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Conserved domains on  [gi|228008343|ref|NP_001153114|]
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bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein isoform b [Homo sapiens]

Protein Classification

BNIP2 family protein( domain architecture ID 10575844)

BNIP2 (Bcl-2/adenovirus E1B 19 kDa-interacting protein 2) family protein containing a Sec14p-like lipid-binding domain, similar to human caytaxin (or BNIP-H) that functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
1-129 4.70e-59

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


:

Pssm-ID: 463609  Cd Length: 135  Bit Score: 184.13  E-value: 4.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343    1 MRKRLSAPELRLSLTKGPGnDGASPTQSaPSSPDGSS----DLEIDELETPSDSEQLD---SGHEFEWEDELPR-AEGLG 72
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSED-SFLSAFLS-PSPDDFSDtddlDINVDDLETPSDSDSLEfpeNGNELEWEDDLPRlGRGSG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 228008343   73 TSETAERLGRGCMWDVTGEDGHHWRVFRMGPREQRVDMTVIEPYKKVLSHGGYHGDG 129
Cdd:pfam12496  79 PSEAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
131-268 1.08e-24

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


:

Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 95.86  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343  131 NAVILFASCYLPRSSIPnyTYVMEHLFRYMVGTL-ELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRA 209
Cdd:pfam13716   2 RPVLVFISKLLPSRPAS--LDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008343  210 LVVVHATWYVKAFLA-LLRPFISSKFTRKIRFLDSLGELAQLISLDQV--HIPeAVRQLDRD 268
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYDEE 140
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
1-129 4.70e-59

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


Pssm-ID: 463609  Cd Length: 135  Bit Score: 184.13  E-value: 4.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343    1 MRKRLSAPELRLSLTKGPGnDGASPTQSaPSSPDGSS----DLEIDELETPSDSEQLD---SGHEFEWEDELPR-AEGLG 72
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSED-SFLSAFLS-PSPDDFSDtddlDINVDDLETPSDSDSLEfpeNGNELEWEDDLPRlGRGSG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 228008343   73 TSETAERLGRGCMWDVTGEDGHHWRVFRMGPREQRVDMTVIEPYKKVLSHGGYHGDG 129
Cdd:pfam12496  79 PSEAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
131-268 1.08e-24

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 95.86  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343  131 NAVILFASCYLPRSSIPnyTYVMEHLFRYMVGTL-ELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRA 209
Cdd:pfam13716   2 RPVLVFISKLLPSRPAS--LDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008343  210 LVVVHATWYVKAFLA-LLRPFISSKFTRKIRFLDSLGELAQLISLDQV--HIPeAVRQLDRD 268
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
113-259 1.24e-22

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 90.86  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343 113 IEPYKKVLSHGGYHG----DGlNAVILFASCYLPRSSIPnytyvMEHLFRYMVGTLELLVAENY------LLVHLSGGTS 182
Cdd:cd00170    1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPKLLD-----LEELLRYLVYLLEKALRELEeqvegfVVIIDLKGFS 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008343 183 RAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALLRPFISSKFTRKIRFLDS-LGELAQLISLDQVHIP 259
Cdd:cd00170   75 LSNLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
113-260 8.44e-18

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 78.11  E-value: 8.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343   113 IEPYKKVLShGGYHGDGLNAVILFASCYLprssIPNYTYVMEHLFRYMVGTLELLVAENYLLVHLSG--------GTSRA 184
Cdd:smart00516   2 LELLKAYIP-GGRGYDKDGRPVLIERAGR----FDLKSVTLEELLRYLVYVLEKILQEEKKTGGIEGftvifdlkGLSMS 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008343   185 QvPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALLRPFISSKFTRKIRFL--DSLGELAQLISLDQvhIPE 260
Cdd:smart00516  77 N-PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVgnDSKEELLEYIDKEQ--LPE 151
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
1-129 4.70e-59

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


Pssm-ID: 463609  Cd Length: 135  Bit Score: 184.13  E-value: 4.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343    1 MRKRLSAPELRLSLTKGPGnDGASPTQSaPSSPDGSS----DLEIDELETPSDSEQLD---SGHEFEWEDELPR-AEGLG 72
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSED-SFLSAFLS-PSPDDFSDtddlDINVDDLETPSDSDSLEfpeNGNELEWEDDLPRlGRGSG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 228008343   73 TSETAERLGRGCMWDVTGEDGHHWRVFRMGPREQRVDMTVIEPYKKVLSHGGYHGDG 129
Cdd:pfam12496  79 PSEAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
131-268 1.08e-24

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 95.86  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343  131 NAVILFASCYLPRSSIPnyTYVMEHLFRYMVGTL-ELLVAENYLLVHLSGGTSRAQVPPLSWIRQCYRTLDRRLRKNLRA 209
Cdd:pfam13716   2 RPVLVFISKLLPSRPAS--LDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008343  210 LVVVHATWYVKAFLA-LLRPFISSKFTRKIRFLDSLGELAQLISLDQV--HIPeAVRQLDRD 268
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLptELP-GVLSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
113-259 1.24e-22

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 90.86  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343 113 IEPYKKVLSHGGYHG----DGlNAVILFASCYLPRSSIPnytyvMEHLFRYMVGTLELLVAENY------LLVHLSGGTS 182
Cdd:cd00170    1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPKLLD-----LEELLRYLVYLLEKALRELEeqvegfVVIIDLKGFS 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008343 183 RAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALLRPFISSKFTRKIRFLDS-LGELAQLISLDQVHIP 259
Cdd:cd00170   75 LSNLSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
113-260 8.44e-18

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 78.11  E-value: 8.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343   113 IEPYKKVLShGGYHGDGLNAVILFASCYLprssIPNYTYVMEHLFRYMVGTLELLVAENYLLVHLSG--------GTSRA 184
Cdd:smart00516   2 LELLKAYIP-GGRGYDKDGRPVLIERAGR----FDLKSVTLEELLRYLVYVLEKILQEEKKTGGIEGftvifdlkGLSMS 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008343   185 QvPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFLALLRPFISSKFTRKIRFL--DSLGELAQLISLDQvhIPE 260
Cdd:smart00516  77 N-PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVgnDSKEELLEYIDKEQ--LPE 151
CRAL_TRIO pfam00650
CRAL/TRIO domain;
153-256 1.88e-07

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 49.56  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008343  153 MEHLFRYMVGTLELLVAENY--------LLVHLSG-GTSRAQVPPLSWIRQCYRTLDRRLRKNLRALVVVHATWYVKAFL 223
Cdd:pfam00650  31 EEELVRFLVLVLERALLLMPegqvegltVIIDLKGlSLSNMDWWSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIW 110
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 228008343  224 ALLRPFISSKFTRKIRFLDS--LGELAQLISLDQV 256
Cdd:pfam00650 111 KLIKPFLDPKTREKIVFLKNsnEEELEKYIPPEQL 145
 
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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