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Q92844 (TANK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TRAF family member-associated NF-kappa-B activator
Alternative name(s):
TRAF-interacting protein
Short name=I-TRAF
Gene names
Name:TANK
Synonyms:ITRAF, TRAF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.15

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.15

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated by IKBKE. Ref.8

Sequence similarities

Contains 1 C2H2-type zinc finger.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q92844-1)

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 Short (identifier: Q92844-2)

The sequence of this isoform differs from the canonical sequence as follows:
     111-117: RRQEVSS → DIASAES
     118-425: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q92844-3)

The sequence of this isoform differs from the canonical sequence as follows:
     111-119: RRQEVSSPR → DIASAESSI
     120-425: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425TRAF family member-associated NF-kappa-B activator
PRO_0000072427

Regions

Zinc finger394 – 42027C2H2-type
Region133 – 17240Interaction with TBK1 and IKBKE By similarity
Region172 – 19120TRAF family member interaction
Coiled coil22 – 6241 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue1261Phosphoserine Ref.13
Modified residue1291Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue3411Phosphoserine Ref.13
Modified residue3541Phosphoserine Ref.13
Modified residue3571Phosphoserine Ref.12 Ref.13

Natural variations

Alternative sequence111 – 1199RRQEVSSPR → DIASAESSI in isoform 3.
VSP_043702
Alternative sequence111 – 1177RRQEVSS → DIASAES in isoform Short.
VSP_004442
Alternative sequence118 – 425308Missing in isoform Short.
VSP_004443
Alternative sequence120 – 425306Missing in isoform 3.
VSP_043703
Natural variant2921G → R.
Corresponds to variant rs10183668 [ dbSNP | Ensembl ].
VAR_051409
Natural variant3581P → L.
Corresponds to variant rs2229759 [ dbSNP | Ensembl ].
VAR_051410
Natural variant3941R → Q.
Corresponds to variant rs3769969 [ dbSNP | Ensembl ].
VAR_051411

Experimental info

Mutagenesis1821Q → A: Abolishes interaction with TRAF2 and TRAF3. Ref.17
Mutagenesis1841T → A: Abolishes interaction with TRAF2 and TRAF3. Ref.17
Mutagenesis1851D → A: Abolishes interaction with TRAF2; greatly diminishes interaction with TRAF3. Ref.17
Mutagenesis1881D → A: Diminishes interaction with TRAF2 and TRAF3. Ref.17
Mutagenesis1941F → A: Diminishes interaction with TRAF2 and TRAF3. Ref.17
Sequence conflict831E → D in AAC50681. Ref.1
Sequence conflict881N → T in AAC50681. Ref.1
Sequence conflict921D → A in AAC50681. Ref.1
Sequence conflict1421F → S in AAC50681. Ref.1
Sequence conflict1951K → T in AAC50681. Ref.1
Sequence conflict2261F → L in AAC50681. Ref.1
Sequence conflict3031L → P in AAC50770. Ref.2

Secondary structure

... 425
Helix Strand Turn

Details...

Sequences

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

Last modified April 3, 2007. Version 2.
Checksum: 718D30CF03EB27FF

FASTA42547,816
        10         20         30         40         50         60 
MDKNIGEQLN KAYEAFRQAC MDRDSAVKEL QQKTENYEQR IREQQEQLSL QQTIIDKLKS 

        70         80         90        100        110        120 
QLLLVNSTQD NNYGCVPLLE DSETRKNNLT LDQPQDKVIS GIAREKLPKV RRQEVSSPRK 

       130        140        150        160        170        180 
ETSARSLGSP LLHERGNIEK TFWDLKEEFH KICMLAKAQK DHLSKLNIPD TATETQCSVP 

       190        200        210        220        230        240 
IQCTDKTDKQ EALFKPQAKD DINRGAPSIT SVTPRGLCRD EEDTSFESLS KFNVKFPPMD 

       250        260        270        280        290        300 
NDSTFLHSTP ERPGILSPAT SEAVCQEKFN MEFRDNPGNF VKTEETLFEI QGIDPIASAI 

       310        320        330        340        350        360 
QNLKTTDKTK PSNLVNTCIR TTLDRAACLP PGDHNALYVN SFPLLDPSDA PFPSLDSPGK 

       370        380        390        400        410        420 
AIRGPQQPIW KPFPNQDSDS VVLSGTDSEL HIPRVCEFCQ AVFPPSITSR GDFLRHLNSH 


FNGET 

« Hide

Isoform Short [UniParc].

Checksum: 22A8BEC63333011C
Show »

FASTA11713,426
Isoform 3 [UniParc].

Checksum: 61E5B2A8BEC63333
Show »

FASTA11913,626

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Functional dissection of the TBK1 molecular network."
Goncalves A., Burckstummer T., Dixit E., Scheicher R., Gorna M.W., Karayel E., Sugar C., Stukalov A., Berg T., Kralovics R., Planyavsky M., Bennett K.L., Colinge J., Superti-Furga G.
PLoS ONE 6:E23971-E23971(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TBK1.
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2215.1. [Q92844-1]
CCDS46436.1. [Q92844-3]
RefSeqNP_001186064.1. NM_001199135.1. [Q92844-1]
NP_004171.2. NM_004180.2. [Q92844-1]
NP_597841.1. NM_133484.1. [Q92844-3]
UniGeneHs.132257.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZZX-ray3.50B177-187[»]
1L0AX-ray2.90B178-195[»]
ProteinModelPortalQ92844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115328. 39 interactions.
DIPDIP-27516N.
IntActQ92844. 30 interactions.
MINTMINT-111947.
STRING9606.ENSP00000259075.

PTM databases

PhosphoSiteQ92844.

Polymorphism databases

DMDM143811466.

Proteomic databases

MaxQBQ92844.
PaxDbQ92844.
PeptideAtlasQ92844.
PRIDEQ92844.

Protocols and materials databases

DNASU10010.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259075; ENSP00000259075; ENSG00000136560. [Q92844-1]
ENST00000392749; ENSP00000376505; ENSG00000136560. [Q92844-1]
ENST00000403609; ENSP00000385983; ENSG00000136560. [Q92844-3]
ENST00000457476; ENSP00000415276; ENSG00000136560. [Q92844-3]
GeneID10010.
KEGGhsa:10010.
UCSCuc002ubq.1. human. [Q92844-3]
uc002ubr.2. human. [Q92844-1]

Organism-specific databases

CTD10010.
GeneCardsGC02P161957.
HGNCHGNC:11562. TANK.
HPACAB010345.
HPA037676.
MIM603893. gene.
neXtProtNX_Q92844.
PharmGKBPA36330.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44252.
HOGENOMHOG000231816.
HOVERGENHBG019299.
InParanoidQ92844.
KOK12650.
OMALHSTPER.
OrthoDBEOG7ZKSBN.
PhylomeDBQ92844.
TreeFamTF336453.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ92844.

Gene expression databases

ArrayExpressQ92844.
BgeeQ92844.
CleanExHS_TANK.
HS_TRAF2.
GenevestigatorQ92844.

Family and domain databases

InterProIPR024581. TBD.
[Graphical view]
PfamPF12845. TBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTANK. human.
EvolutionaryTraceQ92844.
GeneWikiTANK_(gene).
GenomeRNAi10010.
NextBio37817.
PROQ92844.
SOURCESearch...

Entry information

Entry nameTANK_HUMAN
AccessionPrimary (citable) accession number: Q92844
Secondary accession number(s): D3DPB5, Q7Z4J6, Q92885
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 139 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM