/SUMO5 (PubMed:27211601).By similarityCurated28 Publications

(Microbial infection) Interacts with human herpesvirus 6 IE2.1 Publication

(Microbial infection) Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation.2 Publications

(Microbial infection) Interacts with Epstein-barr virus protein LMP1.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	4	Interaction with RANBP2	1
Siteⁱ	25	Interaction with RANBP2	1
Siteⁱ	57	Interaction with RANBP2	1

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	G2XKQ0	3	EBI-80168,EBI-10175576
	P29991	3	EBI-80168,EBI-8826488	From Dengue virus type 2 (strain 16681-PDK53).
BHLHE40	O14503	3	EBI-80168,EBI-711810
CHMP4B	Q9H444	3	EBI-80168,EBI-749627
DAXX	Q9UER7	3	EBI-80168,EBI-77321
DNMT3B	Q9UBC3	3	EBI-80168,EBI-80125
E1	P03116	2	EBI-80168,EBI-7015985	From Bovine papillomavirus type 1.
EDARADD	Q8WWZ3	3	EBI-80168,EBI-2949647
ELK1	P19419	7	EBI-80168,EBI-726632
GMCL1	Q96IK5	4	EBI-80168,EBI-2548508
GOLGA2	Q08379	4	EBI-80168,EBI-618309
HDAC4	P56524	3	EBI-80168,EBI-308629
IPO13	O94829	6	EBI-80168,EBI-747310
LMP1	P03230	5	EBI-80168,EBI-6973030	From Epstein-Barr virus (strain B95-8).
PIAS2	O75928	8	EBI-80168,EBI-348555
RANGAP1	P46060	8	EBI-80168,EBI-396091
RNF111	Q6ZNA4	5	EBI-80168,EBI-2129175
RUVBL1	Q9Y265	3	EBI-80168,EBI-353675
RWDD3	Q9Y3V2	5	EBI-80168,EBI-1549885
SETX	Q7Z333	3	EBI-80168,EBI-1220123
SMAD4	Q13485	4	EBI-80168,EBI-347263
SOX10	P56693	2	EBI-80168,EBI-1167533
SUMO1	P63165	9	EBI-80168,EBI-80140
SUMO2	P61956	6	EBI-80168,EBI-473220
TFAP2A	P05549	4	EBI-80168,EBI-347351
TFAP2C	Q92754	5	EBI-80168,EBI-937309
TFCP2	Q12800	4	EBI-80168,EBI-717422
UBA1	P22314	2	EBI-80168,EBI-709688
ZBTB26	Q9HCK0	3	EBI-80168,EBI-3918996
ZCCHC7	Q8N3Z6	3	EBI-80168,EBI-7265024
ZNF451	Q9Y4E5	3	EBI-80168,EBI-747230

GO - Molecular functionⁱ

bHLH transcription factor binding Source: Ensembl
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17087506
HLH domain binding Source: Ensembl
protein C-terminus binding Source: Ensembl
RING-like zinc finger domain binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19407830
small protein activating enzyme binding
Source: CAFA
Inferred from physical interactionⁱ
- 15660128
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19744555

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	113177, 508 interactors
ComplexPortalⁱ	CPX-3043 sumoylated E2 ligase complex (SUMO1) CPX-3049 sumoylated E2 ligase complex (SUMO2) CPX-3050 sumoylated E2 ligase complex (SUMO3) CPX-3051 sumoylated E2 ligase complex (SUMO4)
CORUMⁱ	P63279
Database of interacting proteins More...DIPⁱ	DIP-29078N
ELMⁱ	P63279
IntActⁱ	P63279, 198 interactors
Molecular INTeraction database More...MINTⁱ	P63279
STRINGⁱ	9606.ENSP00000324897

Chemistry databases

BindingDBⁱ

P63279

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 18	Combined sources	16
Beta strandⁱ	25 – 30	Combined sources	6
Beta strandⁱ	32 – 34	Combined sources	3
Beta strandⁱ	36 – 46	Combined sources	11
Turnⁱ	52 – 55	Combined sources	4
Beta strandⁱ	57 – 63	Combined sources	7
Turnⁱ	66 – 69	Combined sources	4
Beta strandⁱ	74 – 79	Combined sources	6
Beta strandⁱ	90 – 92	Combined sources	3
Helixⁱ	95 – 97	Combined sources	3
Turnⁱ	99 – 102	Combined sources	4
Helixⁱ	109 – 121	Combined sources	13
Helixⁱ	131 – 139	Combined sources	9
Helixⁱ	141 – 154	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	P63279
SMRⁱ	P63279
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P63279

EvolutionaryTraceⁱ

P63279

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	13 – 18	Interaction with SUMO1		6

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG0424 Eukaryota COG5078 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000075088
HOGENOMⁱ	HOG000233454
HOVERGENⁱ	HBG063308
InParanoidⁱ	P63279
KEGG Orthology (KO) More...KOⁱ	K10577
OMAⁱ	KCKFTPP
PhylomeDBⁱ	P63279
TreeFamⁱ	TF101122

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00195 UBCc, 1 hit
Gene3Dⁱ	3.10.110.10, 1 hit
InterProⁱ	View protein in InterPro IPR027230 Ubc9 IPR000608 UBQ-conjugat_E2 IPR023313 UBQ-conjugating_AS IPR016135 UBQ-conjugating_enzyme/RWD
PANTHERⁱ	PTHR43927 PTHR43927, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00179 UQ_con, 1 hit
SUPFAMⁱ	SSF54495 SSF54495, 1 hit
PROSITEⁱ	View protein in PROSITE PS00183 UBIQUITIN_CONJUGAT_1, 1 hit PS50127 UBIQUITIN_CONJUGAT_2, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show all Align All

P63279-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

B0QYN7	B0QYN7_HUMAN	SUMO-conjugating enzyme UBC9 SUMO-conjugating enzyme UBC9	UBE2I	184	Annotation score:
H3BQQ9	H3BQQ9_HUMAN	SUMO-conjugating enzyme UBC9 SUMO-conjugating enzyme UBC9	UBE2I	137	Annotation score:
H3BPC4	H3BPC4_HUMAN	SUMO-conjugating enzyme UBC9 SUMO-conjugating enzyme UBC9	UBE2I	70	Annotation score:
H3BRD1	H3BRD1_HUMAN	SUMO-conjugating enzyme UBC9 SUMO-conjugating enzyme UBC9	UBE2I	29	Annotation score:

Sequence cautionⁱ

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

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	18	K → P in AAC50603 (PubMed:8668125).Curated		1
Sequence conflictⁱ	86 – 89	VYPS → GVPF in AAC50603 (PubMed:8668125).Curated		4

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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 No translation available. 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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10433.1
PIRⁱ	JC6056
NCBI Reference Sequences More...RefSeqⁱ	NP_003336.1, NM_003345.4 NP_919235.1, NM_194259.2 NP_919236.1, NM_194260.2 NP_919237.1, NM_194261.2 XP_016879129.1, XM_017023640.1
UniGeneⁱ	Hs.302903

Genome annotation databases

Ensemblⁱ	ENST00000325437; ENSP00000324897; ENSG00000103275 ENST00000355803; ENSP00000348056; ENSG00000103275 ENST00000397514; ENSP00000380649; ENSG00000103275 ENST00000397515; ENSP00000380650; ENSG00000103275 ENST00000403747; ENSP00000385009; ENSG00000103275 ENST00000406620; ENSP00000384568; ENSG00000103275 ENST00000566587; ENSP00000457064; ENSG00000103275
GeneIDⁱ	7329
KEGGⁱ	hsa:7329
UCSC genome browser More...UCSCⁱ	uc002clc.2 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P63279	SUMO-conjugating enzyme UBC9		CHICK		158	UniRef100_P63279
SUMO-conjugating enzyme UBC9		ICTTR		158
SUMO-conjugating enzyme UBC9	)	MOUSE		158
SUMO-conjugating enzyme UBC9		RAT		158
SUMO-conjugating enzyme UBC9		XENLA		158
+85

Protein	Similar proteins		Species	Score	Length	Source
P63279	SUMO-conjugating enzyme UBC9		CHICK		158	UniRef90_P63279
SUMO-conjugating enzyme UBC9		ICTTR		158
SUMO-conjugating enzyme UBC9	)	MOUSE		158
SUMO-conjugating enzyme UBC9		RAT		158
SUMO-conjugating enzyme UBC9		XENLA		158
+85

Protein	Similar proteins		Species	Score	Length	Source
P63279	SUMO-conjugating enzyme UBC9		CHICK		158	UniRef50_P63279
SUMO-conjugating enzyme UBC9		ICTTR		158
SUMO-conjugating enzyme UBC9	)	MOUSE		158
SUMO-conjugating enzyme UBC9		RAT		158
SUMO-conjugating enzyme UBC9		XENLA		158
+298

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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 No translation available. 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.
CCDSⁱ	CCDS10433.1
PIRⁱ	JC6056
RefSeqⁱ	NP_003336.1, NM_003345.4 NP_919235.1, NM_194259.2 NP_919236.1, NM_194260.2 NP_919237.1, NM_194261.2 XP_016879129.1, XM_017023640.1
UniGeneⁱ	Hs.302903

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4W5V	X-ray	2.50	A	1-158	[»]
	4Y1L	X-ray	2.70	A/B	1-158	[»]
	5D2M	X-ray	2.40	A/D	1-158	[»]
	5F6D	X-ray	1.55	A	2-158	[»]
	5F6E	X-ray	1.12	A	2-158	[»]
	5F6U	X-ray	1.55	A	2-158	[»]
	5F6V	X-ray	1.49	A	2-158	[»]
	5F6W	X-ray	1.70	A	2-158	[»]
	5F6X	X-ray	1.56	A	2-158	[»]
	5F6Y	X-ray	1.14	A	2-158	[»]
	5FQ2	X-ray	2.20	A	1-158	[»]
ProteinModelPortalⁱ	P63279
SMRⁱ	P63279
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	113177, 508 interactors
ComplexPortalⁱ	CPX-3043 sumoylated E2 ligase complex (SUMO1) CPX-3049 sumoylated E2 ligase complex (SUMO2) CPX-3050 sumoylated E2 ligase complex (SUMO3) CPX-3051 sumoylated E2 ligase complex (SUMO4)
CORUMⁱ	P63279
DIPⁱ	DIP-29078N
ELMⁱ	P63279
IntActⁱ	P63279, 198 interactors
MINTⁱ	P63279
STRINGⁱ	9606.ENSP00000324897

Chemistry databases

BindingDBⁱ	P63279
ChEMBLⁱ	CHEMBL1741191

Protein family/group databases

MoonDBⁱ	P63279 Predicted
TCDBⁱ	3.A.20.1.1 the peroxisomal protein importer (ppi) family

PTM databases

iPTMnetⁱ	P63279
PhosphoSitePlusⁱ	P63279
SwissPalmⁱ	P63279

Polymorphism and mutation databases

BioMutaⁱ	UBE2I
DMDMⁱ	54039791

Proteomic databases

EPDⁱ	P63279
MaxQBⁱ	P63279
PaxDbⁱ	P63279
PeptideAtlasⁱ	P63279
PRIDEⁱ	P63279
ProteomicsDBⁱ	12715 57517
TopDownProteomicsⁱ	P63279

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	7329
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000325437; ENSP00000324897; ENSG00000103275 ENST00000355803; ENSP00000348056; ENSG00000103275 ENST00000397514; ENSP00000380649; ENSG00000103275 ENST00000397515; ENSP00000380650; ENSG00000103275 ENST00000403747; ENSP00000385009; ENSG00000103275 ENST00000406620; ENSP00000384568; ENSG00000103275 ENST00000566587; ENSP00000457064; ENSG00000103275
GeneIDⁱ	7329
KEGGⁱ	hsa:7329
UCSCⁱ	uc002clc.2 human

Organism-specific databases

CTDⁱ	7329
DisGeNETⁱ	7329
EuPathDBⁱ	HostDB:ENSG00000103275.18
GeneCardsⁱ	UBE2I
HGNCⁱ	HGNC:12485 UBE2I
HPAⁱ	CAB009021 HPA003909
MIMⁱ	601661 gene
neXtProtⁱ	NX_P63279
OpenTargetsⁱ	ENSG00000103275
PharmGKBⁱ	PA37134
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0424 Eukaryota COG5078 LUCA
GeneTreeⁱ	ENSGT00550000075088
HOGENOMⁱ	HOG000233454
HOVERGENⁱ	HBG063308
InParanoidⁱ	P63279
KOⁱ	K10577
OMAⁱ	KCKFTPP
PhylomeDBⁱ	P63279
TreeFamⁱ	TF101122

Enzyme and pathway databases

UniPathwayⁱ	UPA00886
Reactomeⁱ	R-HSA-1221632 Meiotic synapsis R-HSA-196791 Vitamin D (calciferol) metabolism R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9) R-HSA-3108214 SUMOylation of DNA damage response and repair proteins R-HSA-3232118 SUMOylation of transcription factors R-HSA-3232142 SUMOylation of ubiquitinylation proteins R-HSA-3899300 SUMOylation of transcription cofactors R-HSA-4085377 SUMOylation of SUMOylation proteins R-HSA-4090294 SUMOylation of intracellular receptors R-HSA-4551638 SUMOylation of chromatin organization proteins R-HSA-4570464 SUMOylation of RNA binding proteins R-HSA-4615885 SUMOylation of DNA replication proteins R-HSA-4655427 SUMOylation of DNA methylation proteins R-HSA-4755510 SUMOylation of immune response proteins R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-HSA-5693607 Processing of DNA double-strand break ends R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors
SignaLinkⁱ	P63279
SIGNORⁱ	P63279

Miscellaneous databases

ChiTaRSⁱ	UBE2I human
EvolutionaryTraceⁱ	P63279
GeneWikiⁱ	UBE2I
GenomeRNAiⁱ	7329
Protein Ontology More...PROⁱ	PR:P63279
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000103275 Expressed in 235 organ(s), highest expression level in oocyte
CleanExⁱ	HS_UBE2I
ExpressionAtlasⁱ	P63279 baseline and differential
Genevisibleⁱ	P63279 HS

Family and domain databases

CDDⁱ	cd00195 UBCc, 1 hit
Gene3Dⁱ	3.10.110.10, 1 hit
InterProⁱ	View protein in InterPro IPR027230 Ubc9 IPR000608 UBQ-conjugat_E2 IPR023313 UBQ-conjugating_AS IPR016135 UBQ-conjugating_enzyme/RWD
PANTHERⁱ	PTHR43927 PTHR43927, 1 hit
Pfamⁱ	View protein in Pfam PF00179 UQ_con, 1 hit
SUPFAMⁱ	SSF54495 SSF54495, 1 hit
PROSITEⁱ	View protein in PROSITE PS00183 UBIQUITIN_CONJUGAT_1, 1 hit PS50127 UBIQUITIN_CONJUGAT_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	UBC9_HUMAN
Accessionⁱ	P63279Primary (citable) accession number: P63279 Secondary accession number(s): D3DU69 , P50550, Q15698, Q59GX1, Q86VB3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
	Last sequence update:	October 11, 2004
	Last modified:	November 7, 2018
	This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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UniProtKB - P63279 (UBC9_HUMAN)

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SUMO-conjugating enzyme UBC9

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

Sites

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GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Sites

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: protein sumoylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ