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Conserved domains on  [gi|45502870|emb|CAF86155|]
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unnamed protein product [Homo sapiens]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
LEM super family cl02649
LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner ...
4-41 1.54e-17

LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins; The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions.


The actual alignment was detected with superfamily member cd12941:

Pssm-ID: 470643  Cd Length: 38  Bit Score: 76.10  E-value: 1.54e-17
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 45502870   4 LSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGE 41
Cdd:cd12941   1 LTDAELRRELLALGFRPGPITETTRKVYIKKLSCLRAE 38
MSC super family cl20377
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
278-493 2.01e-10

Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organization. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands.


The actual alignment was detected with superfamily member pfam09402:

Pssm-ID: 430586  Cd Length: 333  Bit Score: 62.31  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45502870   278 NFLAIQAGNFECGNPENLKSKCIPVMEAQEyIANVTSSSSAKfeaaltWILSSNKDVgIW------LKGEDqsELVTTVD 351
Cdd:pfam09402 109 ELLREKNAKVECGEGKDDLGALESGISEEE-LKDILSEKKSP------SLSDEEFEE-LWaaalgeLKKRP--EIVWRQD 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45502870   352 KVVCLE---------SAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVV 422
Cdd:pfam09402 179 SVGNSDgestrllrsTSLAYLPLKCRLRRSVRDTLARYRLILLGLLLLLLAILYLRSRYRRRRAEKARVEELVQEVLERL 258
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45502870   423 QDHYVDWEQDMERYP--YVGILHVRDSLIP--PQSRRRMkRVWDRAVEFLASNESrIQTESHRVAGEDMLVWRWT 493
Cdd:pfam09402 259 KNQKALHAEDPSLYPdpYLSSVQLRDDILRdeHSLKRRN-RLWKRVVKVVEGNSN-VRTSLREVHGEIMRVWEWI 331
 
Name Accession Description Interval E-value
LEM_LEMD2 cd12941
LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2); This CD ...
4-41 1.54e-17

LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2); This CD corresponds to the LEM domain that is responsible for the interaction with chromatin protein barrier-to-autointegration factor (BAF). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization. It also binds to lamin C and plays an important role in the organization of lamin A/C complexes. LEM2 contains an N-terminal LEM domain, two putative transmembrane domains and a MAN1-Src1p C-terminal (MSC) domain, but lacks the Man1-specific C-terminal RNA recognition motif (RRM).


Pssm-ID: 240588  Cd Length: 38  Bit Score: 76.10  E-value: 1.54e-17
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 45502870   4 LSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGE 41
Cdd:cd12941   1 LTDAELRRELLALGFRPGPITETTRKVYIKKLSCLRAE 38
LEM smart00540
in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, ...
1-41 1.79e-13

in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, including lamino-associated polypeptide 2 and emerin.


Pssm-ID: 128813  Cd Length: 44  Bit Score: 64.66  E-value: 1.79e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 45502870      1 MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGE 41
Cdd:smart00540   3 VDRLSDAELRAELKQYGLPPGPITDTTRKLYEKKLRKLRRG 43
LEM pfam03020
LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. ...
1-39 4.18e-13

LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. This domain is found in inner nuclear membrane proteins. It is called the LEM domain after LAP2, Emerin and Man1.


Pssm-ID: 460781  Cd Length: 40  Bit Score: 63.27  E-value: 4.18e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 45502870     1 MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLR 39
Cdd:pfam03020   2 VDQLSDEELREQLKEYGVSPGPITATTRKLYEKKLKKLL 40
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
278-493 2.01e-10

Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organization. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands.


Pssm-ID: 430586  Cd Length: 333  Bit Score: 62.31  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45502870   278 NFLAIQAGNFECGNPENLKSKCIPVMEAQEyIANVTSSSSAKfeaaltWILSSNKDVgIW------LKGEDqsELVTTVD 351
Cdd:pfam09402 109 ELLREKNAKVECGEGKDDLGALESGISEEE-LKDILSEKKSP------SLSDEEFEE-LWaaalgeLKKRP--EIVWRQD 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45502870   352 KVVCLE---------SAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVV 422
Cdd:pfam09402 179 SVGNSDgestrllrsTSLAYLPLKCRLRRSVRDTLARYRLILLGLLLLLLAILYLRSRYRRRRAEKARVEELVQEVLERL 258
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45502870   423 QDHYVDWEQDMERYP--YVGILHVRDSLIP--PQSRRRMkRVWDRAVEFLASNESrIQTESHRVAGEDMLVWRWT 493
Cdd:pfam09402 259 KNQKALHAEDPSLYPdpYLSSVQLRDDILRdeHSLKRRN-RLWKRVVKVVEGNSN-VRTSLREVHGEIMRVWEWI 331
 
Name Accession Description Interval E-value
LEM_LEMD2 cd12941
LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2); This CD ...
4-41 1.54e-17

LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2); This CD corresponds to the LEM domain that is responsible for the interaction with chromatin protein barrier-to-autointegration factor (BAF). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization. It also binds to lamin C and plays an important role in the organization of lamin A/C complexes. LEM2 contains an N-terminal LEM domain, two putative transmembrane domains and a MAN1-Src1p C-terminal (MSC) domain, but lacks the Man1-specific C-terminal RNA recognition motif (RRM).


Pssm-ID: 240588  Cd Length: 38  Bit Score: 76.10  E-value: 1.54e-17
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 45502870   4 LSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGE 41
Cdd:cd12941   1 LTDAELRRELLALGFRPGPITETTRKVYIKKLSCLRAE 38
LEM smart00540
in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, ...
1-41 1.79e-13

in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, including lamino-associated polypeptide 2 and emerin.


Pssm-ID: 128813  Cd Length: 44  Bit Score: 64.66  E-value: 1.79e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 45502870      1 MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGE 41
Cdd:smart00540   3 VDRLSDAELRAELKQYGLPPGPITDTTRKLYEKKLRKLRRG 43
LEM cd12934
LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner ...
4-40 3.82e-13

LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins; The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions.


Pssm-ID: 240585  Cd Length: 37  Bit Score: 63.19  E-value: 3.82e-13
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 45502870   4 LSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRG 40
Cdd:cd12934   1 LSDDELRRELKELGEPPGPITDTTRKVYLKKLAKLLK 37
LEM pfam03020
LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. ...
1-39 4.18e-13

LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. This domain is found in inner nuclear membrane proteins. It is called the LEM domain after LAP2, Emerin and Man1.


Pssm-ID: 460781  Cd Length: 40  Bit Score: 63.27  E-value: 4.18e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 45502870     1 MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLR 39
Cdd:pfam03020   2 VDQLSDEELREQLKEYGVSPGPITATTRKLYEKKLKKLL 40
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
278-493 2.01e-10

Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organization. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands.


Pssm-ID: 430586  Cd Length: 333  Bit Score: 62.31  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45502870   278 NFLAIQAGNFECGNPENLKSKCIPVMEAQEyIANVTSSSSAKfeaaltWILSSNKDVgIW------LKGEDqsELVTTVD 351
Cdd:pfam09402 109 ELLREKNAKVECGEGKDDLGALESGISEEE-LKDILSEKKSP------SLSDEEFEE-LWaaalgeLKKRP--EIVWRQD 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45502870   352 KVVCLE---------SAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVV 422
Cdd:pfam09402 179 SVGNSDgestrllrsTSLAYLPLKCRLRRSVRDTLARYRLILLGLLLLLLAILYLRSRYRRRRAEKARVEELVQEVLERL 258
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45502870   423 QDHYVDWEQDMERYP--YVGILHVRDSLIP--PQSRRRMkRVWDRAVEFLASNESrIQTESHRVAGEDMLVWRWT 493
Cdd:pfam09402 259 KNQKALHAEDPSLYPdpYLSSVQLRDDILRdeHSLKRRN-RLWKRVVKVVEGNSN-VRTSLREVHGEIMRVWEWI 331
LEM_LAP2_LEMD1 cd12940
LEM (Lap2/Emerin/Man1) domain found in lamina-associated polypeptide 2 (LAP2), LEM ...
3-39 7.37e-10

LEM (Lap2/Emerin/Man1) domain found in lamina-associated polypeptide 2 (LAP2), LEM domain-containing protein 1 (LEMP-1) and similar proteins; This CD corresponds to the LEM domain of LAP2, LEMP-1 and similar proteins. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some of LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. All LAP2 isoforms contain an N-terminal LEM domain that is connected to a highly divergent LEM-like domain by an unstructured linker. Although LEM and LEM-like domains share the same structural fold composed of two large parallel alpha helices, the biochemical nature of the solvent-accessible residues is completely different, indicating that the two domains may target different protein surfaces. The LEM domain interacts with the nonspecific DNA binding protein barrier-to-autointegration factor (BAF) while the LEM-like domain is involved in chromosome binding. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. It may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEMP-1 contains an N-terminal LEM domain.


Pssm-ID: 240587  Cd Length: 42  Bit Score: 54.23  E-value: 7.37e-10
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 45502870   3 GLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLR 39
Cdd:cd12940   4 ELSDEELKAQLLKYGVKPGPITASTRKLYEKKLQKLL 40
LEM_Man1 cd12942
LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1; This CD ...
2-43 2.63e-09

LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1; This CD corresponds to the LEM domain of Man1 and similar proteins. Man1, also termed LEM domain-containing protein 3 (LEMD3), is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor beta (TGF-beta) /activin/Nodal signaling pathway and bone morphogenetic protein (BMP) signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Man1 is a unique type of left/right (LR) signaling regulator that acts on the inner nuclear membrane. Furthermore, Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through interactions between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a Man1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of Man1 in the inner nuclear membrane. It has been shown that the C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both, DNA- and Smad-binding.


Pssm-ID: 240589  Cd Length: 44  Bit Score: 52.79  E-value: 2.63e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 45502870   2 AGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEAR 43
Cdd:cd12942   3 AQLTDEELFSELKRLGFSPGPVTESTRPVYLKKLKKLREEER 44
LEM_emerin cd12939
LEM (Lap2/Emerin/Man1) domain found in emerin; This CD corresponds to the LEM domain that is ...
2-43 3.24e-05

LEM (Lap2/Emerin/Man1) domain found in emerin; This CD corresponds to the LEM domain that is critical for binding to lamin A/C and is also involved in interaction with the DNA binding protein barrier-to-autointegration factor (BAF). Emerin is an inner nuclear membrane protein that occurs in four differently phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. It contains an N-terminal LEM domain followed by a poly-serine segment, a region rich in hydrophobic amino acids comprising the nuclear localization signal (NLS) followed by another poly-serine segment, and a C-terminal transmembrane region.


Pssm-ID: 240586  Cd Length: 43  Bit Score: 41.24  E-value: 3.24e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 45502870   2 AGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEAR 43
Cdd:cd12939   2 KDLSDDELIKVLRKYGIKHGPVVGSTRKLYEKKLREAERESK 43
LEM_ANKL1 cd12943
LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 ...
4-39 3.33e-05

LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 (ANKL1); The family includes ANKL1, also termed ankyrin repeat domain-containing protein 41 (ANKRD41), or LEM-domain containing protein 3 (LEM3), and similar proteins. Although their biological roles remain unclear, the family members contain an N-terminal ankyrin repeat region, LEM domain and C-terminal GIY-YIG nuclease domain. The ankyrin repeats are unique motifs mediating protein-protein interactions. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding.


Pssm-ID: 240590  Cd Length: 38  Bit Score: 40.97  E-value: 3.33e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 45502870   4 LSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLR 39
Cdd:cd12943   1 LSDLDLLRGLRALGESPGPITPFTRRVYLRRLEELQ 36
LEM_ANKL2 cd12944
LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 2 ...
1-37 3.43e-03

LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 2 (ANKL2); The family includes ANKL2 and similar proteins. Although their biological roles remain unclear, the family members share an N-terminal LEM domain and an ankyrin repeat region. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding. The ankyrin repeats are unique motifs mediating protein-protein interactions.


Pssm-ID: 240591  Cd Length: 43  Bit Score: 35.48  E-value: 3.43e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 45502870   1 MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRR 37
Cdd:cd12944   2 LKKLSPDELREELRKAGLKCGPITSTTRFLFEKKLAQ 38
 
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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