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Protein

Ubiquitin-conjugating enzyme E2 C

Gene

Ube2c

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

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit (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 sitei114 – 1141Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. small conjugating protein transferase activity Source: GO_Central
  4. ubiquitin conjugating enzyme activity Source: MGI
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: GO_Central
  7. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. cell division Source: UniProtKB-KW
  3. exit from mitosis Source: UniProtKB
  4. free ubiquitin chain polymerization Source: UniProtKB
  5. negative regulation of cyclin-dependent protein serine/threonine kinase by cyclin degradation Source: MGI
  6. positive regulation of exit from mitosis Source: MGI
  7. protein K11-linked ubiquitination Source: UniProtKB
  8. protein K48-linked ubiquitination Source: UniProtKB
  9. protein polyubiquitination Source: GO_Central
  10. protein ubiquitination Source: MGI
  11. regulation of mitotic metaphase/anaphase transition Source: GO_Central
  12. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_205250. Phosphorylation of the APC/C.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_246476. Regulation of APC/C activators between G1/S and early anaphase.
REACT_248037. Inactivation of APC/C via direct inhibition of the APC/C complex.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 C (EC:6.3.2.19)
Alternative name(s):
UbcH10
Ubiquitin carrier protein C
Ubiquitin-protein ligase C
Gene namesi
Name:Ube2c
Synonyms:Ubch10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1915862. Ube2c.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: UniProtKB
  2. cytoplasm Source: GO_Central
  3. nucleus Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 179178Ubiquitin-conjugating enzyme E2 CPRO_0000082561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei3 – 31PhosphoserineBy similarity

Post-translational modificationi

Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Its degradation plays a central role in APC/C regulation, allowing cyclin-A accumulation before S phase entry. APC/C substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active until its substrates have been destroyed (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9D1C1.
PaxDbiQ9D1C1.
PRIDEiQ9D1C1.

PTM databases

PhosphoSiteiQ9D1C1.

Expressioni

Gene expression databases

BgeeiQ9D1C1.
CleanExiMM_UBE2C.
ExpressionAtlasiQ9D1C1. baseline and differential.
GenevestigatoriQ9D1C1.

Interactioni

Subunit structurei

Component of the APC/C complex.By similarity

Protein-protein interaction databases

BioGridi212952. 4 interactions.
STRINGi10090.ENSMUSP00000085581.

Structurei

3D structure databases

ProteinModelPortaliQ9D1C1.
SMRiQ9D1C1. Positions 30-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119350.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiQ9D1C1.
KOiK06688.
OMAiAELWDKD.
OrthoDBiEOG7M0NTH.
PhylomeDBiQ9D1C1.
TreeFamiTF101116.

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.

Q9D1C1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQNRDPAA ASVAAVRKGA EPCGGAARGP VGKRLQQELM ILMTSGDKGI
60 70 80 90 100
SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT
110 120 130 140 150
PCYHPNVDTQ GNICLDILKD KWSALYDVRT ILLSIQSLLG EPNIDSPLNT
160 170
HAAELWKNPT AFKKYLQETY SKQVSSQDP
Length:179
Mass (Da):19,606
Last modified:June 1, 2001 - v1
Checksum:i1FE2F36EB69B117C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003722 mRNA. Translation: BAB22959.1.
AK160740 mRNA. Translation: BAE35981.1.
CCDSiCCDS17055.1.
RefSeqiNP_081061.1. NM_026785.2.
UniGeneiMm.89830.

Genome annotation databases

EnsembliENSMUST00000088248; ENSMUSP00000085581; ENSMUSG00000001403.
GeneIDi68612.
KEGGimmu:68612.
UCSCiuc008nvy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003722 mRNA. Translation: BAB22959.1.
AK160740 mRNA. Translation: BAE35981.1.
CCDSiCCDS17055.1.
RefSeqiNP_081061.1. NM_026785.2.
UniGeneiMm.89830.

3D structure databases

ProteinModelPortaliQ9D1C1.
SMRiQ9D1C1. Positions 30-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212952. 4 interactions.
STRINGi10090.ENSMUSP00000085581.

PTM databases

PhosphoSiteiQ9D1C1.

Proteomic databases

MaxQBiQ9D1C1.
PaxDbiQ9D1C1.
PRIDEiQ9D1C1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088248; ENSMUSP00000085581; ENSMUSG00000001403.
GeneIDi68612.
KEGGimmu:68612.
UCSCiuc008nvy.1. mouse.

Organism-specific databases

CTDi11065.
MGIiMGI:1915862. Ube2c.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119350.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiQ9D1C1.
KOiK06688.
OMAiAELWDKD.
OrthoDBiEOG7M0NTH.
PhylomeDBiQ9D1C1.
TreeFamiTF101116.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_205250. Phosphorylation of the APC/C.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_246476. Regulation of APC/C activators between G1/S and early anaphase.
REACT_248037. Inactivation of APC/C via direct inhibition of the APC/C complex.

Miscellaneous databases

NextBioi327556.
PROiQ9D1C1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1C1.
CleanExiMM_UBE2C.
ExpressionAtlasiQ9D1C1. baseline and differential.
GenevestigatoriQ9D1C1.

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

  1. "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: Embryo and Head.

Entry informationi

Entry nameiUBE2C_MOUSE
AccessioniPrimary (citable) accession number: Q9D1C1
Secondary accession number(s): Q3TUJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 107 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.