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Protein

Ubiquitin/ISG15-conjugating enzyme E2 L6

Gene

Ube2l6

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

Functioni

Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3 (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. ATP binding Source: UniProtKB-KW
  2. ISG15 transferase activity Source: MGI
  3. ligase activity Source: UniProtKB-KW
  4. ubiquitin-like protein transferase activity Source: MGI

GO - Biological processi

  1. ISG15-protein conjugation Source: MGI
  2. modification-dependent protein catabolic process Source: MGI
  3. protein ubiquitination Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_289225. ISG15 antiviral mechanism.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC:6.3.2.19)
Alternative name(s):
UbcM8
Ubiquitin carrier protein L6
Ubiquitin-protein ligase L6
Gene namesi
Name:Ube2l6
Synonyms:Ubce8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914500. Ube2l6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 153153Ubiquitin/ISG15-conjugating enzyme E2 L6PRO_0000082479Add
BLAST

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9QZU9.
PaxDbiQ9QZU9.
PRIDEiQ9QZU9.

PTM databases

PhosphoSiteiQ9QZU9.

Expressioni

Gene expression databases

BgeeiQ9QZU9.
CleanExiMM_UBE2L6.
ExpressionAtlasiQ9QZU9. baseline and differential.
GenevestigatoriQ9QZU9.

Interactioni

Subunit structurei

Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3 (tyrosine phosphorylated) (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000107264.

Structurei

3D structure databases

ProteinModelPortaliQ9QZU9.
SMRiQ9QZU9. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ9QZU9.
KOiK04553.
OMAiEKPPYNL.
OrthoDBiEOG7GXPD8.
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.

Q9QZU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMASKRVAKE LESLSKELPP YLRQLSSDDA NVLVWHMLLL PDQLPYGLKA
60 70 80 90 100
FQVRIDFPRE YPFKPPTLRF TTKIYHPNVR EDGLVCLPLI SNENWKPYTK
110 120 130 140 150
PYQVLEALNV LVSKPNLEEP VRLELADLLT QNPEMFRKKA EEFTLKFGVD

RPS
Length:153
Mass (Da):17,841
Last modified:May 25, 2009 - v3
Checksum:i71EEFF050CDE57F1
GO

Sequence cautioni

The sequence AAD55978.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291D → Y in AAD55978 (Ref. 1) Curated
Sequence conflicti63 – 631F → L in AAH08238 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159230 mRNA. Translation: AAD55978.1. Different initiation.
AK010942 mRNA. Translation: BAB27282.1.
AK013452 mRNA. Translation: BAB28861.1.
AK152010 mRNA. Translation: BAE30873.1.
AK152113 mRNA. Translation: BAE30957.1.
AK168695 mRNA. Translation: BAE40539.1.
AK171629 mRNA. Translation: BAE42574.1.
CH466519 Genomic DNA. Translation: EDL27303.1.
BC008238 mRNA. Translation: AAH08238.1.
CCDSiCCDS16194.2.
RefSeqiNP_064333.2. NM_019949.2.
UniGeneiMm.38261.

Genome annotation databases

EnsembliENSMUST00000102642; ENSMUSP00000099702; ENSMUSG00000027078.
GeneIDi56791.
KEGGimmu:56791.
UCSCiuc012byn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159230 mRNA. Translation: AAD55978.1. Different initiation.
AK010942 mRNA. Translation: BAB27282.1.
AK013452 mRNA. Translation: BAB28861.1.
AK152010 mRNA. Translation: BAE30873.1.
AK152113 mRNA. Translation: BAE30957.1.
AK168695 mRNA. Translation: BAE40539.1.
AK171629 mRNA. Translation: BAE42574.1.
CH466519 Genomic DNA. Translation: EDL27303.1.
BC008238 mRNA. Translation: AAH08238.1.
CCDSiCCDS16194.2.
RefSeqiNP_064333.2. NM_019949.2.
UniGeneiMm.38261.

3D structure databases

ProteinModelPortaliQ9QZU9.
SMRiQ9QZU9. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000107264.

PTM databases

PhosphoSiteiQ9QZU9.

Proteomic databases

MaxQBiQ9QZU9.
PaxDbiQ9QZU9.
PRIDEiQ9QZU9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102642; ENSMUSP00000099702; ENSMUSG00000027078.
GeneIDi56791.
KEGGimmu:56791.
UCSCiuc012byn.1. mouse.

Organism-specific databases

CTDi9246.
MGIiMGI:1914500. Ube2l6.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ9QZU9.
KOiK04553.
OMAiEKPPYNL.
OrthoDBiEOG7GXPD8.
TreeFamiTF313043.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_289225. ISG15 antiviral mechanism.

Miscellaneous databases

ChiTaRSiUbe2l6. mouse.
NextBioi313332.
PROiQ9QZU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZU9.
CleanExiMM_UBE2L6.
ExpressionAtlasiQ9QZU9. baseline and differential.
GenevestigatoriQ9QZU9.

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. "Progression from mammary hyperplasia to adenocarcinoma in MMTV-FGF8b transgenic mice is associated with altered expression of CD63, IGFBP7/mac25, alpha-synuclein, and UbcM8."
    Cook G., Lawshe A., MacArthur C.A.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Embryo and Embryonic liver.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiUB2L6_MOUSE
AccessioniPrimary (citable) accession number: Q9QZU9
Secondary accession number(s): Q3U8R0, Q922F1, Q9CQN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 25, 2004
Last sequence update: May 25, 2009
Last modified: March 31, 2015
This is version 119 of the entry and version 3 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.