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P48023 (TNFL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor ligand superfamily member 6
Alternative name(s):
Apoptosis antigen ligand
Short name=APTL
CD95 ligand
Short name=CD95-L
Fas antigen ligand
Short name=Fas ligand
Short name=FasL
CD_antigen=CD178

Cleaved into the following 4 chains:

  1. Tumor necrosis factor ligand superfamily member 6, membrane form
  2. Tumor necrosis factor ligand superfamily member 6, soluble form
    Alternative name(s):
    Receptor-binding FasL ectodomain
    Soluble Fas ligand
    Short name=sFasL
  3. ADAM10-processed FasL form
    Short name=APL
  4. FasL intracellular domain
    Short name=FasL ICD
    Alternative name(s):
    SPPL2A-processed FasL form
    Short name=SPA
Gene names
Name:FASLG
Synonyms:APT1LG1, CD95L, FASL, TNFSF6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. May be involved in cytotoxic T-cell mediated apoptosis and in T-cell development. TNFRSF6/FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. Binding to the decoy receptor TNFRSF6B/DcR3 modulates its effects. Ref.12

The FasL intracellular domain (FasL ICD) cytoplasmic form induces gene transcription inhibition. Ref.12

Subunit structure

Homotrimer Probable. Interacts with ARHGAP9, BAIAP2L1, BTK, CACNB3, CACNB4, CRK, DLG2, DNMBP, DOCK4, EPS8L3, FGR, FYB, FYN, HCK, ITK, ITSN2, KALRN, LYN, MACC1, MIA, MPP4, MYO15A, NCF1, NCK1, NCK2, NCKIPSD, OSTF1, PIK3R1, PSTPIP1, RIMBP3C, SAMSN1, SH3GL3, SH3PXD2B, SH3PXD2A, SH3RF2, SKAP2, SNX33, SNX9, SORBS3, SPTA1, SRC, SRGAP1, SRGAP2, SRGAP3, TEC, TJP3 and YES1. Ref.13 Ref.14

Subcellular location

Cell membrane; Single-pass type II membrane protein. Cytoplasmic vesicle lumen. Lysosome lumen. Note: Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination. Colocalizes with the SPPL2A protease at the cell membrane. Ref.12 Ref.13

Tumor necrosis factor ligand superfamily member 6, soluble form: Secreted By similarity. Note: May be released into the extracellular fluid, probably by cleavage form the cell surface By similarity. Ref.12 Ref.13

FasL intracellular domain: Nucleus. Note: The FasL ICD cytoplasmic form is translocated into the nucleus. Ref.12 Ref.13

Post-translational modification

The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form undergoes two successive intramembrane proteolytic cleavages. The first one is processed by ADAM10 producing an N-terminal fragment, which lacks the receptor-binding extracellular domain. This ADAM10-processed FasL (FasL APL) remnant form is still membrane anchored and further processed by SPPL2A that liberates the FasL intracellular domain (FasL ICD). FasL shedding by ADAM10 is a prerequisite for subsequent intramembrane cleavage by SPPL2A in T-cells.

N-glycosylated.

Phosphorylated by FGR on tyrosine residues; this is required for ubiquitination and subsequent internalization. Ref.13

Monoubiquitinated.

Involvement in disease

Autoimmune lymphoproliferative syndrome 1B (ALPS1B) [MIM:601859]: A disorder of apoptosis that manifests in early childhood and results in the accumulation of autoreactive lymphocytes. It is characterized by non-malignant lymphadenopathy with hepatosplenomegaly, and autoimmune hemolytic anemia, thrombocytopenia and neutropenia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the tumor necrosis factor family.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasmic vesicle
Lysosome
Membrane
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionCytokine
Repressor
   PTMDisulfide bond
Glycoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell apoptotic process

Inferred from direct assay PubMed 17076679. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 18293083. Source: BHF-UCL

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Inferred from direct assay PubMed 11101870. Source: BHF-UCL

cell-cell signaling

Traceable author statement Ref.2. Source: ProtInc

cellular chloride ion homeostasis

Inferred from electronic annotation. Source: Ensembl

endosomal lumen acidification

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 22891283. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from direct assay PubMed 18835034. Source: BHF-UCL

immune response

Inferred from electronic annotation. Source: InterPro

inflammatory cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

necroptotic process

Inferred from direct assay PubMed 11101870. Source: BHF-UCL

necroptotic signaling pathway

Inferred from direct assay PubMed 11101870. Source: BHF-UCL

negative regulation of angiogenesis

Inferred from direct assay PubMed 18835034. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 21625644. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 18835034. Source: BHF-UCL

positive regulation of epidermal growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement. Source: Reactome

response to growth factor

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

retinal cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.2. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

cytoplasmic membrane-bounded vesicle lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 18835034. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 17076679. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

lysosomal lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12198154PubMed 12887920PubMed 16318909PubMed 16498403PubMed 17761170Ref.14PubMed 21803845. Source: IntAct

receptor binding

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48023-1)

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.
Isoform 2 (identifier: P48023-2)

The sequence of this isoform differs from the canonical sequence as follows:
     117-127: STSQMHTASSL → ATPVHPLKKRS
     128-281: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Tumor necrosis factor ligand superfamily member 6, membrane form
PRO_0000034500
Chain1 – 129129ADAM10-processed FasL form
PRO_0000417152
Chain1 – 8181FasL intracellular domain
PRO_0000416842
Chain130 – 281152Tumor necrosis factor ligand superfamily member 6, soluble form
PRO_0000034501

Regions

Topological domain1 – 8080Cytoplasmic Potential
Transmembrane81 – 10222Helical; Signal-anchor for type II membrane protein; Potential
Topological domain103 – 281179Extracellular Potential
Compositional bias4 – 7067Pro-rich
Compositional bias45 – 6521Poly-Pro

Sites

Site81 – 822Cleavage; by SPPL2A Probable
Site129 – 1302Cleavage; by ADAM10 Probable

Amino acid modifications

Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Disulfide bond202 ↔ 233 Potential

Natural variations

Alternative sequence117 – 12711STSQMHTASSL → ATPVHPLKKRS in isoform 2.
VSP_006443
Alternative sequence128 – 281154Missing in isoform 2.
VSP_006444
Natural variant1891Y → S.
Corresponds to variant rs12079514 [ dbSNP | Ensembl ].
VAR_052583

Experimental info

Mutagenesis2061P → D, F or R: Lowers binding to TNFRSF6 and reduces cytotoxicity more than 100-fold. Ref.10
Mutagenesis2181Y → F or R: Lowers binding to TNFRSF6 and abolishes cytotoxicity. Ref.10
Mutagenesis2751F → L: Abolishes binding to TNRFSF6 and cytotoxicity. Ref.10

Secondary structure

............................ 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A8A6EB358246E9BB

FASTA28131,485
        10         20         30         40         50         60 
MQQPFNYPYP QIYWVDSSAS SPWAPPGTVL PCPTSVPRRP GQRRPPPPPP PPPLPPPPPP 

        70         80         90        100        110        120 
PPLPPLPLPP LKKRGNHSTG LCLLVMFFMV LVALVGLGLG MFQLFHLQKE LAELRESTSQ 

       130        140        150        160        170        180 
MHTASSLEKQ IGHPSPPPEK KELRKVAHLT GKSNSRSMPL EWEDTYGIVL LSGVKYKKGG 

       190        200        210        220        230        240 
LVINETGLYF VYSKVYFRGQ SCNNLPLSHK VYMRNSKYPQ DLVMMEGKMM SYCTTGQMWA 

       250        260        270        280 
RSSYLGAVFN LTSADHLYVN VSELSLVNFE ESQTFFGLYK L 

« Hide

Isoform 2 [UniParc].

Checksum: F617D96B26B8E3BA
Show »

FASTA12714,006

References

« Hide 'large scale' references
[1]"Fas ligand mediates activation-induced cell death in human T lymphocytes."
Alderson M.
J. Exp. Med. 181:71-77(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Human Fas ligand: gene structure, chromosomal location and species specificity."
Takahashi T., Tanaka M., Inazawa J., Abe T., Suda T., Nagata S.
Int. Immunol. 6:1567-1574(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Schaetzlein C.E., Poehlmann R., Philippsen P., Eibel H.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Role of Fas ligand in apoptosis induced by hepatitis C virus infection."
Mita E., Hayashi N., Iio S., Takehara T., Hijioka T., Kasahara A., Fusamoto H., Kamada T.
Biochem. Biophys. Res. Commun. 204:468-474(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Isolation and characterization of a new naturally occurring variant of human Fas ligand that is expressed only in membrane bound form."
Zeytun A., Nagarkatti M., Nagarkatti P.S.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Leukocyte.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Blood.
[8]Matsumura M., Nakanishi Y., Ohba Y.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
Tissue: Blood.
[9]"Fas ligand mutation in a patient with systemic lupus erythematosus and lymphoproliferative disease."
Wu J., Wilson J., He J., Xiang L., Schur P.H., Mountz J.D.
J. Clin. Invest. 98:1107-1113(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ALPS1B.
[10]"Characterization of Fas (Apo-1, CD95)-Fas ligand interaction."
Schneider P., Bodmer J.-L., Holler N., Mattmann C., Scuderi P., Terskikh A., Peitsch M.C., Tschopp J.
J. Biol. Chem. 272:18827-18833(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF PRO-206; TYR-218 AND PHE-275.
[11]"Downregulation of Fas ligand by shedding."
Tanaka M., Itai T., Adachi M., Nagata S.
Nat. Med. 4:31-36(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[12]"The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells."
Kirkin V., Cahuzac N., Guardiola-Serrano F., Huault S., Luckerath K., Friedmann E., Novac N., Wels W.S., Martoglio B., Hueber A.O., Zornig M.
Cell Death Differ. 14:1678-1687(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF FASL INTRACELLULAR DOMAIN, CLEAVAGE BY ADAM10 AND SPPL2A, SUBCELLULAR LOCATION.
[13]"Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation."
Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G., Griffiths G.M.
J. Cell Sci. 120:191-199(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, PHOSPHORYLATION, INTERACTION WITH FGR; FYN AND LYN, SUBCELLULAR LOCATION.
[14]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP9; BAIAP2L1; BTK; CACNB3; CACNB4; CRK; DLG2; DNMBP; DOCK4; EPS8L3; FYB; FYN; HCK; ITK; ITSN2; KALRN; LYN; MACC1; MIA; MPP4; MYO15A; NCF1; NCK1; NCK2; NCKIPSD; OSTF1; PIK3R1; PSTPIP1; RIMBP3C; SAMSN1; SH3GL3; SH3PXD2B; SH3PXD2A; SH3RF2; SKAP2; SNX33; SNX9; SORBS3; SPTA1; SRC; SRGAP1; SRGAP2; SRGAP3; TEC; TJP3 AND YES1.
+Additional computationally mapped references.

Web resources

FASLGbase

FASLG mutation db

Wikipedia

FAS-ligand entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08137 mRNA. Translation: AAC50071.1.
U11821 mRNA. Translation: AAC50124.1.
X89102 mRNA. Translation: CAA61474.1.
D38122 mRNA. Translation: BAA07320.1.
AF288573 mRNA. Translation: AAG60017.1.
Z96050 Genomic DNA. Translation: CAB09424.1.
BC017502 mRNA. Translation: AAH17502.1.
AB013303 Genomic DNA. Translation: BAA32542.1.
CCDSCCDS1304.1. [P48023-1]
PIRI38707.
RefSeqNP_000630.1. NM_000639.1. [P48023-1]
UniGeneHs.2007.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZImodel-B/C1-281[»]
4MSVX-ray2.50A130-281[»]
ProteinModelPortalP48023.
SMRP48023. Positions 143-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106852. 75 interactions.
DIPDIP-2997N.
IntActP48023. 61 interactions.
MINTMINT-238167.
STRING9606.ENSP00000356694.

Chemistry

ChEMBLCHEMBL5714.

Polymorphism databases

DMDM1345957.

Proteomic databases

PaxDbP48023.
PRIDEP48023.

Protocols and materials databases

DNASU356.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340030; ENSP00000344739; ENSG00000117560. [P48023-2]
ENST00000367721; ENSP00000356694; ENSG00000117560. [P48023-1]
GeneID356.
KEGGhsa:356.
UCSCuc001gis.3. human. [P48023-1]
uc001git.3. human. [P48023-2]

Organism-specific databases

CTD356.
GeneCardsGC01P172628.
GeneReviewsFASLG.
HGNCHGNC:11936. FASLG.
HPACAB011435.
MIM134638. gene.
601859. phenotype.
neXtProtNX_P48023.
Orphanet3261. Autoimmune lymphoproliferative syndrome.
PharmGKBPA56.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42315.
HOGENOMHOG000290680.
HOVERGENHBG055128.
InParanoidP48023.
KOK04389.
OMAHLTGKPN.
OrthoDBEOG7V4B0Q.
PhylomeDBP48023.
TreeFamTF332169.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP48023.
BgeeP48023.
CleanExHS_FASLG.
GenevestigatorP48023.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR028326. FASL.
IPR006053. TNF.
IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00229. TNF. 1 hit.
[Graphical view]
PRINTSPR01681. FASLIGAND.
PR01234. TNECROSISFCT.
SMARTSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFas_ligand.
GenomeRNAi356.
NextBio1489.
PMAP-CutDBP48023.
PROP48023.
SOURCESearch...

Entry information

Entry nameTNFL6_HUMAN
AccessionPrimary (citable) accession number: P48023
Secondary accession number(s): Q9BZP9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries