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Q92844

- TANK_HUMAN

UniProt

Q92844 - TANK_HUMAN

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Protein

TRAF family member-associated NF-kappa-B activator

Gene

TANK

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

Functioni

Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri394 – 42027C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  2. innate immune response Source: Reactome
  3. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
SignaLinkiQ92844.

Names & Taxonomyi

Protein namesi
Recommended name:
TRAF family member-associated NF-kappa-B activator
Alternative name(s):
TRAF-interacting protein
Short name:
I-TRAF
Gene namesi
Name:TANK
Synonyms:ITRAF, TRAF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11562. TANK.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi182 – 1821Q → A: Abolishes interaction with TRAF2 and TRAF3. 1 Publication
Mutagenesisi184 – 1841T → A: Abolishes interaction with TRAF2 and TRAF3. 1 Publication
Mutagenesisi185 – 1851D → A: Abolishes interaction with TRAF2; greatly diminishes interaction with TRAF3. 1 Publication
Mutagenesisi188 – 1881D → A: Diminishes interaction with TRAF2 and TRAF3. 1 Publication
Mutagenesisi194 – 1941F → A: Diminishes interaction with TRAF2 and TRAF3. 1 Publication

Organism-specific databases

PharmGKBiPA36330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425TRAF family member-associated NF-kappa-B activatorPRO_0000072427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei129 – 1291Phosphoserine3 Publications
Modified residuei341 – 3411Phosphoserine1 Publication
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei357 – 3571Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by IKBKE.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92844.
PaxDbiQ92844.
PeptideAtlasiQ92844.
PRIDEiQ92844.

PTM databases

PhosphoSiteiQ92844.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ92844.
CleanExiHS_TANK.
HS_TRAF2.
ExpressionAtlasiQ92844. baseline and differential.
GenevestigatoriQ92844.

Organism-specific databases

HPAiCAB010345.
HPA037676.

Interactioni

Subunit structurei

Homodimer. Interacts with TBK1 and IKBKE. Interacts also with TRAF1, TRAF2, and TRAF3 by binding to their TRAF-C domains; the interaction with TRAF2 is disrupted by the phosphorylation of TANK by IKBKE. Interacts more strongly with TRAF1 and TRAF2 than TRAF3. Interacts with IKBKG; the interaction is enhanced by IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APBA3O960182EBI-356349,EBI-6115839
HTTP428583EBI-356349,EBI-466029
IKBKEQ141642EBI-356349,EBI-307369
NSP034952EBI-356349,EBI-2548993From a different organism.
PLK1P533503EBI-356349,EBI-476768
SUMO1P631658EBI-356349,EBI-80140
SUMO2P619563EBI-356349,EBI-473220
TBK1Q9UHD26EBI-356349,EBI-356402
TRAF2Q129334EBI-356349,EBI-355744
TRAF3Q131144EBI-356349,EBI-357631

Protein-protein interaction databases

BioGridi115328. 40 interactions.
DIPiDIP-27516N.
IntActiQ92844. 31 interactions.
MINTiMINT-111947.
STRINGi9606.ENSP00000259075.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi191 – 1933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZZX-ray3.50B177-187[»]
1L0AX-ray2.90B178-195[»]
ProteinModelPortaliQ92844.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92844.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 17240Interaction with TBK1 and IKBKEBy similarityAdd
BLAST
Regioni172 – 19120TRAF family member interactionAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili22 – 6241Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri394 – 42027C2H2-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG44252.
GeneTreeiENSGT00390000008712.
HOGENOMiHOG000231816.
HOVERGENiHBG019299.
InParanoidiQ92844.
KOiK12650.
OMAiLHSTPER.
OrthoDBiEOG7ZKSBN.
PhylomeDBiQ92844.
TreeFamiTF336453.

Family and domain databases

InterProiIPR024581. TBD.
[Graphical view]
PfamiPF12845. TBD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q92844-1) [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
MDKNIGEQLN KAYEAFRQAC MDRDSAVKEL QQKTENYEQR IREQQEQLSL
60 70 80 90 100
QQTIIDKLKS QLLLVNSTQD NNYGCVPLLE DSETRKNNLT LDQPQDKVIS
110 120 130 140 150
GIAREKLPKV RRQEVSSPRK ETSARSLGSP LLHERGNIEK TFWDLKEEFH
160 170 180 190 200
KICMLAKAQK DHLSKLNIPD TATETQCSVP IQCTDKTDKQ EALFKPQAKD
210 220 230 240 250
DINRGAPSIT SVTPRGLCRD EEDTSFESLS KFNVKFPPMD NDSTFLHSTP
260 270 280 290 300
ERPGILSPAT SEAVCQEKFN MEFRDNPGNF VKTEETLFEI QGIDPIASAI
310 320 330 340 350
QNLKTTDKTK PSNLVNTCIR TTLDRAACLP PGDHNALYVN SFPLLDPSDA
360 370 380 390 400
PFPSLDSPGK AIRGPQQPIW KPFPNQDSDS VVLSGTDSEL HIPRVCEFCQ
410 420
AVFPPSITSR GDFLRHLNSH FNGET
Length:425
Mass (Da):47,816
Last modified:April 3, 2007 - v2
Checksum:i718D30CF03EB27FF
GO
Isoform Short (identifier: Q92844-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-117: RRQEVSS → DIASAES
     118-425: Missing.

Note: No experimental confirmation available.

Show »
Length:117
Mass (Da):13,426
Checksum:i22A8BEC63333011C
GO
Isoform 3 (identifier: Q92844-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-119: RRQEVSSPR → DIASAESSI
     120-425: Missing.

Note: No experimental confirmation available.

Show »
Length:119
Mass (Da):13,626
Checksum:i61E5B2A8BEC63333
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831E → D in AAC50681. (PubMed:8710854)Curated
Sequence conflicti88 – 881N → T in AAC50681. (PubMed:8710854)Curated
Sequence conflicti92 – 921D → A in AAC50681. (PubMed:8710854)Curated
Sequence conflicti142 – 1421F → S in AAC50681. (PubMed:8710854)Curated
Sequence conflicti195 – 1951K → T in AAC50681. (PubMed:8710854)Curated
Sequence conflicti226 – 2261F → L in AAC50681. (PubMed:8710854)Curated
Sequence conflicti303 – 3031L → P in AAC50770. (PubMed:8855313)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921G → R.
Corresponds to variant rs10183668 [ dbSNP | Ensembl ].
VAR_051409
Natural varianti358 – 3581P → L.
Corresponds to variant rs2229759 [ dbSNP | Ensembl ].
VAR_051410
Natural varianti394 – 3941R → Q.
Corresponds to variant rs3769969 [ dbSNP | Ensembl ].
VAR_051411

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei111 – 1199RRQEVSSPR → DIASAESSI in isoform 3. 1 PublicationVSP_043702
Alternative sequencei111 – 1177RRQEVSS → DIASAES in isoform Short. 1 PublicationVSP_004442
Alternative sequencei118 – 425308Missing in isoform Short. 1 PublicationVSP_004443Add
BLAST
Alternative sequencei120 – 425306Missing in isoform 3. 1 PublicationVSP_043703Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59863 mRNA. Translation: AAC50681.1.
U63830 mRNA. Translation: AAC50770.1.
BT009855 mRNA. Translation: AAP88857.1.
AC009299 Genomic DNA. No translation available.
AC009313 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11374.1.
CH471058 Genomic DNA. Translation: EAX11375.1.
CH471058 Genomic DNA. Translation: EAX11377.1.
BC003388 mRNA. Translation: AAH03388.1.
CCDSiCCDS2215.1. [Q92844-1]
CCDS46436.1. [Q92844-3]
RefSeqiNP_001186064.1. NM_001199135.1. [Q92844-1]
NP_004171.2. NM_004180.2. [Q92844-1]
NP_597841.1. NM_133484.1. [Q92844-3]
UniGeneiHs.132257.

Genome annotation databases

EnsembliENST00000259075; ENSP00000259075; ENSG00000136560. [Q92844-1]
ENST00000392749; ENSP00000376505; ENSG00000136560. [Q92844-1]
ENST00000403609; ENSP00000385983; ENSG00000136560. [Q92844-3]
GeneIDi10010.
KEGGihsa:10010.
UCSCiuc002ubq.1. human. [Q92844-3]
uc002ubr.2. human. [Q92844-1]

Polymorphism databases

DMDMi143811466.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59863 mRNA. Translation: AAC50681.1 .
U63830 mRNA. Translation: AAC50770.1 .
BT009855 mRNA. Translation: AAP88857.1 .
AC009299 Genomic DNA. No translation available.
AC009313 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11374.1 .
CH471058 Genomic DNA. Translation: EAX11375.1 .
CH471058 Genomic DNA. Translation: EAX11377.1 .
BC003388 mRNA. Translation: AAH03388.1 .
CCDSi CCDS2215.1. [Q92844-1 ]
CCDS46436.1. [Q92844-3 ]
RefSeqi NP_001186064.1. NM_001199135.1. [Q92844-1 ]
NP_004171.2. NM_004180.2. [Q92844-1 ]
NP_597841.1. NM_133484.1. [Q92844-3 ]
UniGenei Hs.132257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KZZ X-ray 3.50 B 177-187 [» ]
1L0A X-ray 2.90 B 178-195 [» ]
ProteinModelPortali Q92844.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115328. 40 interactions.
DIPi DIP-27516N.
IntActi Q92844. 31 interactions.
MINTi MINT-111947.
STRINGi 9606.ENSP00000259075.

PTM databases

PhosphoSitei Q92844.

Polymorphism databases

DMDMi 143811466.

Proteomic databases

MaxQBi Q92844.
PaxDbi Q92844.
PeptideAtlasi Q92844.
PRIDEi Q92844.

Protocols and materials databases

DNASUi 10010.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259075 ; ENSP00000259075 ; ENSG00000136560 . [Q92844-1 ]
ENST00000392749 ; ENSP00000376505 ; ENSG00000136560 . [Q92844-1 ]
ENST00000403609 ; ENSP00000385983 ; ENSG00000136560 . [Q92844-3 ]
GeneIDi 10010.
KEGGi hsa:10010.
UCSCi uc002ubq.1. human. [Q92844-3 ]
uc002ubr.2. human. [Q92844-1 ]

Organism-specific databases

CTDi 10010.
GeneCardsi GC02P161957.
HGNCi HGNC:11562. TANK.
HPAi CAB010345.
HPA037676.
MIMi 603893. gene.
neXtProti NX_Q92844.
PharmGKBi PA36330.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG44252.
GeneTreei ENSGT00390000008712.
HOGENOMi HOG000231816.
HOVERGENi HBG019299.
InParanoidi Q92844.
KOi K12650.
OMAi LHSTPER.
OrthoDBi EOG7ZKSBN.
PhylomeDBi Q92844.
TreeFami TF336453.

Enzyme and pathway databases

Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
SignaLinki Q92844.

Miscellaneous databases

ChiTaRSi TANK. human.
EvolutionaryTracei Q92844.
GeneWikii TANK_(gene).
GenomeRNAii 10010.
NextBioi 37817.
PROi Q92844.
SOURCEi Search...

Gene expression databases

Bgeei Q92844.
CleanExi HS_TANK.
HS_TRAF2.
ExpressionAtlasi Q92844. baseline and differential.
Genevestigatori Q92844.

Family and domain databases

InterProi IPR024581. TBD.
[Graphical view ]
Pfami PF12845. TBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction."
    Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.
    Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  2. "Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein."
    Kaye K.M., Devergne O., Harada J.N., Izumi K.M., Yalamanchili R., Kieff E., Mosialos G.
    Proc. Natl. Acad. Sci. U.S.A. 93:11085-11090(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM SHORT).
    Tissue: Placenta.
  7. "NF-kB activation by a signaling complex containing TRAF2, TANK, and TBK1, a novel IKK-related kinase."
    Pomerantz J.L., Baltimore D.
    EMBO J. 18:6694-6704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TBK1.
    Tissue: Spleen.
  8. "NF-kappaB activation through IKK-i-dependent I-TRAF/TANK phosphorylation."
    Nomura F., Kawai T., Nakanishi K., Akira S.
    Genes Cells 5:191-202(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2, PHOSPHORYLATION BY IKBKE.
  9. "Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases."
    Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.
    J. Biol. Chem. 277:37029-37036(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKG AND IKBKB.
  10. "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK."
    Ryzhakov G., Randow F.
    EMBO J. 26:3180-3190(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKBKE.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-129; SER-341; SER-354 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: FUNCTION, INTERACTION WITH TBK1.
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Downstream regulator TANK binds to the CD40 recognition site on TRAF3."
    Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
    Structure 10:403-411(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 174-194 IN COMPLEX WITH TRAF3, MUTAGENESIS OF GLN-182; THR-184; ASP-185; ASP-188 AND PHE-194.

Entry informationi

Entry nameiTANK_HUMAN
AccessioniPrimary (citable) accession number: Q92844
Secondary accession number(s): D3DPB5, Q7Z4J6, Q92885
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: April 3, 2007
Last modified: November 26, 2014
This is version 143 of the entry and version 2 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 chromosome 2
    Human chromosome 2: 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

External Data

Dasty 3