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Conserved domains on  [gi|5174729|ref|NP_006013|]
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TSC22 domain family protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZIP_TSC22D1 cd21938
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
54-132 6.22e-40

leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


:

Pssm-ID: 409278  Cd Length: 79  Bit Score: 129.11  E-value: 6.22e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174729   54 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPP 132
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPSSSQPPGTTPQP 79
 
Name Accession Description Interval E-value
ZIP_TSC22D1 cd21938
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
54-132 6.22e-40

leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409278  Cd Length: 79  Bit Score: 129.11  E-value: 6.22e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174729   54 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPP 132
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPSSSQPPGTTPQP 79
TSC22 pfam01166
TSC-22/dip/bun family;
59-105 1.55e-26

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 94.30  E-value: 1.55e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 5174729     59 MDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPE 47
PRK13169 PRK13169
DNA replication initiation control protein YabA;
72-101 1.81e-04

DNA replication initiation control protein YabA;


Pssm-ID: 183876  Cd Length: 110  Bit Score: 38.69  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 5174729    72 EEVEVLKEQIKELIEKNSQLEQENNLLKTL 101
Cdd:PRK13169  22 KELGALKKQLAELLEENTALRLENDKLRER 51
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
67-100 5.94e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 34.09  E-value: 5.94e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 5174729   67 MYAVREEVEVLKEQIKELIEKNSQLEQENNLLKT 100
Cdd:COG2919  31 YRELRQEIAELEAENAKLKARNAELEAEVADLKD 64
 
Name Accession Description Interval E-value
ZIP_TSC22D1 cd21938
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
54-132 6.22e-40

leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409278  Cd Length: 79  Bit Score: 129.11  E-value: 6.22e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174729   54 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPP 132
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPSSSQPPGTTPQP 79
ZIP_TSC22D4 cd21941
leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 ...
49-121 9.88e-31

leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 (TSC22D4), also called TSC22-related-inducible leucine zipper protein 2 (TILZ2), or Tsc-22-like protein THG-1, is a transcriptional repressor that acts as a molecular determinant of insulin signalling and glucose handling. It also functions in hepatic lipid handling by regulating hepatic very-low-density-lipoprotein (VLDL) release and lipogenic gene expression. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D4. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409281  Cd Length: 74  Bit Score: 105.41  E-value: 9.88e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5174729   49 VAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPA 121
Cdd:cd21941   1 VAIDNKIEQAMDLVKSHLLFAVREEVEVLKEQIKELSERNAALEQENSLLRSLATPQQLSRLQSRQPTSRKPA 73
ZIP_TSC22D3 cd21940
leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 ...
58-141 1.58e-29

leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 (TSC22D3) is also called DSIP-immunoreactive peptide, protein DIP, delta sleep-inducing peptide immunoreactor, glucocorticoid-induced leucine zipper protein (GILZ), TSC-22-like protein, or TSC-22-related protein (TSC-22R). It protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, it plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, it inhibits anti-CD3-induced NFKB1 nuclear translocation. TSC22D3 contains a leucine zipper motif, a Pro/Glu rich domain, and three potential phosphorylation sites. This model corresponds to the leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409280  Cd Length: 81  Bit Score: 102.72  E-value: 1.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174729   58 AMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLqtgsPPATTQPQgtTQPPAQPAS 137
Cdd:cd21940   1 AMDLVKNHLMYAVREEVEVLKEQIKELVEKNSQLERENSLLKTLASPEQLEKFQSRL----PSEETAPE--TPLDAQPAE 74

                ....
gi 5174729  138 QGSG 141
Cdd:cd21940  75 HSGG 78
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
58-105 4.21e-29

leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; The TGF-beta-stimulated clone-22 domain (TSC22D) family includes TSC22D1-4 and similar proteins. They have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. All family members contain a conserved leucine zipper (ZIP) domain located at the C-terminus. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409276  Cd Length: 49  Bit Score: 100.33  E-value: 4.21e-29
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 5174729   58 AMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:cd21936   1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPE 48
TSC22 pfam01166
TSC-22/dip/bun family;
59-105 1.55e-26

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 94.30  E-value: 1.55e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 5174729     59 MDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPE 47
ZIP_TSC22D2 cd21939
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
58-105 3.67e-22

leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 (TSC22D2), also called transforming growth factor beta-stimulated clone 22 domain family member 2, or TSC22-related-inducible leucine zipper protein 4 (TILZ4), may participate in the regulation of cell growth. It interacts with pyruvate kinase isoform M2 (PKM2) and WD repeat domain 77 (WDR77). The model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D2. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409279  Cd Length: 63  Bit Score: 83.48  E-value: 3.67e-22
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 5174729   58 AMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:cd21939   1 AMDLVKSHLMYAVREEVEVLKEQIKELIERNSLLERENALLKSLSNND 48
ZIP_TSC22D-like cd21927
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding ...
59-105 2.32e-18

leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding protein, and similar proteins; The family includes TGF-beta-stimulated clone-22 domain (TSC22D) leucine zipper transcription factors, TSC22D1-4, as well as c-Myc-binding protein (MycBP). TSC22D proteins have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. Members of this family contain a conserved leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409275  Cd Length: 51  Bit Score: 73.32  E-value: 2.32e-18
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5174729   59 MDLVKSHLMYAVREE--VEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:cd21927   2 LDFLKHHLGAATPENpeIELLRLELAEMKEKYEAIVEENKKLKAKLAQY 50
ZIP_MycBP-like cd21937
leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called ...
58-100 2.04e-05

leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409277 [Multi-domain]  Cd Length: 53  Bit Score: 39.84  E-value: 2.04e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 5174729   58 AMDLVKSHLMYA--VREEVEVLKEQIKELIEKNSQLEQENNLLKT 100
Cdd:cd21937   3 ALDFIKQHLGAPgpEDADVEALRLENEELKQKNEELEEENKELKA 47
PRK13169 PRK13169
DNA replication initiation control protein YabA;
72-101 1.81e-04

DNA replication initiation control protein YabA;


Pssm-ID: 183876  Cd Length: 110  Bit Score: 38.69  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 5174729    72 EEVEVLKEQIKELIEKNSQLEQENNLLKTL 101
Cdd:PRK13169  22 KELGALKKQLAELLEENTALRLENDKLRER 51
DUF6262 pfam19776
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, ...
50-98 3.11e-03

Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, is found in bacteria. Proteins in this family are typically between 124 and 143 amino acids in length. Some members included in this family are hypothetical transposases, associated with transposon Tn554. There is a conserved sequence GV/LSR/K and a highly conserved tyrosine residue.


Pssm-ID: 466180 [Multi-domain]  Cd Length: 110  Bit Score: 35.29  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 5174729     50 AIDNKIEQAMDLVKSH---LMYAVREEVEVLKEQIKELIEKNSQLEQENNLL 98
Cdd:pfam19776  59 ELDEAIEQQGGMVNPKreiLDMALEKRIELLKKEIKELKRENEELKKENEKL 110
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
67-99 3.64e-03

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 34.11  E-value: 3.64e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 5174729     67 MYAVREEVEVLKEQIKELIEKNSQLEQENNLLK 99
Cdd:pfam04977   8 YYQLKQEIAQLQAEIAKLKQENEELEAEIKDLK 40
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
67-100 5.94e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 34.09  E-value: 5.94e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 5174729   67 MYAVREEVEVLKEQIKELIEKNSQLEQENNLLKT 100
Cdd:COG2919  31 YRELRQEIAELEAENAKLKARNAELEAEVADLKD 64
geminin_CC cd22589
central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil ...
72-103 9.46e-03

central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil domain-containing protein 1 (GemC1) and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. Geminin is an inhibitor of Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC) that function in the duplication of chromosomal DNA. Pre-RC assembly culminates in the recruitment of the hexameric mini-chromosome maintenance complex (MCM) onto chromatin. Geminin tightly binds and sequesters Cdt1 in a complex that is unable to recruit MCM to origins, inhibiting DNA replication. It belongs to the geminin family of proteins that also includes GemC1 and McIdas. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of geminin.


Pssm-ID: 439143 [Multi-domain]  Cd Length: 65  Bit Score: 32.96  E-value: 9.46e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 5174729   72 EEVEVLKEQIKELIEKNSQLEQENNLLKTLAS 103
Cdd:cd22589  27 KEIEQLDEEIARLKEENDELEELAEHVQYLAE 58
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
71-99 9.73e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 32.52  E-value: 9.73e-03
                        10        20
                ....*....|....*....|....*....
gi 5174729   71 REEVEVLKEQIKELIEKNSQLEQENNLLK 99
Cdd:cd14686  20 KERIEELEEEVEELEEENEELKAELEELR 48
 
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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