Reviewed, UniProtKB/Swiss-Prot P63279 (UBC9_HUMAN)

Names and origin

Protein names

Recommended name:
    SUMO-conjugating enzyme UBC9
    EC=6.3.2.-
Alternative name(s):
    SUMO-protein ligase
    Ubiquitin-conjugating enzyme E2 I
    Ubiquitin-protein ligase I
    Ubiquitin carrier protein I
    Ubiquitin carrier protein 9
    p18

Gene names

Name:	UBE2I
Synonyms:	UBC9, UBCE9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Essential for nuclear architecture and chromosome segregation. Ref.1 Ref.18
Catalytic activity	ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.
Pathway	Protein modification; protein sumoylation.
Subunit structure	Interacts with HIPK1, HIPK2 and PPM1J By similarity. Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TCF3, TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with human adenovirus E1A and human herpesvirus 6 IE2. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B.
Subcellular location	Nucleus. Ref.25
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Host-virus interaction Mitosis Ubl conjugation pathway
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Ref.25 Inferred from direct assay. Source: UniProtKB post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro ubiquitin-dependent protein catabolic process Ref.3 Traceable author statement. Source: ProtInc
Cellular component	PML body Inferred from direct assay. Source: UniProtKB synaptonemal complex Ref.5 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW small conjugating protein ligase activity Inferred from electronic annotation. Source: InterPro specific transcriptional repressor activity Ref.25 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BHLHE40	O14503	2	EBI-80168,EBI-711810
DNMT3B	Q9UBC3	1	EBI-80168,EBI-80125
HNRNPD	Q14103	2	EBI-80168,EBI-299674
HNRNPD	Q14103-4	1	EBI-80168,EBI-432545
RANBP2	P49792	1	EBI-80168,EBI-973138
RANGAP1	P46060	1	EBI-80168,EBI-396091
RWDD3	Q9Y3V2	1	EBI-80168,EBI-1549885
SAE1	Q9UBE0	1	EBI-80168,EBI-743154
SUMO1	P63165	1	EBI-80168,EBI-80140
SUMO3	P55854	1	EBI-80168,EBI-474067
TFAP2C	Q92754	2	EBI-80168,EBI-937309
UBA1	P22314	1	EBI-80168,EBI-709688
UBA2	Q9UBT2	1	EBI-80168,EBI-718569

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

Cross-link

18

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.28

Experimental info

Mutagenesis

13 – 14

2

RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.20 Ref.21

Mutagenesis

17 – 18

2

RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.20 Ref.21

Mutagenesis

22

1

F → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

25

1

V → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

27

1

V → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

42

1

E → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

48

1

K → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

54

1

E → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

57

1

L → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

59

1

K → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

61

1

R → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23

Mutagenesis

85

1

N → Q: Impairs catalytic activity. Ref.20 Ref.21 Ref.33

Mutagenesis

87

1

Y → A: Impairs catalytic activity. Ref.20 Ref.21 Ref.33

Mutagenesis

93

1

C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. Ref.20 Ref.21

Mutagenesis

100 – 101

2

DK → AA: Impairs catalytic activity. Ref.20 Ref.21

Mutagenesis

127

1

D → A: Impairs catalytic activity. Ref.20 Ref.21 Ref.33

Mutagenesis

127

1

D → S: No effect on catalytic activity. Ref.20 Ref.21 Ref.33

Sequence conflict

18

1

K → P in AAC50603. Ref.6

Sequence conflict

86 – 89

4

VYPS → GVPF in AAC50603. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

158

Helix Strand Turn

Details...

Helix

3 – 18

16

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)
	P63279-1 [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: 8668529] [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: 9067428] [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: 8565643] [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: 9197546] [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: 8610150] [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: 8668125] [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: 8798754] [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: 9333025] [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: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"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: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[15]	"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: 8824223] [Abstract] Cited for: INTERACTION WITH ADENOVIRUS E1A.
[16]	"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: 9334332] [Abstract] Cited for: INTERACTION WITH SIAH1.
[17]	"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: 10383460] [Abstract] Cited for: INTERACTION WITH AR.
[18]	"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: 11451954] [Abstract] Cited for: FUNCTION.
[19]	"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: 12072434] [Abstract] Cited for: INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
[20]	"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: 12641448] [Abstract] Cited for: MUTAGENESIS OF 100-ASP-LYS-101.
[21]	"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: 12924945] [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.
[22]	"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: 15378033] [Abstract] Cited for: INTERACTION WITH RANBP2.
[23]	"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: 15608651] [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.
[24]	"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: 16620772] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[25]	"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: 16631117] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SOX4.
[26]	"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: 17005699] [Abstract] Cited for: INTERACTION WITH HERPESVIRUS 6 IE2.
[27]	"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: 17956732] [Abstract] Cited for: INTERACTION WITH RWDD3.
[28]	"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: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-18, MASS SPECTROMETRY.
[29]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[30]	"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: 9261152] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[31]	"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: 11853669] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH RANGAP1.
[32]	"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex." Reverter D., Lima C.D. Nature 435:687-692(2005) [PubMed: 15931224] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SUMO1; RANGAP1 AND RANBP2.
[33]	"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: 16732283] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH RANGAP1, MUTAGENESIS OF ASN-85; TYR-87 AND ASP-127.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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.
NP_919235.1.
NP_919236.1.
NP_919237.1.

UniGene

Hs.302903

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29078N.

IntAct

P63279. 49 interactions.

PTM databases

PhosphoSite

P63279.

Proteomic databases

PeptideAtlas

P63279.

PRIDE

P63279.

Genome annotation databases

Ensembl

ENSG00000103275. Homo sapiens. [Contig view]

GeneID

7329.

KEGG

hsa:7329.

Organism-specific databases

GeneCards

GC16P001299.

H-InvDB

HIX0012677.
HIX0038735.

HGNC

HGNC:12485. UBE2I.

HPA

CAB009021.
HPA003909.

MIM

601661. gene.

PharmGKB

PA37134.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P63279.

OMA

P63279. KQWRKDH.

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.

Gene expression databases

ArrayExpress

P63279.

Bgee

P63279.

CleanEx

HS_UBE2I.

GermOnline

ENSG00000103275. Homo sapiens.

Family and domain databases

InterPro

IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

ProDom

PD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
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NextBio

28682.

SOURCE

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Entry information

Entry name

UBC9_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)