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Protein

Ubiquitin-conjugating enzyme E2 E3

Gene

UBE2E3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest.2 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei145 – 1451Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. protein K11-linked ubiquitination Source: UniProtKB
  2. protein K48-linked ubiquitination Source: UniProtKB
  3. protein K63-linked ubiquitination Source: UniProtKB
  4. regulation of growth Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Growth regulation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ969T4.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 E3 (EC:6.3.2.19)
Alternative name(s):
UbcH9
Ubiquitin carrier protein E3
Ubiquitin-conjugating enzyme E2-23 kDa
Ubiquitin-protein ligase E3
Gene namesi
Name:UBE2E3
Synonyms:UBCE4, UBCH9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12479. UBE2E3.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451C → S: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA37129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 207206Ubiquitin-conjugating enzyme E2 E3PRO_0000082474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei8 – 81Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ969T4.
PaxDbiQ969T4.
PRIDEiQ969T4.

PTM databases

PhosphoSiteiQ969T4.

Expressioni

Tissue specificityi

Ubiquitously expressed at low levels. Highly expressed in skeletal muscle.1 Publication

Gene expression databases

BgeeiQ969T4.
CleanExiHS_UBE2E3.
ExpressionAtlasiQ969T4. baseline.
GenevestigatoriQ969T4.

Organism-specific databases

HPAiHPA003303.
HPA030445.

Interactioni

Subunit structurei

The ubiquitin-loaded form interacts specifically with importin-11 (IPO11), leading to its import into the nucleus (By similarity). Interacts with NEDD4L.By similarity

Protein-protein interaction databases

BioGridi115740. 87 interactions.
IntActiQ969T4. 56 interactions.
MINTiMINT-1035070.
STRINGi9606.ENSP00000307109.

Structurei

3D structure databases

ProteinModelPortaliQ969T4.
SMRiQ969T4. Positions 60-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ969T4.
KOiK06689.
OMAiETESIKM.
OrthoDBiEOG7PCJGX.
PhylomeDBiQ969T4.
TreeFamiTF101117.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q969T4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK
60 70 80 90 100
LSSKTTAKLS TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP
110 120 130 140 150
PGSVYEGGVF FLDITFSSDY PFKPPKVTFR TRIYHCNINS QGVICLDILK
160 170 180 190 200
DNWSPALTIS KVLLSICSLL TDCNPADPLV GSIATQYLTN RAEHDRIARQ

WTKRYAT
Length:207
Mass (Da):22,913
Last modified:December 1, 2001 - v1
Checksum:i821CB1382478DC9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651R → K in AAP97266 (Ref. 3) Curated
Sequence conflicti91 – 911Y → C in AAP97266 (Ref. 3) Curated
Sequence conflicti101 – 1011P → L in AAP97266 (Ref. 3) Curated
Sequence conflicti134 – 1341Y → D in AAP97266 (Ref. 3) Curated
Sequence conflicti159 – 1591I → V in AAP97266 (Ref. 3) Curated
Sequence conflicti171 – 1711T → M in AAP97266 (Ref. 3) Curated
Sequence conflicti176 – 1761A → V in AAP97266 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011W → R.1 Publication
Corresponds to variant rs2368192 [ dbSNP | Ensembl ].
VAR_023392

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017644 mRNA. Translation: BAA76544.1.
AF085362 mRNA. Translation: AAD40197.1.
AF136176 mRNA. Translation: AAP97266.1.
BT019345 mRNA. Translation: AAV38152.1.
AK314145 mRNA. Translation: BAG36833.1.
AC104076 Genomic DNA. Translation: AAY14882.1.
CH471058 Genomic DNA. Translation: EAX10989.1.
CH471058 Genomic DNA. Translation: EAX10990.1.
BC003554 mRNA. Translation: AAH03554.1.
BC092407 mRNA. Translation: AAH92407.1.
CCDSiCCDS2282.1.
RefSeqiNP_001265483.1. NM_001278554.1.
NP_001265484.1. NM_001278555.1.
NP_006348.1. NM_006357.3.
NP_872619.1. NM_182678.2.
XP_005246301.1. XM_005246244.2.
UniGeneiHs.470804.
Hs.567831.

Genome annotation databases

EnsembliENST00000392415; ENSP00000376215; ENSG00000170035.
ENST00000410062; ENSP00000386788; ENSG00000170035.
ENST00000602710; ENSP00000473623; ENSG00000170035.
ENST00000602959; ENSP00000473639; ENSG00000170035.
GeneIDi10477.
KEGGihsa:10477.
UCSCiuc002unq.1. human.

Polymorphism databases

DMDMi47606197.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017644 mRNA. Translation: BAA76544.1.
AF085362 mRNA. Translation: AAD40197.1.
AF136176 mRNA. Translation: AAP97266.1.
BT019345 mRNA. Translation: AAV38152.1.
AK314145 mRNA. Translation: BAG36833.1.
AC104076 Genomic DNA. Translation: AAY14882.1.
CH471058 Genomic DNA. Translation: EAX10989.1.
CH471058 Genomic DNA. Translation: EAX10990.1.
BC003554 mRNA. Translation: AAH03554.1.
BC092407 mRNA. Translation: AAH92407.1.
CCDSiCCDS2282.1.
RefSeqiNP_001265483.1. NM_001278554.1.
NP_001265484.1. NM_001278555.1.
NP_006348.1. NM_006357.3.
NP_872619.1. NM_182678.2.
XP_005246301.1. XM_005246244.2.
UniGeneiHs.470804.
Hs.567831.

3D structure databases

ProteinModelPortaliQ969T4.
SMRiQ969T4. Positions 60-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115740. 87 interactions.
IntActiQ969T4. 56 interactions.
MINTiMINT-1035070.
STRINGi9606.ENSP00000307109.

PTM databases

PhosphoSiteiQ969T4.

Polymorphism databases

DMDMi47606197.

Proteomic databases

MaxQBiQ969T4.
PaxDbiQ969T4.
PRIDEiQ969T4.

Protocols and materials databases

DNASUi10477.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392415; ENSP00000376215; ENSG00000170035.
ENST00000410062; ENSP00000386788; ENSG00000170035.
ENST00000602710; ENSP00000473623; ENSG00000170035.
ENST00000602959; ENSP00000473639; ENSG00000170035.
GeneIDi10477.
KEGGihsa:10477.
UCSCiuc002unq.1. human.

Organism-specific databases

CTDi10477.
GeneCardsiGC02P181809.
H-InvDBHIX0056142.
HGNCiHGNC:12479. UBE2E3.
HPAiHPA003303.
HPA030445.
MIMi604151. gene.
neXtProtiNX_Q969T4.
PharmGKBiPA37129.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ969T4.
KOiK06689.
OMAiETESIKM.
OrthoDBiEOG7PCJGX.
PhylomeDBiQ969T4.
TreeFamiTF101117.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ969T4.

Miscellaneous databases

ChiTaRSiUBE2E3. human.
GeneWikiiUBE2E3.
GenomeRNAii10477.
NextBioi39740.
PROiQ969T4.
SOURCEiSearch...

Gene expression databases

BgeeiQ969T4.
CleanExiHS_UBE2E3.
ExpressionAtlasiQ969T4. baseline.
GenevestigatoriQ969T4.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme."
    Ito K., Kato S., Matsuda Y., Kimura M., Okano Y.
    Cytogenet. Cell Genet. 84:99-104(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF CYS-145.
    Tissue: Gastric adenocarcinoma.
  2. "Human UbcM2 gene, complete cds."
    Shen Y., Ye M., Fu G., Zhou J., Zhang Q., Huang Q., Xu S., He K., Chen S., Mao M., Chen Z.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Umbilical cord blood.
  3. "Cloning of a new human cDNA homologous to Mus musculus ubiquitin-conjugating enzyme UbcM2."
    Xin Y.R., Yu L., Zhao S.Y.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-201.
  4. "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].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 and PNS.
  9. "Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import."
    Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G.
    J. Cell Biol. 167:649-659(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUB2E3_HUMAN
AccessioniPrimary (citable) accession number: Q969T4
Secondary accession number(s): B2RAD6
, D3DPG3, Q5U0R7, Q7Z4W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 1, 2001
Last modified: March 4, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.