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Protein

Ubiquitin-like modifier-activating enzyme 6

Gene

Uba6

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

Functioni

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34 (By similarity). Essential for embryonic development. Required for UBD/FAT10 conjugation.By similarity1 Publication

Catalytic activityi

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarity
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
Binding sitei470 – 4701ATP; via amide nitrogenBy similarity
Binding sitei497 – 4971ATPBy similarity
Binding sitei508 – 5081ATPBy similarity
Binding sitei521 – 5211ATPBy similarity
Active sitei625 – 6251Glycyl thioester intermediate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi569 – 5702ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • FAT10 activating enzyme activity Source: UniProtKB
  • ubiquitin activating enzyme activity Source: MGI

GO - Biological processi

  • amygdala development Source: MGI
  • dendritic spine development Source: MGI
  • hippocampus development Source: MGI
  • learning Source: MGI
  • locomotory behavior Source: MGI
  • protein ubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 6 (EC:6.2.1.45By similarity)
Short name:
Ubiquitin-activating enzyme 6
Alternative name(s):
Ubiquitin-activating enzyme E1-like protein 2
Short name:
E1-L2
Gene namesi
Name:Uba6
Synonyms:Ube1l2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1913894. Uba6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality at early stage.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10531053Ubiquitin-like modifier-activating enzyme 6PRO_0000277798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei54 – 541PhosphothreonineBy similarity
Modified residuei544 – 5441N6-acetyllysineBy similarity
Modified residuei729 – 7291N6-acetyllysineCombined sources
Modified residuei737 – 7371PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C7R4.
MaxQBiQ8C7R4.
PaxDbiQ8C7R4.
PeptideAtlasiQ8C7R4.
PRIDEiQ8C7R4.

PTM databases

iPTMnetiQ8C7R4.
PhosphoSiteiQ8C7R4.
SwissPalmiQ8C7R4.

Expressioni

Gene expression databases

BgeeiQ8C7R4.
CleanExiMM_UBA6.
ExpressionAtlasiQ8C7R4. baseline and differential.
GenevisibleiQ8C7R4. MM.

Interactioni

Subunit structurei

Forms a thioester with UBD in cells stimulated with tumor necrosis factor-alpha (TNFa) and interferon-gamma (IFNg).

Protein-protein interaction databases

BioGridi231114. 1 interaction.
IntActiQ8C7R4. 2 interactions.
MINTiMINT-4114710.
STRINGi10090.ENSMUSP00000035328.

Structurei

3D structure databases

ProteinModelPortaliQ8C7R4.
SMRiQ8C7R4. Positions 38-1019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ8C7R4.
KOiK10699.
OMAiWLSWTAQ.
OrthoDBiEOG74R1PV.
PhylomeDBiQ8C7R4.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8C7R4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERSEPLAVL SCEEASCSSW GACGASKNLP TMTTESLEID DGLYSRQRYV
60 70 80 90 100
LGDTAMQKMA KSCVFLSGMG GLGVEIAKNL VLAGIKALTI HDTKKCQAWD
110 120 130 140 150
LGTNFFLCED DVVNERNRAE AVLHRIAELN PYVQVSSSSA PLDETTDLSF
160 170 180 190 200
LEKYQCVVLT EIKLTLQKKI NNFCHSHCPP IKFISADVHG IWSRLFCDFG
210 220 230 240 250
DEFEVSDTTG EEPKEIFISN ITQANPGIVT CLESHPHKLE TGQFLTFREI
260 270 280 290 300
HGMTGLNGSV QQITVISPFS FSIGDTTKLD PYLHGGIAVQ VKTPKTFCFE
310 320 330 340 350
PLESQIKHPR CLIADFSKPE APLEIHLAML ALDQFQENYN RKPNIRCQQD
360 370 380 390 400
SDELLKLTVS INETLEEKPE VNADIVHWLS WTAQGFLPPL AAAVGGVASQ
410 420 430 440 450
EVLKAVTGKF SPLCQWLYLE AADTVESLGN PGHEEFLPRG DRYDAIRACI
460 470 480 490 500
GNTLCQKLQN LNIFLVGCGA IGCEMLKNFA LLGVGTGREK GMVTVTDPDL
510 520 530 540 550
IEKSNLNRQF LFRPHHIQKP KSYTAAEATL KINPQLKIDA HLNKVCPATE
560 570 580 590 600
SIYSDEFYTK QDIIITALDN VEARRYVDSR CLANLRPLLD SGTMGTKGHT
610 620 630 640 650
EIIVPQLTES YNSHRDPPEE EIPFCTLKSF PAAIEHTIQW ARDKFESSFS
660 670 680 690 700
HKPSLFNKFW QAYPSAEDVL QKIQNGQSLE GCFQVIKLLS RRPRIWSQCV
710 720 730 740 750
ELARLKFEKY FNHKALQLLH CFPLETRLKD GSLFWQSPKR PPSPIKFDLN
760 770 780 790 800
EPLHLSFLQS AAKLYATVYC IPFSEKDLSV NSLMDILSEV KIEEFKPSNK
810 820 830 840 850
VVQTDETARK PDHVPVSSED ERNAVFQLEE ALSSNKATKS DLQMTVLSFE
860 870 880 890 900
KDDDRNGHID FITAASNLRA KMYSIEPADR FKTKRIAGKI IPAIATSTAA
910 920 930 940 950
VSGLVALEMI KVAGGYPFDA YKNCFLNLAI PIIVFTETSE VRKTEIRNGI
960 970 980 990 1000
SFTIWDRWTV HGKEDFTLSD FINAVKENYG IEPTMVVQGV KMLYVPVMPG
1010 1020 1030 1040 1050
HAKRLKLTMH KLVKPSTEKK YVDLTVSFAP DADGDEDLPG PPVRYYFSHD

TNE
Length:1,053
Mass (Da):117,966
Last modified:March 1, 2003 - v1
Checksum:i90529575F77DE09B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049603 mRNA. Translation: BAC33836.1.
BC063048 mRNA. Translation: AAH63048.1.
CCDSiCCDS19378.1.
RefSeqiNP_766300.1. NM_172712.2.
UniGeneiMm.34012.
Mm.392216.
Mm.393083.
Mm.491297.

Genome annotation databases

EnsembliENSMUST00000039373; ENSMUSP00000035328; ENSMUSG00000035898.
GeneIDi231380.
KEGGimmu:231380.
UCSCiuc008xxj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049603 mRNA. Translation: BAC33836.1.
BC063048 mRNA. Translation: AAH63048.1.
CCDSiCCDS19378.1.
RefSeqiNP_766300.1. NM_172712.2.
UniGeneiMm.34012.
Mm.392216.
Mm.393083.
Mm.491297.

3D structure databases

ProteinModelPortaliQ8C7R4.
SMRiQ8C7R4. Positions 38-1019.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231114. 1 interaction.
IntActiQ8C7R4. 2 interactions.
MINTiMINT-4114710.
STRINGi10090.ENSMUSP00000035328.

PTM databases

iPTMnetiQ8C7R4.
PhosphoSiteiQ8C7R4.
SwissPalmiQ8C7R4.

Proteomic databases

EPDiQ8C7R4.
MaxQBiQ8C7R4.
PaxDbiQ8C7R4.
PeptideAtlasiQ8C7R4.
PRIDEiQ8C7R4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039373; ENSMUSP00000035328; ENSMUSG00000035898.
GeneIDi231380.
KEGGimmu:231380.
UCSCiuc008xxj.2. mouse.

Organism-specific databases

CTDi55236.
MGIiMGI:1913894. Uba6.

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ8C7R4.
KOiK10699.
OMAiWLSWTAQ.
OrthoDBiEOG74R1PV.
PhylomeDBiQ8C7R4.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ8C7R4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C7R4.
CleanExiMM_UBA6.
ExpressionAtlasiQ8C7R4. baseline and differential.
GenevisibleiQ8C7R4. MM.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Spinal cord.
  2. "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: C57BL/6J.
    Tissue: Brain.
  3. "E1-L2 activates both ubiquitin and FAT10."
    Chiu Y.-H., Sun Q., Chen Z.J.
    Mol. Cell 27:1014-1023(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH UBD, THIOESTER FORMATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiUBA6_MOUSE
AccessioniPrimary (citable) accession number: Q8C7R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 125 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

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.