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Q13114

- TRAF3_HUMAN

UniProt

Q13114 - TRAF3_HUMAN

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Protein

TNF receptor-associated factor 3

Gene

TRAF3

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

Functioni

Regulates pathways leading to the activation of NF-kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-linked ubiquitination of target proteins. Inhibits activation of NF-kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa-B. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri68 – 7710RING-typePROSITE-ProRule annotation
Zinc fingeri135 – 19056TRAF-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri191 – 24959TRAF-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. signal transducer activity Source: ProtInc
  3. thioesterase binding Source: UniProtKB
  4. tumor necrosis factor receptor binding Source: UniProt
  5. ubiquitin protein ligase binding Source: UniProtKB
  6. ubiquitin-protein transferase activity Source: InterPro
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. innate immune response Source: Reactome
  3. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  4. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  5. negative regulation of type I interferon production Source: Reactome
  6. regulation of apoptotic process Source: InterPro
  7. regulation of cytokine production Source: UniProtKB
  8. regulation of defense response to virus Source: UniProtKB
  9. regulation of interferon-beta production Source: UniProtKB
  10. regulation of proteolysis Source: UniProtKB
  11. signal transduction Source: ProtInc
  12. toll-like receptor 3 signaling pathway Source: Reactome
  13. toll-like receptor 4 signaling pathway Source: Reactome
  14. toll-like receptor signaling pathway Source: UniProtKB
  15. Toll signaling pathway Source: InterPro
  16. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  17. tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_25026. TRAF3-dependent IRF activation pathway.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ13114.

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 3 (EC:6.3.2.-)
Alternative name(s):
CAP-1
CD40 receptor-associated factor 1
Short name:
CRAF1
CD40-binding protein
Short name:
CD40BP
LMP1-associated protein 1
Short name:
LAP1
Gene namesi
Name:TRAF3
Synonyms:CAP1, CRAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:12033. TRAF3.

Subcellular locationi

Cytoplasm Curated. Endosome By similarity. Mitochondrion
Note: Undergoes endocytosis together with TLR4 upon LPS signaling By similarity. Associated with mitochondria in response to virus.By similarity

GO - Cellular componenti

  1. CD40 receptor complex Source: BHF-UCL
  2. cytoplasmic side of plasma membrane Source: BHF-UCL
  3. cytosol Source: Reactome
  4. endosome Source: UniProtKB-KW
  5. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Herpes simplex encephalitis 3 (HSE3) [MIM:614849]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181R → W in HSE3. 1 Publication
VAR_069081

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi441 – 4411Y → A: Abolishes interaction with RNF216; when associated with A-443. 1 Publication
Mutagenesisi443 – 4431Q → A: Abolishes interaction with RNF216; when associated with A-441. 1 Publication
Mutagenesisi459 – 4591Y → A: Abolishes interaction with LTBR, CD40 and TANK. 1 Publication
Mutagenesisi512 – 5121F → E: Abolishes interaction with LTBR, CD40 and TANK. 1 Publication
Mutagenesisi521 – 5211F → A: Abolishes interaction with LTBR, CD40 and TANK. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614849. phenotype.
Orphaneti1930. Herpetic encephalitis.
PharmGKBiPA36710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568TNF receptor-associated factor 3PRO_0000056401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki107 – 107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki156 – 156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Undergoes 'Lys-48'-linked polyubiquitination, leading to its proteasomal degradation in response to signaling by TNFSF13B, TLR4 or through CD40. 'Lys-48'-linked polyubiquitinated form is deubiquitinated by OTUD7B, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Undergoes 'Lys-63'-linked ubiquitination during early stages of virus infection, and 'Lys-48'-linked ubiquitination during later stages. Undergoes both 'Lys-48'-linked and 'Lys-63'-linked ubiquitination in response to TLR3 and TLR4 signaling. Deubiquitinated by OTUB1, OTUB2 and OTUD5.5 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ13114.
PaxDbiQ13114.
PRIDEiQ13114.

PTM databases

PhosphoSiteiQ13114.

Miscellaneous databases

PMAP-CutDBQ13114.

Expressioni

Gene expression databases

BgeeiQ13114.
CleanExiHS_CAP1.
HS_TRAF3.
ExpressionAtlasiQ13114. baseline and differential.
GenevestigatoriQ13114.

Organism-specific databases

HPAiHPA002933.

Interactioni

Subunit structurei

Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts with LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14, TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and TRAF3IP1. Interaction with TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the same binding site. Interacts with TICAM1. Interacts with TRAFD1. Interacts with OTUB1, OTUB2 and OTUD5. Interacts with RNF216, MAVS, OPTN and TBK1. Identified in a complex with TRAF2, MAP3K14 and BIRC3. Interacts with BIRC2 and BIRC3. Upon exposure to bacterial lipopolysaccharide (LPS), recruited to a transient complex containing TLR4, TRAF3, TRAF6, IKBKG, MAP3K7, MYD88, TICAM1, BIRC2, BIRC3 and UBE2N By similarity. Interacts with Epstein-Barr virus protein LMP1. Interacts (via RING-type zinc finger domain) with SRC. Interacts with CARD14.By similarity35 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Azi2Q9QYP62EBI-357631,EBI-6115874From a different organism.
BRAFP150562EBI-357631,EBI-365980
CD40P259423EBI-357631,EBI-525714
Irf1P153142EBI-357631,EBI-6115486From a different organism.
RIPK2O433535EBI-357631,EBI-358522
TANKQ928444EBI-357631,EBI-356349
TRAF3IP1Q8TDR08EBI-357631,EBI-928811
Zbp1A2APF72EBI-357631,EBI-6115394From a different organism.
ZMYND11Q153262EBI-357631,EBI-2623509

Protein-protein interaction databases

BioGridi113039. 103 interactions.
DIPiDIP-6222N.
IntActiQ13114. 32 interactions.
MINTiMINT-1144408.
STRINGi9606.ENSP00000332468.

Structurei

Secondary structure

1
568
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni54 – 563
Beta strandi59 – 624
Beta strandi67 – 693
Helixi74 – 818
Turni89 – 913
Turni97 – 993
Turni365 – 3739
Turni375 – 3773
Helixi378 – 41033
Beta strandi415 – 4239
Helixi425 – 4339
Beta strandi438 – 4414
Beta strandi445 – 4484
Beta strandi453 – 4597
Helixi464 – 4663
Turni467 – 4693
Beta strandi470 – 4789
Helixi483 – 4853
Beta strandi494 – 4985
Beta strandi502 – 5043
Beta strandi508 – 5125
Beta strandi521 – 5233
Beta strandi525 – 5284
Beta strandi532 – 5398
Helixi540 – 5456
Beta strandi553 – 5608
Beta strandi563 – 5653

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FLKX-ray2.80A/B341-568[»]
1FLLX-ray3.50A/B341-568[»]
1KZZX-ray3.50A377-568[»]
1L0AX-ray2.90A377-568[»]
1RF3X-ray3.50A377-568[»]
1ZMSX-ray2.80A377-568[»]
2ECYNMR-A43-101[»]
2GKWX-ray2.70A377-568[»]
ProteinModelPortaliQ13114.
SMRiQ13114. Positions 38-198, 263-297, 364-568.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 560146MATHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili267 – 33872Sequence AnalysisAdd
BLAST

Domaini

The MATH/TRAF domain binds to receptor cytoplasmic domains.
The Ring-type zinc finger domain is required for its function in down-regulation of NFKB2 proteolytic processing.By similarity

Sequence similaritiesi

Contains 1 MATH domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 2 TRAF-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri68 – 7710RING-typePROSITE-ProRule annotation
Zinc fingeri135 – 19056TRAF-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri191 – 24959TRAF-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG239194.
GeneTreeiENSGT00550000074359.
HOVERGENiHBG058222.
InParanoidiQ13114.
KOiK03174.
OMAiYGCTFQG.
OrthoDBiEOG7966G5.
PhylomeDBiQ13114.
TreeFamiTF321154.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProiIPR002083. MATH.
IPR013323. SIAH-type.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027128. TRAF3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF72. PTHR10131:SF72. 1 hit.
PfamiPF00917. MATH. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 3 hits.
PROSITEiPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13114-1) [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
MESSKKMDSP GALQTNPPLK LHTDRSAGTP VFVPEQGGYK EKFVKTVEDK
60 70 80 90 100
YKCEKCHLVL CSPKQTECGH RFCESCMAAL LSSSSPKCTA CQESIVKDKV
110 120 130 140 150
FKDNCCKREI LALQIYCRNE SRGCAEQLML GHLLVHLKND CHFEELPCVR
160 170 180 190 200
PDCKEKVLRK DLRDHVEKAC KYREATCSHC KSQVPMIALQ KHEDTDCPCV
210 220 230 240 250
VVSCPHKCSV QTLLRSELSA HLSECVNAPS TCSFKRYGCV FQGTNQQIKA
260 270 280 290 300
HEASSAVQHV NLLKEWSNSL EKKVSLLQNE SVEKNKSIQS LHNQICSFEI
310 320 330 340 350
EIERQKEMLR NNESKILHLQ RVIDSQAEKL KELDKEIRPF RQNWEEADSM
360 370 380 390 400
KSSVESLQNR VTELESVDKS AGQVARNTGL LESQLSRHDQ MLSVHDIRLA
410 420 430 440 450
DMDLRFQVLE TASYNGVLIW KIRDYKRRKQ EAVMGKTLSL YSQPFYTGYF
460 470 480 490 500
GYKMCARVYL NGDGMGKGTH LSLFFVIMRG EYDALLPWPF KQKVTLMLMD
510 520 530 540 550
QGSSRRHLGD AFKPDPNSSS FKKPTGEMNI ASGCPVFVAQ TVLENGTYIK
560
DDTIFIKVIV DTSDLPDP
Length:568
Mass (Da):64,490
Last modified:October 17, 2006 - v2
Checksum:i9456E440C0A90FBF
GO
Isoform 2 (identifier: Q13114-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-273: Missing.

Show »
Length:485
Mass (Da):55,306
Checksum:i1280A3E1B054768D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341Missing in AAA56753. (PubMed:7533327)Curated
Sequence conflicti158 – 1581L → F in BAH13910. (PubMed:14702039)Curated
Sequence conflicti218 – 24225Missing in AAA68195. (PubMed:7530216)CuratedAdd
BLAST
Sequence conflicti339 – 3391P → S in AAA68195. (PubMed:7530216)Curated
Sequence conflicti405 – 4051R → G in AAA56753. (PubMed:7533327)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181R → W in HSE3. 1 Publication
VAR_069081
Natural varianti129 – 1291M → T.2 Publications
Corresponds to variant rs1131877 [ dbSNP | Ensembl ].
VAR_052149

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei191 – 27383Missing in isoform 2. 1 PublicationVSP_040040Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U15637 mRNA. Translation: AAA56753.1.
U19260 mRNA. Translation: AAA65732.1.
L38509 mRNA. Translation: AAA68195.1.
U21092 mRNA. Translation: AAC50112.1.
BX247977 mRNA. Translation: CAD62311.1.
AK303172 mRNA. Translation: BAH13910.1.
AL117209 Genomic DNA. No translation available.
BC075087 mRNA. Translation: AAH75087.1.
BC075086 mRNA. Translation: AAH75086.1.
AF110908 mRNA. Translation: AAD29276.1.
CCDSiCCDS55946.1. [Q13114-2]
CCDS9975.1. [Q13114-1]
PIRiA55960.
S68467.
RefSeqiNP_001186356.1. NM_001199427.1. [Q13114-2]
NP_003291.2. NM_003300.3. [Q13114-1]
NP_663777.1. NM_145725.2. [Q13114-1]
NP_663778.1. NM_145726.2.
UniGeneiHs.510528.

Genome annotation databases

EnsembliENST00000392745; ENSP00000376500; ENSG00000131323. [Q13114-1]
ENST00000539721; ENSP00000445998; ENSG00000131323. [Q13114-2]
ENST00000560371; ENSP00000454207; ENSG00000131323. [Q13114-1]
GeneIDi7187.
KEGGihsa:7187.
UCSCiuc001ymc.2. human. [Q13114-1]
uc010txy.2. human. [Q13114-2]

Polymorphism databases

DMDMi116242824.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U15637 mRNA. Translation: AAA56753.1 .
U19260 mRNA. Translation: AAA65732.1 .
L38509 mRNA. Translation: AAA68195.1 .
U21092 mRNA. Translation: AAC50112.1 .
BX247977 mRNA. Translation: CAD62311.1 .
AK303172 mRNA. Translation: BAH13910.1 .
AL117209 Genomic DNA. No translation available.
BC075087 mRNA. Translation: AAH75087.1 .
BC075086 mRNA. Translation: AAH75086.1 .
AF110908 mRNA. Translation: AAD29276.1 .
CCDSi CCDS55946.1. [Q13114-2 ]
CCDS9975.1. [Q13114-1 ]
PIRi A55960.
S68467.
RefSeqi NP_001186356.1. NM_001199427.1. [Q13114-2 ]
NP_003291.2. NM_003300.3. [Q13114-1 ]
NP_663777.1. NM_145725.2. [Q13114-1 ]
NP_663778.1. NM_145726.2.
UniGenei Hs.510528.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FLK X-ray 2.80 A/B 341-568 [» ]
1FLL X-ray 3.50 A/B 341-568 [» ]
1KZZ X-ray 3.50 A 377-568 [» ]
1L0A X-ray 2.90 A 377-568 [» ]
1RF3 X-ray 3.50 A 377-568 [» ]
1ZMS X-ray 2.80 A 377-568 [» ]
2ECY NMR - A 43-101 [» ]
2GKW X-ray 2.70 A 377-568 [» ]
ProteinModelPortali Q13114.
SMRi Q13114. Positions 38-198, 263-297, 364-568.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113039. 103 interactions.
DIPi DIP-6222N.
IntActi Q13114. 32 interactions.
MINTi MINT-1144408.
STRINGi 9606.ENSP00000332468.

PTM databases

PhosphoSitei Q13114.

Polymorphism databases

DMDMi 116242824.

Proteomic databases

MaxQBi Q13114.
PaxDbi Q13114.
PRIDEi Q13114.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392745 ; ENSP00000376500 ; ENSG00000131323 . [Q13114-1 ]
ENST00000539721 ; ENSP00000445998 ; ENSG00000131323 . [Q13114-2 ]
ENST00000560371 ; ENSP00000454207 ; ENSG00000131323 . [Q13114-1 ]
GeneIDi 7187.
KEGGi hsa:7187.
UCSCi uc001ymc.2. human. [Q13114-1 ]
uc010txy.2. human. [Q13114-2 ]

Organism-specific databases

CTDi 7187.
GeneCardsi GC14P103243.
HGNCi HGNC:12033. TRAF3.
HPAi HPA002933.
MIMi 601896. gene.
614849. phenotype.
neXtProti NX_Q13114.
Orphaneti 1930. Herpetic encephalitis.
PharmGKBi PA36710.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239194.
GeneTreei ENSGT00550000074359.
HOVERGENi HBG058222.
InParanoidi Q13114.
KOi K03174.
OMAi YGCTFQG.
OrthoDBi EOG7966G5.
PhylomeDBi Q13114.
TreeFami TF321154.

Enzyme and pathway databases

Reactomei REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
SignaLinki Q13114.

Miscellaneous databases

ChiTaRSi TRAF3. human.
EvolutionaryTracei Q13114.
GeneWikii TRAF3.
GenomeRNAii 7187.
NextBioi 28176.
PMAP-CutDB Q13114.
PROi Q13114.
SOURCEi Search...

Gene expression databases

Bgeei Q13114.
CleanExi HS_CAP1.
HS_TRAF3.
ExpressionAtlasi Q13114. baseline and differential.
Genevestigatori Q13114.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProi IPR002083. MATH.
IPR013323. SIAH-type.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027128. TRAF3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view ]
PANTHERi PTHR10131:SF72. PTHR10131:SF72. 1 hit.
Pfami PF00917. MATH. 1 hit.
[Graphical view ]
PIRSFi PIRSF015614. TRAF. 1 hit.
SMARTi SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 3 hits.
PROSITEi PS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel RING finger protein interacts with the cytoplasmic domain of CD40."
    Hu H.M., O'Rourke K., Boguski M.S., Dixit V.M.
    J. Biol. Chem. 269:30069-30072(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5.
  2. "The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family."
    Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C., Kieff E.
    Cell 80:389-399(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, INTERACTION WITH EBV LMP-1.
    Tissue: Lymphoma.
  3. "A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40."
    Sato T., Irie S., Reed J.C.
    FEBS Lett. 358:113-118(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5, VARIANT THR-129.
    Tissue: Fetal brain.
  4. "Involvement of CRAF1, a relative of TRAF, in CD40 signaling."
    Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.
    Science 267:1494-1498(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5, VARIANT THR-129.
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thymus.
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  9. "A single gene for human TRAF-3 at chromosome 14q32.3 encodes a variety of mRNA species by alternative polyadenylation, mRNA splicing and transcription initiation."
    van Eyndhoven W.G., Frank D., Kalachikov S., Cleary A.M., Hong D.I., Cho E., Nasr S., Perez A.J., Mackus W.J.M., Cayanis E., Wellington S., Fischer S.G., Warburton D., Lederman S.
    Mol. Immunol. 35:1189-1206(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 536-568.
  10. "TRAF5, an activator of NF-kappaB and putative signal transducer for the lymphotoxin-beta receptor."
    Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H., Okumura K.
    J. Biol. Chem. 271:14661-14664(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LTBR.
  11. "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction."
    Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.
    Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TANK.
  12. "Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other members of the TNF receptor superfamily."
    Boucher L.-M., Marengere L.E., Lu Y., Thukral S., Mak T.W.
    Biochem. Biophys. Res. Commun. 233:592-600(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF8.
  13. "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1."
    Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.
    J. Biol. Chem. 272:14029-14032(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF14.
  14. "Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2."
    Song H.Y., Regnier C.H., Kirschning C.J., Goeddel D.V., Rothe M.
    Proc. Natl. Acad. Sci. U.S.A. 94:9792-9796(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K14.
  15. "CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization."
    Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R.
    Biochemistry 37:11836-11845(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF5 AND TRAF5.
  16. "Activation of OX40 signal transduction pathways leads to tumor necrosis factor receptor-associated factor (TRAF) 2- and TRAF5-mediated NF-kappaB activation."
    Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.
    J. Biol. Chem. 273:5808-5814(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF4.
  17. "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."
    Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.
    J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF11A.
  18. Cited for: INTERACTION WITH MAP3K5.
  19. "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB."
    Arch R.H., Thompson C.B.
    Mol. Cell. Biol. 18:558-565(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF4 AND TNFRSF9.
  20. "Identification of a novel activation-inducible protein of the tumor necrosis factor receptor superfamily and its ligand."
    Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D., Wang S.-X., Kwon B.S.
    J. Biol. Chem. 274:6056-6061(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF18.
    Tissue: T-cell.
  21. "Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)."
    Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R.
    Oncogene 18:5814-5820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K5.
  22. "TAJ, a novel member of the tumor necrosis factor receptor family, activates the c-Jun N-terminal kinase pathway and mediates caspase-independent cell death."
    Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.
    J. Biol. Chem. 275:15336-15342(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF19.
  23. "TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation."
    Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.
    J. Biol. Chem. 275:18586-18593(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTRAP.
  24. "MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network."
    Ling L., Goeddel D.V.
    J. Biol. Chem. 275:23852-23860(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF3IP1.
  25. "TNF receptor family member BCMA (B cell maturation) associates with TNF receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and activates NF-kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase."
    Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C., Inoue J., Devergne O., Tsapis A.
    J. Immunol. 165:1322-1330(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF17.
  26. "The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A."
    Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M.
    J. Biol. Chem. 276:2668-2677(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDAR.
  27. "TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation."
    He L., Grammer A.C., Wu X., Lipsky P.E.
    J. Biol. Chem. 279:55855-55865(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  28. "Regulation of the NF-kappaB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation."
    Liao G., Zhang M., Harhaj E.W., Sun S.C.
    J. Biol. Chem. 279:26243-26250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEASOMAL DEGRADATION, INTERACTION WITH MAP3K14.
  29. Cited for: INTERACTION WITH OTUD5 AND TBK1, FUNCTION AS E3 PROTEIN-UBIQUITIN LIGASE, UBIQUITINATION.
  30. "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
    Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
    J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRC.
  31. "The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation."
    Nakhaei P., Mesplede T., Solis M., Sun Q., Zhao T., Yang L., Chuang T.H., Ware C.F., Lin R., Hiscott J.
    PLoS Pathog. 5:E1000650-E1000650(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, MUTAGENESIS OF TYR-441 AND GLN-443, INTERACTION WITH RNF216 AND MAVS.
  32. "Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6."
    Li S., Zheng H., Mao A.P., Zhong B., Li Y., Liu Y., Gao Y., Ran Y., Tien P., Shu H.B.
    J. Biol. Chem. 285:4291-4297(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH OTUB1 AND OTUB2.
  33. "Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response."
    Mao A.P., Li S., Zhong B., Li Y., Yan J., Li Q., Teng C., Shu H.B.
    J. Biol. Chem. 285:9470-9476(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC2 AND BIRC3, SUBCELLULAR LOCATION, UBIQUITINATION.
  34. "TRAF3 controls activation of the canonical and alternative NFkappaB by the lymphotoxin beta receptor."
    Bista P., Zeng W., Ryan S., Bailly V., Browning J.L., Lukashev M.E.
    J. Biol. Chem. 285:12971-12978(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  35. "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
    Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
    Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, FUNCTION.
  36. "Optineurin negatively regulates the induction of IFNbeta in response to RNA virus infection."
    Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M., Kohl A., Elliott R.M., Macdonald A.
    PLoS Pathog. 6:E1000778-E1000778(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OPTN AND TBK1.
  37. "Alternative splicing of CARMA2/CARD14 transcripts generates protein variants with differential effect on NF-kappaB activation and endoplasmic reticulum stress-induced cell death."
    Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.
    J. Cell. Physiol. 226:3121-3131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CARD14.
  38. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 341-568, X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 341-568 IN COMPLEX WITH TNFRSF5.
  39. "Downstream regulator TANK binds to the CD40 recognition site on TRAF3."
    Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
    Structure 10:403-411(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 377-568 IN COMPLEX WITH TANK, X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 377-568 IN COMPLEX WITH TNFRSF5.
  40. "Structurally distinct recognition motifs in lymphotoxin-beta receptor and CD40 for tumor necrosis factor receptor-associated factor (TRAF)-mediated signaling."
    Li C., Norris P.S., Ni C.Z., Havert M.L., Chiong E.M., Tran B.R., Cabezas E., Reed J.C., Satterthwait A.C., Ware C.F., Ely K.R.
    J. Biol. Chem. 278:50523-50529(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 377-568 IN COMPLEX WITH LTBR, MUTAGENESIS OF TYR-459; PHE-512 AND PHE-521, INTERACTION WITH TANK AND CD40, SUBUNIT.
  41. "Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: implications for intracellular signaling regulation."
    Ni C.Z., Oganesyan G., Welsh K., Zhu X., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
    J. Immunol. 173:7394-7400(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 377-568 IN COMPLEX WITH TNFRSF13C PEPTIDE, SUBUNIT, INTERACTION WITH TNFRSF13C.
  42. "LMP1 protein from the Epstein-Barr virus is a structural CD40 decoy in B lymphocytes for binding to TRAF3."
    Wu S., Xie P., Welsh K., Li C., Ni C.Z., Zhu X., Reed J.C., Satterthwait A.C., Bishop G.A., Ely K.R.
    J. Biol. Chem. 280:33620-33626(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 377-568 IN COMPLEX WITH EPSTEIN-BARR VIRUS PROTEIN LMP1, SUBUNIT.
  43. "Solution structure of the zinc finger, C3HC4 type (RING finger) domain of TNF receptor-associated factor 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 43-101.
  44. Cited for: VARIANT HSE3 TRP-118.

Entry informationi

Entry nameiTRAF3_HUMAN
AccessioniPrimary (citable) accession number: Q13114
Secondary accession number(s): B7Z8C4
, Q12990, Q13076, Q13947, Q6AZX1, Q9UNL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 170 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3