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Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

Uba1

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

Functioni

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. 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. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (By similarity).By similarity
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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei632 – 6321Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi478 – 50730ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: MGI
  3. ubiquitin activating enzyme activity Source: MGI
  4. ubiquitin-protein transferase activity Source: GO_Central

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. modification-dependent protein catabolic process Source: GO_Central
  3. protein ubiquitination Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 1
Alternative name(s):
Ubiquitin-activating enzyme E1
Ubiquitin-activating enzyme E1 X
Ubiquitin-like modifier-activating enzyme 1 X
Gene namesi
Name:Uba1
Synonyms:Sbx, Ube1, Ube1ax, Ube1x
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:98890. Uba1.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: GO_Central
  3. desmosome Source: Ensembl
  4. endosome membrane Source: Ensembl
  5. extracellular vesicular exosome Source: MGI
  6. heterochromatin Source: Ensembl
  7. lysosomal membrane Source: Ensembl
  8. mitochondrion Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. rough endoplasmic reticulum membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1PRO_0000194935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei55 – 551Phosphotyrosine1 Publication
Modified residuei528 – 5281N6-succinyllysine1 Publication
Modified residuei671 – 6711N6-acetyllysine1 Publication
Modified residuei800 – 8001PhosphothreonineBy similarity
Modified residuei810 – 8101PhosphoserineBy similarity
Modified residuei816 – 8161Phosphoserine1 Publication
Modified residuei820 – 8201Phosphoserine1 Publication
Modified residuei835 – 8351PhosphoserineBy similarity
Modified residuei980 – 9801N6-acetyllysineBy similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ02053.
PaxDbiQ02053.
PRIDEiQ02053.

PTM databases

PhosphoSiteiQ02053.

Expressioni

Tissue specificityi

Ubiquitously expressed. In testis, expressed in A spermatogonia and spermatids but at very low levels in pachytene spermatocytes.1 Publication

Developmental stagei

In testis, highly expressed from 14.5 days post coitum (dpc) until the day of birth, with levels falling after 10 days post partum (dpp) but peaking again at 28 dpp.1 Publication

Inductioni

May be modulated by the thyroid hormone receptor.

Gene expression databases

BgeeiQ02053.
CleanExiMM_UBA1.
ExpressionAtlasiQ02053. baseline and differential.
GenevestigatoriQ02053.

Interactioni

Subunit structurei

Monomer. Interacts with GAN (via BTB domain).

Protein-protein interaction databases

BioGridi204410. 7 interactions.
IntActiQ02053. 7 interactions.
MINTiMINT-1869675.

Structurei

Secondary structure

1
1058
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni203 – 2053Combined sources
Beta strandi218 – 2258Combined sources
Beta strandi227 – 2348Combined sources
Beta strandi246 – 25510Combined sources
Helixi257 – 2604Combined sources
Beta strandi265 – 27814Combined sources
Helixi280 – 2823Combined sources
Beta strandi288 – 2947Combined sources
Helixi631 – 6355Combined sources
Helixi641 – 65616Combined sources
Helixi658 – 6669Combined sources
Helixi671 – 6777Combined sources
Helixi683 – 69513Combined sources
Turni696 – 6983Combined sources
Helixi703 – 71816Combined sources
Helixi720 – 7289Combined sources
Beta strandi740 – 7423Combined sources
Helixi759 – 77517Combined sources
Helixi784 – 7929Combined sources
Beta strandi809 – 8113Combined sources
Helixi824 – 8329Combined sources
Helixi836 – 8383Combined sources
Helixi858 – 87215Combined sources
Helixi880 – 8867Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7LX-ray2.80A/B/C626-891[»]
2LZJNMR-A202-312[»]
2V31NMR-A202-312[»]
ProteinModelPortaliQ02053.
SMRiQ02053. Positions 50-1053.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati63 – 1991371-1Add
BLAST
Repeati459 – 6111531-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 6115492 approximate repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ02053.
KOiK03178.
OMAiSKFVERT.
OrthoDBiEOG74R1PV.
PhylomeDBiQ02053.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02053-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI
60 70 80 90 100
DESLYSRQLY VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT
110 120 130 140 150
LHDQGTTQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP
160 170 180 190 200
LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH SRGIKLVVAD TRGLFGQLFC
210 220 230 240 250
DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF
260 270 280 290 300
SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
310 320 330 340 350
ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR
360 370 380 390 400
NEEDATELVG LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF
410 420 430 440 450
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EEKCLPRQNR
460 470 480 490 500
YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV
510 520 530 540 550
VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN
560 570 580 590 600
RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT
610 620 630 640 650
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD
660 670 680 690 700
EFEGLFKQPA ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP
710 720 730 740 750
QTWGDCVTWA CHHWHTQYCN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH
760 770 780 790 800
PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG SQDRAAVASL LQSVQVPEFT
810 820 830 840 850
PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE
860 870 880 890 900
KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA
910 920 930 940 950
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ
960 970 980 990 1000
EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF
1010 1020 1030 1040 1050
FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV

PYVRYTIR
Length:1,058
Mass (Da):117,809
Last modified:April 1, 1993 - v1
Checksum:i95D8152ED5C8E037
GO

Sequence cautioni

The sequence CAA44465.1 differs from that shown. Reason: Frameshift at position 1033. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti963 – 9631L → V in CAA44465. (PubMed:1684224)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10576 mRNA. Translation: BAA01433.1.
AK088057 mRNA. Translation: BAC40121.1.
AK088528 mRNA. Translation: BAC40405.1.
AK143416 mRNA. Translation: BAE25369.1.
AK171667 mRNA. Translation: BAE42599.1.
AL807240 Genomic DNA. Translation: CAM23092.1.
BC058630 mRNA. Translation: AAH58630.1.
BC145984 mRNA. Translation: AAI45985.1.
X62580 mRNA. Translation: CAA44465.1. Frameshift.
U09051 Genomic DNA. Translation: AAC52169.1.
U09055 Genomic DNA. Translation: AAC52171.1.
CCDSiCCDS30044.1.
PIRiI48756.
I63168.
JC1254.
RefSeqiNP_001129557.1. NM_001136085.2.
NP_001263245.1. NM_001276316.1.
NP_001263246.1. NM_001276317.1.
NP_033483.2. NM_009457.4.
UniGeneiMm.1104.

Genome annotation databases

EnsembliENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
GeneIDi22201.
KEGGimmu:22201.
UCSCiuc009stl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10576 mRNA. Translation: BAA01433.1.
AK088057 mRNA. Translation: BAC40121.1.
AK088528 mRNA. Translation: BAC40405.1.
AK143416 mRNA. Translation: BAE25369.1.
AK171667 mRNA. Translation: BAE42599.1.
AL807240 Genomic DNA. Translation: CAM23092.1.
BC058630 mRNA. Translation: AAH58630.1.
BC145984 mRNA. Translation: AAI45985.1.
X62580 mRNA. Translation: CAA44465.1. Frameshift.
U09051 Genomic DNA. Translation: AAC52169.1.
U09055 Genomic DNA. Translation: AAC52171.1.
CCDSiCCDS30044.1.
PIRiI48756.
I63168.
JC1254.
RefSeqiNP_001129557.1. NM_001136085.2.
NP_001263245.1. NM_001276316.1.
NP_001263246.1. NM_001276317.1.
NP_033483.2. NM_009457.4.
UniGeneiMm.1104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7LX-ray2.80A/B/C626-891[»]
2LZJNMR-A202-312[»]
2V31NMR-A202-312[»]
ProteinModelPortaliQ02053.
SMRiQ02053. Positions 50-1053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204410. 7 interactions.
IntActiQ02053. 7 interactions.
MINTiMINT-1869675.

PTM databases

PhosphoSiteiQ02053.

Proteomic databases

MaxQBiQ02053.
PaxDbiQ02053.
PRIDEiQ02053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
GeneIDi22201.
KEGGimmu:22201.
UCSCiuc009stl.1. mouse.

Organism-specific databases

CTDi7317.
MGIiMGI:98890. Uba1.

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ02053.
KOiK03178.
OMAiSKFVERT.
OrthoDBiEOG74R1PV.
PhylomeDBiQ02053.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUba1. mouse.
EvolutionaryTraceiQ02053.
NextBioi302189.
PROiQ02053.
SOURCEiSearch...

Gene expression databases

BgeeiQ02053.
CleanExiMM_UBA1.
ExpressionAtlasiQ02053. baseline and differential.
GenevestigatoriQ02053.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence of a functionally active cDNA encoding the mouse ubiquitin-activating enzyme E1."
    Imai N., Kaneda S., Nagai Y., Seno T., Ayusawa D., Hanaoka F., Yamao F.
    Gene 118:279-282(1992) [PubMed] [Europe PMC] [Abstract]
    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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Ovary and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  5. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 69-81; 90-97; 175-182; 227-239; 351-368; 375-384; 386-411; 451-465; 471-485; 538-551; 559-581; 593-604; 636-671; 679-693; 785-802; 844-851; 870-880; 890-923; 945-980 AND 1011-1021, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  6. "Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1."
    Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.
    Nature 354:483-487(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 615-1058.
    Strain: 129/Sv.
  7. "Estimating the intensity of male-driven evolution in rodents by using X-linked and Y-linked Ube 1 genes and pseudogenes."
    Chang B.H.-J., Li W.H.
    J. Mol. Evol. 40:70-77(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 655-763.
    Strain: BALB/c AnCr.
    Tissue: Liver.
  8. "Isolation of genomic DNA fragments corresponding to genes modulated in vivo by a transcription factor."
    Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., Zaballos A.
    Nucleic Acids Res. 22:4132-4138(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION OF EXPRESSION BY THE THYROID HORMONE RECEPTOR.
  9. "Transcriptional analysis of the candidate spermatogenesis gene Ube1y and of the closely related Ube1x shows that they are coexpressed in spermatogonia and spermatids but are repressed in pachytene spermatocytes."
    Odorisio T., Mahadevaiah S.K., McCarrey J.R., Burgoyne P.S.
    Dev. Biol. 180:336-343(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. Cited for: ISGYLATION.
  11. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816 AND SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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-671, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  14. "Crystal structure of a fragment of mouse ubiquitin-activating enzyme."
    Szczepanowski R.H., Filipek R., Bochtler M.
    J. Biol. Chem. 280:22006-22011(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 626-891.

Entry informationi

Entry nameiUBA1_MOUSE
AccessioniPrimary (citable) accession number: Q02053
Secondary accession number(s): A6H6S6, P31253, Q542H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 4, 2015
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.