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Conserved domains on  [gi|282847448|ref|NP_001164023|]
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krev interaction trapped protein 1 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 1.39e-102

NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at the N-terminus of KRIT1 or Krev interaction trapped proteins. NUDIX_5 carries three NPxY-like motifs, and it is found to bind the integrin cytoplasmic-associated protein 1 ICAP1. In the absence of KRIT1 ICAP1 binds via its C-terminal PH/PTB fold domain to the integrin beta-1 cytoplasmic tail. Binding of KRIT1 to ICAP1 via NUDIX_5 out-competes the binding of ICAP1 to integrin cytoplasmic tails such that ICAP1 is sequestered in the nucleus. Integrin activation is thus prevented.


:

Pssm-ID: 465241  Cd Length: 169  Bit Score: 310.52  E-value: 1.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQSNSEIAQGILDYVVETTKPISPANQGIKGKRVVLMRKFPLDGEKTGREAA 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  110 LFIVPSVVKDNTKYAYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 282847448  190 VINPAYAAE 198
Cdd:pfam16705 161 VSNPAYATE 169
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 4.80e-35

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 131.65  E-value: 4.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   421 KVRIYRMDGSyrSVELKHGNNTTAQQIMEGMRLSQETqryftiwICSENLSLQFKPYHKPLQqvhDWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLR---HWLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   501 RETPQLFLRRDVGLPlEVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEET 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282847448   581 LKSIVPITKLKS-KAPHWINRILHEYKNLSlsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 636-696 3.73e-29

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13197:

Pssm-ID: 473070  Cd Length: 100  Bit Score: 111.55  E-value: 3.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETK---------------------------------------A 676
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKalllslkygcfmwqlgdadtcfqihslenkmsfvvhtkqA 80

                         90       100
                 ....*....|....*....|
gi 282847448 677 GLVVKLLMKLNGQLMPSERN 696
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-421 4.99e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282847448 371 VQILLTHpDIDRHITDQQGRSPLNVCEENKQNnweEAAKLLKDAINKPYEK 421
Cdd:COG0666  202 VKLLLEA-GADVNAKDNDGKTALDLAAENGNL---EIVKLLLEAGADLNAK 248
 
Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 1.39e-102

NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at the N-terminus of KRIT1 or Krev interaction trapped proteins. NUDIX_5 carries three NPxY-like motifs, and it is found to bind the integrin cytoplasmic-associated protein 1 ICAP1. In the absence of KRIT1 ICAP1 binds via its C-terminal PH/PTB fold domain to the integrin beta-1 cytoplasmic tail. Binding of KRIT1 to ICAP1 via NUDIX_5 out-competes the binding of ICAP1 to integrin cytoplasmic tails such that ICAP1 is sequestered in the nucleus. Integrin activation is thus prevented.


Pssm-ID: 465241  Cd Length: 169  Bit Score: 310.52  E-value: 1.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQSNSEIAQGILDYVVETTKPISPANQGIKGKRVVLMRKFPLDGEKTGREAA 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  110 LFIVPSVVKDNTKYAYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 282847448  190 VINPAYAAE 198
Cdd:pfam16705 161 VSNPAYATE 169
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 4.80e-35

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 131.65  E-value: 4.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   421 KVRIYRMDGSyrSVELKHGNNTTAQQIMEGMRLSQETqryftiwICSENLSLQFKPYHKPLQqvhDWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLR---HWLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   501 RETPQLFLRRDVGLPlEVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEET 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282847448   581 LKSIVPITKLKS-KAPHWINRILHEYKNLSlsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-696 3.73e-29

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270018  Cd Length: 100  Bit Score: 111.55  E-value: 3.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETK---------------------------------------A 676
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKalllslkygcfmwqlgdadtcfqihslenkmsfvvhtkqA 80

                         90       100
                 ....*....|....*....|
gi 282847448 677 GLVVKLLMKLNGQLMPSERN 696
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 517-640 2.83e-28

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 109.67  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  517 EVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNeetLKSIVPITKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLS---LESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 282847448  596 HWINRILHEYKNLSlsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-421 4.99e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282847448 371 VQILLTHpDIDRHITDQQGRSPLNVCEENKQNnweEAAKLLKDAINKPYEK 421
Cdd:COG0666  202 VKLLLEA-GADVNAKDNDGKTALDLAAENGNL---EIVKLLLEAGADLNAK 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-386 1.30e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  292 LHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77

                          90
                  ....*....|....*
gi 282847448  372 QILLTHpDIDRHITD 386
Cdd:pfam12796  78 KLLLEK-GADINVKD 91
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 531-631 1.83e-10

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 58.03  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNeetLKSIVPITKLKSKAPH-WINRILHEYKNLS 609
Cdd:cd14473    5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLS---LKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                         90       100
                 ....*....|....*....|..
gi 282847448 610 lseGVSKemHHLQRMFLQNCWE 631
Cdd:cd14473   82 ---GLSP--AEAKLKYLKIARK 98
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 296-381 5.48e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 296 ACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 282847448 376 THPDID 381
Cdd:PTZ00322 169 RHSQCH 174
 
Name Accession Description Interval E-value
NUDIX_5 pfam16705
NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at ...
 30-198 1.39e-102

NUDIX, or N-terminal NPxY motif-rich, region of KRIT; NUDIX_5 is found in higher eukaryotes at the N-terminus of KRIT1 or Krev interaction trapped proteins. NUDIX_5 carries three NPxY-like motifs, and it is found to bind the integrin cytoplasmic-associated protein 1 ICAP1. In the absence of KRIT1 ICAP1 binds via its C-terminal PH/PTB fold domain to the integrin beta-1 cytoplasmic tail. Binding of KRIT1 to ICAP1 via NUDIX_5 out-competes the binding of ICAP1 to integrin cytoplasmic tails such that ICAP1 is sequestered in the nucleus. Integrin activation is thus prevented.


Pssm-ID: 465241  Cd Length: 169  Bit Score: 310.52  E-value: 1.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   30 AKSYEILLHEVPIEGQKKKRKKVLLETKLQSNSEIAQGILDYVVETTKPISPANQGIKGKRVVLMRKFPLDGEKTGREAA 109
Cdd:pfam16705   1 AKSYEILLLEVPIEGKKKKRKKVLLETKLRGSQEATKQILDYVYETTKPISPDNQGIKGKRVVHMKKFPLDGEESGREAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  110 LFIVPSVVKDNTKYAYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTN 189
Cdd:pfam16705  81 LFVVPVNVKDNTKPSYSPGSPSFYCLQDIMRVCSESSTHFPTLTSRMLIALDKWLKEQHAVPHAIPALFRPSALERIKTN 160


                  ....*....
gi 282847448  190 VINPAYAAE 198
Cdd:pfam16705 161 VSNPAYATE 169
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 421-640 4.80e-35

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 131.65  E-value: 4.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   421 KVRIYRMDGSyrSVELKHGNNTTAQQIMEGMRLSQETqryftiwICSENLSLQFKPYHKPLQqvhDWPEILAELTNLDPQ 500
Cdd:smart00295   1 VLKVYLLDGT--TLEFEVDSSTTAEELLETVCRKLGI-------RESEYFGLQFEDPDEDLR---HWLDPAKTLLDQDVK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448   501 RETPQLFLRRDVGLPlEVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQgfLNEET 580
Cdd:smart00295  69 SEPLTLYFRVKFYPP-DPNQLKEDPTRLNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDL--RGELS 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282847448   581 LKSIVPITKLKS-KAPHWINRILHEYKNLSlsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:smart00295 146 LKRFLPKQLLDSrKLKEWRERIVELHKELI-----GLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 636-696 3.73e-29

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270018  Cd Length: 100  Bit Score: 111.55  E-value: 3.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 636 GAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETK---------------------------------------A 676
Cdd:cd13197    1 GAAFFTGQIFTKASSSNHKVIPVYVGVNIKGLHLLNMETKalllslkygcfmwqlgdadtcfqihslenkmsfvvhtkqA 80

                         90       100
                 ....*....|....*....|
gi 282847448 677 GLVVKLLMKLNGQLMPSERN 696
Cdd:cd13197   81 GLIVKLLMKLSGQRKPNDRN 100
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 517-640 2.83e-28

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 109.67  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  517 EVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNeetLKSIVPITKL-KSKAP 595
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLS---LESFLPKQLLrKMKSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 282847448  596 HWINRILHEYKNLSlsegvSKEMHHLQRMFLQNCWEIPTYGAAFF 640
Cdd:pfam00373  78 ELEKRVLEAHKNLR-----GLSAEEAKLKYLQIAQSLPTYGVEFF 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-421 4.99e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282847448 371 VQILLTHpDIDRHITDQQGRSPLNVCEENKQNnweEAAKLLKDAINKPYEK 421
Cdd:COG0666  202 VKLLLEA-GADVNAKDNDGKTALDLAAENGNL---EIVKLLLEAGADLNAK 248
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-414 1.15e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEI 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 282847448 371 VQILLTH-PDIDrhITDQQGRSPLNVCEENKQnnwEEAAKLLKDA 414
Cdd:COG0666  169 VKLLLEAgADVN--ARDNDGETPLHLAAENGH---LEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
291-421 1.15e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEI 370
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEI 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 282847448 371 VQILLTHPDIDRHITDQQGRSPLNVCEENKQNNWEEAAKLLKDAINKPYEK 421
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
292-386 1.30e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448  292 LHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGKCNpNLLNGQlsSPLHFAAGGGHAEIV 371
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGR--TALHYAARSGHLEIV 77

                          90
                  ....*....|....*
gi 282847448  372 QILLTHpDIDRHITD 386
Cdd:pfam12796  78 KLLLEK-GADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-414 7.98e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 7.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 288 DDFPLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 282847448 368 AEIVQILLTHpDIDRHITDQQGRSPLNV-CeenkQNNWEEAAKLLKDA 414
Cdd:COG0666  133 LEIVKLLLEA-GADVNAQDNDGNTPLHLaA----ANGNLEIVKLLLEA 175
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 531-631 1.83e-10

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 58.03  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 531 LFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNeetLKSIVPITKLKSKAPH-WINRILHEYKNLS 609
Cdd:cd14473    5 LYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLS---LKRFLPKQLLKQRKPEeWEKRIVELHKKLR 81

                         90       100
                 ....*....|....*....|..
gi 282847448 610 lseGVSKemHHLQRMFLQNCWE 631
Cdd:cd14473   82 ---GLSP--AEAKLKYLKIARK 98
Ank_4 pfam13637
Ankyrin repeats (many copies);
321-375 4.89e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 4.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 282847448  321 HWAPIHYACWYGKVEATRILLEKGKcNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
340-393 4.61e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 4.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 282847448  340 LLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLTHPdIDRHITDQQGRSPL 393
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 296-381 5.48e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 296 ACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ....*.
gi 282847448 376 THPDID 381
Cdd:PTZ00322 169 RHSQCH 174
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
288-414 1.46e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.72  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 288 DDFPLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGH 367
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 282847448 368 AEIVQILLTHpDIDRHITDQQGRSPLNVCEENKQnnwEEAAKLLKDA 414
Cdd:COG0666  100 LEIVKLLLEA-GADVNARDKDGETPLHLAAYNGN---LEIVKLLLEA 142
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 307-381 3.59e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 3.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282847448 307 LLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLTH-PDID 381
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNgPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 292-394 2.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 292 LHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIV 371
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACI 206

                         90       100
                 ....*....|....*....|....*
gi 282847448 372 QILLTHPDidrHITDQ--QGRSPLN 394
Cdd:PHA02874 207 KLLIDHGN---HIMNKckNGFTPLH 228
Ank_4 pfam13637
Ankyrin repeats (many copies);
291-341 3.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 282847448  291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILL 341
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
307-362 1.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 282847448  307 LLDKG-LSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFA 362
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 338-411 1.73e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282847448 338 RILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILLTHpDIDRHITDQQGRSPLNVCEEnkqNNWEEAAKLL 411
Cdd:PTZ00322  99 RILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEE---NGFREVVQLL 167
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 291-395 2.89e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKvEATRILLEKGKCNPNLLNGqlSSPLHFAAG-GGHAE 369
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDIDG--STPLHHAINpPCDID 269

                         90       100
                 ....*....|....*....|....*.
gi 282847448 370 IVQILLTHpDIDRHITDQQGRSPLNV 395
Cdd:PHA02874 270 IIDILLYH-KADISIKDNKGENPIDT 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 291-393 5.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 291 PLHRNACEGDSELLSHLLDKGLSVNQ-LDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAE 369
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100
                 ....*....|....*....|....
gi 282847448 370 IVQILLTHPDIdRHITDQQGRSPL 393
Cdd:PHA02875 150 GIELLIDHKAC-LDIEDCCGCTPL 172
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 296-416 6.79e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 6.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 296 ACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGGGHAEIVQILL 375
Cdd:PLN03192 533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 282847448 376 THPdidrHITDQQGRSPLnVCEENKQNNWEEAAKLLKDAIN 416
Cdd:PLN03192 612 HFA----SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLN 647
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 288-377 2.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 288 DDFPLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYACWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFAAGG-G 366
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYcK 246

                         90
                 ....*....|.
gi 282847448 367 HAEIVQILLTH 377
Cdd:PHA02878 247 DYDILKLLLEH 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 284-375 5.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282847448 284 RQWVDDFPLHRNACEGDSELLSHLLDKGLSVNQLDNDHWAPIHYA-CWYGKVEATRILLEKGkCNPNLLNGQLSSPLHFA 362
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-ANVNSKNKDLSTPLHYA 449

                         90
                 ....*....|....
gi 282847448 363 AGGG-HAEIVQILL 375
Cdd:PHA02876 450 CKKNcKLDVIEMLL 463
 
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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