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Conserved domains on  [gi|1034673945|ref|XP_016884889|]
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TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 isoform X1 [Homo sapiens]

Protein Classification

CUE_TAB2_TAB3 domain-containing protein( domain architecture ID 10198833)

CUE_TAB2_TAB3 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CUE_TAB2_TAB3 cd14362
CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins ...
9-50 9.57e-21

CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins; TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD).


:

Pssm-ID: 270545  Cd Length: 42  Bit Score: 85.43  E-value: 9.57e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034673945   9 DIQVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:cd14362     1 DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES 42
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
245-345 2.23e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673945  245 PQSTPWQssPQGPVPHYSQRPLPVYPHQQNYQPSQYSPKQQQIPQsayhsppPSQCPSPFSSPQHQVQPSQLGHIFMPPS 324
Cdd:PRK10263   751 PVQQPQQ--PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ-------PQQPVAPQPQYQQPQQPVAPQPQYQQPQ 821
                           90       100
                   ....*....|....*....|...
gi 1034673945  325 PSTTPPHPYQ--QGPPSYQKQGS 345
Cdd:PRK10263   822 QPVAPQPQYQqpQQPVAPQPQDT 844
 
Name Accession Description Interval E-value
CUE_TAB2_TAB3 cd14362
CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins ...
9-50 9.57e-21

CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins; TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD).


Pssm-ID: 270545  Cd Length: 42  Bit Score: 85.43  E-value: 9.57e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034673945   9 DIQVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:cd14362     1 DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES 42
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
11-50 2.50e-08

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 50.18  E-value: 2.50e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034673945   11 QVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:smart00546   4 EALHDLKEMFPNLDEEVIEAVLEANTGNVEATINNLLEGS 43
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
11-50 5.61e-08

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 49.40  E-value: 5.61e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034673945  11 QVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:pfam02845   3 QMLETLKEMFPDLDEEVIRAVLEASNGNVEAAINALLEGS 42
PRK10263 PRK10263
DNA translocase FtsK; Provisional
245-345 2.23e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673945  245 PQSTPWQssPQGPVPHYSQRPLPVYPHQQNYQPSQYSPKQQQIPQsayhsppPSQCPSPFSSPQHQVQPSQLGHIFMPPS 324
Cdd:PRK10263   751 PVQQPQQ--PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ-------PQQPVAPQPQYQQPQQPVAPQPQYQQPQ 821
                           90       100
                   ....*....|....*....|...
gi 1034673945  325 PSTTPPHPYQ--QGPPSYQKQGS 345
Cdd:PRK10263   822 QPVAPQPQYQqpQQPVAPQPQDT 844
 
Name Accession Description Interval E-value
CUE_TAB2_TAB3 cd14362
CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins ...
9-50 9.57e-21

CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins; TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD).


Pssm-ID: 270545  Cd Length: 42  Bit Score: 85.43  E-value: 9.57e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034673945   9 DIQVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:cd14362     1 DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES 42
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
11-50 2.50e-08

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 50.18  E-value: 2.50e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1034673945   11 QVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:smart00546   4 EALHDLKEMFPNLDEEVIEAVLEANTGNVEATINNLLEGS 43
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
11-50 5.61e-08

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 49.40  E-value: 5.61e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034673945  11 QVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQES 50
Cdd:pfam02845   3 QMLETLKEMFPDLDEEVIRAVLEASNGNVEAAINALLEGS 42
PRK10263 PRK10263
DNA translocase FtsK; Provisional
245-345 2.23e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673945  245 PQSTPWQssPQGPVPHYSQRPLPVYPHQQNYQPSQYSPKQQQIPQsayhsppPSQCPSPFSSPQHQVQPSQLGHIFMPPS 324
Cdd:PRK10263   751 PVQQPQQ--PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ-------PQQPVAPQPQYQQPQQPVAPQPQYQQPQ 821
                           90       100
                   ....*....|....*....|...
gi 1034673945  325 PSTTPPHPYQ--QGPPSYQKQGS 345
Cdd:PRK10263   822 QPVAPQPQYQqpQQPVAPQPQDT 844
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
13-46 7.42e-04

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 37.45  E-value: 7.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034673945  13 LHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRAL 46
Cdd:cd14279     4 LEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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