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Conserved domains on  [gi|17505955|ref|NP_491370|]
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Eukaryotic translation initiation factor 3 subunit H [Caenorhabditis elegans]

Protein Classification

eukaryotic translation initiation factor 3 subunit H( domain architecture ID 10169158)

eukaryotic translation initiation factor 3 subunit H is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
13-296 6.37e-109

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs.


:

Pssm-ID: 163696 [Multi-domain]  Cd Length: 266  Bit Score: 319.21  E-value: 6.37e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  13 KHILLDSLVVMKIVKHVDSELHagisevsgDACAGVLTGLVflEDSRLEITNCFPTVRNEPVMDDdanaaqQYEEQKQHE 92
Cdd:cd08065   1 TSVQIDGLVVLKIIKHCKEELP--------ELVQGQLLGLD--VGGTLEVTNCFPFPKSEEDDSD------RADEDIADY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  93 MLDMLRKFRTMNIDYEIVGFYQSHQFGAGFSHDLVESMFDYQAMGPENVVLIYDPIKTRQGQLSLRAWRLSTAALDLASK 172
Cdd:cd08065  65 QLEMMRLLREVNVDHNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELYKE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955 173 NDWRPELVKAAGLTYQNMFEELPIIIKSSYLNNVLMSELSLAKSCSSDKYStrHFDLGSKKSLEKSVRAMMANVDELNKS 252
Cdd:cd08065 145 GKFSTESLREANLTFSNIFEEIPVVIRNSHLVNALLSELEEDSPSSQSDFD--RLDLSTNSFLEKNLELLMESVDELSQE 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17505955 253 IQSLTKYTIDKQRHDNMVFSLTQKRQQENESRVARGDPTIPMDD 296
Cdd:cd08065 223 QGKFNYYQRNLARQQAQIQQWLQKRKAENAQREARGEEPLPEED 266
 
Name Accession Description Interval E-value
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
13-296 6.37e-109

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs.


Pssm-ID: 163696 [Multi-domain]  Cd Length: 266  Bit Score: 319.21  E-value: 6.37e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  13 KHILLDSLVVMKIVKHVDSELHagisevsgDACAGVLTGLVflEDSRLEITNCFPTVRNEPVMDDdanaaqQYEEQKQHE 92
Cdd:cd08065   1 TSVQIDGLVVLKIIKHCKEELP--------ELVQGQLLGLD--VGGTLEVTNCFPFPKSEEDDSD------RADEDIADY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  93 MLDMLRKFRTMNIDYEIVGFYQSHQFGAGFSHDLVESMFDYQAMGPENVVLIYDPIKTRQGQLSLRAWRLSTAALDLASK 172
Cdd:cd08065  65 QLEMMRLLREVNVDHNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELYKE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955 173 NDWRPELVKAAGLTYQNMFEELPIIIKSSYLNNVLMSELSLAKSCSSDKYStrHFDLGSKKSLEKSVRAMMANVDELNKS 252
Cdd:cd08065 145 GKFSTESLREANLTFSNIFEEIPVVIRNSHLVNALLSELEEDSPSSQSDFD--RLDLSTNSFLEKNLELLMESVDELSQE 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17505955 253 IQSLTKYTIDKQRHDNMVFSLTQKRQQENESRVARGDPTIPMDD 296
Cdd:cd08065 223 QGKFNYYQRNLARQQAQIQQWLQKRKAENAQREARGEEPLPEED 266
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
150-348 3.22e-44

C-terminal region of eIF3h; This entry represents a C-terminal helical region present in eukaryotic initiation factor 3 chain H. This protein is part of the eIF3 complex that is involved in eukaryotic translation initiation. eIF3 is a large and structurally complex molecular assembly that, in the majority of eukaryotes, consists of 11-13 subunits (eIF3a-IF3m) with a molecular weight of 600-800 kDa.


Pssm-ID: 466087  Cd Length: 196  Bit Score: 151.08  E-value: 3.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955   150 TRQGQLSLRAWRLSTAALDLASKNDWRPELVKAAGLTYQNMFEELPIIIKSSYLNNVLMSELSlAKSCSSDKYSTrhFDL 229
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELE-EKSPVADKHQL--LDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955   230 GSKKSLEKSVRAMMANVDELNKSIQSLTKYTIDKQRHDNMVFSLTQKRQQENESRVARGDPTIPMDDI-KRIKAPQLQTR 308
Cdd:pfam19445  78 ATSSVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDInKLFKPIQPPPR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 17505955   309 nglLDELLASFDTNALADFSKTVTSENITKMFIAEAVAEE 348
Cdd:pfam19445 158 ---LDSLLIAGQINTYCQQVSEFTSQSLGKLFMAESLQEE 194
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
14-165 7.58e-34

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 122.10  E-value: 7.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955     14 HILLDSLVVMKIVKHVDSElhagisevSGDACAGVLTGLVflEDSRLEITNCFPtVRNEPVMDDdanaAQQYEEQKQHEM 93
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRD--------GPEEVCGVLLGKS--NKDRPEVKEVFA-VPNEPQDDS----VQEYDEDYSHLM 65
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17505955     94 LDMLRKfrtMNIDYEIVGFYQSHQ-FGAGFSHDLVESMFDYQAMGPENVVLIYDPIKTRQGQLSLRAWRLSTA 165
Cdd:smart00232  66 DEELKK---VNKDLEIVGWYHSHPdESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLRAFRLTPE 135
 
Name Accession Description Interval E-value
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
13-296 6.37e-109

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs.


Pssm-ID: 163696 [Multi-domain]  Cd Length: 266  Bit Score: 319.21  E-value: 6.37e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  13 KHILLDSLVVMKIVKHVDSELHagisevsgDACAGVLTGLVflEDSRLEITNCFPTVRNEPVMDDdanaaqQYEEQKQHE 92
Cdd:cd08065   1 TSVQIDGLVVLKIIKHCKEELP--------ELVQGQLLGLD--VGGTLEVTNCFPFPKSEEDDSD------RADEDIADY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  93 MLDMLRKFRTMNIDYEIVGFYQSHQFGAGFSHDLVESMFDYQAMGPENVVLIYDPIKTRQGQLSLRAWRLSTAALDLASK 172
Cdd:cd08065  65 QLEMMRLLREVNVDHNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELYKE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955 173 NDWRPELVKAAGLTYQNMFEELPIIIKSSYLNNVLMSELSLAKSCSSDKYStrHFDLGSKKSLEKSVRAMMANVDELNKS 252
Cdd:cd08065 145 GKFSTESLREANLTFSNIFEEIPVVIRNSHLVNALLSELEEDSPSSQSDFD--RLDLSTNSFLEKNLELLMESVDELSQE 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 17505955 253 IQSLTKYTIDKQRHDNMVFSLTQKRQQENESRVARGDPTIPMDD 296
Cdd:cd08065 223 QGKFNYYQRNLARQQAQIQQWLQKRKAENAQREARGEEPLPEED 266
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
150-348 3.22e-44

C-terminal region of eIF3h; This entry represents a C-terminal helical region present in eukaryotic initiation factor 3 chain H. This protein is part of the eIF3 complex that is involved in eukaryotic translation initiation. eIF3 is a large and structurally complex molecular assembly that, in the majority of eukaryotes, consists of 11-13 subunits (eIF3a-IF3m) with a molecular weight of 600-800 kDa.


Pssm-ID: 466087  Cd Length: 196  Bit Score: 151.08  E-value: 3.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955   150 TRQGQLSLRAWRLSTAALDLASKNDWRPELVKAAGLTYQNMFEELPIIIKSSYLNNVLMSELSlAKSCSSDKYSTrhFDL 229
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELE-EKSPVADKHQL--LDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955   230 GSKKSLEKSVRAMMANVDELNKSIQSLTKYTIDKQRHDNMVFSLTQKRQQENESRVARGDPTIPMDDI-KRIKAPQLQTR 308
Cdd:pfam19445  78 ATSSVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDInKLFKPIQPPPR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 17505955   309 nglLDELLASFDTNALADFSKTVTSENITKMFIAEAVAEE 348
Cdd:pfam19445 158 ---LDSLLIAGQINTYCQQVSEFTSQSLGKLFMAESLQEE 194
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
10-139 5.86e-35

JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain and PAD-1-like domain, JABP1 domain or JAMM domain. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates.


Pssm-ID: 396120  Cd Length: 117  Bit Score: 124.38  E-value: 5.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955    10 PSVKHILLDSLVVMKIVKHVDSELHagisevSGDACAGVLTGLVFlEDSRLEITNCFPTVRNEPVMDDDANAAQQYEEQK 89
Cdd:pfam01398   1 SSVRTVIIHPLVLLKILDHANRGGK------IGEEVMGVLLGKLE-GDGTIEITNSFALPQEETEDDVNAVALDQEYMEN 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 17505955    90 QHEMLDMLRKfrtmniDYEIVGFYQSHQFGAGFSHDLVESMFDYQAMGPE 139
Cdd:pfam01398  74 MHEMLKKVNR------KEEVVGWYHTHPGLCWLSSVDVHTHALYQRMIPE 117
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
14-165 7.58e-34

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 122.10  E-value: 7.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955     14 HILLDSLVVMKIVKHVDSElhagisevSGDACAGVLTGLVflEDSRLEITNCFPtVRNEPVMDDdanaAQQYEEQKQHEM 93
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRD--------GPEEVCGVLLGKS--NKDRPEVKEVFA-VPNEPQDDS----VQEYDEDYSHLM 65
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17505955     94 LDMLRKfrtMNIDYEIVGFYQSHQ-FGAGFSHDLVESMFDYQAMGPENVVLIYDPIKTRQGQLSLRAWRLSTA 165
Cdd:smart00232  66 DEELKK---VNKDLEIVGWYHSHPdESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLRAFRLTPE 135
MPN_euk_non_mb cd08057
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non ...
15-152 9.36e-06

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non metal-binding); eukaryotic; This family contains MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains variants lacking key residues in the JAB1/MPN/Mov34 metalloenzyme (JAMM) motif and are unable to coordinate a metal ion. Comparisons of key catalytic and metal binding residues explain why the MPN-containing proteins Rpn7/PSMD7, Rpn8/PSMD8, CSN6, Prp8p, and the translation initiation factor 3 subunits f and h do not show catalytic isopeptidase activity. It has been proposed that the MPN domain in these proteins has a primarily structural function. Rpn7 is known to be critical for the integrity of the 26S proteasome complex by establishing a correct lid structure. It is necessary for the incorporation/anchoring of Rpn3 and Rpn12 to the lid and essential for viability and normal mitosis. CSN6 is a highly conserved protein complex with diverse functions, including several important intracellular pathways such as the ubiquitin/proteasome system, DNA repair, cell cycle, developmental changes, and some aspects of immune responses. It cleaves ubiquitin-like protein Nedd8 (neural precursor cell expressed, developmentally downregulated 8)) in the cullin 1 in cells. EIF3f s a potent inhibitor of HIV-1 replication as well as an important negative regulator of cell growth and proliferation. EIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells.


Pssm-ID: 163688 [Multi-domain]  Cd Length: 157  Bit Score: 45.13  E-value: 9.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  15 ILLDSLVVMKIVKHVDSElhagisEVSGDACAGVLTGLVflEDSRLEITNCF--PTVRNEPVMDDDANAAQQyeeqkqhe 92
Cdd:cd08057   1 VQLHPLVLLNISDHYTRR------KYGIKRVIGVLLGYV--DGDKIEVTNSFelPFDEEEESIFIDTEYLEK-------- 64
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17505955  93 mldMLRKFRTMNIDYEIVGFYQ----SHQFGAGFSHDLVESMFDYQAMGPenVVLIYDPIKTRQ 152
Cdd:cd08057  65 ---RYNLHKKVYPQEKIVGWYSigsnNSNEISKSDNSLHSQFSLISEENP--LILILDPSLQSD 123
MPN_euk_mb cd08058
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
39-148 1.50e-04

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); eukaryotic; This family contains eukaryotic MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains found in proteins with a variety of functions, including AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM), H2A-DUB (histone H2A deubiquitinase), BRCC36 (BRCA1/BRCA2-containing complex subunit 36), as well as Rpn11 (regulatory particle number 11) and CSN5 (COP9 signalosome complex subunit 5). These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology. CSN5 is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Over-expression of CSN5 has been implicated in cancer initiation and progression. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. It is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity; it is targeted to DNA damage foci after irradiation. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. It is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene and serves as a marker in prostate tumors.


Pssm-ID: 163689  Cd Length: 119  Bit Score: 41.03  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  39 EVSGdACAGVLTGLVFlEDSRLEITNCFPtvrnEPVMDDDANAAQQYEEQKQHEMLdmlrkfrtmnidyeIVGFYQSH-Q 117
Cdd:cd08058  17 EVMG-LLCGELTHNEF-TDKHVIVPKQSA----GPDSCTGENVEELFNVQTGRPLL--------------VVGWYHSHpT 76
                        90       100       110
                ....*....|....*....|....*....|.
gi 17505955 118 FGAGFSHDLVESMFDYQAMGPENVVLIYDPI 148
Cdd:cd08058  77 FTAWLSSVDIHTQASYQLMLPEAIAIVVSPK 107
MPN_RPN11_CSN5 cd08069
Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit ...
13-268 5.91e-04

Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit CSN5; This family contains proteasomal regulatory protein Rpn11 (26S proteasome regulatory subunit rpn11; PAD1; POH1; RPN11; PSMD14; Rpn11 subunit of the 19S-proteasome; regulatory particle number 11) and signalosomal CSN5 (COP9 signalosome complex subunit 5; COP9 complex homolog subunit 5; c-Jun activation domain-binding protein-1; CSN5/JAB1; JAB1). COP9 signalosome (CSN) and the proteasome lid are paralogous complexes and their respective subunits CSN5 and Rpn11 are most closely related between the two complexes, both containing the conserved JAMM (JAB1/MPN/Mov34 metalloenzyme) motif involved in zinc ion coordination and providing the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology; mutations in Rpn11 cause cell cycle and mitochondrial defects, temperature sensitivity and sensitivity to DNA damaging reagents such as UV. It has been shown that the C-terminal region of Rpn11 is involved in the regulation of the mitochondrial fission and tubulation processes. CSN5, one of the eight subunits of CSN, is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Its MPN+ domain is critical for the physical interaction of RUNX3 and Jab1. It has been suggested that the direct interaction of CSN5/JAB1 with p27 provides p27 with a leucine-rich nuclear export signal (NES), which is required for binding to chromosomal region maintenance 1 (CRM1), and facilitates nuclear export. The over-expression of CSN5/JAB1 also has been implicated in cancer initiation and progression, including cancer of the lung, pancreas, mouth, thyroid, and breast, suggesting that the oncogenic activity of CSN5 is associated with the down-regulation of RUNX3.


Pssm-ID: 163700 [Multi-domain]  Cd Length: 268  Bit Score: 41.08  E-value: 5.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  13 KHILLDSLVVMKIVKHVDselhAGIS-EVsgdacAGVLTGLVflEDSRLEITNCFPTvrnePV--------MDDDAnaaq 83
Cdd:cd08069  10 EKVYISSLALLKMLKHAR----AGGPiEV-----MGLMLGKV--DDYTIIVVDVFAL----PVegtetrvnAQDEF---- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955  84 qYEEQKQHEMLDMLRKfrtmniDYEIVGFYQSHQ-FGAGFSHDLVESMFDYQAMGPENVVLIYDPIKT-RQGQLSLRAWR 161
Cdd:cd08069  71 -QEYMVQYEMLKQTGR------PENVVGWYHSHPgYGCWLSGIDVNTQQLNQQLQDPFVAVVVDPIRSlVKGKVVIGAFR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505955 162 L------STAALDLASKNDWRP----ELVKAAGLTYQnmfeELPI-IIKSSYLNNVLMSELSlakscssdKYSTRHFDLG 230
Cdd:cd08069 144 TippgykPLEPRQTTSNIGHLPkpkiEDFGGHNKQYY----SLPIeYFKSSLDRKLLLNLWN--------KYWVNTLSLS 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17505955 231 S--KKSLEKSVRAMMANVDELNKSIQSLTKYTIDKQRHDN 268
Cdd:cd08069 212 PllENSNEYTIKQILDLAEKLEKAEQQEERLTGEELDIAN 251
 
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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