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P21580

- TNAP3_HUMAN

UniProt

P21580 - TNAP3_HUMAN

Protein

Tumor necrosis factor alpha-induced protein 3

Gene

TNFAIP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    Functioni

    Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages.12 Publications

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei100 – 1001By similarity
    Active sitei103 – 1031Nucleophile1 Publication
    Active sitei256 – 2561Proton acceptor1 Publication
    Sitei439 – 4402Cleavage; by MALT1

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri381 – 41636A20-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri472 – 50736A20-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri515 – 54834A20-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri601 – 63636A20-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri651 – 68636A20-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri710 – 74536A20-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri756 – 79035A20-type 7PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. ligase activity Source: UniProtKB-KW
    3. protease binding Source: BHF-UCL
    4. protein binding Source: IntAct
    5. protein self-association Source: BHF-UCL
    6. ubiquitin binding Source: BHF-UCL
    7. ubiquitin-protein transferase activity Source: UniProtKB
    8. ubiquitin-specific protease activity Source: UniProtKB
    9. ubiquitin thiolesterase activity Source: UniProtKB
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. B-1 B cell homeostasis Source: BHF-UCL
    3. cellular response to hydrogen peroxide Source: UniProtKB
    4. cellular response to lipopolysaccharide Source: BHF-UCL
    5. inflammatory response Source: UniProtKB-KW
    6. innate immune response Source: Reactome
    7. negative regulation of B cell activation Source: BHF-UCL
    8. negative regulation of bone resorption Source: BHF-UCL
    9. negative regulation of CD40 signaling pathway Source: BHF-UCL
    10. negative regulation of chronic inflammatory response Source: Ensembl
    11. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
    12. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
    13. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    14. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    15. negative regulation of inflammatory response Source: BHF-UCL
    16. negative regulation of innate immune response Source: UniProtKB
    17. negative regulation of interleukin-1 beta production Source: Ensembl
    18. negative regulation of interleukin-2 production Source: BHF-UCL
    19. negative regulation of interleukin-6 production Source: BHF-UCL
    20. negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    21. negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway Source: Ensembl
    22. negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: Ensembl
    23. negative regulation of osteoclast proliferation Source: BHF-UCL
    24. negative regulation of protein ubiquitination Source: BHF-UCL
    25. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
    26. negative regulation of toll-like receptor 2 signaling pathway Source: BHF-UCL
    27. negative regulation of toll-like receptor 3 signaling pathway Source: BHF-UCL
    28. negative regulation of toll-like receptor 4 signaling pathway Source: BHF-UCL
    29. negative regulation of toll-like receptor 5 signaling pathway Source: Ensembl
    30. negative regulation of tumor necrosis factor production Source: BHF-UCL
    31. negative regulation of type I interferon production Source: Reactome
    32. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    33. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
    34. positive regulation of hepatocyte proliferation Source: Ensembl
    35. positive regulation of protein catabolic process Source: BHF-UCL
    36. protein deubiquitination Source: BHF-UCL
    37. protein K11-linked deubiquitination Source: UniProtKB
    38. protein K48-linked deubiquitination Source: UniProtKB
    39. protein K48-linked ubiquitination Source: UniProtKB
    40. protein K63-linked deubiquitination Source: UniProtKB
    41. protein oligomerization Source: BHF-UCL
    42. regulation of defense response to virus by host Source: BHF-UCL
    43. regulation of germinal center formation Source: BHF-UCL
    44. regulation of vascular wound healing Source: BHF-UCL
    45. response to molecule of bacterial origin Source: BHF-UCL
    46. response to muramyl dipeptide Source: Ensembl
    47. tolerance induction to lipopolysaccharide Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Ligase, Protease, Thiol protease

    Keywords - Biological processi

    Apoptosis, Inflammatory response, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiP21580.

    Protein family/group databases

    MEROPSiC64.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor alpha-induced protein 3 (EC:3.4.19.12, EC:6.3.2.-)
    Short name:
    TNF alpha-induced protein 3
    Alternative name(s):
    OTU domain-containing protein 7C
    Putative DNA-binding protein A20
    Zinc finger protein A20
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TNFAIP3
    Synonyms:OTUD7C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11896. TNFAIP3.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. lysosome Source: UniProtKB-SubCell
    6. nucleus Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Lysosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701D → A: Minor effect on 'Lys-48' deubiquitinase activity. Strongly reduced 'Lys-63' deubiquitinase activity. 2 Publications
    Mutagenesisi97 – 971T → A: Minor effect on 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi100 – 1001D → A: Strongly reduced deubiquitinase activity. 1 Publication
    Mutagenesisi103 – 1031C → A: Loss of deubiquitinase activity. 4 Publications
    Mutagenesisi103 – 1031C → S: Loss of 'Lys-63' deubiquitinating activity. Down-regulation of TNF-induced NF-kappa-B activity less effective. 4 Publications
    Mutagenesisi157 – 1571L → A: Strongly reduced 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi159 – 1591Y → A: Strongly reduced 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi190 – 1901S → A: Strongly reduced 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi192 – 1921E → A: Strongly reduced 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi224 – 2241F → A: Strongly reduced 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi227 – 2271L → A: Strongly reduced 'Lys-48' deubiquitinase activity. 1 Publication
    Mutagenesisi256 – 2561H → A: Loss of deubiquitinase activity. 1 Publication
    Mutagenesisi521 – 5211C → A: No effect on ubiquitin ligase activity; when associated with A-524. 1 Publication
    Mutagenesisi524 – 5241C → A: No effect on ubiquitin ligase activity; when associated with A-521. 1 Publication
    Mutagenesisi562 – 5621R → A: Abolishes interactionj with YWHAZ AND YWHAH; no effect on inhibitory activity of TNF-induced NF-kappa-B activation. 1 Publication
    Mutagenesisi565 – 5651S → A: Abolishes interactionj with YWHAZ AND YWHAH; no effect on inhibitory activity of TNF-induced NF-kappa-B activation. 1 Publication
    Mutagenesisi614 – 6141Y → A: Impairs ubiquitination activity. Loss of down-regulation of NF-kappa-B activity; when associated with A-615 or R-626. 1 Publication
    Mutagenesisi615 – 6151F → A: Impairs ubiquitination activity. Loss of down-regulation of NF-kappa-B activity; when associated with A-614. 1 Publication
    Mutagenesisi624 – 6241C → A: Marked attenuation of ubiquitin ligase activity and inhibition of RIPK1 degradation; when associated with A-627. 1 Publication
    Mutagenesisi626 – 6261L → R: Impairs ubiquitination activity. Loss of down-regulation of NF-kappa-B activity; when associated with A-614. 1 Publication
    Mutagenesisi627 – 6271C → A: Marked attenuation of ubiquitin ligase activity and inhibition of RIPK1 degradation; when associated with A-624. 1 Publication
    Mutagenesisi770 – 7712FG → AA: Impairs polyubiquitin binding, abolishes inhibition of IKK activation.
    Mutagenesisi779 – 7791C → A: Impairs polyubiquitin binding, abolishes inhibition of IKK activation; when associated with A-782. 1 Publication
    Mutagenesisi782 – 7821C → A: Impairs polyubiquitin binding, abolishes inhibition of IKK activation; when associated with A-779. 1 Publication

    Organism-specific databases

    Orphaneti536. Systemic lupus erythematosus.
    PharmGKBiPA36593.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 790789Tumor necrosis factor alpha-induced protein 3PRO_0000188791Add
    BLAST
    Chaini2 – 439438A20p50PRO_0000418127Add
    BLAST
    Chaini440 – 790351A20p37PRO_0000418128Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei459 – 4591Phosphoserine1 Publication

    Post-translational modificationi

    Proteolytically cleaved by MALT1 upon TCR stimulation; disrupts NF-kappa-B inhibitory function and results in increased IL-2 production. It is proposed that only a fraction of TNFAIP3 colocalized with TCR and CBM complex is cleaved, leaving the main TNFAIP3 pool intact.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP21580.
    PaxDbiP21580.
    PRIDEiP21580.

    PTM databases

    PhosphoSiteiP21580.

    Expressioni

    Inductioni

    By TNF.

    Gene expression databases

    ArrayExpressiP21580.
    BgeeiP21580.
    CleanExiHS_TNFAIP3.
    GenevestigatoriP21580.

    Organism-specific databases

    HPAiHPA002116.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TNIP1, TAX1BP1 and TRAF2. Interacts with RNF11, ITCH and TAX1BP1 only after TNF stimulation; these interaction are transient and they are lost after 1 hour of stimulation with TNF By similarity. Interacts with YWHAZ and YWHAH. Interacts with IKBKG; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with RIPK1. Interacts with UBE2N; the interaction requires TAX1BP1. Interacts with TRAF6; the interaction is inhibited by HTLV-1 protein Tax.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKBKGQ9Y6K94EBI-527670,EBI-81279
    RNF11Q9Y3C52EBI-527670,EBI-396669
    YwhahP685103EBI-527670,EBI-444641From a different organism.

    Protein-protein interaction databases

    BioGridi112983. 69 interactions.
    DIPiDIP-33804N.
    IntActiP21580. 21 interactions.
    MINTiMINT-97330.
    STRINGi9606.ENSP00000237289.

    Structurei

    Secondary structure

    1
    790
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 134
    Helixi15 – 2713
    Beta strandi33 – 353
    Beta strandi39 – 424
    Helixi43 – 453
    Beta strandi54 – 563
    Helixi58 – 6811
    Helixi71 – 799
    Beta strandi82 – 843
    Beta strandi87 – 893
    Beta strandi92 – 954
    Helixi103 – 11311
    Helixi121 – 13212
    Helixi136 – 14712
    Helixi164 – 17411
    Beta strandi176 – 1783
    Beta strandi181 – 1855
    Helixi193 – 20311
    Beta strandi207 – 2115
    Beta strandi231 – 2333
    Helixi240 – 2423
    Beta strandi248 – 2536
    Beta strandi256 – 2638
    Beta strandi267 – 2704
    Beta strandi272 – 2798
    Beta strandi282 – 2854
    Helixi293 – 2975
    Helixi299 – 3068
    Beta strandi309 – 3157
    Beta strandi317 – 32913
    Helixi337 – 3393
    Helixi341 – 35414
    Helixi359 – 3613
    Beta strandi384 – 3863
    Turni398 – 4025
    Helixi405 – 4128
    Beta strandi604 – 6063
    Beta strandi613 – 6153
    Helixi618 – 6203
    Helixi625 – 63410
    Helixi773 – 7753
    Helixi780 – 7889

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EQENMR-A597-631[»]
    2EQFNMR-A758-790[»]
    2EQGNMR-A381-416[»]
    2VFJX-ray3.20A/B/C/D1-366[»]
    3DKBX-ray2.50A/B/C/D/E/F1-370[»]
    3OJ3X-ray2.50I/J/K/L/M/N/O/P592-635[»]
    3OJ4X-ray3.40C/F592-635[»]
    3VUWX-ray1.95E/F/G757-789[»]
    3VUXX-ray1.70E/F/G757-790[»]
    3VUYX-ray1.98D/E/F757-790[»]
    3ZJDX-ray1.87A/B1-366[»]
    3ZJEX-ray1.84A/B1-366[»]
    3ZJFX-ray2.20A/B1-366[»]
    3ZJGX-ray1.92A/B1-366[»]
    ProteinModelPortaliP21580.
    SMRiP21580. Positions 3-362, 382-419, 603-635, 758-790.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21580.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 263172OTUPROSITE-ProRule annotationAdd
    BLAST
    Repeati286 – 317321Add
    BLAST
    Repeati324 – 356332Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 300243TRAF-bindingAdd
    BLAST
    Regioni157 – 1593Interaction with ubiquitinCurated
    Regioni190 – 1923Interaction with ubiquitinCurated
    Regioni224 – 2274Interaction with ubiquitinCurated
    Regioni286 – 356712 X approximate repeatsAdd
    BLAST
    Regioni369 – 775407Interaction with TNIP1By similarityAdd
    BLAST
    Regioni386 – 45368Interaction with RIPK1Add
    BLAST
    Regioni605 – 65551Required for proteosomal degradation of UBE2N and UBE2D3, TRAF6 deubiquitination, and TAX1BP1 interaction with UBE2NBy similarityAdd
    BLAST
    Regioni606 – 790185Sufficient for inhibitory activity of TNF-induced NF-kappa-B activityBy similarityAdd
    BLAST
    Regioni697 – 79094Required for lysosomal localization and for TRAF2 lysosomal degradationAdd
    BLAST

    Domaini

    The A20-type zinc fingers mediate the ubiquitin ligase activity. The A20-type zinc finger 4 selectively recognizes 'Lys-63'-linked polyubiquitin. The A20-type zinc finger 4-7 are sufficient to bind polyubiquitin.1 Publication
    The OTU domain mediates the deubiquitinase activity.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C64 family.Curated
    Contains 7 A20-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 OTU domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri381 – 41636A20-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri472 – 50736A20-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri515 – 54834A20-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri601 – 63636A20-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri651 – 68636A20-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri710 – 74536A20-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri756 – 79035A20-type 7PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG248343.
    HOGENOMiHOG000133004.
    HOVERGENiHBG059260.
    InParanoidiP21580.
    KOiK11859.
    OMAiCETPNCP.
    OrthoDBiEOG7JHM57.
    PhylomeDBiP21580.
    TreeFamiTF323312.

    Family and domain databases

    InterProiIPR003323. OTU.
    IPR002653. Znf_A20.
    [Graphical view]
    PfamiPF02338. OTU. 1 hit.
    PF01754. zf-A20. 6 hits.
    [Graphical view]
    SMARTiSM00259. ZnF_A20. 7 hits.
    [Graphical view]
    PROSITEiPS50802. OTU. 1 hit.
    PS51036. ZF_A20. 7 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P21580-1 [UniParc]FASTAAdd to Basket

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    MAEQVLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIHHF KTMHRYTLEM    50
    FRTCQFCPQF REIIHKALID RNIQATLESQ KKLNWCREVR KLVALKTNGD 100
    GNCLMHATSQ YMWGVQDTDL VLRKALFSTL KETDTRNFKF RWQLESLKSQ 150
    EFVETGLCYD TRNWNDEWDN LIKMASTDTP MARSGLQYNS LEEIHIFVLC 200
    NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA QECYRYPIVL 250
    GYDSHHFVPL VTLKDSGPEI RAVPLVNRDR GRFEDLKVHF LTDPENEMKE 300
    KLLKEYLMVI EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ 350
    HEYKKWQENS EQGRREGHAQ NPMEPSVPQL SLMDVKCETP NCPFFMSVNT 400
    QPLCHECSER RQKNQNKLPK LNSKPGPEGL PGMALGASRG EAYEPLAWNP 450
    EESTGGPHSA PPTAPSPFLF SETTAMKCRS PGCPFTLNVQ HNGFCERCHN 500
    ARQLHASHAP DHTRHLDPGK CQACLQDVTR TFNGICSTCF KRTTAEASSS 550
    LSTSLPPSCH QRSKSDPSRL VRSPSPHSCH RAGNDAPAGC LSQAARTPGD 600
    RTGTSKCRKA GCVYFGTPEN KGFCTLCFIE YRENKHFAAA SGKVSPTASR 650
    FQNTIPCLGR ECGTLGSTMF EGYCQKCFIE AQNQRFHEAK RTEEQLRSSQ 700
    RRDVPRTTQS TSRPKCARAS CKNILACRSE ELCMECQHPN QRMGPGAHRG 750
    EPAPEDPPKQ RCRAPACDHF GNAKCNGYCN ECFQFKQMYG 790
    Length:790
    Mass (Da):89,614
    Last modified:May 1, 1991 - v1
    Checksum:i320AEA97F58D4491
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251A → V.1 Publication
    Corresponds to variant rs5029941 [ dbSNP | Ensembl ].
    VAR_020447
    Natural varianti127 – 1271F → C.1 Publication
    Corresponds to variant rs2230926 [ dbSNP | Ensembl ].
    VAR_022143
    Natural varianti766 – 7661A → P.1 Publication
    Corresponds to variant rs5029957 [ dbSNP | Ensembl ].
    VAR_029319

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59465 mRNA. Translation: AAA51550.1.
    AK312862 mRNA. Translation: BAG35714.1.
    AY248754 Genomic DNA. Translation: AAO61093.1.
    AL357060 Genomic DNA. Translation: CAH72937.1.
    CH471051 Genomic DNA. Translation: EAW47925.1.
    CH471051 Genomic DNA. Translation: EAW47926.1.
    BC113871 mRNA. Translation: AAI13872.1.
    BC114480 mRNA. Translation: AAI14481.1.
    AL157444 mRNA. Translation: CAB75664.1.
    CCDSiCCDS5187.1.
    PIRiA35797.
    RefSeqiNP_001257436.1. NM_001270507.1.
    NP_001257437.1. NM_001270508.1.
    NP_006281.1. NM_006290.3.
    XP_005267176.1. XM_005267119.1.
    UniGeneiHs.211600.

    Genome annotation databases

    EnsembliENST00000237289; ENSP00000237289; ENSG00000118503.
    GeneIDi7128.
    KEGGihsa:7128.
    UCSCiuc003qhr.4. human.

    Polymorphism databases

    DMDMi112894.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59465 mRNA. Translation: AAA51550.1 .
    AK312862 mRNA. Translation: BAG35714.1 .
    AY248754 Genomic DNA. Translation: AAO61093.1 .
    AL357060 Genomic DNA. Translation: CAH72937.1 .
    CH471051 Genomic DNA. Translation: EAW47925.1 .
    CH471051 Genomic DNA. Translation: EAW47926.1 .
    BC113871 mRNA. Translation: AAI13872.1 .
    BC114480 mRNA. Translation: AAI14481.1 .
    AL157444 mRNA. Translation: CAB75664.1 .
    CCDSi CCDS5187.1.
    PIRi A35797.
    RefSeqi NP_001257436.1. NM_001270507.1.
    NP_001257437.1. NM_001270508.1.
    NP_006281.1. NM_006290.3.
    XP_005267176.1. XM_005267119.1.
    UniGenei Hs.211600.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EQE NMR - A 597-631 [» ]
    2EQF NMR - A 758-790 [» ]
    2EQG NMR - A 381-416 [» ]
    2VFJ X-ray 3.20 A/B/C/D 1-366 [» ]
    3DKB X-ray 2.50 A/B/C/D/E/F 1-370 [» ]
    3OJ3 X-ray 2.50 I/J/K/L/M/N/O/P 592-635 [» ]
    3OJ4 X-ray 3.40 C/F 592-635 [» ]
    3VUW X-ray 1.95 E/F/G 757-789 [» ]
    3VUX X-ray 1.70 E/F/G 757-790 [» ]
    3VUY X-ray 1.98 D/E/F 757-790 [» ]
    3ZJD X-ray 1.87 A/B 1-366 [» ]
    3ZJE X-ray 1.84 A/B 1-366 [» ]
    3ZJF X-ray 2.20 A/B 1-366 [» ]
    3ZJG X-ray 1.92 A/B 1-366 [» ]
    ProteinModelPortali P21580.
    SMRi P21580. Positions 3-362, 382-419, 603-635, 758-790.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112983. 69 interactions.
    DIPi DIP-33804N.
    IntActi P21580. 21 interactions.
    MINTi MINT-97330.
    STRINGi 9606.ENSP00000237289.

    Protein family/group databases

    MEROPSi C64.003.

    PTM databases

    PhosphoSitei P21580.

    Polymorphism databases

    DMDMi 112894.

    Proteomic databases

    MaxQBi P21580.
    PaxDbi P21580.
    PRIDEi P21580.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000237289 ; ENSP00000237289 ; ENSG00000118503 .
    GeneIDi 7128.
    KEGGi hsa:7128.
    UCSCi uc003qhr.4. human.

    Organism-specific databases

    CTDi 7128.
    GeneCardsi GC06P138188.
    HGNCi HGNC:11896. TNFAIP3.
    HPAi HPA002116.
    MIMi 191163. gene.
    neXtProti NX_P21580.
    Orphaneti 536. Systemic lupus erythematosus.
    PharmGKBi PA36593.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248343.
    HOGENOMi HOG000133004.
    HOVERGENi HBG059260.
    InParanoidi P21580.
    KOi K11859.
    OMAi CETPNCP.
    OrthoDBi EOG7JHM57.
    PhylomeDBi P21580.
    TreeFami TF323312.

    Enzyme and pathway databases

    Reactomei REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki P21580.

    Miscellaneous databases

    ChiTaRSi TNFAIP3. human.
    EvolutionaryTracei P21580.
    GeneWikii TNFAIP3.
    GenomeRNAii 7128.
    NextBioi 27895.
    PROi P21580.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21580.
    Bgeei P21580.
    CleanExi HS_TNFAIP3.
    Genevestigatori P21580.

    Family and domain databases

    InterProi IPR003323. OTU.
    IPR002653. Znf_A20.
    [Graphical view ]
    Pfami PF02338. OTU. 1 hit.
    PF01754. zf-A20. 6 hits.
    [Graphical view ]
    SMARTi SM00259. ZnF_A20. 7 hits.
    [Graphical view ]
    PROSITEi PS50802. OTU. 1 hit.
    PS51036. ZF_A20. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The A20 cDNA induced by tumor necrosis factor alpha encodes a novel type of zinc finger protein."
      Opipari A.W. Jr., Boguski M.S., Dixit V.M.
      J. Biol. Chem. 265:14705-14708(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Tissue: Trachea.
    3. SeattleSNPs variation discovery resource
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-125; CYS-127 AND PRO-766.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-790.
      Tissue: Testis.
    8. "The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation."
      Song H.Y., Rothe M., Goeddel D.V.
      Proc. Natl. Acad. Sci. U.S.A. 93:6721-6725(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRAF1 AND TRAF2.
    9. "A20 inhibits NF-kappaB activation independently of binding to 14-3-3 proteins."
      De Valck D., Heyninck K., Van Criekinge W., Vandenabeele P., Fiers W., Beyaert R.
      Biochem. Biophys. Res. Commun. 238:590-594(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YWHAZ AND YWHAH, MUTAGENESIS OF ARG-562 AND SER-565.
    10. "Epstein-Barr virus-encoded latent membrane protein 1 activates the JNK pathway through its extreme C-terminus via a mechanism involving TRADD and TRAF2."
      Eliopoulos A.G., Blake S.M., Floettmann J.E., Rowe M., Young L.S.
      J. Virol. 73:1023-1035(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRAF2.
    11. "The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases."
      de Valck D., Jin D.-Y., Heyninck K., van de Craen M., Contreras R., Fiers W., Jeang K.-T., Beyaert R.
      Oncogene 18:4182-4190(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAX1BP1.
    12. "Isolation and characterization of two novel A20-like proteins."
      Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R., Kilshaw P.J.
      Biochem. J. 357:617-623(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity."
      Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S., Ploegh H.L., Smith T.S.
      Biochem. J. 378:727-734(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-103.
    14. "De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling."
      Wertz I.E., O'Rourke K.M., Zhou H., Eby M., Aravind L., Seshagiri S., Wu P., Wiesmann C., Baker R., Boone D.L., Ma A., Koonin E.V., Dixit V.M.
      Nature 430:694-699(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN OTU, DOMAIN A20-TYPE ZINC-FINGER, MUTAGENESIS OF CYS-103; CYS-521; CYS-524; CYS-624 AND CYS-627.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB."
      Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A.
      J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKBKG AND TNIP1.
    17. "T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20."
      Coornaert B., Baens M., Heyninck K., Bekaert T., Haegman M., Staal J., Sun L., Chen Z.J., Marynen P., Beyaert R.
      Nat. Immunol. 9:263-271(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "The zinc finger protein A20 targets TRAF2 to the lysosomes for degradation."
      Li L., Soetandyo N., Wang Q., Ye Y.
      Biochim. Biophys. Acta 1793:346-353(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    20. "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling."
      Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.
      EMBO J. 28:513-522(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAX1BP1; RNF11 AND RIPK1.
    21. "A20 negatively regulates T cell receptor signaling to NF-kappaB by cleaving Malt1 ubiquitin chains."
      Duwel M., Welteke V., Oeckinghaus A., Baens M., Kloo B., Ferch U., Darnay B.G., Ruland J., Marynen P., Krappmann D.
      J. Immunol. 182:7718-7728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. Cited for: PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION.
    24. "Direct, noncatalytic mechanism of IKK inhibition by A20."
      Skaug B., Chen J., Du F., He J., Ma A., Chen Z.J.
      Mol. Cell 44:559-571(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKBKG, MUTAGENESIS OF 770-PHE-GLY-771; CYS-779 AND CYS-782.
    25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    26. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
      Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
      Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    27. "Solution structure of the A20-type zinc finger domains from human tumor necrosis factor, alpha-induced protein 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 381-790.
    28. "Structure of the A20 OTU domain and mechanistic insights into deubiquitination."
      Komander D., Barford D.
      Biochem. J. 409:77-85(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-366, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-70; CYS-103 AND HIS-256.
    29. "Molecular basis for the unique deubiquitinating activity of the NF-kappaB inhibitor A20."
      Lin S.C., Chung J.Y., Lamothe B., Rajashankar K., Lu M., Lo Y.C., Lam A.Y., Darnay B.G., Wu H.
      J. Mol. Biol. 376:526-540(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-370, ACTIVE SITE, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-70; THR-97; ASP-100; CYS-103; LEU-157; TYR-159; SER-190; GLU-192; PHE-224 AND LEU-227.
    30. "Ubiquitin binding to A20 ZnF4 is required for modulation of NF-kappaB signaling."
      Bosanac I., Wertz I.E., Pan B., Yu C., Kusam S., Lam C., Phu L., Phung Q., Maurer B., Arnott D., Kirkpatrick D.S., Dixit V.M., Hymowitz S.G.
      Mol. Cell 40:548-557(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 592-635 IN COMPLEX WITH UBIQUITIN, X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 592-635 IN COMPLEX WITH UBIQUITIN AND UBE2D1, MUTAGENESIS OF TYR-614; PHE-615 AND LEU-626.

    Entry informationi

    Entry nameiTNAP3_HUMAN
    AccessioniPrimary (citable) accession number: P21580
    Secondary accession number(s): B2R767
    , E1P588, Q2HIX9, Q5VXQ7, Q9NSR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3