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P50591

- TNF10_HUMAN

UniProt

P50591 - TNF10_HUMAN

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Protein

Tumor necrosis factor ligand superfamily member 10

Gene

TNFSF10

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

Functioni

Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.

Cofactori

Zn2+Note: Binds 1 zinc ion per trimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi230 – 2301Zinc

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. receptor binding Source: ProtInc

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  2. apoptotic process Source: Reactome
  3. apoptotic signaling pathway Source: Reactome
  4. cell-cell signaling Source: ProtInc
  5. immune response Source: InterPro
  6. male gonad development Source: Ensembl
  7. positive regulation of apoptotic process Source: UniProtKB
  8. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  9. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  11. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  12. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
  13. response to insulin Source: Ensembl
  14. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1503. Caspase-8 activation by cleavage.
REACT_164011. Regulation by c-FLIP.
REACT_402. TRAIL signaling.
REACT_832. Dimerization of procaspase-8.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor ligand superfamily member 10
Alternative name(s):
Apo-2 ligand
Short name:
Apo-2L
TNF-related apoptosis-inducing ligand
Short name:
Protein TRAIL
CD_antigen: CD253
Gene namesi
Name:TNFSF10
Synonyms:APO2L, TRAIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:11925. TNFSF10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei18 – 3821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini39 – 281243ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProt
  4. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36618.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Tumor necrosis factor ligand superfamily member 10PRO_0000185503Add
BLAST

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP50591.
PaxDbiP50591.
PRIDEiP50591.

PTM databases

PhosphoSiteiP50591.

Expressioni

Tissue specificityi

Widespread; most predominant in spleen, lung and prostate.

Gene expression databases

BgeeiP50591.
CleanExiHS_TNFSF10.
ExpressionAtlasiP50591. baseline and differential.
GenevestigatoriP50591.

Organism-specific databases

HPAiCAB002446.

Interactioni

Subunit structurei

Homotrimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL3Q136182EBI-495373,EBI-456129
TNFRSF10AO002204EBI-495373,EBI-518861
TNFRSF10BO1476321EBI-495373,EBI-518882

Protein-protein interaction databases

BioGridi114280. 14 interactions.
DIPiDIP-6230N.
IntActiP50591. 17 interactions.
MINTiMINT-109168.
STRINGi9606.ENSP00000241261.

Structurei

Secondary structure

1
281
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi123 – 1275Combined sources
Turni137 – 1393Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1503Combined sources
Turni158 – 1614Combined sources
Beta strandi163 – 1708Combined sources
Beta strandi173 – 1786Combined sources
Beta strandi180 – 19314Combined sources
Beta strandi205 – 2139Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi220 – 2289Combined sources
Beta strandi237 – 25014Combined sources
Beta strandi255 – 2628Combined sources
Helixi263 – 2653Combined sources
Turni270 – 2723Combined sources
Beta strandi273 – 2797Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0GX-ray2.40A/B/D114-281[»]
1D2QX-ray2.80A/B114-281[»]
1D4VX-ray2.20B119-281[»]
1DG6X-ray1.30A91-281[»]
1DU3X-ray2.20D/E/F/J/K/L114-281[»]
4N90X-ray3.30A/B/C114-281[»]
ProteinModelPortaliP50591.
SMRiP50591. Positions 119-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50591.

Family & Domainsi

Sequence similaritiesi

Belongs to the tumor necrosis factor family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46547.
GeneTreeiENSGT00530000063443.
HOGENOMiHOG000230484.
HOVERGENiHBG059007.
InParanoidiP50591.
KOiK04721.
OMAiQTCVLIL.
PhylomeDBiP50591.
TreeFamiTF332169.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR017355. TNF_ligand_10/11.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00229. TNF. 1 hit.
[Graphical view]
PIRSFiPIRSF038013. TNF10_TNF11. 1 hit.
SMARTiSM00207. TNF. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50591-1) [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
MAMMEVQGGP SLGQTCVLIV IFTVLLQSLC VAVTYVYFTN ELKQMQDKYS
60 70 80 90 100
KSGIACFLKE DDSYWDPNDE ESMNSPCWQV KWQLRQLVRK MILRTSEETI
110 120 130 140 150
STVQEKQQNI SPLVRERGPQ RVAAHITGTR GRSNTLSSPN SKNEKALGRK
160 170 180 190 200
INSWESSRSG HSFLSNLHLR NGELVIHEKG FYYIYSQTYF RFQEEIKENT
210 220 230 240 250
KNDKQMVQYI YKYTSYPDPI LLMKSARNSC WSKDAEYGLY SIYQGGIFEL
260 270 280
KENDRIFVSV TNEHLIDMDH EASFFGAFLV G
Length:281
Mass (Da):32,509
Last modified:October 1, 1996 - v1
Checksum:iDDAAAF78DAAB2F6D
GO
Isoform 2 (identifier: P50591-2) [UniParc]FASTAAdd to Basket

Also known as: TRAIL-short, TRAIL-s

The sequence of this isoform differs from the canonical sequence as follows:
     91-101: MILRTSEETIS → TPRMKRLWAAK
     102-281: Missing.

Note: Induced upon HIV infection, antagonizes signaling via TRAIL receptor R2 (TNFRSF10B).

Show »
Length:101
Mass (Da):11,746
Checksum:i205B6BA004A7C104
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331V → I.
Corresponds to variant rs6763816 [ dbSNP | Ensembl ].
VAR_052584
Natural varianti47 – 471D → E.
Corresponds to variant rs16845759 [ dbSNP | Ensembl ].
VAR_052585

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei91 – 10111MILRTSEETIS → TPRMKRLWAAK in isoform 2. 3 PublicationsVSP_043507Add
BLAST
Alternative sequencei102 – 281180Missing in isoform 2. 3 PublicationsVSP_043508Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37518 mRNA. Translation: AAC50332.1.
U57059 mRNA. Translation: AAB01233.1.
DQ848564 mRNA. Translation: ABI24016.1.
EU183231 mRNA. Translation: ABW24658.1.
AK296085 mRNA. Translation: BAG58840.1.
AC007919 Genomic DNA. No translation available.
AC016938 Genomic DNA. No translation available.
BC032722 mRNA. Translation: AAH32722.1.
CCDSiCCDS3219.1. [P50591-1]
CCDS54680.1. [P50591-2]
RefSeqiNP_001177871.1. NM_001190942.1. [P50591-2]
NP_003801.1. NM_003810.3. [P50591-1]
UniGeneiHs.478275.

Genome annotation databases

EnsembliENST00000241261; ENSP00000241261; ENSG00000121858. [P50591-1]
ENST00000420541; ENSP00000389931; ENSG00000121858. [P50591-2]
GeneIDi8743.
KEGGihsa:8743.
UCSCiuc003fid.3. human. [P50591-1]
uc003fie.3. human. [P50591-2]

Polymorphism databases

DMDMi1730015.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37518 mRNA. Translation: AAC50332.1 .
U57059 mRNA. Translation: AAB01233.1 .
DQ848564 mRNA. Translation: ABI24016.1 .
EU183231 mRNA. Translation: ABW24658.1 .
AK296085 mRNA. Translation: BAG58840.1 .
AC007919 Genomic DNA. No translation available.
AC016938 Genomic DNA. No translation available.
BC032722 mRNA. Translation: AAH32722.1 .
CCDSi CCDS3219.1. [P50591-1 ]
CCDS54680.1. [P50591-2 ]
RefSeqi NP_001177871.1. NM_001190942.1. [P50591-2 ]
NP_003801.1. NM_003810.3. [P50591-1 ]
UniGenei Hs.478275.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D0G X-ray 2.40 A/B/D 114-281 [» ]
1D2Q X-ray 2.80 A/B 114-281 [» ]
1D4V X-ray 2.20 B 119-281 [» ]
1DG6 X-ray 1.30 A 91-281 [» ]
1DU3 X-ray 2.20 D/E/F/J/K/L 114-281 [» ]
4N90 X-ray 3.30 A/B/C 114-281 [» ]
ProteinModelPortali P50591.
SMRi P50591. Positions 119-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114280. 14 interactions.
DIPi DIP-6230N.
IntActi P50591. 17 interactions.
MINTi MINT-109168.
STRINGi 9606.ENSP00000241261.

Chemistry

BindingDBi P50591.
ChEMBLi CHEMBL5813.

PTM databases

PhosphoSitei P50591.

Polymorphism databases

DMDMi 1730015.

Proteomic databases

MaxQBi P50591.
PaxDbi P50591.
PRIDEi P50591.

Protocols and materials databases

DNASUi 8743.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000241261 ; ENSP00000241261 ; ENSG00000121858 . [P50591-1 ]
ENST00000420541 ; ENSP00000389931 ; ENSG00000121858 . [P50591-2 ]
GeneIDi 8743.
KEGGi hsa:8743.
UCSCi uc003fid.3. human. [P50591-1 ]
uc003fie.3. human. [P50591-2 ]

Organism-specific databases

CTDi 8743.
GeneCardsi GC03M172223.
HGNCi HGNC:11925. TNFSF10.
HPAi CAB002446.
MIMi 603598. gene.
neXtProti NX_P50591.
PharmGKBi PA36618.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46547.
GeneTreei ENSGT00530000063443.
HOGENOMi HOG000230484.
HOVERGENi HBG059007.
InParanoidi P50591.
KOi K04721.
OMAi QTCVLIL.
PhylomeDBi P50591.
TreeFami TF332169.

Enzyme and pathway databases

Reactomei REACT_1503. Caspase-8 activation by cleavage.
REACT_164011. Regulation by c-FLIP.
REACT_402. TRAIL signaling.
REACT_832. Dimerization of procaspase-8.

Miscellaneous databases

ChiTaRSi TNFSF10. human.
EvolutionaryTracei P50591.
GeneWikii TRAIL.
GenomeRNAii 8743.
NextBioi 32805.
PROi P50591.
SOURCEi Search...

Gene expression databases

Bgeei P50591.
CleanExi HS_TNFSF10.
ExpressionAtlasi P50591. baseline and differential.
Genevestigatori P50591.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR021184. TNF_CS.
IPR006052. TNF_dom.
IPR017355. TNF_ligand_10/11.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00229. TNF. 1 hit.
[Graphical view ]
PIRSFi PIRSF038013. TNF10_TNF11. 1 hit.
SMARTi SM00207. TNF. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a new member of the TNF family that induces apoptosis."
    Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K., Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G.
    Immunity 3:673-682(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family."
    Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A.
    J. Biol. Chem. 271:12687-12690(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  4. "Novel TRAIL splice variant TRAIL-delta."
    Woods D.C., Haugen M.J., Johnson A.L.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thalamus.
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(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: Lymph.
  8. Cited for: PHOSPHORYLATION.
  9. "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5."
    Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., Kelley R.F., Ashkenazi A., de Vos A.M.
    Mol. Cell 4:563-571(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 114-281.
  10. "Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation."
    Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y., Screaton G.R.
    Nat. Struct. Biol. 6:1048-1053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 119-281.
  11. "2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity."
    Cha S.-S., Kim M.S., Choi Y.H., Sung B.J., Shin N.K., Shin H.C., Sung Y.C., Oh B.-H.
    Immunity 11:253-261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-281.

Entry informationi

Entry nameiTNF10_HUMAN
AccessioniPrimary (citable) accession number: P50591
Secondary accession number(s): A1Y9B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 150 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, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3