Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00421
Entry Name
UniProt Accession
Theoretical PI
5.49
Molecular Weight
117849.0
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ubiquitin-like modifier-activating enzyme 1
Protein Synonyms/Alias
Protein A1S9; Ubiquitin-activating enzyme E1;
Gene Name
UBA1
Gene Synonyms/Alias
A1S9T; UBE1;
Created Date
01-AUG-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
588
Canonical
RMYMDRRCVYYRKPL
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Nucleotide-binding: 478 507 ATP.
Region: 5 11 Nuclear localization signal.
Region: 63 611 2 approximate repeats.
Active site: 632 632 Glycyl thioester intermediate.
Modified residue: 2 2 N-acetylserine.
Modified residue: 4 4 Phosphoserine.
Modified residue: 13 13 Phosphoserine.
Modified residue: 46 46 Phosphoserine.
Modified residue: 55 55 Phosphotyrosine.
Modified residue: 528 528 N6-succinyllysine.
Modified residue: 671 671 N6-acetyllysine.
Modified residue: 800 800 Phosphothreonine.
Modified residue: 810 810 Phosphoserine.
Modified residue: 816 816 Phosphoserine.
Modified residue: 820 820 Phosphoserine.
Modified residue: 835 835 Phosphoserine.
Modified residue: 980 980 N6-acetyllysine.
Protein Length
1058 AA.
Protein Sequence
(Canonical)
MSSSPLSKKR RVSGPDPKPG SNCSPAQSVL SEVPSVPTNG MAKNGSEADI DEGLYSRQLY  60
VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTAQWA DLSSQFYLRE  120
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSGFQ VVVLTNTPLE DQLRVGEFCH  180
NRGIKLVVAD TRGLFGQLFC DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH  240
GFESGDFVSF SEVQGMVELN GNQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK  300
ISFKSLVASL AEPDFVVTDF AKFSRPAQLH IGFQALHQFC AQHGRPPRPR NEEDAAELVA  360
LAQAVNARAL PAVQQNNLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI  420
MQWLYFDALE CLPEDKEVLT EDKCLQRQNR YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG  480
CELLKNFAMI GLGCGEGGEI IVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN  540
PHIRVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT  600
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA  660
ENVNQYLTDP KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWADCVTWA CHHWHTQYSN  720
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNPL HLDYVMAAAN LFAQTYGLTG  780
SQDRAAVATF LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP  840
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDIPSADR HKSKLIAGKI IPAIATTTAA  900
VVGLVCLELY KVVQGHRQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV  960
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS  1020
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR                          1058
FASTA
(Canonical)
>LipidDB-9606-00421|P22314
MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLY
VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLRE
EDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCH
NRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARH
GFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKK
ISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVA
LAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPI
MQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIG
CELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMN
PHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGT
LGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPA
ENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSN
NIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTG
SQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLP
GFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAA
VVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEV
QGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVS
RVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; IBA:RefGenome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005739; C:mitochondrion; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0004839; F:ubiquitin activating enzyme activity; IBA:RefGenome
GO:0004842; F:ubiquitin-protein transferase activity; IBA:RefGenome
GO:0008219; P:cell death; IEA:UniProtKB-KW
GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB
GO:0019941; P:modification-dependent protein catabolic process; IBA:RefGenome
GO:0016567; P:protein ubiquitination; IBA:RefGenome
Interpro
InterPro; IPR009036; Molybdenum_cofac_synth_MoeB
InterPro; IPR016040; NAD(P)-bd_dom
InterPro; IPR000594; ThiF_NAD_FAD-bd
InterPro; IPR018965; Ub-activating_enz_e1_C
InterPro; IPR023280; Ub-like_act_enz_cat_cys_dom
InterPro; IPR000127; UBact_repeat
InterPro; IPR019572; Ubiquitin-activating_enzyme
InterPro; IPR018075; UBQ-activ_enz_E1
InterPro; IPR018074; UBQ-activ_enz_E1_AS
InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like
Pfam
Pfam; PF00899; ThiF;
Pfam; PF09358; UBA_e1_C;
Pfam; PF10585; UBA_e1_thiolCys;
Pfam; PF02134; UBACT;
SMART
SMART; SM00985; UBA_e1_C;
PROSITE
PROSITE; PS00536; UBIQUITIN_ACTIVAT_1;
PROSITE; PS00865; UBIQUITIN_ACTIVAT_2;
PRINTS
PRINTS; PR01849; UBIQUITINACT;