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Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

UBA1

Organism
Homo sapiens (Human)
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.1 Publication

Pathway:iprotein 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 sitei632 – 6321Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • ubiquitin activating enzyme activity Source: MGI
  • ubiquitin-protein transferase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B5. 2681.
6.2.1.B9. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 1
Alternative name(s):
Protein A1S9
Ubiquitin-activating enzyme E1
Gene namesi
Name:UBA1
Synonyms:A1S9T, UBE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12469. UBA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinal muscular atrophy X-linked 2 (SMAX2)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA lethal infantile form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Clinical features include hypotonia, areflexia, and multiple congenital contractures.

See also OMIM:301830
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti539 – 5391M → I in SMAX2. 1 Publication
VAR_043501
Natural varianti547 – 5471S → G in SMAX2. 1 Publication
VAR_043502
Natural varianti557 – 5571E → V in SMAX2. 1 Publication
VAR_071121

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41S → A: Reduces phosphorylation. 1 Publication
Mutagenesisi8 – 114KKRR → AAAA: Loss of nuclear localization and a 90-95% decrease in the phosphorylation. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi301830. phenotype.
Orphaneti1145. X-linked distal arthrogryposis multiplex congenita.
PharmGKBiPA37119.

Polymorphism and mutation databases

BioMutaiUBA1.
DMDMi24418865.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1PRO_0000194934Add
BLAST
Isoform 2 (identifier: P22314-2)
Initiator methioninei1 – 11Removed1 Publication

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei46 – 461Phosphoserine4 Publications
Modified residuei55 – 551PhosphotyrosineBy similarity
Modified residuei528 – 5281N6-succinyllysineBy similarity
Modified residuei671 – 6711N6-acetyllysine1 Publication
Modified residuei800 – 8001Phosphothreonine1 Publication
Modified residuei810 – 8101Phosphoserine2 Publications
Modified residuei816 – 8161PhosphoserineBy similarity
Modified residuei820 – 8201Phosphoserine1 Publication
Modified residuei835 – 8351Phosphoserine1 Publication
Modified residuei980 – 9801N6-acetyllysine1 Publication
Isoform 2 (identifier: P22314-2)
Modified residuei2 – 21N-acetylalanine1 Publication

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP22314.
PaxDbiP22314.
PeptideAtlasiP22314.
PRIDEiP22314.

2D gel databases

REPRODUCTION-2DPAGEIPI00645078.

PTM databases

PhosphoSiteiP22314.

Expressioni

Gene expression databases

BgeeiP22314.
CleanExiHS_UBA1.
ExpressionAtlasiP22314. baseline and differential.
GenevisibleiP22314. HS.

Organism-specific databases

HPAiCAB019435.
CAB073410.
HPA000289.
HPA001506.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with GAN (via BTB domain).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q763532EBI-709688,EBI-6248077From a different organism.
GANQ9H2C05EBI-709688,EBI-764342
UBE2IP632792EBI-709688,EBI-80168

Protein-protein interaction databases

BioGridi113165. 95 interactions.
DIPiDIP-33686N.
IntActiP22314. 110 interactions.
MINTiMINT-1130980.
STRINGi9606.ENSP00000338413.

Structurei

Secondary structure

1
1058
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi55 – 628Combined sources
Beta strandi74 – 785Combined sources
Helixi82 – 9312Combined sources
Beta strandi97 – 1026Combined sources
Helixi109 – 1124Combined sources
Helixi120 – 1223Combined sources
Helixi127 – 13610Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi144 – 1474Combined sources
Helixi153 – 1564Combined sources
Beta strandi160 – 1645Combined sources
Helixi169 – 18113Combined sources
Beta strandi185 – 1928Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi219 – 2246Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi244 – 2529Combined sources
Helixi257 – 2593Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi291 – 30111Combined sources
Helixi306 – 3116Combined sources
Helixi326 – 34318Combined sources
Helixi352 – 36817Combined sources
Turni371 – 3733Combined sources
Helixi380 – 3889Combined sources
Helixi395 – 41319Combined sources
Beta strandi422 – 4287Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P22X-ray2.75A/B1-439[»]
ProteinModelPortaliP22314.
SMRiP22314. Positions 201-312, 629-889.
ModBaseiSearch...
MobiDBiSearch...

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 117Nuclear localization signal

Domaini

The first 11 amino acids are essential for phosphorylation and exclusive nuclear localization.

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiP22314.
KOiK03178.
OMAiPPGFRMK.
OrthoDBiEOG74R1PV.
PhylomeDBiP22314.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P22314-1) [UniParc]FASTAAdd to basket

Also known as: E1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSSPLSKKR RVSGPDPKPG SNCSPAQSVL SEVPSVPTNG MAKNGSEADI
60 70 80 90 100
DEGLYSRQLY VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT
110 120 130 140 150
LHDQGTAQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP
160 170 180 190 200
LVEDFLSGFQ VVVLTNTPLE DQLRVGEFCH NRGIKLVVAD TRGLFGQLFC
210 220 230 240 250
DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFESGDFVSF
260 270 280 290 300
SEVQGMVELN GNQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
310 320 330 340 350
ISFKSLVASL AEPDFVVTDF AKFSRPAQLH IGFQALHQFC AQHGRPPRPR
360 370 380 390 400
NEEDAAELVA LAQAVNARAL PAVQQNNLDE DLIRKLAYVA AGDLAPINAF
410 420 430 440 450
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEVLT EDKCLQRQNR
460 470 480 490 500
YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEI
510 520 530 540 550
IVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PHIRVTSHQN
560 570 580 590 600
RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT
610 620 630 640 650
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD
660 670 680 690 700
EFEGLFKQPA ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQRP
710 720 730 740 750
QTWADCVTWA CHHWHTQYSN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH
760 770 780 790 800
PLTFDVNNPL HLDYVMAAAN LFAQTYGLTG SQDRAAVATF LQSVQVPEFT
810 820 830 840 850
PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE
860 870 880 890 900
KDDDSNFHMD FIVAASNLRA ENYDIPSADR HKSKLIAGKI IPAIATTTAA
910 920 930 940 950
VVGLVCLELY KVVQGHRQLD 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):117,849
Last modified:October 25, 2002 - v3
Checksum:i4B413AAA75FAA562
GO
Isoform 2 (identifier: P22314-2) [UniParc]FASTAAdd to basket

Also known as: E1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: Missing.

Show »
Length:1,018
Mass (Da):113,800
Checksum:i9A508347FE29FB19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901D → G in CAA40296 (PubMed:1606621).Curated
Sequence conflicti434 – 4341E → Q in CAA40296 (PubMed:1606621).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti447 – 4471R → H.
Corresponds to variant rs2070169 [ dbSNP | Ensembl ].
VAR_043500
Natural varianti539 – 5391M → I in SMAX2. 1 Publication
VAR_043501
Natural varianti547 – 5471S → G in SMAX2. 1 Publication
VAR_043502
Natural varianti557 – 5571E → V in SMAX2. 1 Publication
VAR_071121

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040Missing in isoform 2. CuratedVSP_055913Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56976 mRNA. Translation: CAA40296.1.
M58028 mRNA. Translation: AAA61246.1.
AL513366 Genomic DNA. Translation: CAI41708.1.
CH471164 Genomic DNA. Translation: EAW59290.1.
BC013041 mRNA. Translation: AAH13041.1.
X52897 mRNA. Translation: CAA37078.1.
CCDSiCCDS14275.1. [P22314-1]
PIRiA38564.
RefSeqiNP_003325.2. NM_003334.3. [P22314-1]
NP_695012.1. NM_153280.2. [P22314-1]
XP_005272707.1. XM_005272650.1. [P22314-1]
XP_011542258.1. XM_011543956.1. [P22314-1]
UniGeneiHs.533273.

Genome annotation databases

EnsembliENST00000335972; ENSP00000338413; ENSG00000130985.
ENST00000377351; ENSP00000366568; ENSG00000130985.
GeneIDi7317.
KEGGihsa:7317.
UCSCiuc004dhj.4. human. [P22314-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56976 mRNA. Translation: CAA40296.1.
M58028 mRNA. Translation: AAA61246.1.
AL513366 Genomic DNA. Translation: CAI41708.1.
CH471164 Genomic DNA. Translation: EAW59290.1.
BC013041 mRNA. Translation: AAH13041.1.
X52897 mRNA. Translation: CAA37078.1.
CCDSiCCDS14275.1. [P22314-1]
PIRiA38564.
RefSeqiNP_003325.2. NM_003334.3. [P22314-1]
NP_695012.1. NM_153280.2. [P22314-1]
XP_005272707.1. XM_005272650.1. [P22314-1]
XP_011542258.1. XM_011543956.1. [P22314-1]
UniGeneiHs.533273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P22X-ray2.75A/B1-439[»]
ProteinModelPortaliP22314.
SMRiP22314. Positions 201-312, 629-889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113165. 95 interactions.
DIPiDIP-33686N.
IntActiP22314. 110 interactions.
MINTiMINT-1130980.
STRINGi9606.ENSP00000338413.

Chemistry

BindingDBiP22314.
ChEMBLiCHEMBL5924.

PTM databases

PhosphoSiteiP22314.

Polymorphism and mutation databases

BioMutaiUBA1.
DMDMi24418865.

2D gel databases

REPRODUCTION-2DPAGEIPI00645078.

Proteomic databases

MaxQBiP22314.
PaxDbiP22314.
PeptideAtlasiP22314.
PRIDEiP22314.

Protocols and materials databases

DNASUi7317.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335972; ENSP00000338413; ENSG00000130985.
ENST00000377351; ENSP00000366568; ENSG00000130985.
GeneIDi7317.
KEGGihsa:7317.
UCSCiuc004dhj.4. human. [P22314-1]

Organism-specific databases

CTDi7317.
GeneCardsiGC0XP047050.
GeneReviewsiUBA1.
HGNCiHGNC:12469. UBA1.
HPAiCAB019435.
CAB073410.
HPA000289.
HPA001506.
MIMi301830. phenotype.
314370. gene.
neXtProtiNX_P22314.
Orphaneti1145. X-linked distal arthrogryposis multiplex congenita.
PharmGKBiPA37119.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiP22314.
KOiK03178.
OMAiPPGFRMK.
OrthoDBiEOG74R1PV.
PhylomeDBiP22314.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B5. 2681.
6.2.1.B9. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUBA1. human.
GeneWikiiUBA1.
GenomeRNAii7317.
NextBioi28604.
PROiP22314.
SOURCEiSearch...

Gene expression databases

BgeeiP22314.
CleanExiHS_UBA1.
ExpressionAtlasiP22314. baseline and differential.
GenevisibleiP22314. HS.

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. "Complementation by a cloned human ubiquitin-activating enzyme E1 of the S-phase-arrested mouse FM3A cell mutant with thermolabile E1."
    Ayusawa D., Kaneda S., Itoh Y., Yasuda H., Murakami Y., Sugasawa K., Hanaoka F., Seno T.
    Cell Struct. Funct. 17:113-122(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1."
    Handley P.M., Mueckler M., Siegel N.R., Ciechanover A., Schwartz A.L.
    Proc. Natl. Acad. Sci. U.S.A. 88:258-262(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 136-158; 369-383; 417-430 AND 559-580.
    Tissue: Placenta.
  3. Erratum
    Handley P.M., Mueckler M., Siegel N.R., Ciechanover A., Schwartz A.L.
    Proc. Natl. Acad. Sci. U.S.A. 88:7456-7456(1991) [PubMed] [Europe PMC] [Abstract]
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Lymph.
  7. "Molecular cloning, primary structure and expression of the human X linked A1S9 gene cDNA which complements the ts A1S9 mouse L cell defect in DNA replication."
    Zacksenhaus E., Sheinin R.
    EMBO J. 9:2923-2929(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-989.
  8. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 559-581 AND 924-944, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  9. "Isoforms of mammalian ubiquitin-activating enzyme."
    Cook J.C., Chock P.B.
    J. Biol. Chem. 267:24315-24321(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  10. "Immunoelectron microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells."
    Schwartz A.L., Trausch J.S., Ciechanover A., Slot J.W., Geuze H.
    Proc. Natl. Acad. Sci. U.S.A. 89:5542-5546(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs."
    Handley-Gearhart P.M., Stephen A.G., Trausch-Azar J.S., Ciechanover A., Schwartz A.L.
    J. Biol. Chem. 269:33171-33178(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF ISOFORM 1 AND ISOFORM 2.
  12. "Identification of a region within the ubiquitin-activating enzyme required for nuclear targeting and phosphorylation."
    Stephen A.G., Trausch-Azar J.S., Handley-Gearhart P.M., Ciechanover A., Schwartz A.L.
    J. Biol. Chem. 272:10895-10903(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-4, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-4 AND 8-LYS--ARG-11.
  13. Cited for: ISGYLATION.
  14. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
    Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
    Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-46; THR-800 AND SER-835, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-671 AND LYS-980, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-810, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage."
    Moudry P., Lukas C., Macurek L., Hanzlikova H., Hodny Z., Lukas J., Bartek J.
    Cell Cycle 11:1573-1582(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  26. "Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy."
    Ramser J., Ahearn M.E., Lenski C., Yariz K.O., Hellebrand H., von Rhein M., Clark R.D., Schmutzler R.K., Lichtner P., Hoffman E.P., Meindl A., Baumbach-Reardon L.
    Am. J. Hum. Genet. 82:188-193(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SMAX2 ILE-539 AND GLY-547.
  27. "Clinical and neuropathological features of X-linked spinal muscular atrophy (SMAX2) associated with a novel mutation in the UBA1 gene."
    Dlamini N., Josifova D.J., Paine S.M., Wraige E., Pitt M., Murphy A.J., King A., Buk S., Smith F., Abbs S., Sewry C., Jacques T.S., Jungbluth H.
    Neuromuscul. Disord. 23:391-398(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SMAX2 VAL-557.

Entry informationi

Entry nameiUBA1_HUMAN
AccessioniPrimary (citable) accession number: P22314
Secondary accession number(s): Q5JRR8, Q96E13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 25, 2002
Last modified: July 22, 2015
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.