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Reviewed, UniProtKB/Swiss-Prot P63279 (UBC9_HUMAN)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158SUMO-conjugating enzyme UBC9
PRO_0000082454

Regions

Region13 – 186Interaction with SUMO1

Sites

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

Amino acid modifications

Cross-link18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.28

Experimental info

Mutagenesis13 – 142RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.20 Ref.21
Mutagenesis17 – 182RK → AA: Impairs binding to SUMO1 and catalytic activity. Ref.20 Ref.21
Mutagenesis221F → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis251V → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis271V → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis421E → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis481K → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis541E → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis571L → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis591K → A: Impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis611R → A: Slightly impairs binding to RANBP2. Ref.20 Ref.21 Ref.23
Mutagenesis851N → Q: Impairs catalytic activity. Ref.20 Ref.21 Ref.33
Mutagenesis871Y → A: Impairs catalytic activity. Ref.20 Ref.21 Ref.33
Mutagenesis931C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. Ref.20 Ref.21
Mutagenesis100 – 1012DK → AA: Impairs catalytic activity. Ref.20 Ref.21
Mutagenesis1271D → A: Impairs catalytic activity. Ref.20 Ref.21 Ref.33
Mutagenesis1271D → S: No effect on catalytic activity. Ref.20 Ref.21 Ref.33
Sequence conflict181K → P in AAC50603. Ref.6
Sequence conflict86 – 894VYPS → GVPF in AAC50603. Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P63279-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E2C826E9C8D0683D

FASTA15818,007
        10         20         30         40         50         60 
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL 

        70         80         90        100        110        120 
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL 

       130        140        150 
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9."
Yasugi T., Howley P.M.
Nucleic Acids Res. 24:2005-2010(1996) [PubMed: 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. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed: 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

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.
IPIIPI00032957.
PIRJC6056.
RefSeqNP_003336.1.
NP_919235.1.
NP_919236.1.
NP_919237.1.
UniGeneHs.302903

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A3SX-ray2.80A1-158[»]
1KPSX-ray2.50A/C1-158[»]
1Z5Qmodel-A1-158[»]
1Z5SX-ray3.01A1-158[»]
2GRNX-ray1.80A1-158[»]
2GROX-ray1.70A1-158[»]
2GRPX-ray2.05A1-158[»]
2GRQX-ray1.70A1-158[»]
2GRRX-ray1.30A1-158[»]
2O25X-ray2.60C/D1-158[»]
2PE6X-ray2.40A1-158[»]
2PX9NMR-B1-158[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29078N.
IntActP63279. 49 interactions.

PTM databases

PhosphoSiteP63279.

Proteomic databases

PeptideAtlasP63279.
PRIDEP63279.

Genome annotation databases

EnsemblENSG00000103275. Homo sapiens. [Contig view]
GeneID7329.
KEGGhsa:7329.

Organism-specific databases

GeneCardsGC16P001299.
H-InvDBHIX0012677.
HIX0038735.
HGNCHGNC:12485. UBE2I.
HPACAB009021.
HPA003909.
MIM601661. gene.
PharmGKBPA37134.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP63279.
OMAP63279. KQWRKDH.

Enzyme and pathway databases

Pathway_Interaction_DBar_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

ArrayExpressP63279.
BgeeP63279.
CleanExHS_UBE2I.
GermOnlineENSG00000103275. Homo sapiens.

Family and domain databases

InterProIPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]
Gene3DG3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
ProDomPD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00212. UBCc. 1 hit.
[Graphical view]
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio28682.
SOURCESearch...

Entry information

Entry nameUBC9_HUMAN
AccessionPrimary (citable) accession number: P63279
Secondary accession number(s): P50550 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents