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Protein

Tumor necrosis factor

Gene

TNF

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

Functioni

Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line (PubMed:22517918).3 Publications
The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells.1 Publication

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • protease binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: UniProtKB
  • tumor necrosis factor receptor binding Source: BHF-UCL

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • activation of MAPK activity Source: BHF-UCL
  • activation of MAPKKK activity Source: BHF-UCL
  • cellular response to amino acid stimulus Source: Ensembl
  • cellular response to nicotine Source: UniProtKB
  • cellular response to organic cyclic compound Source: UniProtKB
  • chronic inflammatory response to antigenic stimulus Source: BHF-UCL
  • cortical actin cytoskeleton organization Source: UniProtKB
  • cytokine-mediated signaling pathway Source: Reactome
  • death-inducing signaling complex assembly Source: Reactome
  • defense response to Gram-positive bacterium Source: Ensembl
  • embryonic digestive tract development Source: DFLAT
  • endothelial cell apoptotic process Source: Ensembl
  • epithelial cell proliferation involved in salivary gland morphogenesis Source: Ensembl
  • extracellular matrix organization Source: Ensembl
  • extrinsic apoptotic signaling pathway Source: UniProtKB
  • extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
  • glucose metabolic process Source: Ensembl
  • humoral immune response Source: Ensembl
  • I-kappaB kinase/NF-kappaB signaling Source: Reactome
  • inflammatory response Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  • JNK cascade Source: Ensembl
  • leukocyte tethering or rolling Source: BHF-UCL
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • necroptotic signaling pathway Source: UniProtKB
  • negative regulation of alkaline phosphatase activity Source: Ensembl
  • negative regulation of bicellular tight junction assembly Source: UniProtKB
  • negative regulation of branching involved in lung morphogenesis Source: UniProtKB
  • negative regulation of cytokine secretion involved in immune response Source: BHF-UCL
  • negative regulation of endothelial cell proliferation Source: Ensembl
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • negative regulation of fat cell differentiation Source: BHF-UCL
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of glucose import Source: Ensembl
  • negative regulation of growth of symbiont in host Source: Ensembl
  • negative regulation of interleukin-6 production Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of lipid storage Source: BHF-UCL
  • negative regulation of mitotic cell cycle Source: Ensembl
  • negative regulation of myoblast differentiation Source: Ensembl
  • negative regulation of myosin-light-chain-phosphatase activity Source: UniProtKB
  • negative regulation of osteoblast differentiation Source: Ensembl
  • negative regulation of protein complex disassembly Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: UniProtKB
  • negative regulation of viral genome replication Source: BHF-UCL
  • osteoclast differentiation Source: Ensembl
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of blood microparticle formation Source: BHF-UCL
  • positive regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  • positive regulation of calcineurin-NFAT signaling cascade Source: MGI
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of ceramide biosynthetic process Source: Reactome
  • positive regulation of chemokine (C-X-C motif) ligand 2 production Source: BHF-UCL
  • positive regulation of chemokine biosynthetic process Source: BHF-UCL
  • positive regulation of chemokine production Source: BHF-UCL
  • positive regulation of chronic inflammatory response to antigenic stimulus Source: Ensembl
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of cytokine production Source: BHF-UCL
  • positive regulation of cytokine secretion Source: BHF-UCL
  • positive regulation of DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of fever generation Source: BHF-UCL
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of hair follicle development Source: Ensembl
  • positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  • positive regulation of humoral immune response mediated by circulating immunoglobulin Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  • positive regulation of interferon-gamma production Source: Ensembl
  • positive regulation of interleukin-6 production Source: Ensembl
  • positive regulation of interleukin-8 biosynthetic process Source: BHF-UCL
  • positive regulation of interleukin-8 production Source: UniProtKB
  • positive regulation of JUN kinase activity Source: UniProtKB
  • positive regulation of leukocyte adhesion to arterial endothelial cell Source: BHF-UCL
  • positive regulation of leukocyte adhesion to vascular endothelial cell Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • positive regulation of mononuclear cell migration Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of NIK/NF-kappaB signaling Source: UniProtKB
  • positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  • positive regulation of osteoclast differentiation Source: BHF-UCL
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of phagocytosis Source: AgBase
  • positive regulation of podosome assembly Source: BHF-UCL
  • positive regulation of programmed cell death Source: UniProtKB
  • positive regulation of protein catabolic process Source: AgBase
  • positive regulation of protein complex assembly Source: BHF-UCL
  • positive regulation of protein complex disassembly Source: UniProtKB
  • positive regulation of protein kinase activity Source: AgBase
  • positive regulation of protein kinase B signaling Source: Ensembl
  • positive regulation of protein localization to cell surface Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of protein transport Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  • positive regulation of superoxide dismutase activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription by RNA polymerase II Source: UniProtKB
  • positive regulation of translational initiation by iron Source: Ensembl
  • positive regulation of vascular smooth muscle cell proliferation Source: Ensembl
  • positive regulation of vitamin D biosynthetic process Source: BHF-UCL
  • protein import into nucleus, translocation Source: UniProtKB
  • protein kinase B signaling Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
  • receptor biosynthetic process Source: BHF-UCL
  • regulation of branching involved in salivary gland morphogenesis Source: Ensembl
  • regulation of establishment of endothelial barrier Source: UniProtKB
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  • regulation of immunoglobulin secretion Source: Ensembl
  • regulation of insulin secretion Source: BHF-UCL
  • regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
  • response to glucocorticoid Source: BHF-UCL
  • response to salt stress Source: BHF-UCL
  • response to virus Source: BHF-UCL
  • sequestering of triglyceride Source: BHF-UCL
  • tumor necrosis factor-mediated signaling pathway Source: BHF-UCL

Keywordsi

Molecular functionCytokine

Enzyme and pathway databases

ReactomeiR-HSA-381340 Transcriptional regulation of white adipocyte differentiation
R-HSA-5357786 TNFR1-induced proapoptotic signaling
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5626978 TNFR1-mediated ceramide production
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-6783783 Interleukin-10 signaling
R-HSA-6785807 Interleukin-4 and 13 signaling
R-HSA-75893 TNF signaling
SIGNORiP01375

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor
Alternative name(s):
Cachectin
TNF-alpha
Tumor necrosis factor ligand superfamily member 2
Short name:
TNF-a
Cleaved into the following 6 chains:
Gene namesi
Name:TNF
Synonyms:TNFA, TNFSF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000232810.3
HGNCiHGNC:11892 TNF
MIMi191160 gene
neXtProtiNX_P01375

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 35CytoplasmicSequence analysisAdd BLAST35
Transmembranei36 – 56Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini57 – 233ExtracellularSequence analysisAdd BLAST177

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Psoriatic arthritis (PSORAS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionAn inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy. Five types of psoriatic arthritis have been defined: asymmetrical oligoarthritis characterized by primary involvement of the small joints of the fingers or toes; asymmetrical arthritis which involves the joints of the extremities; symmetrical polyarthritis characterized by a rheumatoid like pattern that can involve hands, wrists, ankles, and feet; arthritis mutilans, which is a rare but deforming and destructive condition; arthritis of the sacroiliac joints and spine (psoriatic spondylitis).
See also OMIM:607507

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105L → S: Low activity. 1 Publication1
Mutagenesisi108R → W: Biologically inactive. 1 Publication1
Mutagenesisi112L → F: Biologically inactive. 1 Publication1
Mutagenesisi160A → V: Biologically inactive. 1 Publication1
Mutagenesisi162S → F: Biologically inactive. 1 Publication1
Mutagenesisi167V → A or D: Biologically inactive. 1 Publication1
Mutagenesisi222E → K: Biologically inactive. 1 Publication1

Organism-specific databases

DisGeNETi7124
MalaCardsiTNF
MIMi607507 phenotype
610424 phenotype
611162 phenotype
OpenTargetsiENSG00000232810
Orphaneti40050 Adult psoriatic arthritis
PharmGKBiPA435

Chemistry databases

ChEMBLiCHEMBL1825
DrugBankiDB05250 681323
DB00051 Adalimumab
DB04956 Afelimomab
DB05879 AME-527
DB01427 Amrinone
DB05676 Apremilast
DB05066 AV411
DB08904 Certolizumab pegol
DB00608 Chloroquine
DB01407 Clenbuterol
DB05744 CRx-139
DB05869 CTI-01
DB05758 CYT007-TNFQb
DB00668 Epinephrine
DB00005 Etanercept
DB01296 Glucosamine
DB06674 Golimumab
DB05767 HMPL-004
DB00065 Infliximab
DB02325 Isopropyl Alcohol
DB05303 OMS-103HP
DB05218 PN0621
DB08910 Pomalidomide
DB01411 Pranlukast
DB00852 Pseudoephedrine
DB05412 SCIO-469
DB05207 SD118
DB01041 Thalidomide
DB05470 VX-702
DB05017 YSIL6

Polymorphism and mutation databases

BioMutaiTNF
DMDMi135934

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000344231 – 233Tumor necrosis factor, membrane formAdd BLAST233
ChainiPRO_00004172311 – 39Intracellular domain 1Add BLAST39
ChainiPRO_00004172321 – 35Intracellular domain 2Add BLAST35
ChainiPRO_000041723350 – ?C-domain 1
ChainiPRO_000041723452 – ?C-domain 2
ChainiPRO_000003442477 – 233Tumor necrosis factor, soluble form1 PublicationAdd BLAST157

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Phosphoserine; by CK1Curated1
Lipidationi19N6-myristoyl lysine1 Publication1
Lipidationi20N6-myristoyl lysine1 Publication1
Glycosylationi80O-linked (GalNAc...) serine; in soluble form1 Publication1
Disulfide bondi145 ↔ 177

Post-translational modificationi

The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space.3 Publications
The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.2 Publications
O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei35 – 36Cleavage; by SPPL2A or SPPL2B2
Sitei39 – 40Cleavage; by SPPL2A or SPPL2B2
Sitei49 – 50Cleavage; by SPPL2A or SPPL2B2
Sitei51 – 52Cleavage; by SPPL2A or SPPL2B2
Sitei76 – 77Cleavage; by ADAM172

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP01375
PeptideAtlasiP01375
PRIDEiP01375
ProteomicsDBi12707
51379

PTM databases

GlyConnecti609
iPTMnetiP01375
PhosphoSitePlusiP01375
SwissPalmiP01375
UniCarbKBiP01375

Miscellaneous databases

PMAP-CutDBiP01375

Expressioni

Gene expression databases

BgeeiENSG00000232810
CleanExiHS_TNF
ExpressionAtlasiP01375 baseline and differential
GenevisibleiP01375 HS

Interactioni

Subunit structurei

Homotrimer. Interacts with SPPL2B.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • protease binding Source: BHF-UCL
  • tumor necrosis factor receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112979, 103 interactors
CORUMiP01375
DIPiDIP-2895N
IntActiP01375, 81 interactors
MINTiP01375
STRINGi9606.ENSP00000398698

Chemistry databases

BindingDBiP01375

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi89 – 94Combined sources6
Beta strandi96 – 98Combined sources3
Beta strandi99 – 101Combined sources3
Beta strandi104 – 106Combined sources3
Beta strandi108 – 110Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi123 – 125Combined sources3
Beta strandi128 – 143Combined sources16
Beta strandi146 – 148Combined sources3
Beta strandi152 – 159Combined sources8
Beta strandi161 – 163Combined sources3
Beta strandi166 – 174Combined sources9
Beta strandi177 – 179Combined sources3
Beta strandi182 – 185Combined sources4
Beta strandi189 – 202Combined sources14
Beta strandi207 – 213Combined sources7
Helixi215 – 217Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi225 – 232Combined sources8

3D structure databases

ProteinModelPortaliP01375
SMRiP01375
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01375

Family & Domainsi

Sequence similaritiesi

Belongs to the tumor necrosis factor family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410ISAN Eukaryota
ENOG410YQC4 LUCA
GeneTreeiENSGT00530000062992
HOGENOMiHOG000048729
HOVERGENiHBG012516
InParanoidiP01375
KOiK03156
OMAiPWYEPIY
OrthoDBiEOG091G0HIG
PhylomeDBiP01375
TreeFamiTF332169

Family and domain databases

Gene3Di2.60.120.40, 1 hit
InterProiView protein in InterPro
IPR006053 TNF
IPR002959 TNF_alpha
IPR021184 TNF_CS
IPR006052 TNF_dom
IPR008983 Tumour_necrosis_fac-like_dom
PANTHERiPTHR11471:SF23 PTHR11471:SF23, 1 hit
PfamiView protein in Pfam
PF00229 TNF, 1 hit
PRINTSiPR01234 TNECROSISFCT
PR01235 TNFALPHA
SMARTiView protein in SMART
SM00207 TNF, 1 hit
SUPFAMiSSF49842 SSF49842, 1 hit
PROSITEiView protein in PROSITE
PS00251 TNF_1, 1 hit
PS50049 TNF_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P01375-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTESMIRDV ELAEEALPKK TGGPQGSRRC LFLSLFSFLI VAGATTLFCL
60 70 80 90 100
LHFGVIGPQR EEFPRDLSLI SPLAQAVRSS SRTPSDKPVA HVVANPQAEG
110 120 130 140 150
QLQWLNRRAN ALLANGVELR DNQLVVPSEG LYLIYSQVLF KGQGCPSTHV
160 170 180 190 200
LLTHTISRIA VSYQTKVNLL SAIKSPCQRE TPEGAEAKPW YEPIYLGGVF
210 220 230
QLEKGDRLSA EINRPDYLDF AESGQVYFGI IAL
Length:233
Mass (Da):25,644
Last modified:July 21, 1986 - v1
Checksum:i3DF90F96C9031FFE
GO

Sequence cautioni

The sequence AAF71992 differs from that shown. Reason: Frameshift at positions 91 and 157.Curated
The sequence CAA75070 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63F → S in AAA61198 (PubMed:3856324).Curated1
Sequence conflicti84 – 86PSD → VNR in AAF71992 (Ref. 17) Curated3
Sequence conflicti183E → R in AAC03542 (Ref. 16) Curated1

Polymorphismi

Genetic variations in TNF influence susceptibility to hepatitis B virus (HBV) infection [MIMi:610424].
Genetic variations in TNF are involved in susceptibility to malaria [MIMi:611162].

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01937884P → L1 PublicationCorresponds to variant dbSNP:rs4645843Ensembl.1
Natural variantiVAR_01192794A → T. Corresponds to variant dbSNP:rs1800620Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16441 Genomic DNA Translation: AAA61200.1
X02910 Genomic DNA Translation: CAA26669.1
X01394 mRNA Translation: CAA25650.1
M10988 mRNA Translation: AAA61198.1
M26331 Genomic DNA Translation: AAA36758.1
Z15026 Genomic DNA Translation: CAA78745.1
Y14768 Genomic DNA Translation: CAA75070.1 Sequence problems.
AF129756 Genomic DNA Translation: AAD18091.1
BA000025 Genomic DNA Translation: BAB63396.1
AB088112 Genomic DNA Translation: BAC54944.1
AY066019 Genomic DNA Translation: AAL47581.1
AY214167 Genomic DNA Translation: AAO21132.1
BC028148 mRNA Translation: AAH28148.1
AF043342 mRNA Translation: AAC03542.1
AF098751 mRNA Translation: AAF71992.1 Frameshift.
CCDSiCCDS4702.1
PIRiA93585 QWHUN
RefSeqiNP_000585.2, NM_000594.3
UniGeneiHs.241570

Genome annotation databases

EnsembliENST00000376122; ENSP00000365290; ENSG00000204490
ENST00000383496; ENSP00000372988; ENSG00000206439
ENST00000412275; ENSP00000392858; ENSG00000228321
ENST00000420425; ENSP00000410668; ENSG00000228849
ENST00000443707; ENSP00000389492; ENSG00000230108
ENST00000448781; ENSP00000389490; ENSG00000223952
ENST00000449264; ENSP00000398698; ENSG00000232810
GeneIDi7124
KEGGihsa:7124

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTNFA_HUMAN
AccessioniPrimary (citable) accession number: P01375
Secondary accession number(s): O43647, Q9P1Q2, Q9UIV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 18, 2018
This is version 238 of the entry and version 1 of the sequence. See 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, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

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