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P41226

- UBA7_HUMAN

UniProt

P41226 - UBA7_HUMAN

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Protein

Ubiquitin-like modifier-activating enzyme 7

Gene

UBA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei599 – 5991Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi442 – 47130ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ISG15 activating enzyme activity Source: HGNC
  3. ubiquitin activating enzyme activity Source: RefGenome
  4. ubiquitin-protein transferase activity Source: RefGenome

GO - Biological processi

  1. cellular protein modification process Source: HGNC
  2. cytokine-mediated signaling pathway Source: Reactome
  3. innate immune response Source: Reactome
  4. ISG15-protein conjugation Source: HGNC
  5. modification-dependent protein catabolic process Source: RefGenome
  6. negative regulation of type I interferon production Source: Reactome
  7. protein ubiquitination Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 7
Short name:
Ubiquitin-activating enzyme 7
Alternative name(s):
D8
Ubiquitin-activating enzyme E1 homolog
Gene namesi
Name:UBA7
Synonyms:UBE1L, UBE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:12471. UBA7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. nucleus Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162407761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10121012Ubiquitin-like modifier-activating enzyme 7PRO_0000194937Add
BLAST

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP41226.
PaxDbiP41226.
PRIDEiP41226.

PTM databases

PhosphoSiteiP41226.

Expressioni

Tissue specificityi

Expressed in a variety of normal and tumor cell types, but is reduced in lung cancer cell lines.

Gene expression databases

BgeeiP41226.
CleanExiHS_UBA7.
GenevestigatoriP41226.

Organism-specific databases

HPAiCAB015444.

Interactioni

Subunit structurei

Monomer (By similarity). Binds and is involved in the conjugation of G1P2/ISG15.By similarity

Protein-protein interaction databases

BioGridi113166. 5 interactions.
DIPiDIP-60526N.
IntActiP41226. 1 interaction.
MINTiMINT-1454413.
STRINGi9606.ENSP00000333266.

Structurei

3D structure databases

ProteinModelPortaliP41226.
SMRiP41226. Positions 10-1006.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati23 – 1591371-1Add
BLAST
Repeati423 – 5751531-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 5755532 approximate repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiP41226.
KOiK10698.
OMAiLGHWQLC.
OrthoDBiEOG74R1PV.
PhylomeDBiP41226.
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.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41226-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDALDASKLL DEELYSRQLY VLGSPAMQRI QGARVLVSGL QGLGAEVAKN
60 70 80 90 100
LVLMGVGSLT LHDPHPTCWS DLAAQFLLSE QDLERSRAEA SQELLAQLNR
110 120 130 140 150
AVQVVVHTGD ITEDLLLDFQ VVVLTAAKLE EQLKVGTLCH KHGVCFLAAD
160 170 180 190 200
TRGLVGQLFC DFGEDFTVQD PTEAEPLTAA IQHISQGSPG ILTLRKGANT
210 220 230 240 250
HYFRDGDLVT FSGIEGMVEL NDCDPRSIHV REDGSLEIGD TTTFSRYLRG
260 270 280 290 300
GAITEVKRPK TVRHKSLDTA LLQPHVVAQS SQEVHHAHCL HQAFCALHKF
310 320 330 340 350
QHLHGRPPQP WDPVDAETVV GLARDLEPLK RTEEEPLEEP LDEALVRTVA
360 370 380 390 400
LSSAGVLSPM VAMLGAVAAQ EVLKAISRKF MPLDQWLYFD ALDCLPEDGE
410 420 430 440 450
LLPSPEDCAL RGSRYDGQIA VFGAGFQEKL RRQHYLLVGA GAIGCELLKV
460 470 480 490 500
FALVGLGAGN SGGLTVVDMD HIERSNLSRQ FLFRSQDVGR PKAEVAAAAA
510 520 530 540 550
RGLNPDLQVI PLTYPLDPTT EHIYGDNFFS RVDGVAAALD SFQARRYVAA
560 570 580 590 600
RCTHYLKPLL EAGTSGTWGS ATVFMPHVTE AYRAPASAAA SEDAPYPVCT
610 620 630 640 650
VRYFPSTAEH TLQWARHEFE ELFRLSAETI NHHQQAHTSL ADMDEPQTLT
660 670 680 690 700
LLKPVLGVLR VRPQNWQDCV AWALGHWKLC FHYGIKQLLR HFPPNKVLED
710 720 730 740 750
GTPFWSGPKQ CPQPLEFDTN QDTHLLYVLA AANLYAQMHG LPGSQDWTAL
760 770 780 790 800
RELLKLLPQP DPQQMAPIFA SNLELASASA EFGPEQQKEL NKALEVWSVG
810 820 830 840 850
PPLKPLMFEK DDDSNFHVDF VVAAASLRCQ NYGIPPVNRA QSKRIVGQII
860 870 880 890 900
PAIATTTAAV AGLLGLELYK VVSGPRPRSA FRHSYLHLAE NYLIRYMPFA
910 920 930 940 950
PAIQTFHHLK WTSWDRLKVP AGQPERTLES LLAHLQEQHG LRVRILLHGS
960 970 980 990 1000
ALLYAAGWSP EKQAQHLPLR VTELVQQLTG QAPAPGQRVL VLELSCEGDD
1010
EDTAFPPLHY EL
Length:1,012
Mass (Da):111,694
Last modified:November 25, 2008 - v2
Checksum:iA01E1106D81778EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 37824GVLSP…KAISR → RCLEPMVACWVSSCPGSAEG NLQ in AAA75388. (PubMed:8327486)CuratedAdd
BLAST
Sequence conflicti355 – 37824GVLSP…KAISR → RCLEPMVACWVSSCPGSAEG NLQ in AAG49557. (PubMed:7734949)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti712 – 7121P → S.
Corresponds to variant rs11928913 [ dbSNP | Ensembl ].
VAR_052434
Natural varianti817 – 8171H → R.
Corresponds to variant rs2230149 [ dbSNP | Ensembl ].
VAR_047793

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13852 mRNA. Translation: AAA75388.1.
AF294032 Genomic DNA. Translation: AAG49557.1.
BT007026 mRNA. Translation: AAP35672.1.
CH471055 Genomic DNA. Translation: EAW65023.1.
BC006378 mRNA. Translation: AAH06378.1.
CCDSiCCDS2805.1.
RefSeqiNP_003326.2. NM_003335.2.
UniGeneiHs.16695.

Genome annotation databases

EnsembliENST00000333486; ENSP00000333266; ENSG00000182179.
GeneIDi7318.
KEGGihsa:7318.
UCSCiuc003cxr.3. human.

Polymorphism databases

DMDMi215273977.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13852 mRNA. Translation: AAA75388.1 .
AF294032 Genomic DNA. Translation: AAG49557.1 .
BT007026 mRNA. Translation: AAP35672.1 .
CH471055 Genomic DNA. Translation: EAW65023.1 .
BC006378 mRNA. Translation: AAH06378.1 .
CCDSi CCDS2805.1.
RefSeqi NP_003326.2. NM_003335.2.
UniGenei Hs.16695.

3D structure databases

ProteinModelPortali P41226.
SMRi P41226. Positions 10-1006.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113166. 5 interactions.
DIPi DIP-60526N.
IntActi P41226. 1 interaction.
MINTi MINT-1454413.
STRINGi 9606.ENSP00000333266.

Chemistry

BindingDBi P41226.
ChEMBLi CHEMBL2321623.

PTM databases

PhosphoSitei P41226.

Polymorphism databases

DMDMi 215273977.

Proteomic databases

MaxQBi P41226.
PaxDbi P41226.
PRIDEi P41226.

Protocols and materials databases

DNASUi 7318.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333486 ; ENSP00000333266 ; ENSG00000182179 .
GeneIDi 7318.
KEGGi hsa:7318.
UCSCi uc003cxr.3. human.

Organism-specific databases

CTDi 7318.
GeneCardsi GC03M049848.
HGNCi HGNC:12471. UBA7.
HPAi CAB015444.
MIMi 191325. gene.
neXtProti NX_P41226.
PharmGKBi PA162407761.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00390000016689.
HOGENOMi HOG000167329.
HOVERGENi HBG054199.
InParanoidi P41226.
KOi K10698.
OMAi LGHWQLC.
OrthoDBi EOG74R1PV.
PhylomeDBi P41226.
TreeFami TF300586.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi UBA7. human.
GeneWikii UBE1L.
GenomeRNAii 7318.
NextBioi 28610.
PROi P41226.
SOURCEi Search...

Gene expression databases

Bgeei P41226.
CleanExi HS_UBA7.
Genevestigatori P41226.

Family and domain databases

Gene3Di 1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProi IPR009036. 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 ]
Pfami PF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view ]
PRINTSi PR01849. UBIQUITINACT.
SMARTi SM00985. UBA_e1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 2 hits.
TIGRFAMsi TIGR01408. Ube1. 1 hit.
PROSITEi PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A gene in the chromosomal region 3p21 with greatly reduced expression in lung cancer is similar to the gene for ubiquitin-activating enzyme."
    Kok K., Hofstra R., Pilz A., van den Berg A., Terpstra P., Buys C.H.C.M., Carritt B.
    Proc. Natl. Acad. Sci. U.S.A. 90:6071-6075(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell.
  2. "The genomic structure of the human UBE1L gene."
    Kok K., Van den Berg A., Veldhuis P.M., Franke M., Terpstra P., Buys C.H.C.M.
    Gene Expr. 4:163-175(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Eye.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-17.
    Tissue: Platelet.
  7. "Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein."
    Yuan W., Krug R.M.
    EMBO J. 20:362-371(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 973-987, INTERACTION WITH G1P2, PATHWAY.
  8. "Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo."
    Lenschow D.J., Giannakopoulos N.V., Gunn L.J., Johnston C., O'Guin A.K., Schmidt R.E., Levine B., Virgin H.W. IV
    J. Virol. 79:13974-13983(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells."
    Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M.
    Proc. Natl. Acad. Sci. U.S.A. 107:2253-2258(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Covalent protein modification with ISG15 via a conserved cysteine in the hinge region."
    Bade V.N., Nickels J., Keusekotten K., Praefcke G.J.
    PLoS ONE 7:E38294-E38294(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION.

Entry informationi

Entry nameiUBA7_HUMAN
AccessioniPrimary (citable) accession number: P41226
Secondary accession number(s): Q9BRB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 141 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3