NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907072701|ref|XP_036011352|]
View 

centrosomal protein CEP57L1 isoform X2 [Mus musculus]

Protein Classification

Cep57_CLD and Cep57_MT_bd domain-containing protein( domain architecture ID 12163498)

Cep57_CLD and Cep57_MT_bd domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 102-263 1.06e-55

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


:

Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 183.21  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 102 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKK----------------EKQL 165
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 166 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 245
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1907072701 246 QDRACELQTGFEISKILM 263
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 319-392 2.67e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


:

Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 73.38  E-value: 2.67e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072701 319 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 392
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 102-263 1.06e-55

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 183.21  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 102 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKK----------------EKQL 165
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 166 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 245
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1907072701 246 QDRACELQTGFEISKILM 263
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 319-392 2.67e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 73.38  E-value: 2.67e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072701 319 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 392
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-227 6.70e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQkkEKQLEYTKRMVLNVEREKT 180
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLE 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907072701 181 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDK 227
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 101-217 2.74e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEdnlnllsrEAAQYKKALEEETNErnlaHQELIKQKKEKQLEYTKRMVLNVEREKT 180
Cdd:cd16269   184 EAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLEEQQRE----LEQKLEDQERSYEEHLRQLKEKMEEERE 251

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907072701 181 MILEQQAQLQREKEQDQMKLHAK--LEKLHVLEKECLRL 217
Cdd:cd16269   252 NLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 108-206 8.14e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 108 KTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLEYTKRMVLNVEREKTMILEQQA 187
Cdd:PRK00409  530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHEL 609

                          90       100
                  ....*....|....*....|
gi 1907072701 188 Q-LQREKEQDQMKLHAKLEK 206
Cdd:PRK00409  610 IeARKRLNKANEKKEKKKKK 629
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 102-263 1.06e-55

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 183.21  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 102 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKK----------------EKQL 165
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 166 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 245
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1907072701 246 QDRACELQTGFEISKILM 263
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 319-392 2.67e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 73.38  E-value: 2.67e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072701 319 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 392
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-227 6.70e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQkkEKQLEYTKRMVLNVEREKT 180
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLE 319

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907072701 181 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDK 227
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-229 7.36e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELikQKKEKQLEYTKRMVLNVEREKT 180
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELAEAEEALLEAEAELA 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907072701 181 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 229
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-229 2.90e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAhQELIKQKKEKQLEYTKRMvlnvEREKT 180
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEEL----AELEE 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907072701 181 MILEQQAQLQR---EKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 229
Cdd:COG1196   331 ELEELEEELEEleeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-229 1.51e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLeytkrmvlnVEREKT 180
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---------AEAELA 361

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907072701 181 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 229
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 105-213 2.14e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 105 SALKTLQEKIRRLELERTQAEDNLNLLSRE-AAQYKKALEEETNERNLAHQeliKQKKEKQLeytkrmvLNVEREKTMIL 183
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKA---RWEAEKEL-------IEEIQELKEEL 480

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907072701 184 EQQAQLQREKEQDQMKLHAKLEKLHVLEKE 213
Cdd:COG0542   481 EQRYGKIPELEKELAELEEELAELAPLLRE 510
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 101-217 2.74e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAEdnlnllsrEAAQYKKALEEETNErnlaHQELIKQKKEKQLEYTKRMVLNVEREKT 180
Cdd:cd16269   184 EAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLEEQQRE----LEQKLEDQERSYEEHLRQLKEKMEEERE 251

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907072701 181 MILEQQAQLQREKEQDQMKLHAK--LEKLHVLEKECLRL 217
Cdd:cd16269   252 NLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-229 4.28e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 101 QALVSALKTLQEKIRRLELERTQAE-----DNLNLLSREAAQYKK---ALEEETNERNLAHQELIKQKKEKQLEYTKRM- 171
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAEleeleAELEELEAELEELEAelaELEAELEELRLELEELELELEEAQAEEYELLa 295

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907072701 172 -VLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 229
Cdd:COG1196   296 eLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 108-206 8.14e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072701 108 KTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLEYTKRMVLNVEREKTMILEQQA 187
Cdd:PRK00409  530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHEL 609

                          90       100
                  ....*....|....*....|
gi 1907072701 188 Q-LQREKEQDQMKLHAKLEK 206
Cdd:PRK00409  610 IeARKRLNKANEKKEKKKKK 629
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH