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Protein

NEDD8-activating enzyme E1 catalytic subunit

Gene

UBA3

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

Functioni

Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.3 Publications

Enzyme regulationi

Binding of TP53BP2 to the regulatory subunit NAE1 decreases activity.

Pathwayi: protein neddylation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei211Determines specificity for NEDD81
Active sitei237Glycyl thioester intermediate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi100 – 124ATP1 PublicationAdd BLAST25
Nucleotide bindingi148 – 171ATP1 PublicationAdd BLAST24

GO - Molecular functioni

  • acid-amino acid ligase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • NEDD8 activating enzyme activity Source: MGI
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • cellular protein modification process Source: ProtInc
  • endomitotic cell cycle Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: Ensembl
  • NIK/NF-kappaB signaling Source: Reactome
  • protein neddylation Source: GO_Central
  • proteolysis Source: ProtInc
  • regulation of cell cycle Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07200-MONOMER.
BRENDAi2.3.2.B5. 2681.
6.2.1.B9. 2681.
ReactomeiR-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ8TBC4.
UniPathwayiUPA00885.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-activating enzyme E1 catalytic subunit (EC:6.3.2.-)
Alternative name(s):
NEDD8-activating enzyme E1C
Ubiquitin-activating enzyme E1C
Ubiquitin-like modifier-activating enzyme 3
Short name:
Ubiquitin-activating enzyme 3
Gene namesi
Name:UBA3
Synonyms:UBE1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:12470. UBA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65F → G: Reduces affinity for UBE2M. 1 Publication1
Mutagenesisi148I → A: No effect on NEDD8 adenylation. 1 Publication1
Mutagenesisi160 – 161HI → AA: Reduces affinity for UBE2M. 1 Publication2
Mutagenesisi167D → A: Abolishes NEDD8 adenylation. 1 Publication1
Mutagenesisi192P → A: Reduces affinity for UBE2M; when associated with A-195 and A-197. 1 Publication1
Mutagenesisi195I → A: Reduces affinity for UBE2M; when associated with A-192 and A-197. 1 Publication1
Mutagenesisi197P → A: Reduces affinity for UBE2M; when associated with A-192 and A-195. 1 Publication1
Mutagenesisi211R → Q: Abolishes specificity for NEDD8. 1 Publication1
Mutagenesisi214L → A: Reduces affinity for UBE2M; when associated with A-217. 1 Publication1
Mutagenesisi217M → A: Reduces affinity for UBE2M; when associated with A-214. 1 Publication1
Mutagenesisi227 – 228LY → DD: Strongly reduces NEDD8 adenylation. 1 Publication2
Mutagenesisi237C → S: Abolishes thioester intermediate formation. 1 Publication1
Mutagenesisi238T → A: No effect on NEDD8 adenylation; impairs thioester intermediate formation. 1 Publication1
Mutagenesisi310I → A: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi331I → A: Reduces affinity for UBE2M. 1 Publication1
Mutagenesisi352 – 357YTYTFE → ATATA: Abolishes NEDD8 adenylation. 1 Publication6
Mutagenesisi368S → P: Impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi369Q → P: No effect on NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi370L → P: Impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi412T → A: Impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi415L → A: Impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi418V → A: Impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi421I → A: Impairs NEDD8 transfer to UBE2M. 1 Publication1
Mutagenesisi424R → A: No effect on NEDD8 transfer to UBE2M. 1 Publication1

Organism-specific databases

DisGeNETi9039.
OpenTargetsiENSG00000144744.
PharmGKBiPA162407622.

Chemistry databases

ChEMBLiCHEMBL2016430.

Polymorphism and mutation databases

BioMutaiUBA3.
DMDMi83305811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001949412 – 463NEDD8-activating enzyme E1 catalytic subunitAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8TBC4.
MaxQBiQ8TBC4.
PaxDbiQ8TBC4.
PeptideAtlasiQ8TBC4.
PRIDEiQ8TBC4.

PTM databases

iPTMnetiQ8TBC4.
PhosphoSitePlusiQ8TBC4.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000144744.
CleanExiHS_UBA3.
ExpressionAtlasiQ8TBC4. baseline and differential.
GenevisibleiQ8TBC4. HS.

Organism-specific databases

HPAiHPA034873.
HPA034874.
HPA065335.

Interactioni

Subunit structurei

Heterodimer of UBA3 and NAE1. Interacts with NEDD8, UBE2F and UBE2M. Binds ESR1 and ESR2 with bound steroid ligand (By similarity). Interacts with TBATA (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-717567,EBI-717567
CPNE2Q96FN45EBI-717567,EBI-7097057
IMPA2O147323EBI-717567,EBI-725233
RAD23BP547272EBI-717567,EBI-954531
UBE2MP610812EBI-717567,EBI-1041660

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi114503. 33 interactors.
IntActiQ8TBC4. 14 interactors.
MINTiMINT-1375257.
STRINGi9606.ENSP00000354340.

Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni35 – 38Combined sources4
Helixi39 – 46Combined sources8
Helixi62 – 68Combined sources7
Beta strandi72 – 75Combined sources4
Helixi80 – 90Combined sources11
Beta strandi96 – 100Combined sources5
Helixi106 – 108Combined sources3
Turni109 – 111Combined sources3
Helixi117 – 119Combined sources3
Helixi124 – 135Combined sources12
Beta strandi142 – 146Combined sources5
Helixi148 – 150Combined sources3
Helixi153 – 156Combined sources4
Beta strandi160 – 164Combined sources5
Helixi169 – 181Combined sources13
Beta strandi185 – 188Combined sources4
Beta strandi189 – 191Combined sources3
Helixi192 – 194Combined sources3
Beta strandi198 – 204Combined sources7
Beta strandi207 – 213Combined sources7
Turni215 – 217Combined sources3
Helixi221 – 227Combined sources7
Helixi236 – 241Combined sources6
Helixi246 – 255Combined sources10
Helixi257 – 260Combined sources4
Helixi275 – 291Combined sources17
Helixi299 – 306Combined sources8
Helixi314 – 333Combined sources20
Beta strandi341 – 346Combined sources6
Beta strandi348 – 350Combined sources3
Beta strandi352 – 356Combined sources5
Turni365 – 367Combined sources3
Beta strandi372 – 376Combined sources5
Beta strandi377 – 379Combined sources3
Helixi382 – 391Combined sources10
Turni393 – 395Combined sources3
Beta strandi401 – 406Combined sources6
Beta strandi409 – 414Combined sources6
Helixi419 – 430Combined sources12
Beta strandi431 – 433Combined sources3
Helixi434 – 436Combined sources3
Helixi437 – 440Combined sources4
Beta strandi443 – 447Combined sources5
Beta strandi451 – 453Combined sources3
Beta strandi455 – 460Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R4MX-ray3.00B/D/F/H33-463[»]
1R4NX-ray3.60B/D/F/H33-463[»]
1TT5X-ray2.60B/D33-463[»]
1Y8XX-ray2.40B368-463[»]
1YOVX-ray2.60B/D22-463[»]
2LQ7NMR-A369-463[»]
2NVUX-ray2.80B33-463[»]
3DBHX-ray2.85B/D/F/H33-463[»]
3DBLX-ray2.90B/D/F/H33-463[»]
3DBRX-ray3.05B/D/F/H33-463[»]
3FN1X-ray2.50A368-463[»]
3GZNX-ray3.00B/D1-463[»]
ProteinModelPortaliQ8TBC4.
SMRiQ8TBC4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TBC4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 70Interaction with UBE2M N-terminusAdd BLAST18
Regioni157 – 161Interaction with UBE2M N-terminus5
Regioni192 – 217Interaction with UBE2M N-terminusAdd BLAST26
Regioni227 – 229Interaction with NEDD83
Regioni242 – 248Interaction with NAE11 Publication7
Regioni292 – 295Interaction with NAE11 Publication4
Regioni331 – 338Interaction with UBE2M N-terminus8
Regioni352 – 357Interaction with NEDD86
Regioni368 – 463Interaction with UBE2M core domainAdd BLAST96

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2015. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000074831.
HOGENOMiHOG000166793.
HOVERGENiHBG082736.
InParanoidiQ8TBC4.
KOiK10686.
OMAiNNASLQM.
OrthoDBiEOG091G0B0K.
PhylomeDBiQ8TBC4.
TreeFamiTF300499.

Family and domain databases

Gene3Di1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR014929. E2_binding.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR030468. Uba3.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PANTHERiPTHR10953:SF6. PTHR10953:SF6. 1 hit.
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM01181. E2_bind. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. 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 splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TBC4-1) [UniParc]FASTAAdd to basket

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
MADGEEPEKK RRRIEELLAE KMAVDGGCGD TGDWEGRWNH VKKFLERSGP
60 70 80 90 100
FTHPDFEPST ESLQFLLDTC KVLVIGAGGL GCELLKNLAL SGFRQIHVID
110 120 130 140 150
MDTIDVSNLN RQFLFRPKDI GRPKAEVAAE FLNDRVPNCN VVPHFNKIQD
160 170 180 190 200
FNDTFYRQFH IIVCGLDSII ARRWINGMLI SLLNYEDGVL DPSSIVPLID
210 220 230 240 250
GGTEGFKGNA RVILPGMTAC IECTLELYPP QVNFPMCTIA SMPRLPEHCI
260 270 280 290 300
EYVRMLQWPK EQPFGEGVPL DGDDPEHIQW IFQKSLERAS QYNIRGVTYR
310 320 330 340 350
LTQGVVKRII PAVASTNAVI AAVCATEVFK IATSAYIPLN NYLVFNDVDG
360 370 380 390 400
LYTYTFEAER KENCPACSQL PQNIQFSPSA KLQEVLDYLT NSASLQMKSP
410 420 430 440 450
AITATLEGKN RTLYLQSVTS IEERTRPNLS KTLKELGLVD GQELAVADVT
460
TPQTVLFKLH FTS
Length:463
Mass (Da):51,852
Last modified:December 6, 2005 - v2
Checksum:i4C16DC0EEDE31A76
GO
Isoform 2 (identifier: Q8TBC4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-21: Missing.

Show »
Length:449
Mass (Da):50,072
Checksum:iC624B0B917B2482B
GO

Sequence cautioni

The sequence AAC27648 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti146N → Y in CAB55996 (PubMed:11230166).Curated1
Sequence conflicti271D → G in CAB55996 (PubMed:11230166).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0239459K → R.2 PublicationsCorresponds to variant rs17852113dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0411278 – 21Missing in isoform 2. 1 PublicationAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL117566 mRNA. Translation: CAB55996.2.
AK002159 mRNA. Translation: BAG51021.1.
AK289392 mRNA. Translation: BAF82081.1.
AC092060 Genomic DNA. No translation available.
AC109587 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65470.1.
BC022853 mRNA. Translation: AAH22853.1.
AF046024 mRNA. Translation: AAC27648.1. Different initiation.
AB012190 mRNA. Translation: BAA33144.1.
CCDSiCCDS2909.1. [Q8TBC4-1]
CCDS2910.1. [Q8TBC4-2]
PIRiT17306.
RefSeqiNP_003959.3. NM_003968.3. [Q8TBC4-1]
NP_937838.1. NM_198195.1. [Q8TBC4-2]
UniGeneiHs.154320.

Genome annotation databases

EnsembliENST00000349511; ENSP00000340041; ENSG00000144744. [Q8TBC4-2]
ENST00000361055; ENSP00000354340; ENSG00000144744. [Q8TBC4-1]
GeneIDi9039.
KEGGihsa:9039.
UCSCiuc003dno.4. human. [Q8TBC4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL117566 mRNA. Translation: CAB55996.2.
AK002159 mRNA. Translation: BAG51021.1.
AK289392 mRNA. Translation: BAF82081.1.
AC092060 Genomic DNA. No translation available.
AC109587 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65470.1.
BC022853 mRNA. Translation: AAH22853.1.
AF046024 mRNA. Translation: AAC27648.1. Different initiation.
AB012190 mRNA. Translation: BAA33144.1.
CCDSiCCDS2909.1. [Q8TBC4-1]
CCDS2910.1. [Q8TBC4-2]
PIRiT17306.
RefSeqiNP_003959.3. NM_003968.3. [Q8TBC4-1]
NP_937838.1. NM_198195.1. [Q8TBC4-2]
UniGeneiHs.154320.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R4MX-ray3.00B/D/F/H33-463[»]
1R4NX-ray3.60B/D/F/H33-463[»]
1TT5X-ray2.60B/D33-463[»]
1Y8XX-ray2.40B368-463[»]
1YOVX-ray2.60B/D22-463[»]
2LQ7NMR-A369-463[»]
2NVUX-ray2.80B33-463[»]
3DBHX-ray2.85B/D/F/H33-463[»]
3DBLX-ray2.90B/D/F/H33-463[»]
3DBRX-ray3.05B/D/F/H33-463[»]
3FN1X-ray2.50A368-463[»]
3GZNX-ray3.00B/D1-463[»]
ProteinModelPortaliQ8TBC4.
SMRiQ8TBC4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114503. 33 interactors.
IntActiQ8TBC4. 14 interactors.
MINTiMINT-1375257.
STRINGi9606.ENSP00000354340.

Chemistry databases

ChEMBLiCHEMBL2016430.

PTM databases

iPTMnetiQ8TBC4.
PhosphoSitePlusiQ8TBC4.

Polymorphism and mutation databases

BioMutaiUBA3.
DMDMi83305811.

Proteomic databases

EPDiQ8TBC4.
MaxQBiQ8TBC4.
PaxDbiQ8TBC4.
PeptideAtlasiQ8TBC4.
PRIDEiQ8TBC4.

Protocols and materials databases

DNASUi9039.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349511; ENSP00000340041; ENSG00000144744. [Q8TBC4-2]
ENST00000361055; ENSP00000354340; ENSG00000144744. [Q8TBC4-1]
GeneIDi9039.
KEGGihsa:9039.
UCSCiuc003dno.4. human. [Q8TBC4-1]

Organism-specific databases

CTDi9039.
DisGeNETi9039.
GeneCardsiUBA3.
HGNCiHGNC:12470. UBA3.
HPAiHPA034873.
HPA034874.
HPA065335.
MIMi603172. gene.
neXtProtiNX_Q8TBC4.
OpenTargetsiENSG00000144744.
PharmGKBiPA162407622.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2015. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000074831.
HOGENOMiHOG000166793.
HOVERGENiHBG082736.
InParanoidiQ8TBC4.
KOiK10686.
OMAiNNASLQM.
OrthoDBiEOG091G0B0K.
PhylomeDBiQ8TBC4.
TreeFamiTF300499.

Enzyme and pathway databases

UniPathwayiUPA00885.
BioCyciZFISH:HS07200-MONOMER.
BRENDAi2.3.2.B5. 2681.
6.2.1.B9. 2681.
ReactomeiR-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ8TBC4.

Miscellaneous databases

ChiTaRSiUBA3. human.
EvolutionaryTraceiQ8TBC4.
GeneWikiiUBE1C.
GenomeRNAii9039.
PROiQ8TBC4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000144744.
CleanExiHS_UBA3.
ExpressionAtlasiQ8TBC4. baseline and differential.
GenevisibleiQ8TBC4. HS.

Family and domain databases

Gene3Di1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR014929. E2_binding.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR030468. Uba3.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PANTHERiPTHR10953:SF6. PTHR10953:SF6. 1 hit.
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM01181. E2_bind. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBA3_HUMAN
AccessioniPrimary (citable) accession number: Q8TBC4
Secondary accession number(s): A6NLB5
, A8K027, O76088, Q9NTU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 6, 2005
Last modified: November 30, 2016
This is version 153 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

Arg-211 acts as a selectivity gate, preventing misactivation of ubiquitin by this NEDD8-specific E1 complex.

Keywords - Technical termi

3D-structure, Complete proteome, 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. 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.