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Protein

TNF receptor-associated factor 2

Gene

Traf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Isoform 2 does not seem to mediate activation of NF-kappa-B but inhibits isoform 1 activity. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.8 Publications

Enzyme regulationi

Has very low E3 ubiquitin ligase activity in the absence of sphingosine-1-phosphate. E3 ubiquitin ligase activity is strongly activated by cytoplasmic sphingosine-1-phosphate (By similarity).By similarity

Pathwayi: protein ubiquitination

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 73RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri124 – 180TRAF-type 1PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri177 – 233TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3371378. Regulation by c-FLIP.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5218900. CASP8 activity is inhibited.
R-MMU-5357786. TNFR1-induced proapoptotic signaling.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676594. TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-69416. Dimerization of procaspase-8.
R-MMU-75893. TNF signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 2 (EC:6.3.2.-)
Alternative name(s):
E3 ubiquitin-protein ligase TRAF2
Gene namesi
Name:Traf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:101835. Traf2.

Subcellular locationi

GO - Cellular componenti

  • CD40 receptor complex Source: BHF-UCL
  • cell cortex Source: Ensembl
  • cytoplasm Source: AgBase
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • cytosol Source: MGI
  • IRE1-TRAF2-ASK1 complex Source: ParkinsonsUK-UCL
  • membrane raft Source: MGI
  • TRAF2-GSTP1 complex Source: MGI
  • ubiquitin ligase complex Source: MGI
  • vesicle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Important embryonic and perinatal mortality. Life-born mutants appear normal at birth, but are smaller than their littermates after three days, fail to thrive, and few survive more than three weeks. Thymus and spleen are severely atrophic, and mice display lymphopenia of both T and B lymphocytes, with normal erythrocyte counts. Their thymocytes are abnormally sensitive to TNF-induced cell death and exhibit high levels of spontaneous apoptosis. Macrophages are highly sensitive to TNF and produce high levels of nitric oxide (NO) in response to TNF. Likewise, endogenous TNF production is abnormally increased upon exposure to TNF. Symptoms are much attenuated in mice that are deficient for both Traf2 and Tnfrsf1a/Tnfr1, or Traf2 and Tnf. Likewise, deletion of one Map3k14 allele alleviates symptoms and rescues splenic atrophy and reduction of splenocyte numbers. Mice show normal IgM production in response to viral infection, but lack CD40-mediated proliferation of B-cells. They are deficient in antibody isotype switching and fail to produce IgG.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34C → S: Loss of autoubiquitination. 1 Publication1
Mutagenesisi283E → A: Reduces interaction with BIRC2. 1 Publication1
Mutagenesisi292E → A: Almost abolishes interaction with BIRC2; when associated with A-294. 1 Publication1
Mutagenesisi294E → A: Almost abolishes interaction with BIRC2; when associated with A-292. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000564002 – 501TNF receptor-associated factor 2Add BLAST500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei7PhosphothreonineBy similarity1
Modified residuei11PhosphoserineBy similarity1
Modified residuei22PhosphothreonineBy similarity1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei117Phosphothreonine; by PKCBy similarity1

Post-translational modificationi

Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B (By similarity).By similarity
Undergoes both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination. Polyubiquitinated via 'Lys-63'-linked ubiquitin in response to TNF signaling; this requires prior phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination promotes TRAF2-mediated activation of NF-kappa-B. Can be polyubiquitinated at several Lys residues via 'Lys-48'-linked ubiquitin chains in response to TNF signaling, leading to proteasomal degradation. Autoubiquitinated, leading to its subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and SIAH2, leading to its subsequent proteasomal degradation. Not ubiquitinated by BIRC3 or SIAH1. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP39429.
PaxDbiP39429.
PeptideAtlasiP39429.
PRIDEiP39429.

PTM databases

iPTMnetiP39429.
PhosphoSitePlusiP39429.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in spleen, adipose tissues, skeletal muscles, thymus, testis, heart, lung, brain. Isoform 2 is very weakly expressed in heart, lung and brain.

Gene expression databases

BgeeiENSMUSG00000026942.
CleanExiMM_TRAF2.
ExpressionAtlasiP39429. baseline and differential.
GenevisibleiP39429. MM.

Interactioni

Subunit structurei

Homotrimer, and heterotrimer with TRAF1 and TRAF3 (via TRAF domain). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro). Interacts with TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, CD27/TNFRSF7, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1 and IL15RA. Interacts with CDK9, CSK, MAP3K1, MAP3K5, MAP3K11, MAP4K2, RIPK2, TNIK, TBK1, SPHK1, TRAIP, TANK/ITRAF, TDP2, MAVS/IPS1, TICAM1 and TRPC4AP. Interacts with CASP8AP2, NFATC2IP, PEG3 and HIVEP3. Interacts with CYLD, USP48, IKKA and IKKB. Interacts (via 'Lys-63'-linked polyubiquitin chains) with TAB2 and TAB3. Interaction with TAOK3 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation. Interacts with CASP12 under resting conditions; this interaction is reduced in ER stress conditions. Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts with ERN1; the interaction requires DAB2IP. Interacts with DAB2IP. Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14 (By similarity). Interacts with TRAFD1, TRADD and TNFAIP3. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer. Identified in a complex composed of TRAF2, TRAF3, BIRC2 and/or BIRC3. Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with MAP3K14 and RIPK1. Interacts with PTPN2; probably involved in tumor necrosis factor-mediated signaling.By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279585EBI-520016,EBI-8753518From a different organism.
Birc3O088637EBI-520016,EBI-642236
FcrlaQ920A95EBI-520016,EBI-646587
Irak1Q624062EBI-520016,EBI-448533
Map3k7Q620732EBI-520016,EBI-1775345
Mknk2Q8CDB03EBI-520016,EBI-646209
TankP70347-17EBI-520016,EBI-646125
Tnfaip3Q607693EBI-520016,EBI-646595
Tnfrsf11aO353052EBI-520016,EBI-647362
Tnfrsf4P477413EBI-520016,EBI-520001
Traf3Q608032EBI-520016,EBI-520135

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204303. 32 interactors.
DIPiDIP-468N.
IntActiP39429. 48 interactors.
MINTiMINT-197749.
STRINGi10090.ENSMUSP00000028311.

Structurei

3D structure databases

ProteinModelPortaliP39429.
SMRiP39429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini351 – 496MATHPROSITE-ProRule annotationAdd BLAST146

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni283 – 293Important for interaction with BIRC2 and BIRC3Add BLAST11

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili298 – 348By similarityAdd BLAST51

Domaini

The coiled coil domain mediates homo- and hetero-oligomerization.1 Publication
The MATH/TRAF domain binds to receptor cytoplasmic domains.1 Publication
The RING-type zinc finger domain is essential for E3 ubiquitin-protein ligase activity. It is not essential for the stabilization of BIRC2, or for the ubiquitination of RIPK1 in response to TNFR1 signaling (By similarity).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)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 73RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri124 – 180TRAF-type 1PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri177 – 233TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ISDM. Eukaryota.
ENOG4111M70. LUCA.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiP39429.
KOiK03173.
OMAiKFQDHVR.
OrthoDBiEOG091G0GHD.
PhylomeDBiP39429.
TreeFamiTF321154.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR002083. MATH/TRAF_dom.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027133. TRAF2.
IPR032070. TRAF_BIRC3-bd.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF21. PTHR10131:SF21. 1 hit.
PfamiPF16673. TRAF_BIRC3_bd. 1 hit.
PF00097. zf-C3HC4. 1 hit.
PF02176. zf-TRAF. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 2 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.

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: P39429-1) [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
MAAASVTSPG SLELLQPGFS KTLLGTRLEA KYLCSACKNI LRRPFQAQCG
60 70 80 90 100
HRYCSFCLTS ILSSGPQNCA ACVYEGLYEE GISILESSSA FPDNAARREV
110 120 130 140 150
ESLPAVCPND GCTWKGTLKE YESCHEGLCP FLLTECPACK GLVRLSEKEH
160 170 180 190 200
HTEQECPKRS LSCQHCRAPC SHVDLEVHYE VCPKFPLTCD GCGKKKIPRE
210 220 230 240 250
TFQDHVRACS KCRVLCRFHT VGCSEMVETE NLQDHELQRL REHLALLLSS
260 270 280 290 300
FLEAQASPGT LNQVGPELLQ RCQILEQKIA TFENIVCVLN REVERVAVTA
310 320 330 340 350
EACSRQHRLD QDKIEALSNK VQQLERSIGL KDLAMADLEQ KVSELEVSTY
360 370 380 390 400
DGVFIWKISD FTRKRQEAVA GRTPAIFSPA FYTSRYGYKM CLRVYLNGDG
410 420 430 440 450
TGRGTHLSLF FVVMKGPNDA LLQWPFNQKV TLMLLDHNNR EHVIDAFRPD
460 470 480 490 500
VTSSSFQRPV SDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG

L
Length:501
Mass (Da):56,026
Last modified:February 1, 1995 - v1
Checksum:i043B391180365F10
GO
Isoform 2 (identifier: P39429-2) [UniParc]FASTAAdd to basket
Also known as: TRAF2A

The sequence of this isoform differs from the canonical sequence as follows:
     62-62: L → LRCASILS

Note: No experimental confirmation available. On mRNA level, has a significantly shorter half-life than isoform 1.
Show »
Length:508
Mass (Da):56,757
Checksum:i74B8B26BFCF9B1C4
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00740262L → LRCASILS in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35303 mRNA. Translation: AAC37662.1.
AF027570 mRNA. Translation: AAC53545.1.
AF233332
, AF233326, AF233327, AF233328, AF233329, AF233330, AF233331 Genomic DNA. Translation: AAF59928.1.
AL732590 Genomic DNA. Translation: CAM25164.1.
BC003801 mRNA. Translation: AAH03801.1.
CCDSiCCDS15779.1. [P39429-1]
CCDS71002.1. [P39429-2]
PIRiI61512.
RefSeqiNP_001277342.1. NM_001290413.1. [P39429-2]
NP_033448.2. NM_009422.3. [P39429-1]
UniGeneiMm.3399.

Genome annotation databases

EnsembliENSMUST00000028311; ENSMUSP00000028311; ENSMUSG00000026942. [P39429-1]
ENSMUST00000114234; ENSMUSP00000109872; ENSMUSG00000026942. [P39429-2]
GeneIDi22030.
KEGGimmu:22030.
UCSCiuc008isl.2. mouse. [P39429-2]
uc008ism.2. mouse. [P39429-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35303 mRNA. Translation: AAC37662.1.
AF027570 mRNA. Translation: AAC53545.1.
AF233332
, AF233326, AF233327, AF233328, AF233329, AF233330, AF233331 Genomic DNA. Translation: AAF59928.1.
AL732590 Genomic DNA. Translation: CAM25164.1.
BC003801 mRNA. Translation: AAH03801.1.
CCDSiCCDS15779.1. [P39429-1]
CCDS71002.1. [P39429-2]
PIRiI61512.
RefSeqiNP_001277342.1. NM_001290413.1. [P39429-2]
NP_033448.2. NM_009422.3. [P39429-1]
UniGeneiMm.3399.

3D structure databases

ProteinModelPortaliP39429.
SMRiP39429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204303. 32 interactors.
DIPiDIP-468N.
IntActiP39429. 48 interactors.
MINTiMINT-197749.
STRINGi10090.ENSMUSP00000028311.

PTM databases

iPTMnetiP39429.
PhosphoSitePlusiP39429.

Proteomic databases

EPDiP39429.
PaxDbiP39429.
PeptideAtlasiP39429.
PRIDEiP39429.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028311; ENSMUSP00000028311; ENSMUSG00000026942. [P39429-1]
ENSMUST00000114234; ENSMUSP00000109872; ENSMUSG00000026942. [P39429-2]
GeneIDi22030.
KEGGimmu:22030.
UCSCiuc008isl.2. mouse. [P39429-2]
uc008ism.2. mouse. [P39429-1]

Organism-specific databases

CTDi7186.
MGIiMGI:101835. Traf2.

Phylogenomic databases

eggNOGiENOG410ISDM. Eukaryota.
ENOG4111M70. LUCA.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiP39429.
KOiK03173.
OMAiKFQDHVR.
OrthoDBiEOG091G0GHD.
PhylomeDBiP39429.
TreeFamiTF321154.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-3371378. Regulation by c-FLIP.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5218900. CASP8 activity is inhibited.
R-MMU-5357786. TNFR1-induced proapoptotic signaling.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676594. TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-69416. Dimerization of procaspase-8.
R-MMU-75893. TNF signaling.

Miscellaneous databases

PROiP39429.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026942.
CleanExiMM_TRAF2.
ExpressionAtlasiP39429. baseline and differential.
GenevisibleiP39429. MM.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR002083. MATH/TRAF_dom.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027133. TRAF2.
IPR032070. TRAF_BIRC3-bd.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF21. PTHR10131:SF21. 1 hit.
PfamiPF16673. TRAF_BIRC3_bd. 1 hit.
PF00097. zf-C3HC4. 1 hit.
PF02176. zf-TRAF. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 2 hits.
PROSITEiPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRAF2_MOUSE
AccessioniPrimary (citable) accession number: P39429
Secondary accession number(s): A2AJA3, O54896
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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. 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.