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Protein

TGF-beta-activated kinase 1 and MAP3K7-binding protein 3

Gene

TAB3

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

Functioni

Adapter linking MAP3K7/TAK1 and TRAF6 or TRAF2. Mediator of MAP3K7 activation, respectively in the IL1 and TNF signaling pathways. Plays a role in activation of NF-kappa-B and AP1 transcription factor. Isoform 2 may be an oncogenic factor.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri682 – 71231RanBP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-937042. IRAK2 mediated activation of TAK1 complex.
R-HSA-937072. TRAF6 mediated induction of TAK1 complex.
R-HSA-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SIGNORiQ8N5C8.

Names & Taxonomyi

Protein namesi
Recommended name:
TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
Alternative name(s):
Mitogen-activated protein kinase kinase kinase 7-interacting protein 3
NF-kappa-B-activating protein 1
TAK1-binding protein 3
Short name:
TAB-3
TGF-beta-activated kinase 1-binding protein 3
Gene namesi
Name:TAB3
Synonyms:MAP3K7IP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:30681. TAB3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • endosome membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165757406.

Polymorphism and mutation databases

BioMutaiTAB3.
DMDMi229462756.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 712711TGF-beta-activated kinase 1 and MAP3K7-binding protein 3PRO_0000226972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei60 – 601PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineCombined sources
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei385 – 3851Phosphoserine; in variant Arg-394Combined sources
Modified residuei404 – 4041PhosphothreonineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei492 – 4921PhosphoserineCombined sources
Modified residuei506 – 5061Phosphoserine; by MAPKAPK2 and MAPKAPK31 Publication

Post-translational modificationi

Ubiquitinated; following IL1 stimulation or TRAF6 overexpression.1 Publication
Phosphorylated at Ser-506 by MAPKAPK2 and MAPKAPK3 following IL1 treatment.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8N5C8.
MaxQBiQ8N5C8.
PaxDbiQ8N5C8.
PeptideAtlasiQ8N5C8.
PRIDEiQ8N5C8.

PTM databases

iPTMnetiQ8N5C8.
PhosphoSiteiQ8N5C8.

Expressioni

Tissue specificityi

Widely expressed. Constitutively overexpressed in certain tumor tissues. Isoform 1 is a major transcript while isoform 2 is a minor transcript.2 Publications

Gene expression databases

BgeeiQ8N5C8.
CleanExiHS_MAP3K7IP3.
ExpressionAtlasiQ8N5C8. baseline and differential.
GenevisibleiQ8N5C8. HS.

Organism-specific databases

HPAiHPA034980.
HPA034981.

Interactioni

Subunit structurei

Interacts with TAB1, TAB2, MAP3K7, TRAF2 and TRAF6. The minimal TAB3-containing complex (TAB1-MAP3K7-TAB3) appears not to contain TAB2. However, it seems sensible to consider that TAB2 may also join this complex and may act in a cooperative manner with TAB3. Interacts with WDR34 (via the WD domains). Interacts with RBCK1. Binds 'Lys-63'-linked polyubiquitin chains. Interacts with TRIM5.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BECN1Q144579EBI-359964,EBI-949378
CEP57L1Q8IYX8-23EBI-359964,EBI-10181988
MAP3K7O433183EBI-359964,EBI-358684
Map3k7Q620732EBI-359964,EBI-1775345From a different organism.
MAP3K7CLP57077-43EBI-359964,EBI-10215880
PIN1Q135263EBI-359964,EBI-714158

Protein-protein interaction databases

BioGridi129216. 25 interactions.
DIPiDIP-32489N.
IntActiQ8N5C8. 12 interactions.
MINTiMINT-1145071.
STRINGi9606.ENSP00000288422.

Structurei

3D structure databases

ProteinModelPortaliQ8N5C8.
SMRiQ8N5C8. Positions 4-57, 684-712.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 5144CUEPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili517 – 55943Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi152 – 451300Pro-richAdd
BLAST
Compositional biasi504 – 5096Poly-Ser
Compositional biasi659 – 6624Poly-Ala

Domaini

The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins.By similarity

Sequence similaritiesi

Contains 1 CUE domain.PROSITE-ProRule annotation
Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri682 – 71231RanBP2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IG4E. Eukaryota.
ENOG410XPAC. LUCA.
HOGENOMiHOG000261646.
HOVERGENiHBG056952.
InParanoidiQ8N5C8.
KOiK12793.
OrthoDBiEOG776SPP.
PhylomeDBiQ8N5C8.
TreeFamiTF332021.

Family and domain databases

InterProiIPR003892. CUE.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF90209. SSF90209. 1 hit.
PROSITEiPS51140. CUE. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N5C8-1) [UniParc]FASTAAdd to basket

Also known as: Tab3a

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
MAQSSPQLDI QVLHDLRQRF PEIPEGVVSQ CMLQNNNNLE ACCRALSQES
60 70 80 90 100
SKYLYMEYHS PDDNRMNRNR LLHINLGIHS PSSYHPGDGA QLNGGRTLVH
110 120 130 140 150
SSSDGHIDPQ HAAGKQLICL VQEPHSAPAV VAATPNYNPF FMNEQNRSAA
160 170 180 190 200
TPPSQPPQQP SSMQTGMNPS AMQGPSPPPP PPSYMHIPRY STNPITVTVS
210 220 230 240 250
QNLPSGQTVP RALQILPQIP SNLYGSPGSI YIRQTSQSSS GRQTPQSTPW
260 270 280 290 300
QSSPQGPVPH YSQRPLPVYP HQQNYQPSQY SPKQQQIPQS AYHSPPPSQC
310 320 330 340 350
PSPFSSPQHQ VQPSQLGHIF MPPSPSTTPP HPYQQGPPSY QKQGSHSVAY
360 370 380 390 400
LPYTASSLSK GSMKKIEITV EPSQRPGTAI NRSPSPISNQ PSPWNQHSLY
410 420 430 440 450
TATTPPSSSP SRGISSQPKP PFSVNPVYIT YTQPTGPSCT PSPSPRVIPN
460 470 480 490 500
PTTVFKITVG RATTENLLNL VDQEERSAAP EPIQPISVIP GSGGEKGSHK
510 520 530 540 550
YQRSSSSGSD DYAYTQALLL HQRARMERLA KQLKLEKEEL ERLKSEVNGM
560 570 580 590 600
EHDLMQRRLR RVSCTTAIPT PEEMTRLRSM NRQLQINVDC TLKEVDLLQS
610 620 630 640 650
RGNFDPKAMN NFYDNIEPGP VVPPKPSKKD SSDPCTIERK ARRISVTSKV
660 670 680 690 700
QADIHDTQAA AADEHRTGST QSPRTQPRDE DYEGAPWNCD SCTFLNHPAL
710
NRCEQCEMPR YT
Length:712
Mass (Da):78,683
Last modified:May 5, 2009 - v2
Checksum:i591DAC3E74CE9294
GO
Isoform 2 (identifier: Q8N5C8-2) [UniParc]FASTAAdd to basket

Also known as: Tab3b

The sequence of this isoform differs from the canonical sequence as follows:
     602-629: Missing.

Show »
Length:684
Mass (Da):75,599
Checksum:i56FD54E4E2082928
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti394 – 3941W → R.Combined sources4 Publications
Corresponds to variant rs5927629 [ dbSNP | Ensembl ].
VAR_055294

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei602 – 62928Missing in isoform 2. 1 PublicationVSP_017516Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY437560 mRNA. Translation: AAR06179.1.
AY371491 mRNA. Translation: AAQ88279.1.
AY331591 mRNA. Translation: AAQ92938.1.
AY331592 mRNA. Translation: AAQ92939.1.
AC108359 Genomic DNA. No translation available.
BC032526 mRNA. Translation: AAH32526.1.
CCDSiCCDS14226.1. [Q8N5C8-1]
RefSeqiNP_690000.3. NM_152787.4.
XP_005274539.2. XM_005274482.3.
XP_005274540.2. XM_005274483.2.
UniGeneiHs.188256.

Genome annotation databases

EnsembliENST00000378930; ENSP00000368212; ENSG00000157625.
ENST00000378932; ENSP00000368214; ENSG00000157625.
ENST00000378933; ENSP00000368215; ENSG00000157625.
GeneIDi257397.
KEGGihsa:257397.
UCSCiuc004dck.3. human. [Q8N5C8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY437560 mRNA. Translation: AAR06179.1.
AY371491 mRNA. Translation: AAQ88279.1.
AY331591 mRNA. Translation: AAQ92938.1.
AY331592 mRNA. Translation: AAQ92939.1.
AC108359 Genomic DNA. No translation available.
BC032526 mRNA. Translation: AAH32526.1.
CCDSiCCDS14226.1. [Q8N5C8-1]
RefSeqiNP_690000.3. NM_152787.4.
XP_005274539.2. XM_005274482.3.
XP_005274540.2. XM_005274483.2.
UniGeneiHs.188256.

3D structure databases

ProteinModelPortaliQ8N5C8.
SMRiQ8N5C8. Positions 4-57, 684-712.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129216. 25 interactions.
DIPiDIP-32489N.
IntActiQ8N5C8. 12 interactions.
MINTiMINT-1145071.
STRINGi9606.ENSP00000288422.

PTM databases

iPTMnetiQ8N5C8.
PhosphoSiteiQ8N5C8.

Polymorphism and mutation databases

BioMutaiTAB3.
DMDMi229462756.

Proteomic databases

EPDiQ8N5C8.
MaxQBiQ8N5C8.
PaxDbiQ8N5C8.
PeptideAtlasiQ8N5C8.
PRIDEiQ8N5C8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378930; ENSP00000368212; ENSG00000157625.
ENST00000378932; ENSP00000368214; ENSG00000157625.
ENST00000378933; ENSP00000368215; ENSG00000157625.
GeneIDi257397.
KEGGihsa:257397.
UCSCiuc004dck.3. human. [Q8N5C8-1]

Organism-specific databases

CTDi257397.
GeneCardsiTAB3.
H-InvDBHIX0016717.
HGNCiHGNC:30681. TAB3.
HPAiHPA034980.
HPA034981.
MIMi300480. gene.
neXtProtiNX_Q8N5C8.
PharmGKBiPA165757406.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG4E. Eukaryota.
ENOG410XPAC. LUCA.
HOGENOMiHOG000261646.
HOVERGENiHBG056952.
InParanoidiQ8N5C8.
KOiK12793.
OrthoDBiEOG776SPP.
PhylomeDBiQ8N5C8.
TreeFamiTF332021.

Enzyme and pathway databases

ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-937042. IRAK2 mediated activation of TAK1 complex.
R-HSA-937072. TRAF6 mediated induction of TAK1 complex.
R-HSA-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SIGNORiQ8N5C8.

Miscellaneous databases

GeneWikiiMAP3K7IP3.
GenomeRNAii257397.
PROiQ8N5C8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N5C8.
CleanExiHS_MAP3K7IP3.
ExpressionAtlasiQ8N5C8. baseline and differential.
GenevisibleiQ8N5C8. HS.

Family and domain databases

InterProiIPR003892. CUE.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF90209. SSF90209. 1 hit.
PROSITEiPS51140. CUE. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling."
    Ishitani T., Takaesu G., Ninomiya-Tsuji J., Shibuya H., Gaynor R.B., Matsumoto K.
    EMBO J. 22:6277-6288(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP3K7; TRAF2 AND TRAF6, UBIQUITINATION, PHOSPHORYLATION, FUNCTION, VARIANT ARG-394.
    Tissue: Kidney.
  2. "TAB3, a new binding partner of the protein kinase TAK1."
    Cheung P.C., Nebreda A.R., Cohen P.
    Biochem. J. 378:27-34(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH TAB1; TAB2 AND MAP3K7, VARIANT ARG-394.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH MAP3K7 AND TRAF6, TISSUE SPECIFICITY, FUNCTION, VARIANT ARG-394.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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), VARIANT ARG-394.
    Tissue: Eye.
  6. "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
    Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.
    J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBCK1.
  7. "Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex."
    Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N., Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L., Ghosh S., Cohen P.
    Biochem. J. 409:711-722(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-506.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-404 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."
    Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.
    Cell. Mol. Life Sci. 66:2573-2584(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WDR34.
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: INTERACTION WITH TRIM5.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; THR-404 AND SER-409, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385 (VARIANT ARG-394), VARIANT [LARGE SCALE ANALYSIS] ARG-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTAB3_HUMAN
AccessioniPrimary (citable) accession number: Q8N5C8
Secondary accession number(s): A6NDD9, Q6VQR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 5, 2009
Last modified: July 6, 2016
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.