UniProtKB - P22314 (UBA1_HUMAN)

BLAST

>sp|P22314|UBA1_HUMAN Ubiquitin-like modifier-activating enzyme 1 OS=Homo sapiens OX=9606 GN=UBA1 PE=1 SV=3
MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLY
VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLRE
EDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCH
NRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARH
GFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKK
ISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVA
LAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPI
MQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIG
CELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMN
PHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGT
LGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPA
ENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSN
NIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTG
SQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLP
GFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAA
VVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEV
QGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVS
RVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR

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History
Entry version 212 (07 Nov 2018)
Sequence version 3 (25 Oct 2002)
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Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

UBA1

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1606621, PubMed:1447181). 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 (PubMed:1447181). 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 (PubMed:22456334).3 Publications

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.By similarity

Catalytic activityⁱ

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.1 Publication

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	478	ATP; via amide nitrogenBy similarity	1
Binding siteⁱ	504	ATPBy similarity	1
Binding siteⁱ	515	ATPBy similarity	1
Binding siteⁱ	528	ATPBy similarity	1
Active siteⁱ	632	Glycyl thioester intermediatePROSITE-ProRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	576 – 577	ATPBy similarity		2

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
- 22681889
ubiquitin activating enzyme activity
Source: MGI
Inferred from direct assayⁱ
- 12629039
- 21685362

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to DNA damage stimulus
Source: UniProtKB
Inferred from direct assayⁱ
- 22456334
protein ubiquitination
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ligase
Biological process	Ubl conjugation pathway
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS05465-MONOMER
BRENDAⁱ	2.3.2.B5 2681 6.2.1.B9 2681
Reactomeⁱ	R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORⁱ	P22314
UniPathwayⁱ	UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ubiquitin-like modifier-activating enzyme 1 (EC:6.2.1.451 Publication) Alternative name(s): Protein A1S9 Ubiquitin-activating enzyme E1
Gene namesⁱ	Name:UBA1 Synonyms:A1S9T, UBE1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome X

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000130985.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:12469 UBA1
MIMⁱ	314370 gene
neXtProtⁱ	NX_P22314

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.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_043501	539	M → I in SMAX2. 1 PublicationCorresponds to variant dbSNP:rs80356545EnsemblClinVar.	1
Natural variantⁱVAR_043502	547	S → G in SMAX2. 1 PublicationCorresponds to variant dbSNP:rs80356546EnsemblClinVar.	1
Natural variantⁱVAR_071121	557	E → V in SMAX2. 1 Publication	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	4	S → A: Reduces phosphorylation. 1 Publication		1
Mutagenesisⁱ	8 – 11	KKRR → AAAA: Loss of nuclear localization and a 90-95% decrease in the phosphorylation. 1 Publication		4

Keywords - Diseaseⁱ

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET More...DisGeNETⁱ	7317
GeneReviewsⁱ	UBA1
MalaCards human disease database More...MalaCardsⁱ	UBA1
MIMⁱ	301830 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000130985
Orphanetⁱ	1145 Infantile-onset X-linked spinal muscular atrophy
PharmGKBⁱ	PA37119

Chemistry databases

ChEMBLⁱ	CHEMBL5924
Drug and drug target database More...DrugBankⁱ	DB04119 Hexatantalum Dodecabromide

Polymorphism and mutation databases

BioMutaⁱ	UBA1
DMDMⁱ	24418865

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000194934	2 – 1058	Ubiquitin-like modifier-activating enzyme 1Add BLAST	1057
Isoform 2 (identifier: P22314-2)
Initiator methionineⁱ		RemovedCombined sources

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineCombined sources	1
Modified residueⁱ	4	Phosphoserine1 Publication	1
Modified residueⁱ	13	PhosphoserineCombined sources	1
Modified residueⁱ	21	PhosphoserineBy similarity	1
Modified residueⁱ	24	PhosphoserineBy similarity	1
Modified residueⁱ	46	PhosphoserineCombined sources	1
Modified residueⁱ	55	PhosphotyrosineBy similarity	1
Modified residueⁱ	528	N6-succinyllysineBy similarity	1
Modified residueⁱ	671	N6-acetyllysineCombined sources	1
Modified residueⁱ	800	PhosphothreonineCombined sources	1
Modified residueⁱ	810	PhosphoserineCombined sources	1
Modified residueⁱ	816	PhosphoserineBy similarity	1
Modified residueⁱ	820	PhosphoserineCombined sources	1
Modified residueⁱ	835	PhosphoserineCombined sources	1
Modified residueⁱ	980	N6-acetyllysineCombined sources	1
Isoform 2 (identifier: P22314-2)
Modified residueⁱ	2	N-acetylalanineCombined sources	1

Post-translational modificationⁱ

ISGylated.1 Publication

Keywords - PTMⁱ

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P22314
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P22314
PaxDbⁱ	P22314
PeptideAtlas More...PeptideAtlasⁱ	P22314
PRIDEⁱ	P22314
ProteomicsDBⁱ	53983

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00645078

REPRODUCTION-2DPAGEⁱ

IPI00645078

PTM databases

iPTMnetⁱ	P22314
PhosphoSitePlusⁱ	P22314
SwissPalmⁱ	P22314

Expressionⁱ

Tissue specificityⁱ

Detected in erythrocytes (at protein level). Ubiquitous.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000130985 Expressed in 243 organ(s), highest expression level in pituitary gland
CleanExⁱ	HS_UBA1
ExpressionAtlasⁱ	P22314 baseline and differential
Genevisibleⁱ	P22314 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB019435 CAB073410 HPA000289 HPA001506

HPAⁱ

CAB019435
CAB073410
HPA000289
HPA001506

Interactionⁱ

Subunit structureⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	Q76353	2	EBI-709688,EBI-6248077	From Human immunodeficiency virus 1.
GAN	Q9H2C0	5	EBI-709688,EBI-764342
UBE2I	P63279	2	EBI-709688,EBI-80168

Protein-protein interaction databases

BioGridⁱ	113165, 150 interactors
Database of interacting proteins More...DIPⁱ	DIP-33686N
IntActⁱ	P22314, 137 interactors
Molecular INTeraction database More...MINTⁱ	P22314
STRINGⁱ	9606.ENSP00000338413

Chemistry databases

BindingDBⁱ

P22314

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	55 – 62	Combined sources	8
Beta strandⁱ	74 – 78	Combined sources	5
Helixⁱ	82 – 93	Combined sources	12
Beta strandⁱ	97 – 102	Combined sources	6
Helixⁱ	109 – 112	Combined sources	4
Helixⁱ	120 – 122	Combined sources	3
Helixⁱ	127 – 136	Combined sources	10
Beta strandⁱ	140 – 142	Combined sources	3
Beta strandⁱ	144 – 147	Combined sources	4
Helixⁱ	153 – 156	Combined sources	4
Beta strandⁱ	160 – 164	Combined sources	5
Helixⁱ	169 – 181	Combined sources	13
Beta strandⁱ	185 – 192	Combined sources	8
Beta strandⁱ	195 – 201	Combined sources	7
Beta strandⁱ	206 – 210	Combined sources	5
Beta strandⁱ	219 – 224	Combined sources	6
Beta strandⁱ	226 – 229	Combined sources	4
Beta strandⁱ	231 – 234	Combined sources	4
Beta strandⁱ	244 – 252	Combined sources	9
Helixⁱ	257 – 259	Combined sources	3
Beta strandⁱ	265 – 269	Combined sources	5
Beta strandⁱ	271 – 273	Combined sources	3
Beta strandⁱ	291 – 301	Combined sources	11
Helixⁱ	306 – 311	Combined sources	6
Helixⁱ	326 – 343	Combined sources	18
Helixⁱ	352 – 368	Combined sources	17
Turnⁱ	371 – 373	Combined sources	3
Helixⁱ	380 – 388	Combined sources	9
Helixⁱ	395 – 413	Combined sources	19
Beta strandⁱ	422 – 428	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P22314
SMRⁱ	P22314
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Repeatⁱ	63 – 199	1-1Add BLAST		137
Repeatⁱ	459 – 611	1-2Add BLAST		153

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	63 – 611	2 approximate repeatsAdd BLAST		549

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	5 – 11	Nuclear localization signal		7

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

eggNOGⁱ	KOG2012 Eukaryota COG0476 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000016689
HOGENOMⁱ	HOG000167329
HOVERGENⁱ	HBG054199
InParanoidⁱ	P22314
KEGG Orthology (KO) More...KOⁱ	K03178
OMAⁱ	CIVWARL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0130
PhylomeDBⁱ	P22314
TreeFamⁱ	TF300586

Family and domain databases

Gene3Dⁱ	3.10.290.60, 1 hit
InterProⁱ	View protein in InterPro IPR032420 E1_4HB IPR032418 E1_FCCH IPR000594 ThiF_NAD_FAD-bd IPR018965 Ub-activating_enz_E1_C IPR038252 UBA_E1_C_sf IPR019572 UBA_E1_Cys IPR035985 Ubiquitin-activating_enz IPR018075 UBQ-activ_enz_E1 IPR018074 UBQ-activ_enz_E1_CS IPR033127 UBQ-activ_enz_E1_Cys_AS IPR000011 UBQ/SUMO-activ_enz_E1-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16191 E1_4HB, 1 hit PF16190 E1_FCCH, 1 hit PF09358 E1_UFD, 1 hit PF00899 ThiF, 2 hits PF10585 UBA_e1_thiolCys, 1 hit
PRINTSⁱ	PR01849 UBIQUITINACT
SMARTⁱ	View protein in SMART SM00985 UBA_e1_C, 1 hit
SUPFAMⁱ	SSF69572 SSF69572, 2 hits
TIGRFAMsⁱ	TIGR01408 Ube1, 1 hit
PROSITEⁱ	View protein in PROSITE PS00536 UBIQUITIN_ACTIVAT_1, 1 hit PS00865 UBIQUITIN_ACTIVAT_2, 1 hit

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. Align Add to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P22314-1) [UniParc]FASTA Add 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

Isoform 2 (identifier: P22314-2) [UniParc]FASTA Add to basket

Also known as: E1b

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

« Hide

        10         20         30         40         50
MAKNGSEADI DEGLYSRQLY VLGHEAMKRL QTSSVLVSGL RGLGVEIAKN 
        60         70         80         90        100
IILGGVKAVT LHDQGTAQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS 
       110        120        130        140        150
YVPVTAYTGP LVEDFLSGFQ VVVLTNTPLE DQLRVGEFCH NRGIKLVVAD 
       160        170        180        190        200
TRGLFGQLFC DFGEEMILTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH 
       210        220        230        240        250
GFESGDFVSF SEVQGMVELN GNQPMEIKVL GPYTFSICDT SNFSDYIRGG 
       260        270        280        290        300
IVSQVKVPKK ISFKSLVASL AEPDFVVTDF AKFSRPAQLH IGFQALHQFC 
       310        320        330        340        350
AQHGRPPRPR NEEDAAELVA LAQAVNARAL PAVQQNNLDE DLIRKLAYVA 
       360        370        380        390        400
AGDLAPINAF IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEVLT 
       410        420        430        440        450
EDKCLQRQNR YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI 
       460        470        480        490        500
GLGCGEGGEI IVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN 
       510        520        530        540        550
PHIRVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY 
       560        570        580        590        600
YRKPLLESGT LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA 
       610        620        630        640        650
IEHTLQWARD EFEGLFKQPA ENVNQYLTDP KFVERTLRLA GTQPLEVLEA 
       660        670        680        690        700
VQRSLVLQRP QTWADCVTWA CHHWHTQYSN NIRQLLHNFP PDQLTSSGAP 
       710        720        730        740        750
FWSGPKRCPH PLTFDVNNPL HLDYVMAAAN LFAQTYGLTG SQDRAAVATF 
       760        770        780        790        800
LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP 
       810        820        830        840        850
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDIPSADR HKSKLIAGKI 
       860        870        880        890        900
IPAIATTTAA VVGLVCLELY KVVQGHRQLD SYKNGFLNLA LPFFGFSEPL 
       910        920        930        940        950
AAPRHQYYNQ EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML 
       960        970        980        990       1000
SQGVSMLYSF FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC 
      1010 
NDESGEDVEV PYVRYTIR

Show »

Length:1,018

Mass (Da):113,800

Checksum:ⁱ9A508347FE29FB19

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q5JRR6	Q5JRR6_HUMAN	Ubiquitin-like modifier-activating ... Ubiquitin-like modifier-activating enzyme 1	UBA1	506	Annotation score:
Q5JRS0	Q5JRS0_HUMAN	Ubiquitin-like modifier-activating ... Ubiquitin-like modifier-activating enzyme 1	UBA1	284	Annotation score:
Q5JRR9	Q5JRR9_HUMAN	Ubiquitin-like modifier-activating ... Ubiquitin-like modifier-activating enzyme 1	UBA1	270	Annotation score:
Q5JRS2	Q5JRS2_HUMAN	Ubiquitin-like modifier-activating ... Ubiquitin-like modifier-activating enzyme 1	UBA1	234	Annotation score:
Q5JRS3	Q5JRS3_HUMAN	Ubiquitin-like modifier-activating ... Ubiquitin-like modifier-activating enzyme 1	UBA1	195	Annotation score:
Q5JRS1	Q5JRS1_HUMAN	Ubiquitin-like modifier-activating ... Ubiquitin-like modifier-activating enzyme 1	UBA1	173	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	190	D → G in CAA40296 (PubMed:1606621).Curated		1
Sequence conflictⁱ	434	E → Q in CAA40296 (PubMed:1606621).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_043500	447	R → H. Corresponds to variant dbSNP:rs2070169EnsemblClinVar.	1
Natural variantⁱVAR_043501	539	M → I in SMAX2. 1 PublicationCorresponds to variant dbSNP:rs80356545EnsemblClinVar.	1
Natural variantⁱVAR_043502	547	S → G in SMAX2. 1 PublicationCorresponds to variant dbSNP:rs80356546EnsemblClinVar.	1
Natural variantⁱVAR_071121	557	E → V in SMAX2. 1 Publication	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_055913	1 – 40	Missing in isoform 2. CuratedAdd BLAST		40

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X56976 mRNA Translation: CAA40296.1 M58028 mRNA Translation: AAA61246.1 AL513366 Genomic DNA No translation available. CH471164 Genomic DNA Translation: EAW59290.1 BC013041 mRNA Translation: AAH13041.1 X52897 mRNA Translation: CAA37078.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS14275.1 [P22314-1]
PIRⁱ	A38564
NCBI Reference Sequences More...RefSeqⁱ	NP_003325.2, NM_003334.3 [P22314-1] NP_695012.1, NM_153280.2 [P22314-1] XP_016885269.1, XM_017029780.1 [P22314-1] XP_016885270.1, XM_017029781.1 [P22314-1]
UniGeneⁱ	Hs.533273

Genome annotation databases

Ensemblⁱ	ENST00000335972; ENSP00000338413; ENSG00000130985 [P22314-1] ENST00000377351; ENSP00000366568; ENSG00000130985 [P22314-1]
GeneIDⁱ	7317
KEGGⁱ	hsa:7317
UCSC genome browser More...UCSCⁱ	uc004dhj.5 human [P22314-1]

Keywords - Coding sequence diversityⁱ

Alternative initiation, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P22314	Testicular secretory protein Li 63		HUMAN		1058	UniRef100_P22314
UBA1 isoform 5 (Fragment)		PONAB		271
UBA1 isoform 2 (Fragment)		PANTR		271
Isoform 2 of Ubiquitin-like modifier-activating enzyme 1		HUMAN		1018
Ubiquitin-like modifier-activating enzyme 1 (Fragment)		HUMAN		234
+7

Protein	Similar proteins		Species	Score	Length	Source
P22314	Ubiquitin-like modifier-activating enzyme 1	)	MOUSE		1058	UniRef90_P22314
Ubiquitin-like modifier-activating enzyme 1		BOVIN		1058
Ubiquitin-like modifier-activating enzyme 1		RABIT		1058
Ubiquitin-like modifier-activating enzyme 1		RAT		1058
Testicular secretory protein Li 63		HUMAN		1058
+199

Protein	Similar proteins		Species	Score	Length	Source
P22314	Ubiquitin-like modifier-activating enzyme 1		RAT		1058	UniRef50_P22314
Ubiquitin-like modifier-activating enzyme 1		BOVIN		1058
Ubiquitin-like modifier-activating enzyme 1		RABIT		1058
Ubiquitin-like modifier-activating enzyme 1	)	MOUSE		1058
Testicular secretory protein Li 63		HUMAN		1058
+395

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 No translation available. CH471164 Genomic DNA Translation: EAW59290.1 BC013041 mRNA Translation: AAH13041.1 X52897 mRNA Translation: CAA37078.1
CCDSⁱ	CCDS14275.1 [P22314-1]
PIRⁱ	A38564
RefSeqⁱ	NP_003325.2, NM_003334.3 [P22314-1] NP_695012.1, NM_153280.2 [P22314-1] XP_016885269.1, XM_017029780.1 [P22314-1] XP_016885270.1, XM_017029781.1 [P22314-1]
UniGeneⁱ	Hs.533273

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4P22	X-ray	2.75	A/B	1-439	[»]
ProteinModelPortalⁱ	P22314
SMRⁱ	P22314
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	113165, 150 interactors
DIPⁱ	DIP-33686N
IntActⁱ	P22314, 137 interactors
MINTⁱ	P22314
STRINGⁱ	9606.ENSP00000338413

Chemistry databases

BindingDBⁱ	P22314
ChEMBLⁱ	CHEMBL5924
DrugBankⁱ	DB04119 Hexatantalum Dodecabromide

PTM databases

iPTMnetⁱ	P22314
PhosphoSitePlusⁱ	P22314
SwissPalmⁱ	P22314

Polymorphism and mutation databases

BioMutaⁱ	UBA1
DMDMⁱ	24418865

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00645078

REPRODUCTION-2DPAGEⁱ

IPI00645078

Proteomic databases

EPDⁱ	P22314
MaxQBⁱ	P22314
PaxDbⁱ	P22314
PeptideAtlasⁱ	P22314
PRIDEⁱ	P22314
ProteomicsDBⁱ	53983

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	7317
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000335972; ENSP00000338413; ENSG00000130985 [P22314-1] ENST00000377351; ENSP00000366568; ENSG00000130985 [P22314-1]
GeneIDⁱ	7317
KEGGⁱ	hsa:7317
UCSCⁱ	uc004dhj.5 human [P22314-1]

Organism-specific databases

CTDⁱ	7317
DisGeNETⁱ	7317
EuPathDBⁱ	HostDB:ENSG00000130985.16
GeneCardsⁱ	UBA1
GeneReviewsⁱ	UBA1
HGNCⁱ	HGNC:12469 UBA1
HPAⁱ	CAB019435 CAB073410 HPA000289 HPA001506
MalaCardsⁱ	UBA1
MIMⁱ	301830 phenotype 314370 gene
neXtProtⁱ	NX_P22314
OpenTargetsⁱ	ENSG00000130985
Orphanetⁱ	1145 Infantile-onset X-linked spinal muscular atrophy
PharmGKBⁱ	PA37119
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2012 Eukaryota COG0476 LUCA
GeneTreeⁱ	ENSGT00390000016689
HOGENOMⁱ	HOG000167329
HOVERGENⁱ	HBG054199
InParanoidⁱ	P22314
KOⁱ	K03178
OMAⁱ	CIVWARL
OrthoDBⁱ	EOG091G0130
PhylomeDBⁱ	P22314
TreeFamⁱ	TF300586

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
BioCycⁱ	MetaCyc:HS05465-MONOMER
BRENDAⁱ	2.3.2.B5 2681 6.2.1.B9 2681
Reactomeⁱ	R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORⁱ	P22314

Miscellaneous databases

ChiTaRSⁱ	UBA1 human
GeneWikiⁱ	UBA1
GenomeRNAiⁱ	7317
Protein Ontology More...PROⁱ	PR:P22314
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000130985 Expressed in 243 organ(s), highest expression level in pituitary gland
CleanExⁱ	HS_UBA1
ExpressionAtlasⁱ	P22314 baseline and differential
Genevisibleⁱ	P22314 HS

Family and domain databases

Gene3Dⁱ	3.10.290.60, 1 hit
InterProⁱ	View protein in InterPro IPR032420 E1_4HB IPR032418 E1_FCCH IPR000594 ThiF_NAD_FAD-bd IPR018965 Ub-activating_enz_E1_C IPR038252 UBA_E1_C_sf IPR019572 UBA_E1_Cys IPR035985 Ubiquitin-activating_enz IPR018075 UBQ-activ_enz_E1 IPR018074 UBQ-activ_enz_E1_CS IPR033127 UBQ-activ_enz_E1_Cys_AS IPR000011 UBQ/SUMO-activ_enz_E1-like
Pfamⁱ	View protein in Pfam PF16191 E1_4HB, 1 hit PF16190 E1_FCCH, 1 hit PF09358 E1_UFD, 1 hit PF00899 ThiF, 2 hits PF10585 UBA_e1_thiolCys, 1 hit
PRINTSⁱ	PR01849 UBIQUITINACT
SMARTⁱ	View protein in SMART SM00985 UBA_e1_C, 1 hit
SUPFAMⁱ	SSF69572 SSF69572, 2 hits
TIGRFAMsⁱ	TIGR01408 Ube1, 1 hit
PROSITEⁱ	View protein in PROSITE PS00536 UBIQUITIN_ACTIVAT_1, 1 hit PS00865 UBIQUITIN_ACTIVAT_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	UBA1_HUMAN
Accessionⁱ	P22314Primary (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:	November 7, 2018
	This is version 212 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
Human chromosome X
Human chromosome X: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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Help

UniRef

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Supporting data

UniProtKB - P22314 (UBA1_HUMAN)

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Ubiquitin-like modifier-activating enzyme 1

UBA1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Mitochondrion

Other locations

Nucleus

Other locations

Cytosol

Extracellular region or secreted

Mitochondrion

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Your basket is currently empty. ⁱ

Functionⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ