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Protein

Ubiquitin-conjugating enzyme E2 L3

Gene

Ube2l3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis (By similarity).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. transcription coactivator activity Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle phase transition Source: UniProtKB
  2. cell proliferation Source: UniProtKB
  3. cellular response to glucocorticoid stimulus Source: UniProtKB
  4. cellular response to steroid hormone stimulus Source: UniProtKB
  5. protein K11-linked ubiquitination Source: UniProtKB
  6. protein polyubiquitination Source: UniProtKB
  7. protein ubiquitination Source: UniProtKB
  8. regulation of transcription, DNA-templated Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 L3 (EC:6.3.2.19)
Alternative name(s):
UbcM4
Ubiquitin carrier protein L3
Ubiquitin-protein ligase L3
Gene namesi
Name:Ube2l3
Synonyms:Ubce7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:109240. Ube2l3.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154Ubiquitin-conjugating enzyme E2 L3PRO_0000082477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei138 – 1381N6-acetyllysineBy similarity

Post-translational modificationi

Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiP68037.
PaxDbiP68037.
PRIDEiP68037.

PTM databases

PhosphoSiteiP68037.

Expressioni

Gene expression databases

BgeeiP68037.
CleanExiMM_UBE2L3.
ExpressionAtlasiP68037. baseline and differential.
GenevestigatoriP68037.

Interactioni

Subunit structurei

Interacts with PARK2; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity (By similarity).By similarity

Protein-protein interaction databases

BioGridi204407. 11 interactions.
IntActiP68037. 4 interactions.
MINTiMINT-2736773.

Structurei

3D structure databases

ProteinModelPortaliP68037.
SMRiP68037. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

In contrast to other ubiquitin-conjugating enzymes E2, residues essential for lysine reactivity are absent: Pro and a His residues are present instead of an Asp and an Asp residues in positions 88 and 119,respectively.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP68037.
KOiK04552.
OMAiIALVNDX.
OrthoDBiEOG7GXPD8.
PhylomeDBiP68037.
TreeFamiTF313043.

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.

P68037-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA
60 70 80 90 100
FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK
110 120 130 140 150
TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK

RPVD
Length:154
Mass (Da):17,862
Last modified:October 11, 2004 - v1
Checksum:iF5A30243BE3C9985
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021D → V in AAB36018. (PubMed:8901595)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81004 Genomic DNA. Translation: AAB36018.1.
X97042 mRNA. Translation: CAA65755.1.
AJ130961 mRNA. Translation: CAA10265.1.
AK007265 mRNA. Translation: BAB24925.1.
CCDSiCCDS27997.1.
PIRiJC6163.
RefSeqiNP_033482.1. NM_009456.2.
XP_006543833.1. XM_006543770.1.
UniGeneiMm.3074.

Genome annotation databases

EnsembliENSMUST00000090192; ENSMUSP00000087658; ENSMUSG00000038965.
ENSMUST00000115699; ENSMUSP00000111363; ENSMUSG00000038965.
GeneIDi100042355.
22195.
KEGGimmu:100042355.
mmu:22195.
UCSCiuc007ykl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81004 Genomic DNA. Translation: AAB36018.1.
X97042 mRNA. Translation: CAA65755.1.
AJ130961 mRNA. Translation: CAA10265.1.
AK007265 mRNA. Translation: BAB24925.1.
CCDSiCCDS27997.1.
PIRiJC6163.
RefSeqiNP_033482.1. NM_009456.2.
XP_006543833.1. XM_006543770.1.
UniGeneiMm.3074.

3D structure databases

ProteinModelPortaliP68037.
SMRiP68037. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204407. 11 interactions.
IntActiP68037. 4 interactions.
MINTiMINT-2736773.

PTM databases

PhosphoSiteiP68037.

Proteomic databases

MaxQBiP68037.
PaxDbiP68037.
PRIDEiP68037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090192; ENSMUSP00000087658; ENSMUSG00000038965.
ENSMUST00000115699; ENSMUSP00000111363; ENSMUSG00000038965.
GeneIDi100042355.
22195.
KEGGimmu:100042355.
mmu:22195.
UCSCiuc007ykl.1. mouse.

Organism-specific databases

CTDi7332.
MGIiMGI:109240. Ube2l3.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP68037.
KOiK04552.
OMAiIALVNDX.
OrthoDBiEOG7GXPD8.
PhylomeDBiP68037.
TreeFamiTF313043.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi28696.
PROiP68037.
SOURCEiSearch...

Gene expression databases

BgeeiP68037.
CleanExiMM_UBE2L3.
ExpressionAtlasiP68037. baseline and differential.
GenevestigatoriP68037.

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. "Provirus integration into a gene encoding a ubiquitin-conjugating enzyme results in a placental defect and embryonic lethality."
    Harbers K., Mueller U., Grams A., Li E., Jaenisch R., Franz T.
    Proc. Natl. Acad. Sci. U.S.A. 93:12412-12417(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3."
    Robinson P.A., Leek J.P., Thompson J., Carr I.M., Bailey A., Moynihan T.P., Coletta P.L., Lench N.J., Markham A.F.
    Mamm. Genome 6:725-731(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.

Entry informationi

Entry nameiUB2L3_MOUSE
AccessioniPrimary (citable) accession number: P68037
Secondary accession number(s): P51966, P70653, Q9HAV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 7, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.