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Protein

Transitional endoplasmic reticulum ATPase

Gene

Vcp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response (By similarity). Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation. May more particularly play a role in caveolins sorting in cells. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei348ATP 1By similarity1
Binding sitei384ATP 12 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi247 – 253ATP 12 Publications7
Nucleotide bindingi521 – 526ATP 22 Publications6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processAutophagy, DNA damage, DNA repair, Transport, Ubl conjugation pathway
LigandATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-110320 Translesion Synthesis by POLH
R-MMU-3371511 HSF1 activation
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6798695 Neutrophil degranulation
R-MMU-8876725 Protein methylation

Names & Taxonomyi

Protein namesi
Recommended name:
Transitional endoplasmic reticulum ATPase (EC:3.6.4.6By similarity)
Short name:
TER ATPase
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
Short name:
VCP
Gene namesi
Name:Vcp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:99919 Vcp

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi144R → A: Loss of phospholipid-binding. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3988606

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000845732 – 806Transitional endoplasmic reticulum ATPaseAdd BLAST805

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei3PhosphoserineBy similarity1
Modified residuei7PhosphoserineBy similarity1
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei13PhosphoserineBy similarity1
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei37PhosphoserineBy similarity1
Modified residuei315N6,N6,N6-trimethyllysine; by VCPKMT1 Publication1
Modified residuei436PhosphothreonineBy similarity1
Modified residuei462PhosphoserineBy similarity1
Modified residuei502N6-acetyllysineCombined sources1
Modified residuei505N6-acetyllysineCombined sources1
Modified residuei668N6-acetyllysine; alternateCombined sources1
Modified residuei668N6-succinyllysine; alternateCombined sources1
Modified residuei702PhosphoserineBy similarity1
Modified residuei754N6-acetyllysineCombined sources1
Modified residuei770PhosphoserineCombined sources1
Modified residuei775PhosphoserineBy similarity1
Modified residuei787PhosphoserineBy similarity1
Modified residuei805PhosphotyrosineCombined sources1

Post-translational modificationi

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells.By similarity
ISGylated.1 Publication
Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ01853
MaxQBiQ01853
PaxDbiQ01853
PeptideAtlasiQ01853
PRIDEiQ01853

2D gel databases

REPRODUCTION-2DPAGEiQ01853
UCD-2DPAGEiQ01853

PTM databases

iPTMnetiQ01853
PhosphoSitePlusiQ01853
SwissPalmiQ01853

Expressioni

Gene expression databases

BgeeiENSMUSG00000028452 Expressed in 277 organ(s), highest expression level in female gonad
CleanExiMM_VCP
GenevisibleiQ01853 MM

Interactioni

Subunit structurei

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1, binding to this heterodimer inhibits Golgi-membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-terminal domain). Interacts with SPRTN; leading to recruitment to stalled replication forks. Interacts with SELENOS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXN4 and RNF19A. Interacts with CASR. Interacts with UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with WASHC5. Interacts with UBOX5. Interacts (via N- terminus) with UBXN7, UBXN8, and probably several other UBX domain-containing proteins (via UBX domains); the interactions are mutually exclusive with VIM-dependent interactions such as those with AMFR and SELENOS. Forms a complex with UBQLN1 and UBXN4 (By similarity). Interacts (via the PIM motif) with RNF31 (via the PUB domain) (By similarity). Interacts with DDX58/RIG-I and RNF125; interaction takes place when DDX58/RIG-I is ubiquitinated via'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I (By similarity). Interacts with BAG6 (By similarity). Interacts with UBXN10 (By similarity). Interacts with UBXN6; the interaction with UBXN6 is direct and competitive with UFD1 (By similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts with PLAA, UBXN6 and YOD1; may form a complex involved in macroautophagy (By similarity). Interacts with ANKZF1 (By similarity). Interacts with ubiquitin-binding protein FAF1 (By similarity). Interacts with ZFAND2B (via VIM motif); the interaction is direct (PubMed:24160817, PubMed:26337389). Interacts with ZFAND1 (via its ubiquitin-like region); this interaction occurs in an arsenite-dependent manner (By similarity).By similarity7 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi234661, 53 interactors
ComplexPortaliCPX-136 Vcp-Npl4-Ufd1 AAA ATPase complex
CPX-264 Nsfl1c-Vcp complex
CORUMiQ01853
DIPiDIP-29796N
IntActiQ01853, 40 interactors
MINTiQ01853
STRINGi10090.ENSMUSP00000030164

Chemistry databases

BindingDBiQ01853

Structurei

Secondary structure

1806
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00435
ProteinModelPortaliQ01853
SMRiQ01853
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01853

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni797 – 806Interaction with UBXN6By similarity10

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi802 – 806PIM motifBy similarity5

Domaini

The N-terminal domain shows evolutionary conservation with that of PEX1, and is able to bind phospholipids with a preference for phosphatidylinositol mono- and bisphosphates.
The PIM (PUB-interaction motif) motif mediates interaction with the PUB domain of RNF31.By similarity

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0730 Eukaryota
COG0464 LUCA
GeneTreeiENSGT00900000141071
HOVERGENiHBG001226
InParanoidiQ01853
KOiK13525
OMAiPIDDTTE
OrthoDBiEOG091G024K
PhylomeDBiQ01853
TreeFamiTF300542

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005938 AAA_ATPase_CDC48
IPR009010 Asp_de-COase-like_dom_sf
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR004201 Cdc48_dom2
IPR029067 CDC48_domain_2-like_sf
IPR003338 CDC4_N-term_subdom
IPR027417 P-loop_NTPase
IPR015415 Vps4_C
PfamiView protein in Pfam
PF00004 AAA, 2 hits
PF02933 CDC48_2, 1 hit
PF02359 CDC48_N, 1 hit
PF09336 Vps4_C, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SM01072 CDC48_2, 1 hit
SM01073 CDC48_N, 1 hit
SUPFAMiSSF50692 SSF50692, 1 hit
SSF52540 SSF52540, 2 hits
SSF54585 SSF54585, 1 hit
TIGRFAMsiTIGR01243 CDC48, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01853-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ
60 70 80 90 100
LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI
110 120 130 140 150
SIQPCPDVKY GKRIHVLPID DTVEGITGNL FEVYLKPYFL EAYRPIRKGD
160 170 180 190 200
IFLVRGGMRA VEFKVVETDP SPYCIVAPDT VIHCEGEPIK REDEEESLNE
210 220 230 240 250
VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG ILLYGPPGTG
260 270 280 290 300
KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
310 320 330 340 350
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP
360 370 380 390 400
NSIDPALRRF GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA
410 420 430 440 450
NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD
460 470 480 490 500
DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ ELVQYPVEHP
510 520 530 540 550
DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM
560 570 580 590 600
WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
610 620 630 640 650
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE
660 670 680 690 700
KSRVAILKAN LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR
710 720 730 740 750
ESIESEIRRE RERQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN
760 770 780 790 800
DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG AGPSQGSGGG TGGSVYTEDN

DDDLYG
Length:806
Mass (Da):89,322
Last modified:May 1, 2007 - v4
Checksum:i501B721D3A77BA8A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73S → Y in BAC27119 (PubMed:16141072).Curated1
Sequence conflicti199N → Y in BAE39824 (PubMed:16141072).Curated1
Sequence conflicti206I → V in CAA78412 (PubMed:1382975).Curated1
Sequence conflicti359R → Q in BAC27119 (PubMed:16141072).Curated1
Sequence conflicti439A → T in BAE40919 (PubMed:16141072).Curated1
Sequence conflicti624N → S in BAE34876 (PubMed:16141072).Curated1
Sequence conflicti684G → V in BAC25849 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14044 mRNA Translation: CAA78412.1
AK028264 mRNA Translation: BAC25849.1
AK030751 mRNA Translation: BAC27119.1
AK149931 mRNA Translation: BAE29175.1
AK151109 mRNA Translation: BAE30119.1
AK151418 mRNA Translation: BAE30383.1
AK153249 mRNA Translation: BAE31840.1
AK159177 mRNA Translation: BAE34876.1
AK159509 mRNA Translation: BAE35141.1
AK167794 mRNA Translation: BAE39824.1
AK169140 mRNA Translation: BAE40919.1
AL672276 Genomic DNA No translation available.
BC043053 mRNA Translation: AAH43053.1
BC049114 mRNA Translation: AAH49114.1
CCDSiCCDS18086.1
PIRiS25197
RefSeqiNP_033529.3, NM_009503.4
UniGeneiMm.245976
Mm.262053
Mm.469106

Genome annotation databases

EnsembliENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452
GeneIDi269523
KEGGimmu:269523
UCSCiuc008sor.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14044 mRNA Translation: CAA78412.1
AK028264 mRNA Translation: BAC25849.1
AK030751 mRNA Translation: BAC27119.1
AK149931 mRNA Translation: BAE29175.1
AK151109 mRNA Translation: BAE30119.1
AK151418 mRNA Translation: BAE30383.1
AK153249 mRNA Translation: BAE31840.1
AK159177 mRNA Translation: BAE34876.1
AK159509 mRNA Translation: BAE35141.1
AK167794 mRNA Translation: BAE39824.1
AK169140 mRNA Translation: BAE40919.1
AL672276 Genomic DNA No translation available.
BC043053 mRNA Translation: AAH43053.1
BC049114 mRNA Translation: AAH49114.1
CCDSiCCDS18086.1
PIRiS25197
RefSeqiNP_033529.3, NM_009503.4
UniGeneiMm.245976
Mm.262053
Mm.469106

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E32X-ray2.90A1-458[»]
1R7RX-ray3.60A1-806[»]
1S3SX-ray2.90A/B/C/D/E/F1-458[»]
2PJHNMR-B21-213[»]
3CF0X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N463-763[»]
3CF1X-ray4.40A/B/C1-806[»]
3CF2X-ray3.50A/B/C/D1-806[»]
3CF3X-ray4.25A/B/C1-806[»]
DisProtiDP00435
ProteinModelPortaliQ01853
SMRiQ01853
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234661, 53 interactors
ComplexPortaliCPX-136 Vcp-Npl4-Ufd1 AAA ATPase complex
CPX-264 Nsfl1c-Vcp complex
CORUMiQ01853
DIPiDIP-29796N
IntActiQ01853, 40 interactors
MINTiQ01853
STRINGi10090.ENSMUSP00000030164

Chemistry databases

BindingDBiQ01853
ChEMBLiCHEMBL3988606

PTM databases

iPTMnetiQ01853
PhosphoSitePlusiQ01853
SwissPalmiQ01853

2D gel databases

REPRODUCTION-2DPAGEiQ01853
UCD-2DPAGEiQ01853

Proteomic databases

EPDiQ01853
MaxQBiQ01853
PaxDbiQ01853
PeptideAtlasiQ01853
PRIDEiQ01853

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452
GeneIDi269523
KEGGimmu:269523
UCSCiuc008sor.2 mouse

Organism-specific databases

CTDi7415
MGIiMGI:99919 Vcp

Phylogenomic databases

eggNOGiKOG0730 Eukaryota
COG0464 LUCA
GeneTreeiENSGT00900000141071
HOVERGENiHBG001226
InParanoidiQ01853
KOiK13525
OMAiPIDDTTE
OrthoDBiEOG091G024K
PhylomeDBiQ01853
TreeFamiTF300542

Enzyme and pathway databases

ReactomeiR-MMU-110320 Translesion Synthesis by POLH
R-MMU-3371511 HSF1 activation
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6798695 Neutrophil degranulation
R-MMU-8876725 Protein methylation

Miscellaneous databases

ChiTaRSiVcp mouse
EvolutionaryTraceiQ01853
PROiPR:Q01853
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028452 Expressed in 277 organ(s), highest expression level in female gonad
CleanExiMM_VCP
GenevisibleiQ01853 MM

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005938 AAA_ATPase_CDC48
IPR009010 Asp_de-COase-like_dom_sf
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR004201 Cdc48_dom2
IPR029067 CDC48_domain_2-like_sf
IPR003338 CDC4_N-term_subdom
IPR027417 P-loop_NTPase
IPR015415 Vps4_C
PfamiView protein in Pfam
PF00004 AAA, 2 hits
PF02933 CDC48_2, 1 hit
PF02359 CDC48_N, 1 hit
PF09336 Vps4_C, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SM01072 CDC48_2, 1 hit
SM01073 CDC48_N, 1 hit
SUPFAMiSSF50692 SSF50692, 1 hit
SSF52540 SSF52540, 2 hits
SSF54585 SSF54585, 1 hit
TIGRFAMsiTIGR01243 CDC48, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiTERA_MOUSE
AccessioniPrimary (citable) accession number: Q01853
Secondary accession number(s): Q3TFH9
, Q3TIM2, Q3TXN9, Q6PI18, Q8BSR6, Q8CEG4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 1, 2007
Last modified: November 7, 2018
This is version 202 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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