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Conserved domains on  [gi|17505552|ref|NP_491442|]
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HP domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VHP smart00153
Villin headpiece domain;
883-918 1.35e-13

Villin headpiece domain;


:

Pssm-ID: 128458  Cd Length: 36  Bit Score: 65.42  E-value: 1.35e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17505552    883 YLTDDDFMKVFKIERSEFYAQKTWKQNDARKRVGLF 918
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 362-446 5.82e-13

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 65.08  E-value: 5.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 362 EIMKPSEVLIFDFGSEIYVWTGRYSNKVSSAYAQEYAKQLMKKPvkngkfilgdaesidqDGRPEWTLSRKIHQgvlDTL 441
Cdd:cd11280  23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEER----------------KGKPEIVRIRQGQE---PRE 83


                ....*
gi 17505552 442 FKAKF 446
Cdd:cd11280  84 FWSLF 88
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 545-628 1.45e-12

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


The actual alignment was detected with superfamily member cd11280:

Pssm-ID: 472830  Cd Length: 88  Bit Score: 63.93  E-value: 1.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 545 SRRCYVLRWK--YRIQKSGVRR--IKTGKEEERETGRsriAFWYWLGEHTTPKQHGLCALRIKEIDR---DNSPRIRIAD 617
Cdd:cd11280   1 PPRLYRVRGSkaIEIEEVPLASssLDSDDVFVLDTGS---EIYIWQGRASSQAELAAAALLAKELDEerkGKPEIVRIRQ 77

                        90
                ....*....|.
gi 17505552 618 GNEPALFLALF 628
Cdd:cd11280  78 GQEPREFWSLF 88
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 218-296 4.55e-08

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


The actual alignment was detected with superfamily member cd11289:

Pssm-ID: 472830  Cd Length: 92  Bit Score: 51.47  E-value: 4.55e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17505552 218 DVMLIQVRGSKNVDVRLVAPAMSSVHEVACFVVVHQKHLMKYEGLYSNILEKTKASQLCIEILGKSDLNCTAESIVTVT 296
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEG 79
 
Name Accession Description Interval E-value
VHP smart00153
Villin headpiece domain;
883-918 1.35e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 65.42  E-value: 1.35e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17505552    883 YLTDDDFMKVFKIERSEFYAQKTWKQNDARKRVGLF 918
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 362-446 5.82e-13

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 65.08  E-value: 5.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 362 EIMKPSEVLIFDFGSEIYVWTGRYSNKVSSAYAQEYAKQLMKKPvkngkfilgdaesidqDGRPEWTLSRKIHQgvlDTL 441
Cdd:cd11280  23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEER----------------KGKPEIVRIRQGQE---PRE 83


                ....*
gi 17505552 442 FKAKF 446
Cdd:cd11280  84 FWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 545-628 1.45e-12

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.93  E-value: 1.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 545 SRRCYVLRWK--YRIQKSGVRR--IKTGKEEERETGRsriAFWYWLGEHTTPKQHGLCALRIKEIDR---DNSPRIRIAD 617
Cdd:cd11280   1 PPRLYRVRGSkaIEIEEVPLASssLDSDDVFVLDTGS---EIYIWQGRASSQAELAAAALLAKELDEerkGKPEIVRIRQ 77

                        90
                ....*....|.
gi 17505552 618 GNEPALFLALF 628
Cdd:cd11280  78 GQEPREFWSLF 88
VHP pfam02209
Villin headpiece domain;
883-918 3.43e-12

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 61.24  E-value: 3.43e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17505552   883 YLTDDDFMKVFKIERSEFYAQKTWKQNDARKRVGLF 918
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 218-296 4.55e-08

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 51.47  E-value: 4.55e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17505552 218 DVMLIQVRGSKNVDVRLVAPAMSSVHEVACFVVVHQKHLMKYEGLYSNILEKTKASQLCIEILGKSDLNCTAESIVTVT 296
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEG 79
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 526-631 9.53e-08

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 50.37  E-value: 9.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552    526 WVLRGEVLQSIEEFT-----EHFDSRRCYVLRWKYRIqksgvrriktgkeeeretgrsriafWYWLGEHTTPKQHGLCAL 600
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpfsqGSLNSGDCYILDTGSEI-------------------------YVWVGKKSSQDEKKKAAE 55

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 17505552    601 RIKEIDRDNSPR----IRIADGNEPALFLALFDGK 631
Cdd:smart00262  56 LAVELDDTLGPGpvqvRVVDEGKEPPEFWSLFGGW 90
 
Name Accession Description Interval E-value
VHP smart00153
Villin headpiece domain;
883-918 1.35e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 65.42  E-value: 1.35e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17505552    883 YLTDDDFMKVFKIERSEFYAQKTWKQNDARKRVGLF 918
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 362-446 5.82e-13

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 65.08  E-value: 5.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 362 EIMKPSEVLIFDFGSEIYVWTGRYSNKVSSAYAQEYAKQLMKKPvkngkfilgdaesidqDGRPEWTLSRKIHQgvlDTL 441
Cdd:cd11280  23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEER----------------KGKPEIVRIRQGQE---PRE 83


                ....*
gi 17505552 442 FKAKF 446
Cdd:cd11280  84 FWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 545-628 1.45e-12

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.93  E-value: 1.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 545 SRRCYVLRWK--YRIQKSGVRR--IKTGKEEERETGRsriAFWYWLGEHTTPKQHGLCALRIKEIDR---DNSPRIRIAD 617
Cdd:cd11280   1 PPRLYRVRGSkaIEIEEVPLASssLDSDDVFVLDTGS---EIYIWQGRASSQAELAAAALLAKELDEerkGKPEIVRIRQ 77

                        90
                ....*....|.
gi 17505552 618 GNEPALFLALF 628
Cdd:cd11280  78 GQEPREFWSLF 88
VHP pfam02209
Villin headpiece domain;
883-918 3.43e-12

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 61.24  E-value: 3.43e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17505552   883 YLTDDDFMKVFKIERSEFYAQKTWKQNDARKRVGLF 918
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 218-296 4.55e-08

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 51.47  E-value: 4.55e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17505552 218 DVMLIQVRGSKNVDVRLVAPAMSSVHEVACFVVVHQKHLMKYEGLYSNILEKTKASQLCIEILGKSDLNCTAESIVTVT 296
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEG 79
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 526-631 9.53e-08

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 50.37  E-value: 9.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552    526 WVLRGEVLQSIEEFT-----EHFDSRRCYVLRWKYRIqksgvrriktgkeeeretgrsriafWYWLGEHTTPKQHGLCAL 600
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpfsqGSLNSGDCYILDTGSEI-------------------------YVWVGKKSSQDEKKKAAE 55

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 17505552    601 RIKEIDRDNSPR----IRIADGNEPALFLALFDGK 631
Cdd:smart00262  56 LAVELDDTLGPGpvqvRVVDEGKEPPEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 531-628 1.63e-06

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 47.27  E-value: 1.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 531 EVLQSIEEFTeHFDSRRCYVLRWKYRIqksgvrrikTGKEEEretgrsriAFWYWLGEHTTPKQHGLCALRIKEIDRD-- 608
Cdd:cd11293  19 KVPVPKEEYG-QFYGGDCYIVLYTYQG---------GGKEEH--------ILYFWQGRHSSQDERAAAALLTVELDEElk 80

                        90       100
                ....*....|....*....|.
gi 17505552 609 -NSPRIRIADGNEPALFLALF 628
Cdd:cd11293  81 gRAVQVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 359-448 8.95e-06

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 44.93  E-value: 8.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505552 359 LSYEIMKPSEVLIFDFGSEIYVWTGRYSNKVSSAYAQEYAKQLMKKpvkngkfilgdaesidqDGRPEWTLSRKIHQGVL 438
Cdd:cd11292  26 LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRK-----------------KKRPPYTQVTRVTEGGE 88

                        90
                ....*....|
gi 17505552 439 DTLFKAKFSD 448
Cdd:cd11292  89 SALFKSKFAN 98
 
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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