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Conserved domains on  [gi|1907094480|ref|XP_036014056|]
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tubulin-specific chaperone E isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 187-269 6.82e-35

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.


:

Pssm-ID: 340564  Cd Length: 83  Bit Score: 120.38  E-value: 6.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480 187 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 266
Cdd:cd17044     1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                  ...
gi 1907094480 267 LVR 269
Cdd:cd17044    81 LVR 83
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
4-112 1.61e-06

Leucine-rich repeat (LRR) protein [Transcription];


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480   4 LDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpDAEIGCktsmFPALKYLIVNDNQISEWSfiNELDKLQSL 81
Cdd:COG4886   141 LDLSNNQltDLPEP----LGNLTNLKSLDLSNNQLTDL---PEELGN----LTNLKELDLSNNQITDLP--EPLGNLTNL 207

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907094480  82 QALSCTRNPLSKADKAeeiiIAKIAQLRTLN 112
Cdd:COG4886   208 EELDLSGNQLTDLPEP----LANLTNLETLD 234
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 187-269 6.82e-35

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.


Pssm-ID: 340564  Cd Length: 83  Bit Score: 120.38  E-value: 6.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480 187 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 266
Cdd:cd17044     1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                  ...
gi 1907094480 267 LVR 269
Cdd:cd17044    81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-112 1.61e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480   4 LDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpDAEIGCktsmFPALKYLIVNDNQISEWSfiNELDKLQSL 81
Cdd:COG4886   141 LDLSNNQltDLPEP----LGNLTNLKSLDLSNNQLTDL---PEELGN----LTNLKELDLSNNQITDLP--EPLGNLTNL 207

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907094480  82 QALSCTRNPLSKADKAeeiiIAKIAQLRTLN 112
Cdd:COG4886   208 EELDLSGNQLTDLPEP----LANLTNLETLD 234
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 18-122 4.06e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480  18 SLIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEWSFINE-LDKLQSLQALSCTRNPLSKADK 96
Cdd:cd21340   114 SLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKKPK 185

                          90       100
                  ....*....|....*....|....*.
gi 1907094480  97 AEEIIIAKIAQLRTLNRCQILPEERR 122
Cdd:cd21340   186 YRDKIILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
54-138 8.11e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 42.06  E-value: 8.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480  54 PALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRGAELDYRKAFG 133
Cdd:pfam14580  88 PNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQG 167


                  ....*
gi 1907094480 134 NEWRK 138
Cdd:pfam14580 168 KQLAK 172
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 189-264 4.69e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 38.01  E-value: 4.69e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094480  189 LTLKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEsskmpGREIElenDLQPLQFYSVENGD 264
Cdd:smart00213   1 IELTVKTLDGKTITL---EVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 189-268 9.01e-03

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 34.42  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480 189 LTLKIKCSNQpERQILEKQLPDSMTVQKVKGLLSRLLKVPVS--ELLLSYESSKMPGreiELENDLQPLQFYSVENGDCL 266
Cdd:pfam14560   1 VKLFITHSLT-KAVSSERRFDKSLTIEELKEKLELITGTPPSsmRLQLYDDDDNLVA---KLDDDDALLGSYGVRDGMRI 76


                  ..
gi 1907094480 267 LV 268
Cdd:pfam14560  77 HV 78
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 187-269 6.82e-35

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.


Pssm-ID: 340564  Cd Length: 83  Bit Score: 120.38  E-value: 6.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480 187 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 266
Cdd:cd17044     1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                  ...
gi 1907094480 267 LVR 269
Cdd:cd17044    81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-112 1.61e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480   4 LDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpDAEIGCktsmFPALKYLIVNDNQISEWSfiNELDKLQSL 81
Cdd:COG4886   141 LDLSNNQltDLPEP----LGNLTNLKSLDLSNNQLTDL---PEELGN----LTNLKELDLSNNQITDLP--EPLGNLTNL 207

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907094480  82 QALSCTRNPLSKADKAeeiiIAKIAQLRTLN 112
Cdd:COG4886   208 EELDLSGNQLTDLPEP----LANLTNLETLD 234
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 18-122 4.06e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480  18 SLIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEWSFINE-LDKLQSLQALSCTRNPLSKADK 96
Cdd:cd21340   114 SLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKKPK 185

                          90       100
                  ....*....|....*....|....*.
gi 1907094480  97 AEEIIIAKIAQLRTLNRCQILPEERR 122
Cdd:cd21340   186 YRDKIILASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
3-112 7.34e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480   3 LLDLSSNPSIDESQLSLIADLPRLEHLVLSDIGLSSIhfpDAEIGcktsMFPALKYLIVNDNQISewSFINELDKLQSLQ 82
Cdd:COG4886    92 LGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDL---PEELA----NLTNLKELDLSNNQLT--DLPEPLGNLTNLK 162

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907094480  83 ALSCTRNPLSKADKAeeiiIAKIAQLRTLN 112
Cdd:COG4886   163 SLDLSNNQLTDLPEE----LGNLTNLKELD 188
LRR_9 pfam14580
Leucine-rich repeat;
54-138 8.11e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 42.06  E-value: 8.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480  54 PALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRGAELDYRKAFG 133
Cdd:pfam14580  88 PNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQG 167


                  ....*
gi 1907094480 134 NEWRK 138
Cdd:pfam14580 168 KQLAK 172
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 191-269 1.40e-04

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 39.12  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907094480 191 LKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYesskmpgREIELENDlQPLQFYSVENGDCLLVR 269
Cdd:cd17039     1 ITVKTLDGKTYTV---EVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-92 2.65e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480   4 LDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEwsfINELDKLQSL 81
Cdd:COG4886   210 LDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNL 274

                          90
                  ....*....|.
gi 1907094480  82 QALSCTRNPLS 92
Cdd:COG4886   275 KTLDLSNNQLT 285
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 189-264 4.69e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 38.01  E-value: 4.69e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907094480  189 LTLKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEsskmpGREIElenDLQPLQFYSVENGD 264
Cdd:smart00213   1 IELTVKTLDGKTITL---EVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-112 1.04e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.92  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480   4 LDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpDAEIGcktsMFPALKYLIVNDNQISEwsfINELDKLQSL 81
Cdd:COG4886   187 LDLSNNQitDLPEP----LGNLTNLEELDLSGNQLTDL---PEPLA----NLTNLETLDLSNNQLTD---LPELGNLTNL 252

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907094480  82 QALSCTRNPLSKADKaeeiiIAKIAQLRTLN 112
Cdd:COG4886   253 EELDLSNNQLTDLPP-----LANLTNLKTLD 278
Ubl_IQUB cd17061
ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) ...
 190-241 3.20e-03

ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) and similar proteins; IQUB is an IQ motif and ubiquitin domain-containing protein that may play roles in cilia formation and/or maintenance. It contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340581  Cd Length: 79  Bit Score: 35.70  E-value: 3.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907094480 190 TLKIKCsnQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKM 241
Cdd:cd17061     4 TVKFVL--MPSGQVITLAFTLGQTIGELKEHFSSELKIPPDVLQIMFDGKLV 53
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 189-268 9.01e-03

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 34.42  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094480 189 LTLKIKCSNQpERQILEKQLPDSMTVQKVKGLLSRLLKVPVS--ELLLSYESSKMPGreiELENDLQPLQFYSVENGDCL 266
Cdd:pfam14560   1 VKLFITHSLT-KAVSSERRFDKSLTIEELKEKLELITGTPPSsmRLQLYDDDDNLVA---KLDDDDALLGSYGVRDGMRI 76


                  ..
gi 1907094480 267 LV 268
Cdd:pfam14560  77 HV 78
 
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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