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P41226 (UBA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like modifier-activating enzyme 7

Short name=Ubiquitin-activating enzyme 7
Alternative name(s):
D8
Ubiquitin-activating enzyme E1 homolog
Gene names
Name:UBA7
Synonyms:UBE1L, UBE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Pathway

Protein modification; protein ubiquitination. Ref.7

Subunit structure

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

Tissue specificity

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

Post-translational modification

ISGylated. Ref.10

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.

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10121012Ubiquitin-like modifier-activating enzyme 7
PRO_0000194937

Regions

Repeat23 – 1591371-1
Repeat423 – 5751531-2
Nucleotide binding442 – 47130ATP By similarity
Region23 – 5755532 approximate repeats

Sites

Active site5991Glycyl thioester intermediate By similarity

Natural variations

Natural variant7121P → S.
Corresponds to variant rs11928913 [ dbSNP | Ensembl ].
VAR_052434
Natural variant8171H → R.
Corresponds to variant rs2230149 [ dbSNP | Ensembl ].
VAR_047793

Experimental info

Sequence conflict355 – 37824GVLSP…KAISR → RCLEPMVACWVSSCPGSAEG NLQ in AAA75388. Ref.1
Sequence conflict355 – 37824GVLSP…KAISR → RCLEPMVACWVSSCPGSAEG NLQ in AAG49557. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P41226 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: A01E1106D81778EB

FASTA1,012111,694
        10         20         30         40         50         60 
MDALDASKLL DEELYSRQLY VLGSPAMQRI QGARVLVSGL QGLGAEVAKN LVLMGVGSLT 

        70         80         90        100        110        120 
LHDPHPTCWS DLAAQFLLSE QDLERSRAEA SQELLAQLNR AVQVVVHTGD ITEDLLLDFQ 

       130        140        150        160        170        180 
VVVLTAAKLE EQLKVGTLCH KHGVCFLAAD TRGLVGQLFC DFGEDFTVQD PTEAEPLTAA 

       190        200        210        220        230        240 
IQHISQGSPG ILTLRKGANT HYFRDGDLVT FSGIEGMVEL NDCDPRSIHV REDGSLEIGD 

       250        260        270        280        290        300 
TTTFSRYLRG GAITEVKRPK TVRHKSLDTA LLQPHVVAQS SQEVHHAHCL HQAFCALHKF 

       310        320        330        340        350        360 
QHLHGRPPQP WDPVDAETVV GLARDLEPLK RTEEEPLEEP LDEALVRTVA LSSAGVLSPM 

       370        380        390        400        410        420 
VAMLGAVAAQ EVLKAISRKF MPLDQWLYFD ALDCLPEDGE LLPSPEDCAL RGSRYDGQIA 

       430        440        450        460        470        480 
VFGAGFQEKL RRQHYLLVGA GAIGCELLKV FALVGLGAGN SGGLTVVDMD HIERSNLSRQ 

       490        500        510        520        530        540 
FLFRSQDVGR PKAEVAAAAA RGLNPDLQVI PLTYPLDPTT EHIYGDNFFS RVDGVAAALD 

       550        560        570        580        590        600 
SFQARRYVAA RCTHYLKPLL EAGTSGTWGS ATVFMPHVTE AYRAPASAAA SEDAPYPVCT 

       610        620        630        640        650        660 
VRYFPSTAEH TLQWARHEFE ELFRLSAETI NHHQQAHTSL ADMDEPQTLT LLKPVLGVLR 

       670        680        690        700        710        720 
VRPQNWQDCV AWALGHWKLC FHYGIKQLLR HFPPNKVLED GTPFWSGPKQ CPQPLEFDTN 

       730        740        750        760        770        780 
QDTHLLYVLA AANLYAQMHG LPGSQDWTAL RELLKLLPQP DPQQMAPIFA SNLELASASA 

       790        800        810        820        830        840 
EFGPEQQKEL NKALEVWSVG PPLKPLMFEK DDDSNFHVDF VVAAASLRCQ NYGIPPVNRA 

       850        860        870        880        890        900 
QSKRIVGQII PAIATTTAAV AGLLGLELYK VVSGPRPRSA FRHSYLHLAE NYLIRYMPFA 

       910        920        930        940        950        960 
PAIQTFHHLK WTSWDRLKVP AGQPERTLES LLAHLQEQHG LRVRILLHGS ALLYAAGWSP 

       970        980        990       1000       1010 
EKQAQHLPLR VTELVQQLTG QAPAPGQRVL VLELSCEGDD EDTAFPPLHY EL 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003326.2. NM_003335.2.
UniGeneHs.16695.

3D structure databases

ProteinModelPortalP41226.
SMRP41226. Positions 10-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113166. 4 interactions.
DIPDIP-60526N.
IntActP41226. 1 interaction.
MINTMINT-1454413.
STRING9606.ENSP00000333266.

Chemistry

ChEMBLCHEMBL2321623.

PTM databases

PhosphoSiteP41226.

Polymorphism databases

DMDM215273977.

Proteomic databases

PaxDbP41226.
PRIDEP41226.

Protocols and materials databases

DNASU7318.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333486; ENSP00000333266; ENSG00000182179.
GeneID7318.
KEGGhsa:7318.
UCSCuc003cxr.3. human.

Organism-specific databases

CTD7318.
GeneCardsGC03M049844.
HGNCHGNC:12471. UBA7.
HPACAB015444.
MIM191325. gene.
neXtProtNX_P41226.
PharmGKBPA162407761.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000167329.
HOVERGENHBG054199.
InParanoidP41226.
KOK10698.
OMALGHWQLC.
OrthoDBEOG74R1PV.
PhylomeDBP41226.
TreeFamTF300586.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

BgeeP41226.
CleanExHS_UBA7.
GenevestigatorP41226.

Family and domain databases

Gene3D1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProIPR009036. 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]
PfamPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SMARTSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 2 hits.
TIGRFAMsTIGR01408. Ube1. 1 hit.
PROSITEPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUBE1L.
GenomeRNAi7318.
NextBio28610.
PROP41226.
SOURCESearch...

Entry information

Entry nameUBA7_HUMAN
AccessionPrimary (citable) accession number: P41226
Secondary accession number(s): Q9BRB2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM