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Conserved domains on  [gi|24308303|ref|NP_085148|]
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SH3 domain-binding protein 5-like isoform 1 [Homo sapiens]

Protein Classification

SH3BP5 family protein( domain architecture ID 11156898)

SH3BP5 family protein similar to human SH3 domain-binding protein 5 (SH3BP5) that functions as guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
54-283 1.79e-109

SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.


:

Pssm-ID: 461608 [Multi-domain]  Cd Length: 231  Bit Score: 320.38  E-value: 1.79e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    54 EELDPRIQEELEHLNQASEEINQVELQLDEARTTYRRILQESARKLNTQGSHLGSCIEKARPYYEARRLAKEAQQETQKA 133
Cdd:pfam05276   1 EELDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   134 ALRYERAVSMHNAAREMVFVAEQGVMADKNR-LDPTWQEMLNHATCKVNEAEEERLRGEREHQRVTRLCQQAEARVQALQ 212
Cdd:pfam05276  81 ALRFERANSAHAAAKEMVALAEQGLLNNDEGtFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24308303   213 KTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHARRRGGLPPHP 283
Cdd:pfam05276 161 KKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
54-283 1.79e-109

SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.


Pssm-ID: 461608 [Multi-domain]  Cd Length: 231  Bit Score: 320.38  E-value: 1.79e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    54 EELDPRIQEELEHLNQASEEINQVELQLDEARTTYRRILQESARKLNTQGSHLGSCIEKARPYYEARRLAKEAQQETQKA 133
Cdd:pfam05276   1 EELDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   134 ALRYERAVSMHNAAREMVFVAEQGVMADKNR-LDPTWQEMLNHATCKVNEAEEERLRGEREHQRVTRLCQQAEARVQALQ 212
Cdd:pfam05276  81 ALRFERANSAHAAAKEMVALAEQGLLNNDEGtFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24308303   213 KTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHARRRGGLPPHP 283
Cdd:pfam05276 161 KKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
52-282 5.04e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   52 EEEELDPRI---QEELEHLNQASEEI----NQVELqLDEARTTYRRILQESARKlntqgSHLGSCIEKARPYYEARRLAK 124
Cdd:COG4913  219 EEPDTFEAAdalVEHFDDLERAHEALedarEQIEL-LEPIRELAERYAAARERL-----AELEYLRAALRLWFAQRRLEL 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303  125 ------EAQQETQKAALRYERAVSMHNAAREMVFVAEQGVMADK-NRLDPtWQEMLNHATckvneaeEERLRGEREHQRV 197
Cdd:COG4913  293 leaeleELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQ-LEREIERLE-------RELEERERRRARL 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303  198 TRLCQQAEARVQALQKTLRraigksrpyfELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHA--RR 275
Cdd:COG4913  365 EALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASleRR 434

                 ....*..
gi 24308303  276 RGGLPPH 282
Cdd:COG4913  435 KSNIPAR 441
mukB PRK04863
chromosome partition protein MukB;
46-271 1.95e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    46 AKLSPREEE-----ELDPRIQEELE-HLNQASEEINQVELQL-------DEART---TYRRILQ--ESARKLNtQGSHLG 107
Cdd:PRK04863  358 EELEERLEEqnevvEEADEQQEENEaRAEAAEEEVDELKSQLadyqqalDVQQTraiQYQQAVQalERAKQLC-GLPDLT 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   108 scIEKARPYYEArrLAKEAQQETQkAALRYERAVSMHNAAREMVFVAEQGVMA-----DKNRLDPTWQEMLNHATCKVNE 182
Cdd:PRK04863  437 --ADNAEDWLEE--FQAKEQEATE-ELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRHL 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   183 AEEERLRGEREHQRVTRLCQQaearvQALQKTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALR 262
Cdd:PRK04863  512 AEQLQQLRMRLSELEQRLRQQ-----QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586

                  ....*....
gi 24308303   263 NLEQISEQI 271
Cdd:PRK04863  587 QLEQLQARI 595
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
51-271 6.92e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303     51 REEEELDPRIQEELEHLNQASEEINQVELQLDEARTTY-------------RRILQESARKLNTQGSHLGSCIEKA-RPY 116
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqKQILRERLANLERQLEELEAQLEELeSKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    117 YEARRLAKEAQQETQKAALRYERAVSMHNAAREMVFVAEQGVMAdknrldptWQEMLNHATCKVNEAEEERLRGEREHQR 196
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE--------LEEQLETLRSKVAQLELQIASLNNEIER 404
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24308303    197 vtrlcqqAEARVQALQKtlRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQI 271
Cdd:TIGR02168  405 -------LEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
 
Name Accession Description Interval E-value
SH3BP5 pfam05276
SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 ...
54-283 1.79e-109

SH3 domain-binding protein 5 (SH3BP5); This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule.


Pssm-ID: 461608 [Multi-domain]  Cd Length: 231  Bit Score: 320.38  E-value: 1.79e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    54 EELDPRIQEELEHLNQASEEINQVELQLDEARTTYRRILQESARKLNTQGSHLGSCIEKARPYYEARRLAKEAQQETQKA 133
Cdd:pfam05276   1 EELDPRIQGELEKLNQATDEINKLEIELEEARSTFRELLAESSRKLKALSKKLGSCIDKARPYYEAKRRAKEAQQESQKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   134 ALRYERAVSMHNAAREMVFVAEQGVMADKNR-LDPTWQEMLNHATCKVNEAEEERLRGEREHQRVTRLCQQAEARVQALQ 212
Cdd:pfam05276  81 ALRFERANSAHAAAKEMVALAEQGLLNNDEGtFDPAWQEMLNHATQKVMEAENEKTRAEREHQRKTKLCLAAETKVQQLE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24308303   213 KTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHARRRGGLPPHP 283
Cdd:pfam05276 161 KKLKRSIKKSRPYFELKAQLNKQLEAQKEKVLQLEEEVKEAKARYSTALRNLEQISEEIHEQRRSEKSEPP 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
52-282 5.04e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   52 EEEELDPRI---QEELEHLNQASEEI----NQVELqLDEARTTYRRILQESARKlntqgSHLGSCIEKARPYYEARRLAK 124
Cdd:COG4913  219 EEPDTFEAAdalVEHFDDLERAHEALedarEQIEL-LEPIRELAERYAAARERL-----AELEYLRAALRLWFAQRRLEL 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303  125 ------EAQQETQKAALRYERAVSMHNAAREMVFVAEQGVMADK-NRLDPtWQEMLNHATckvneaeEERLRGEREHQRV 197
Cdd:COG4913  293 leaeleELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQ-LEREIERLE-------RELEERERRRARL 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303  198 TRLCQQAEARVQALQKTLRraigksrpyfELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHA--RR 275
Cdd:COG4913  365 EALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASleRR 434

                 ....*..
gi 24308303  276 RGGLPPH 282
Cdd:COG4913  435 KSNIPAR 441
mukB PRK04863
chromosome partition protein MukB;
46-271 1.95e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    46 AKLSPREEE-----ELDPRIQEELE-HLNQASEEINQVELQL-------DEART---TYRRILQ--ESARKLNtQGSHLG 107
Cdd:PRK04863  358 EELEERLEEqnevvEEADEQQEENEaRAEAAEEEVDELKSQLadyqqalDVQQTraiQYQQAVQalERAKQLC-GLPDLT 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   108 scIEKARPYYEArrLAKEAQQETQkAALRYERAVSMHNAAREMVFVAEQGVMA-----DKNRLDPTWQEMLNHATCKVNE 182
Cdd:PRK04863  437 --ADNAEDWLEE--FQAKEQEATE-ELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRHL 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303   183 AEEERLRGEREHQRVTRLCQQaearvQALQKTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALR 262
Cdd:PRK04863  512 AEQLQQLRMRLSELEQRLRQQ-----QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586

                  ....*....
gi 24308303   263 NLEQISEQI 271
Cdd:PRK04863  587 QLEQLQARI 595
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
51-271 6.92e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303     51 REEEELDPRIQEELEHLNQASEEINQVELQLDEARTTY-------------RRILQESARKLNTQGSHLGSCIEKA-RPY 116
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqKQILRERLANLERQLEELEAQLEELeSKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303    117 YEARRLAKEAQQETQKAALRYERAVSMHNAAREMVFVAEQGVMAdknrldptWQEMLNHATCKVNEAEEERLRGEREHQR 196
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE--------LEEQLETLRSKVAQLELQIASLNNEIER 404
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24308303    197 vtrlcqqAEARVQALQKtlRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQI 271
Cdd:TIGR02168  405 -------LEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
51-276 8.38e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 8.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303  51 REEEELDPRIQEELEHLNQASEEINQVELQLDEARTTYRRiLQESARKLNTQGSHLGSCIEKArpyyEARRLAKEAQQET 130
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAEL----EKEIAELRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308303 131 QKAAL-RYERAVSMHNAAREMVFVAEQGVMADKNRLdptwQEMLNHATckvNEAEEERLRGEREHQRVTRLCQQAEARVQ 209
Cdd:COG4942 102 QKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRR----LQYLKYLA---PARREQAEELRADLAELAALRAELEAERA 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24308303 210 ALQKTLRRAIGKSRPYFELKAQFSQILEEHKAKVTELEQQVAQAKTRYSVALRNLEQISEQIHARRR 276
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
 
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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