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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 (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

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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei478ATP; via amide nitrogenBy similarity1
Binding sitei504ATPBy similarity1
Binding sitei515ATPBy similarity1
Binding sitei528ATPBy similarity1
Active sitei632Glycyl thioester intermediatePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi576 – 577ATPBy similarity2

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

BioCyciMetaCyc:HS05465-MONOMER.
ZFISH:HS05465-MONOMER.
BRENDAi2.3.2.B5. 2681.
6.2.1.B9. 2681.
ReactomeiR-HSA-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiP22314.
UniPathwayiUPA00143.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12469. UBA1.

Subcellular locationi

Isoform 1 :
Isoform 2 :
  • Cytoplasm 1 Publication

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_043501539M → I in SMAX2. 1 PublicationCorresponds to variant rs80356545dbSNPEnsembl.1
Natural variantiVAR_043502547S → G in SMAX2. 1 PublicationCorresponds to variant rs80356546dbSNPEnsembl.1
Natural variantiVAR_071121557E → V in SMAX2. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4S → A: Reduces phosphorylation. 1 Publication1
Mutagenesisi8 – 11KKRR → AAAA: Loss of nuclear localization and a 90-95% decrease in the phosphorylation. 1 Publication4

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi7317.
MalaCardsiUBA1.
MIMi301830. phenotype.
OpenTargetsiENSG00000130985.
Orphaneti1145. X-linked distal arthrogryposis multiplex congenita.
PharmGKBiPA37119.

Chemistry databases

ChEMBLiCHEMBL5924.

Polymorphism and mutation databases

BioMutaiUBA1.
DMDMi24418865.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001949342 – 1058Ubiquitin-like modifier-activating enzyme 1Add BLAST1057
Isoform 2 (identifier: P22314-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei4Phosphoserine1 Publication1
Modified residuei13PhosphoserineCombined sources1
Modified residuei21PhosphoserineBy similarity1
Modified residuei24PhosphoserineBy similarity1
Modified residuei46PhosphoserineCombined sources1
Modified residuei55PhosphotyrosineBy similarity1
Modified residuei528N6-succinyllysineBy similarity1
Modified residuei671N6-acetyllysineCombined sources1
Modified residuei800PhosphothreonineCombined sources1
Modified residuei810PhosphoserineCombined sources1
Modified residuei816PhosphoserineBy similarity1
Modified residuei820PhosphoserineCombined sources1
Modified residuei835PhosphoserineCombined sources1
Modified residuei980N6-acetyllysineCombined sources1
Isoform 2 (identifier: P22314-2)
Modified residuei2N-acetylalanineCombined sources1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP22314.
MaxQBiP22314.
PaxDbiP22314.
PeptideAtlasiP22314.
PRIDEiP22314.

2D gel databases

REPRODUCTION-2DPAGEIPI00645078.

PTM databases

iPTMnetiP22314.
PhosphoSitePlusiP22314.
SwissPalmiP22314.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000130985.
CleanExiHS_UBA1.
ExpressionAtlasiP22314. baseline and differential.
GenevisibleiP22314. HS.

Organism-specific databases

HPAiCAB019435.
CAB073410.
HPA000289.

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. 136 interactors.
DIPiDIP-33686N.
IntActiP22314. 122 interactors.
MINTiMINT-1130980.
STRINGi9606.ENSP00000338413.

Chemistry databases

BindingDBiP22314.

Structurei

Secondary structure

11058
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi55 – 62Combined sources8
Beta strandi74 – 78Combined sources5
Helixi82 – 93Combined sources12
Beta strandi97 – 102Combined sources6
Helixi109 – 112Combined sources4
Helixi120 – 122Combined sources3
Helixi127 – 136Combined sources10
Beta strandi140 – 142Combined sources3
Beta strandi144 – 147Combined sources4
Helixi153 – 156Combined sources4
Beta strandi160 – 164Combined sources5
Helixi169 – 181Combined sources13
Beta strandi185 – 192Combined sources8
Beta strandi195 – 201Combined sources7
Beta strandi206 – 210Combined sources5
Beta strandi219 – 224Combined sources6
Beta strandi226 – 229Combined sources4
Beta strandi231 – 234Combined sources4
Beta strandi244 – 252Combined sources9
Helixi257 – 259Combined sources3
Beta strandi265 – 269Combined sources5
Beta strandi271 – 273Combined sources3
Beta strandi291 – 301Combined sources11
Helixi306 – 311Combined sources6
Helixi326 – 343Combined sources18
Helixi352 – 368Combined sources17
Turni371 – 373Combined sources3
Helixi380 – 388Combined sources9
Helixi395 – 413Combined sources19
Beta strandi422 – 428Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4P22X-ray2.75A/B1-439[»]
ProteinModelPortaliP22314.
SMRiP22314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati63 – 1991-1Add BLAST137
Repeati459 – 6111-2Add BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 6112 approximate repeatsAdd BLAST549

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi5 – 11Nuclear localization signal7

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

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiP22314.
KOiK03178.
OMAiFISCESR.
OrthoDBiEOG091G0130.
PhylomeDBiP22314.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
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.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti190D → G in CAA40296 (PubMed:1606621).Curated1
Sequence conflicti434E → Q in CAA40296 (PubMed:1606621).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043500447R → H.Corresponds to variant rs2070169dbSNPEnsembl.1
Natural variantiVAR_043501539M → I in SMAX2. 1 PublicationCorresponds to variant rs80356545dbSNPEnsembl.1
Natural variantiVAR_043502547S → G in SMAX2. 1 PublicationCorresponds to variant rs80356546dbSNPEnsembl.1
Natural variantiVAR_071121557E → V in SMAX2. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0559131 – 40Missing in isoform 2. CuratedAdd BLAST40

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_016885269.1. XM_017029780.1. [P22314-1]
XP_016885270.1. XM_017029781.1. [P22314-1]
UniGeneiHs.533273.

Genome annotation databases

EnsembliENST00000335972; ENSP00000338413; ENSG00000130985. [P22314-1]
ENST00000377351; ENSP00000366568; ENSG00000130985. [P22314-1]
GeneIDi7317.
KEGGihsa:7317.
UCSCiuc004dhj.5. 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_016885269.1. XM_017029780.1. [P22314-1]
XP_016885270.1. XM_017029781.1. [P22314-1]
UniGeneiHs.533273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4P22X-ray2.75A/B1-439[»]
ProteinModelPortaliP22314.
SMRiP22314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113165. 136 interactors.
DIPiDIP-33686N.
IntActiP22314. 122 interactors.
MINTiMINT-1130980.
STRINGi9606.ENSP00000338413.

Chemistry databases

BindingDBiP22314.
ChEMBLiCHEMBL5924.

PTM databases

iPTMnetiP22314.
PhosphoSitePlusiP22314.
SwissPalmiP22314.

Polymorphism and mutation databases

BioMutaiUBA1.
DMDMi24418865.

2D gel databases

REPRODUCTION-2DPAGEIPI00645078.

Proteomic databases

EPDiP22314.
MaxQBiP22314.
PaxDbiP22314.
PeptideAtlasiP22314.
PRIDEiP22314.

Protocols and materials databases

DNASUi7317.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335972; ENSP00000338413; ENSG00000130985. [P22314-1]
ENST00000377351; ENSP00000366568; ENSG00000130985. [P22314-1]
GeneIDi7317.
KEGGihsa:7317.
UCSCiuc004dhj.5. human. [P22314-1]

Organism-specific databases

CTDi7317.
DisGeNETi7317.
GeneCardsiUBA1.
GeneReviewsiUBA1.
HGNCiHGNC:12469. UBA1.
HPAiCAB019435.
CAB073410.
HPA000289.
MalaCardsiUBA1.
MIMi301830. phenotype.
314370. gene.
neXtProtiNX_P22314.
OpenTargetsiENSG00000130985.
Orphaneti1145. X-linked distal arthrogryposis multiplex congenita.
PharmGKBiPA37119.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiP22314.
KOiK03178.
OMAiFISCESR.
OrthoDBiEOG091G0130.
PhylomeDBiP22314.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciMetaCyc:HS05465-MONOMER.
ZFISH:HS05465-MONOMER.
BRENDAi2.3.2.B5. 2681.
6.2.1.B9. 2681.
ReactomeiR-HSA-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiP22314.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000130985.
CleanExiHS_UBA1.
ExpressionAtlasiP22314. baseline and differential.
GenevisibleiP22314. HS.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
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.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[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...

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: November 30, 2016
This is version 192 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.By similarity

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

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 one 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.