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Conserved domains on  [gi|4508007|ref|NP_003441|]
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zinc finger protein 174 isoform a [Homo sapiens]

Protein Classification

SCAN and zf-H2C2_2 domain-containing protein( domain architecture ID 12210951)

protein containing domains SCAN, zf-C2H2, and zf-H2C2_2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-152 1.09e-60

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 192.13  E-value: 1.09e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007      42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 4508007     122 EDFHRASKKPKQWVAVCMQGQKVLLEKTGSQ 152
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPL 111
zf-H2C2_2 pfam13465
Zinc-finger double domain;
369-393 2.04e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.04e-05
                          10        20
                  ....*....|....*....|....*
gi 4508007    369 LKLHQRIHTGEKPYQCGQCGKSFRQ 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-363 1.93e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|....
gi 4508007    340 ELKRHKRVHTGERPYTCGECGNCF 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 326-348 1.02e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|...
gi 4508007    326 YKCDDCGKSFTWNSELKRHKRVH 348
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-152 1.09e-60

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 192.13  E-value: 1.09e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007      42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 4508007     122 EDFHRASKKPKQWVAVCMQGQKVLLEKTGSQ 152
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPL 111
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-130 5.70e-49

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 160.73  E-value: 5.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007     42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 4508007    122 EDFHRASKK 130
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 42-126 2.33e-41

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 140.86  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007   42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:cd07936   1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                ....*
gi 4508007  122 EDFHR 126
Cdd:cd07936  81 EDLLA 85
zf-H2C2_2 pfam13465
Zinc-finger double domain;
369-393 2.04e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.04e-05
                          10        20
                  ....*....|....*....|....*
gi 4508007    369 LKLHQRIHTGEKPYQCGQCGKSFRQ 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-363 1.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|....
gi 4508007    340 ELKRHKRVHTGERPYTCGECGNCF 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 326-348 1.02e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|...
gi 4508007    326 YKCDDCGKSFTWNSELKRHKRVH 348
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
352-407 1.36e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 1.36e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4508007  352 RPYTCGECGNCFGRQSTLKLHQRIHTGEKPYQCGQ--CGKSFRQSSNLHQHHRLHHGD 407
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNN 89
ZnF_C2H2 smart00355
zinc finger;
326-348 8.78e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 8.78e-03
                           10        20
                   ....*....|....*....|...
gi 4508007     326 YKCDDCGKSFTWNSELKRHKRVH 348
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-152 1.09e-60

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 192.13  E-value: 1.09e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007      42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 4508007     122 EDFHRASKKPKQWVAVCMQGQKVLLEKTGSQ 152
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPL 111
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-130 5.70e-49

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 160.73  E-value: 5.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007     42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 4508007    122 EDFHRASKK 130
Cdd:pfam02023  81 EDLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 42-126 2.33e-41

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 140.86  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007   42 PELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLV 121
Cdd:cd07936   1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                ....*
gi 4508007  122 EDFHR 126
Cdd:cd07936  81 EDLLA 85
zf-H2C2_2 pfam13465
Zinc-finger double domain;
369-393 2.04e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.04e-05
                          10        20
                  ....*....|....*....|....*
gi 4508007    369 LKLHQRIHTGEKPYQCGQCGKSFRQ 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-363 1.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|....
gi 4508007    340 ELKRHKRVHTGERPYTCGECGNCF 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 382-404 2.35e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 2.35e-04
                          10        20
                  ....*....|....*....|...
gi 4508007    382 YQCGQCGKSFRQSSNLHQHHRLH 404
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 326-348 1.02e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|...
gi 4508007    326 YKCDDCGKSFTWNSELKRHKRVH 348
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
352-407 1.36e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 1.36e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4508007  352 RPYTCGECGNCFGRQSTLKLHQRIHTGEKPYQCGQ--CGKSFRQSSNLHQHHRLHHGD 407
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNN 89
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 324-407 3.44e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.32  E-value: 3.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007  324 KPYKCD--DCGKSFTWNSELKRHkRVHtgerpytcGECGNCFGRQSTLKLHQRIHTGEKPYQCGQCGKSFRQSSNLhQHH 401
Cdd:COG5189 348 KPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGL-KYH 417


                ....*.
gi 4508007  402 RLHHGD 407
Cdd:COG5189 418 RKHSHD 423
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
285-406 4.83e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.91  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4508007  285 ISSPLKSHPLRELKKSKGGKRSLSNRLQHLGHQPTRSAKKPYKCDDCGKSFTWNSELKRHKR--VHTGE--RPYTCGE-- 358
Cdd:COG5048 249 SSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYsl 328

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4508007  359 CGNCFGRQSTLKLHQRIHTGEKPYQC--GQCGKSFRQSSN--LHQHHRLHHG 406
Cdd:COG5048 329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNnePPQSLQQYKD 380
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
326-350 6.76e-03

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 34.06  E-value: 6.76e-03
                          10        20
                  ....*....|....*....|....*
gi 4508007    326 YKCDDCGKSFTWNSELKRHKRVHTG 350
Cdd:pfam13909   1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 354-376 6.91e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 6.91e-03
                          10        20
                  ....*....|....*....|...
gi 4508007    354 YTCGECGNCFGRQSTLKLHQRIH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
ZnF_C2H2 smart00355
zinc finger;
326-348 8.78e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 33.59  E-value: 8.78e-03
                           10        20
                   ....*....|....*....|...
gi 4508007     326 YKCDDCGKSFTWNSELKRHKRVH 348
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
 
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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