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Protein

Ubiquitin-protein ligase E3C

Gene

Ube3c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains. Has preference for 'Lys-48' linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1051 – 10511Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-protein ligase E3C (EC:6.3.2.-)
Gene namesi
Name:Ube3c
Synonyms:Kiaa0010, Kiaa10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2140998. Ube3c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10831083Ubiquitin-protein ligase E3CPRO_0000194983Add
BLAST

Proteomic databases

EPDiQ80U95.
MaxQBiQ80U95.
PaxDbiQ80U95.
PRIDEiQ80U95.

PTM databases

iPTMnetiQ80U95.
PhosphoSiteiQ80U95.

Expressioni

Gene expression databases

BgeeiQ80U95.
CleanExiMM_UBE3C.
ExpressionAtlasiQ80U95. baseline and differential.
GenevisibleiQ80U95. MM.

Interactioni

Subunit structurei

Interacts with 26S proteasomes. Interacts (via the N-terminal) with CAND2; the interaction stimulates ubiquitination of CAND2 in vitro (By similarity).By similarity

Protein-protein interaction databases

BioGridi221524. 1 interaction.
IntActiQ80U95. 2 interactions.
MINTiMINT-4111985.
STRINGi10090.ENSMUSP00000045998.

Structurei

3D structure databases

ProteinModelPortaliQ80U95.
SMRiQ80U95. Positions 723-1077.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 7430IQPROSITE-ProRule annotationAdd
BLAST
Domaini744 – 1083340HECTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060Cis-determinant of acceptor ubiquitin-bindingBy similarityAdd
BLAST

Domaini

The C-terminal is necessary and sufficient for the poly-ubiquitin chain assembly.By similarity

Sequence similaritiesi

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 1 IQ domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0942. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00550000074668.
HOGENOMiHOG000030618.
HOVERGENiHBG073375.
InParanoidiQ80U95.
KOiK10589.
OMAiSARHVWR.
OrthoDBiEOG7R56RN.
PhylomeDBiQ80U95.
TreeFamiTF106144.

Family and domain databases

InterProiIPR000569. HECT_dom.
IPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00015. IQ. 1 hit.
[Graphical view]
SUPFAMiSSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50096. IQ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80U95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSFEGDFKT RPKVSLGGAS RKEEKASLLH RTQEERRKRE EERRRLKNAV
60 70 80 90 100
IIQSFIRGYR DRKQQYFIQR SAFDQCTDSA QPGGTFCLAD GPNLTLLVRQ
110 120 130 140 150
LLFFYKQSED SKRLIWLYQN LIKHSSLFVK QLDGSERLTC LFQIKRLMSL
160 170 180 190 200
CCRLLQNCSD DSLNVALPMR MLEVFTSENT YLPVLQDSSY VVSVIEQILH
210 220 230 240 250
YMVHSGYYRS LYLLINSKLP SSIEYSDLSR VPIAKILLEN VLKPLHFTYS
260 270 280 290 300
SCPEASRHQV FSAFTEEFLG APFTDQIFHF VIPAFADAQT VFPYEPFLNA
310 320 330 340 350
LLLLESQSSK RCSGVPWLFY FVLTVGENYL GALSEDGLLV YLRVLQTFLS
360 370 380 390 400
QLPASPTGTG CPDSTSDSED DNEETDQPNS PEDGRVSAPY ITEECLRKLD
410 420 430 440 450
TKQQTNTLLN LVWRDSASEE VFTRMASICH TLMVQHRMMV PKVRLLYSLA
460 470 480 490 500
FNARFLRHLW FLISSMTTQM ITGSMVPLLQ LISRGSPMSF EDSSRIIPLF
510 520 530 540 550
YLFSSLFSHS LISIHDNEFF GDPIEVVGQR QSSMMPFTLE ELILLSRCLR
560 570 580 590 600
DACLGIIKLA YPETKPEVRE EYVTAFQSIG VTTNSEMQQC IQMEQKRWVQ
610 620 630 640 650
LFKVITNLVK MLKSRDTRRN FCPPNHWLSE QEDIKADKVT QLYVPASRHV
660 670 680 690 700
WRFRRMGRIG PLQSTLEVGL ESLPLSVSEE RQLAILTELP FVVPFEERVK
710 720 730 740 750
IFQRLIYADK QEVQGDGPFL DGINVTIRRN YIYEDAYDKL SPENEPDLKK
760 770 780 790 800
RIRVHLLNAH GLDEAGIDGG GIFREFLNEL LKSGFNPNQG FFKTTNEGLL
810 820 830 840 850
YPNPAAQMLV GDSFARHYYF LGRMLGKALY ENMLVELPFA GFFLSKLLGT
860 870 880 890 900
SADVDIHHLA SLDPEVYRNL LFLKSYEEDV EELGLNFTVV NNDLGEAQVV
910 920 930 940 950
ELKFGGKDIP VTGANRIAYI HLVADYRLNK QIRPHCLAFR QGLANVVSLE
960 970 980 990 1000
WLRMFDQQEI QVLISGAQVP VSLEDLKSFT NYSGGYSADH PVIKIFWRVV
1010 1020 1030 1040 1050
EGFTDEEKRK LLKFVTSCSR PPLLGFKELY PAFCIHNGGS DLERLPTAST
1060 1070 1080
CMNLLKLPEF YDEALLRSKL LYAIECAAGF ELS
Length:1,083
Mass (Da):123,976
Last modified:June 7, 2005 - v2
Checksum:iB7098CB9792946BE
GO

Sequence cautioni

The sequence AAH21525.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti570 – 5701E → G in BAC26709 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122187 mRNA. Translation: BAC65469.1.
AK029973 mRNA. Translation: BAC26709.1.
AK046056 mRNA. Translation: BAC32585.1.
AK049125 mRNA. Translation: BAC33557.1.
BC021525 mRNA. Translation: AAH21525.1. Different initiation.
BC120731 mRNA. Translation: AAI20732.1.
BC137626 mRNA. Translation: AAI37627.1.
CCDSiCCDS39042.1.
RefSeqiNP_598668.1. NM_133907.3.
UniGeneiMm.137746.

Genome annotation databases

EnsembliENSMUST00000049453; ENSMUSP00000045998; ENSMUSG00000039000.
GeneIDi100763.
KEGGimmu:100763.
UCSCiuc008wum.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122187 mRNA. Translation: BAC65469.1.
AK029973 mRNA. Translation: BAC26709.1.
AK046056 mRNA. Translation: BAC32585.1.
AK049125 mRNA. Translation: BAC33557.1.
BC021525 mRNA. Translation: AAH21525.1. Different initiation.
BC120731 mRNA. Translation: AAI20732.1.
BC137626 mRNA. Translation: AAI37627.1.
CCDSiCCDS39042.1.
RefSeqiNP_598668.1. NM_133907.3.
UniGeneiMm.137746.

3D structure databases

ProteinModelPortaliQ80U95.
SMRiQ80U95. Positions 723-1077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221524. 1 interaction.
IntActiQ80U95. 2 interactions.
MINTiMINT-4111985.
STRINGi10090.ENSMUSP00000045998.

PTM databases

iPTMnetiQ80U95.
PhosphoSiteiQ80U95.

Proteomic databases

EPDiQ80U95.
MaxQBiQ80U95.
PaxDbiQ80U95.
PRIDEiQ80U95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049453; ENSMUSP00000045998; ENSMUSG00000039000.
GeneIDi100763.
KEGGimmu:100763.
UCSCiuc008wum.1. mouse.

Organism-specific databases

CTDi9690.
MGIiMGI:2140998. Ube3c.
RougeiSearch...
Search...

Phylogenomic databases

eggNOGiKOG0942. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00550000074668.
HOGENOMiHOG000030618.
HOVERGENiHBG073375.
InParanoidiQ80U95.
KOiK10589.
OMAiSARHVWR.
OrthoDBiEOG7R56RN.
PhylomeDBiQ80U95.
TreeFamiTF106144.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbe3c. mouse.
PROiQ80U95.
SOURCEiSearch...

Gene expression databases

BgeeiQ80U95.
CleanExiMM_UBE3C.
ExpressionAtlasiQ80U95. baseline and differential.
GenevisibleiQ80U95. MM.

Family and domain databases

InterProiIPR000569. HECT_dom.
IPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
[Graphical view]
SMARTiSM00119. HECTc. 1 hit.
SM00015. IQ. 1 hit.
[Graphical view]
SUPFAMiSSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS50096. IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Testis.
  3. "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].
    Strain: FVB/N.
    Tissue: Brain and Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiUBE3C_MOUSE
AccessioniPrimary (citable) accession number: Q80U95
Secondary accession number(s): Q0VB95
, Q8BQZ6, Q8C7W6, Q8CDJ1, Q8VDL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 8, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.By similarity

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

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 one 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.