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Protein

Roquin-1

Gene

Rc3h1

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

Functioni

Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF, TNFRSF4 and in many more mRNAs (PubMed:23663784, PubMed:25026077, PubMed:18172933). Cleaves translationally inactive mRNAs harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-independent manner (PubMed:26000482). Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (PubMed:20412057, PubMed:20639877). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4/Ox40 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (PubMed:23583642, PubMed:23583643, PubMed:15917799). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (PubMed:25282160). Recognizes and binds mRNAs containing an hexaloop stem-loop motif, called alternative decay element (ADE) (PubMed:27010430). Able to interact with double-stranded RNA (By similarity). miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression (PubMed:25697406). Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2A, UBE2B, UBE2D2, UBE2F, UBE2G1, UBE2G2 and UBE2L3 and produces polyubiquitin chains. Show the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains (By similarity).By similarity12 Publications

Miscellaneous

Treatment of C57BL/6 males with ethylnitrosourea led to the identification of the sanroque mouse strain. The causative mutation in sanroque appears to be RC3H1 Arg-199. Homozygous sanroque mice develop high titers of autoantibodies and display excessive numbers of follicular helper T-cells and germinal centers with pattern of pathology consistent with lupus (PubMed:15917799). Sanroque mice reproducibly develop intestinal inflammation in the small intestine but not the colon. Extensive cytokine dysregulation resulting in both over-expression and under-expression of chemotactic cytokines occurs in the ileum, the region most prone to the development of inflammation in sanroque mice (PubMed:23451046). They show up-regulation of expression of at least 15 miRNAs in T cells (PubMed:25697406). The lack of compensation of RC3H1 defects by the RC3H2 paralog in sanroque mice may be due to the fact that the mutated protein may retain its scaffolding position within RNA granules, preventing RC3H2 to access mRNAs to be regulated (PubMed:23583642).3 Publications1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarity
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
Metal bindingi14Zinc 1Combined sources1 Publication1
Metal bindingi17Zinc 1Combined sources1 Publication1
Metal bindingi33Zinc 2Combined sources1 Publication1
Metal bindingi35Zinc 2; via pros nitrogenCombined sources1 Publication1
Metal bindingi38Zinc 1Combined sources1 Publication1
Metal bindingi50Zinc 2Combined sources1 Publication1
Metal bindingi53Zinc 2Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri14 – 54RING-type; degeneratePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri413 – 441C3H1-typePROSITE-ProRule annotationAdd BLAST29

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRepressor, RNA-binding, Transferase
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
Roquin-1Curated (EC:2.3.2.27By similarity)
Short name:
RoquinCurated
Alternative name(s):
Protein Sanroque1 Publication
RING finger and C3H zinc finger protein 1
RING finger and CCCH-type zinc finger domain-containing protein 1
Gene namesi
Name:Rc3h1Imported
Synonyms:Gm551, Kiaa2025
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2685397 Rc3h1

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mutant animals are born at Mendelian ratio, but die within 6 hours after birth. They displayed a curly tail and malformations of the caudal spinal column. Lethality can be rescued by changing the genetic background from C57BL/6 to outbred CD1, which allows about 4% of the animals to survive to adulthood. These animals display enlarged spleens with a trend toward increased numbers of eosinophils and monocytic/macrophage populations, dramatic and selective expansion of CD8+ effector-like T-cells. Splenic follicular organization is normal, and the numbers of CD4+ T-cell subtypes and B-cells are not significantly altered. No spontaneous germinal center formation, autoantibody production, nor autoimmune tissue damage. Ablation of Rc3h1 gene in the T lineage leads to elevated ICOS levels and expansion of effector CD8+ T-cells, but not autoimmunity (PubMed:21844204). Mice lacking both Rc3h1 and Rc3h2 genes in CD4+ T-cells develop lymphadenopathy and splenomegaly with increased spleen weight and cellularity, already at young age. They show a prominent lung pathology with a progressive reduction in the alveolar space concomitant with inflammation. They show an average survival of 130 days. CD4+ T-cells of these mutants show a pronounced bias toward Th17 differentiation (PubMed:21844204, PubMed:23583643).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14C → A: No effect on localization to stress granules. 1 Publication1
Mutagenesisi188R → A: No effect on CDE RNA-binding. 1 Publication1
Mutagenesisi199M → R in sanroque; partial loss of ICOS regulation, no effect on localization to stress granules, no effect on RNA-binding. 4 Publications1
Mutagenesisi219R → A: No effect on CDE RNA-binding. 1 Publication1
Mutagenesisi220K → A: Strongly decreases CDE and ADE RNA-binding. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-239 and A-260. 3 Publications1
Mutagenesisi229R → A: No effect on CDE RNA-binding. 2 Publications1
Mutagenesisi233R → A: No effect on CDE RNA-binding. 1 Publication1
Mutagenesisi238S → A: Decreases CDE RNA-binding. 1 Publication1
Mutagenesisi239K → A: Strongly decresases CDE and ADE RNA-binding. Increases target-mRNA expression. Abolishes CDE RNA-binding and highly increases target-mRNA expression; when associated with A-260. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-220 and A-260. 3 Publications1
Mutagenesisi250Y → A: Decreases CDE RNA-binding. Increases target-mRNA expression. 2 Publications1
Mutagenesisi251R → A: No effect on CDE RNA-binding. 1 Publication1
Mutagenesisi253S → A: Slightly decresases CDE and ADE RNA-binding. 2 Publications1
Mutagenesisi259K → A: Strongly decresases CDE and ADE RNA-binding. 2 Publications1
Mutagenesisi260R → A: Strongly decresases CDE and ADE RNA-binding. Increases target-mRNA expression. Abolishes CDE RNA-binding and highly increases target-mRNA expression; when associated with A-239. Increases target-mRNA expression. Increases ICOS surface expression; when associated with A-220 and A-239. 3 Publications1
Mutagenesisi264S → A: Decreases CDE RNA-binding. 1 Publication1
Mutagenesisi265S → Y: Decresases CDE and ADE RNA-binding. 2 Publications1
Mutagenesisi293E → A: No effect on CDE RNA-binding. 1 Publication1
Mutagenesisi314K → A: No effect on CDE RNA-binding. 1 Publication1
Mutagenesisi419C → R: No effect on RNA-binding. 1 Publication1
Mutagenesisi434C → R: No effect on localization to stress granules, reduces RNA-binding. 1
Mutagenesisi488R → G: No effect on cleavage. 1 Publication1
Mutagenesisi510R → G: Abolishes the formation of a preferential cleavage product. Abolishes protein cleavage; when associated with G-579. 1 Publication1
Mutagenesisi560R → G: No effect on cleavage. 1 Publication1
Mutagenesisi579R → G: Abolishes the formation of an alternative cleavage product. Abolishes protein cleavage; when associated with G-510. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000559661 – 1130Roquin-1Add BLAST1130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei462PhosphoserineBy similarity1
Modified residuei531PhosphoserineCombined sources1
Modified residuei535PhosphoserineCombined sources1
Modified residuei861PhosphoserineBy similarity1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1110PhosphoserineCombined sources1

Post-translational modificationi

Proteolytically cleaved after Arg-510 and Arg-579 by MALT1 in activated CD4+ T cells; cleavage at Arg-510 and Arg-579 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei510Cleavage; by MALT11 Publication1
Sitei579Cleavage; by MALT11 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ4VGL6
MaxQBiQ4VGL6
PaxDbiQ4VGL6
PRIDEiQ4VGL6

PTM databases

iPTMnetiQ4VGL6
PhosphoSitePlusiQ4VGL6

Expressioni

Tissue specificityi

Widely expressed, with highest levels in lymph node and thymus and slightly lesser amounts in brain, lung, and spleen (at protein level). Very weak expression in heart, muscle, and kidney (at protein level). Expressed in CD4+ helper T-cells (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000040423 Expressed in 243 organ(s), highest expression level in mesenteric lymph node
CleanExiMM_RC3H1
ExpressionAtlasiQ4VGL6 baseline and differential
GenevisibleiQ4VGL6 MM

Interactioni

Subunit structurei

Interacts with DDX6 and EDC4 (PubMed:20639877, PubMed:23583643). Interacts with CCR4-NOT deadenylase complex (PubMed:23663784). Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406).4 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi237867, 5 interactors
IntActiQ4VGL6, 54 interactors
MINTiQ4VGL6
STRINGi10090.ENSMUSP00000124871

Structurei

Secondary structure

11130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ4VGL6
SMRiQ4VGL6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni128 – 176HEPN-N1 PublicationAdd BLAST49
Regioni177 – 326ROQ1 PublicationAdd BLAST150
Regioni327 – 399HEPN-C1 PublicationAdd BLAST73

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi533 – 786Pro-richAdd BLAST254

Domaini

The ROQ region is required for CDE RNA-binding (PubMed:27010430, PubMed:25026077, PubMed:23663784). Has 2 separate RNA-binding sites, one for CDE RNA and the other for dsRNA, both sites are important for mRNA decay (By similarity). ADE RNA-binding involves an extended binding surface on the ROQ region with a number of additional residues compared with the CDE RNA (PubMed:27010430). It may also be involved in localization to stress granules (PubMed:20412057, PubMed:23583642).By similarity5 Publications
The RING-type zinc finger may be required for proper localization to stress granules, but not to P-bodies.1 Publication
HEPN (higher eukaryotes and prokaryotes nucleotide-binding) are observed in both N- and C-terminal sides of ROQ domain with 3D structure even if they are poredcted on the basis of sequence.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri14 – 54RING-type; degeneratePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri413 – 441C3H1-typePROSITE-ProRule annotationAdd BLAST29

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG3161 Eukaryota
ENOG410YWQD LUCA
GeneTreeiENSGT00390000004311
HOGENOMiHOG000232030
HOVERGENiHBG080524
InParanoidiQ4VGL6
KOiK15690
OrthoDBiEOG091G02I2
PhylomeDBiQ4VGL6
TreeFamiTF317698

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR032671 RC3H1
IPR027370 Znf-RING_LisH
IPR000571 Znf_CCCH
IPR036855 Znf_CCCH_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR13139:SF6 PTHR13139:SF6, 1 hit
PfamiView protein in Pfam
PF00642 zf-CCCH, 1 hit
PF13445 zf-RING_UBOX, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
SM00356 ZnF_C3H1, 1 hit
SUPFAMiSSF90229 SSF90229, 1 hit
PROSITEiView protein in PROSITE
PS50103 ZF_C3H1, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q4VGL6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC
60 70 80 90 100
PFDQTTINTD IELLPVNSAL LQLVGAQIPE QQPITLCSGV EDTKHYEEAK
110 120 130 140 150
KCVEELALYL KPLSSARGVG LNSTTQSVLS RPMQRKLVTL VHCQLVEEEG
160 170 180 190 200
RIRAMRAARS LGERTVTELI LQHQNPQQLS SNLWAAVRAR GCQFLGPAMQ
210 220 230 240 250
EEALKLVLLA LEDGSALSRK VLVLFVVQRL EPRFPQASKT SIGHVVQLLY
260 270 280 290 300
RASCFKVTKR DEDSSLMQLK EEFRTYEALR REHDSQIVQI AMEAGLRIAP
310 320 330 340 350
DQWSSLLYGD QSHKSHMQSI IDKLQTPASF AQSVQELTIA LQRTGDPANL
360 370 380 390 400
NRLRPHLELL ANIDPSPDAP PPTWEQLENG LVAVRTVVHG LVDYIQNHSK
410 420 430 440 450
KGADQQQPPQ HSKYKTYMCR DMKQRGGCPR GASCTFAHSQ EELEKFRKMN
460 470 480 490 500
KRLVPRRPLS ASLGQLNEVG LPSAPILSDE SAVDLSNRKP PALPNGIASS
510 520 530 540 550
GSTVTQLIPR GTDPSFDSSL KPVKLDHLSS SAPGSPPDLL ESAPKSISAL
560 570 580 590 600
PVNPHPVPPR GPTDLPPMPV TKPIQMVPRG SQLYPAQQAD VYYQDPRGSA
610 620 630 640 650
PAFETAPYQQ GMYYTPPPCV SRFVRPPPSA PEPGPPYLDH YSPYLQDRVI
660 670 680 690 700
NSQYGTQPQQ YPPMYPAHYD GRRVYPAQSY TREEMFRESP IPIDIPSAAV
710 720 730 740 750
PSYVPESRER YQQVEGYYPV APHPAQIRPS YPRDPPYSRL PPPQPHPSLD
760 770 780 790 800
ELHRRRKEIM AQLEERKVIS PPPFAPSPTL PPAFHPEEFL DEDLKVAGKY
810 820 830 840 850
KANDYSQYSP WSCDTIGSYI GTKDAKPKDV VAAGSVEMMN VESKGTREQR
860 870 880 890 900
LDLQRRAVET SDDDLIPFGD RPTVSRFGAI SRTSKTLYQG AGPLQAIAPQ
910 920 930 940 950
GAPTKSINIS DYSAYGAHGG WGDSPYSPHA NIPPQGHFIE REKMSMAEVA
960 970 980 990 1000
SHGKPLLSAE REQLRLELQQ LNHQISQQTQ LRGLEAVSNR LVLQREVNTL
1010 1020 1030 1040 1050
ASQPQPPQLP PKWPGMISSE QLSLELHQVE REIGKRTREL SMENQCSVDM
1060 1070 1080 1090 1100
KSKLGTSKQA ENGQPEPQNK IRTEDLTLTF SDVPNGSALT QENLSLLSNK
1110 1120 1130
TSSLNLSEDS EGGGDNNDSQ RSGVVSNSAP
Length:1,130
Mass (Da):125,378
Last modified:July 5, 2005 - v1
Checksum:i5B750E5D28FC86F2
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7BX02H7BX02_MOUSE
Roquin-1
Rc3h1
1,121Annotation score:

Sequence cautioni

The sequence BAD32613 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY948287 mRNA Translation: AAY16368.1
AK173335 mRNA Translation: BAD32613.1 Different initiation.
BC138663 mRNA Translation: AAI38664.1
CCDSiCCDS15410.1
RefSeqiNP_001020123.1, NM_001024952.2
UniGeneiMm.329667

Genome annotation databases

EnsembliENSMUST00000161609; ENSMUSP00000124871; ENSMUSG00000040423
GeneIDi381305
KEGGimmu:381305
UCSCiuc007del.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY948287 mRNA Translation: AAY16368.1
AK173335 mRNA Translation: BAD32613.1 Different initiation.
BC138663 mRNA Translation: AAI38664.1
CCDSiCCDS15410.1
RefSeqiNP_001020123.1, NM_001024952.2
UniGeneiMm.329667

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QI0X-ray1.94A/B147-326[»]
4QI2X-ray3.00A/B/C/D147-326[»]
4TXAX-ray2.75A1-484[»]
5F5FX-ray3.00A/C/E/G171-360[»]
5F5HX-ray2.23A/B147-326[»]
ProteinModelPortaliQ4VGL6
SMRiQ4VGL6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237867, 5 interactors
IntActiQ4VGL6, 54 interactors
MINTiQ4VGL6
STRINGi10090.ENSMUSP00000124871

PTM databases

iPTMnetiQ4VGL6
PhosphoSitePlusiQ4VGL6

Proteomic databases

EPDiQ4VGL6
MaxQBiQ4VGL6
PaxDbiQ4VGL6
PRIDEiQ4VGL6

Protocols and materials databases

DNASUi381305
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000161609; ENSMUSP00000124871; ENSMUSG00000040423
GeneIDi381305
KEGGimmu:381305
UCSCiuc007del.2 mouse

Organism-specific databases

CTDi149041
MGIiMGI:2685397 Rc3h1
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3161 Eukaryota
ENOG410YWQD LUCA
GeneTreeiENSGT00390000004311
HOGENOMiHOG000232030
HOVERGENiHBG080524
InParanoidiQ4VGL6
KOiK15690
OrthoDBiEOG091G02I2
PhylomeDBiQ4VGL6
TreeFamiTF317698

Enzyme and pathway databases

UniPathwayi
UPA00143

Miscellaneous databases

PROiPR:Q4VGL6
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000040423 Expressed in 243 organ(s), highest expression level in mesenteric lymph node
CleanExiMM_RC3H1
ExpressionAtlasiQ4VGL6 baseline and differential
GenevisibleiQ4VGL6 MM

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR032671 RC3H1
IPR027370 Znf-RING_LisH
IPR000571 Znf_CCCH
IPR036855 Znf_CCCH_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR13139:SF6 PTHR13139:SF6, 1 hit
PfamiView protein in Pfam
PF00642 zf-CCCH, 1 hit
PF13445 zf-RING_UBOX, 1 hit
SMARTiView protein in SMART
SM00184 RING, 1 hit
SM00356 ZnF_C3H1, 1 hit
SUPFAMiSSF90229 SSF90229, 1 hit
PROSITEiView protein in PROSITE
PS50103 ZF_C3H1, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRC3H1_MOUSE
AccessioniPrimary (citable) accession number: Q4VGL6
Secondary accession number(s): B2RS13, Q69Z31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2005
Last modified: November 7, 2018
This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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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