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Conserved domains on  [gi|52078426|gb|AAH82276|]
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Hectd3 protein, partial [Mus musculus]

Protein Classification

HECT-type E3 ubiquitin-protein ligase( domain architecture ID 10457544)

HECT-type E3 ubiquitin-protein ligase catalyzes the attachment of ubiquitin chains to target proteins

CATH:  3.30.2410.10
EC:  2.3.2.26
Gene Ontology:  GO:0000209|GO:0061630|GO:0006511
SCOP:  4002196

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
82-348 1.18e-70

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


:

Pssm-ID: 459880  Cd Length: 304  Bit Score: 222.87  E-value: 1.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    82 TGEARDMYV-PNPSCRDFA------KYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEV 154
Cdd:pfam00632  17 YETEDDRTYwFNPSSSESPdlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426   155 MEGVDKETFEFKfgkELTFT-TVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQA 232
Cdd:pfam00632  96 LLNMDNDDDEDL---GLTFTiPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVIPKE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426   233 VLDLLTWQELEKKVCGDPEVTVDALRKLTRFED-FEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------R 304
Cdd:pfam00632 173 ALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVggfkslpK 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 52078426   305 IYIypDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 348
Cdd:pfam00632 253 FTI--VRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
 
Name Accession Description Interval E-value
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
82-348 1.18e-70

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 222.87  E-value: 1.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    82 TGEARDMYV-PNPSCRDFA------KYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEV 154
Cdd:pfam00632  17 YETEDDRTYwFNPSSSESPdlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426   155 MEGVDKETFEFKfgkELTFT-TVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQA 232
Cdd:pfam00632  96 LLNMDNDDDEDL---GLTFTiPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVIPKE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426   233 VLDLLTWQELEKKVCGDPEVTVDALRKLTRFED-FEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------R 304
Cdd:pfam00632 173 ALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVggfkslpK 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 52078426   305 IYIypDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 348
Cdd:pfam00632 253 FTI--VRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
31-356 1.58e-64

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 208.57  E-value: 1.58e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426  31 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSCRDFAK----YEWIGQ 106
Cdd:cd00078  30 LEVEFVGEEGIDAGGVTREFFTLVSKELFNPS------YGLFRYTPD-------DSGLLYPNPSSFADEDhlklFRFLGR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 107 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSV----LVKLLEvMEGvDKETFEfkfgkeLTFTTVLSDQ-- 180
Cdd:cd00078  97 LLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPElyksLKELLD-NDG-DEDDLE------LTFTIELDSSfg 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 181 --QVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDAL 257
Cdd:cd00078 168 gaVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGiEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 258 RKLTRFEDFEPSDTR-VQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDklgYETTDALPESSTCSS 328
Cdd:cd00078 248 KKNTEYKGGYSSDSPtIQWFWEVLESFTNEERKKFLQFVTGSSRLPVggfadlnpKFTIRRV---GSPDDRLPTAHTCFN 324
                       330       340
                ....*....|....*....|....*...
gi 52078426 329 TLFLPHYASAKVCEEKLRYAAYNCVAID 356
Cdd:cd00078 325 LLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
31-352 4.33e-56

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 186.29  E-value: 4.33e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426     31 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSC----RDFAKYEWIGQ 106
Cdd:smart00119   7 LEIEFEGEEGLDGGGVTREFFFLLSKELFNPD------YGLFRYSPN-------DYLLYPNPRSGfaneEHLSYFRFIGR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    107 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWsKDFPAVDSV----LVKLLEVMEGVDKEtfefkfgkELTFTTVLSDQ-- 180
Cdd:smart00119  74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPElyksLKWLLLNNDTSEEL--------DLTFSIVLTSEfg 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    181 --QVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDAL 257
Cdd:smart00119 145 qvKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGiEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    258 RKLTRFED-FEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDKLGYETtdaLPESSTCSS 328
Cdd:smart00119 225 KSNTEYKGgYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVggfaalspKFTIRKAGSDDER---LPTAHTCFN 301
                          330       340
                   ....*....|....*....|....
gi 52078426    329 TLFLPHYASAKVCEEKLRYAAYNC 352
Cdd:smart00119 302 RLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
92-348 2.21e-40

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 151.84  E-value: 2.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426  92 NPSCRDFakYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSwSKDFPAVDSV----LVKLLEvmEGVDKETfefkf 167
Cdd:COG5021 598 NPEHLSY--FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVS-LVDLESLDPElyrsLVWLLN--NDIDETI----- 667
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 168 gKELTFTT---VLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELE 243
Cdd:COG5021 668 -LDLTFTVeddSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRvEKQFSAFKSGFSEIIPPDLLQIFDESELE 746
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 244 KKVCGDPEVT-VDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------------RIYIyp 309
Cdd:COG5021 747 LLIGGIPEDIdIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIngfkdlqgsdgvrKFTI-- 824
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 52078426 310 dKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 348
Cdd:COG5021 825 -EKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTA 862
 
Name Accession Description Interval E-value
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
82-348 1.18e-70

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 222.87  E-value: 1.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    82 TGEARDMYV-PNPSCRDFA------KYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSVLVKLLEV 154
Cdd:pfam00632  17 YETEDDRTYwFNPSSSESPdlelldYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE-DLESIDPELYKSLKS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426   155 MEGVDKETFEFKfgkELTFT-TVLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQA 232
Cdd:pfam00632  96 LLNMDNDDDEDL---GLTFTiPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSiEPQLEAFRKGFYSVIPKE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426   233 VLDLLTWQELEKKVCGDPEVTVDALRKLTRFED-FEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------R 304
Cdd:pfam00632 173 ALSLFTPEELELLICGSPEIDVEDLKKNTEYDGgYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVggfkslpK 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 52078426   305 IYIypDKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 348
Cdd:pfam00632 253 FTI--VRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIA 294
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
31-356 1.58e-64

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 208.57  E-value: 1.58e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426  31 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSCRDFAK----YEWIGQ 106
Cdd:cd00078  30 LEVEFVGEEGIDAGGVTREFFTLVSKELFNPS------YGLFRYTPD-------DSGLLYPNPSSFADEDhlklFRFLGR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 107 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWSkDFPAVDSV----LVKLLEvMEGvDKETFEfkfgkeLTFTTVLSDQ-- 180
Cdd:cd00078  97 LLGKALYEGRLLDLPFSRAFYKKLLGKPLSLE-DLEELDPElyksLKELLD-NDG-DEDDLE------LTFTIELDSSfg 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 181 --QVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDAL 257
Cdd:cd00078 168 gaVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGiEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDIDLEDL 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 258 RKLTRFEDFEPSDTR-VQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDklgYETTDALPESSTCSS 328
Cdd:cd00078 248 KKNTEYKGGYSSDSPtIQWFWEVLESFTNEERKKFLQFVTGSSRLPVggfadlnpKFTIRRV---GSPDDRLPTAHTCFN 324
                       330       340
                ....*....|....*....|....*...
gi 52078426 329 TLFLPHYASAKVCEEKLRYAAYNCVAID 356
Cdd:cd00078 325 LLKLPPYSSKEILREKLLYAINEGAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
31-352 4.33e-56

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 186.29  E-value: 4.33e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426     31 WECKFIAEGIIDQGGGFRDSLADMSEELCPSSadtpvpLPFFVRTANqgngtgeARDMYVPNPSC----RDFAKYEWIGQ 106
Cdd:smart00119   7 LEIEFEGEEGLDGGGVTREFFFLLSKELFNPD------YGLFRYSPN-------DYLLYPNPRSGfaneEHLSYFRFIGR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    107 LMGAALRGKEFLVLALPGFVWKQLSGEEVSWsKDFPAVDSV----LVKLLEVMEGVDKEtfefkfgkELTFTTVLSDQ-- 180
Cdd:smart00119  74 VLGKALYDNRLLDLFFARPFYKKLLGKPVTL-HDLESLDPElyksLKWLLLNNDTSEEL--------DLTFSIVLTSEfg 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    181 --QVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELEKKVCGDPEVTVDAL 257
Cdd:smart00119 145 qvKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGiEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426    258 RKLTRFED-FEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA--------RIYIYPDKLGYETtdaLPESSTCSS 328
Cdd:smart00119 225 KSNTEYKGgYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVggfaalspKFTIRKAGSDDER---LPTAHTCFN 301
                          330       340
                   ....*....|....*....|....
gi 52078426    329 TLFLPHYASAKVCEEKLRYAAYNC 352
Cdd:smart00119 302 RLKLPPYSSKEILREKLLLAINEG 325
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
92-348 2.21e-40

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 151.84  E-value: 2.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426  92 NPSCRDFakYEWIGQLMGAALRGKEFLVLALPGFVWKQLSGEEVSwSKDFPAVDSV----LVKLLEvmEGVDKETfefkf 167
Cdd:COG5021 598 NPEHLSY--FKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVS-LVDLESLDPElyrsLVWLLN--NDIDETI----- 667
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 168 gKELTFTT---VLSDQQVVELIPGGTGIVVEYEDRSRFIQLVRKARLEES-KEQVAAMQAGLLKVVPQAVLDLLTWQELE 243
Cdd:COG5021 668 -LDLTFTVeddSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRvEKQFSAFKSGFSEIIPPDLLQIFDESELE 746
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52078426 244 KKVCGDPEVT-VDALRKLTRFEDFEPSDTRVQYFWEALNNFTNEDRSRFLRFVTGRSRLPA-------------RIYIyp 309
Cdd:COG5021 747 LLIGGIPEDIdIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPIngfkdlqgsdgvrKFTI-- 824
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 52078426 310 dKLGYETTDALPESSTCSSTLFLPHYASAKVCEEKLRYA 348
Cdd:COG5021 825 -EKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTA 862
 
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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