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Conserved domains on  [gi|7656952|ref|NP_055227|]
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calcyclin-binding protein isoform 1 [Homo sapiens]

Protein Classification

Siah-Interact_N and p23_CacyBP domain-containing protein( domain architecture ID 13759603)

Siah-Interact_N and p23_CacyBP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p23_CacyBP cd06468
p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP) ...
 75-167 1.48e-38

p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP)/Siah-1-interacting protein (SIP). CacyBP/SIP interacts with S100A6 (calcyclin), with some other members of the S100 family, with tubulin, and with Siah-1 and Skp-1. The latter two are components of the ubiquitin ligase that regulates beta-catenin degradation. The beta-catenin gene is an oncogene participating in tumorigenesis in many different cancers. Overexpression of CacyBP/SIP, in part through its effect on the expression of beta-catenin, inhibits the proliferation, tumorigenicity, and invasion of gastric cancer cells. CacyBP/SIP is abundant in neurons and neuroblastoma NB2a cells. An extensive re-organization of microtubules accompanies the differentiation of NB2a cells. CacyBP/SIP may contribute to NB2a cell differentiation through binding to and increasing the oligomerization of tubulin. CacyBP/SIP is also implicated in differentiation of erythroid cells, rat neonatal cardiomyocytes, in mouse endometrial events, and in thymocyte development.


:

Pssm-ID: 107225  Cd Length: 92  Bit Score: 128.92  E-value: 1.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   75 ISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKSYSMIVNNLLKPISVEGSSKKVKTDTVLILC 154
Cdd:cd06468   1 ITKYAWDQSDKFVKIYITLKGVHQLPKENIQVEFTERSFELKVHDLNGKNYRFTINRLLKKIDPEKSSFKVKTDRIVITL 80

                        90
                ....*....|...
gi 7656952  155 RKKvENTRWDYLT 167
Cdd:cd06468  81 AKK-KEKKWESLT 92
Siah-Interact_N pfam09032
Siah interacting protein, N terminal; The N terminal domain of Siah interacting protein (SIP) ...
 1-75 5.00e-27

Siah interacting protein, N terminal; The N terminal domain of Siah interacting protein (SIP) adopts a helical hairpin structure with a hydrophobic core stabilized by a classic knobs-and-holes arrangement of side chains contributed by the two amphipathic helices. Little is known about this domain's function, except that it is crucial for interactions with Siah. It has also been hypothesized that SIP can dimerize through this N terminal domain.


:

Pssm-ID: 462660  Cd Length: 77  Bit Score: 98.98  E-value: 5.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952      1 MASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEI-------KNKMQQKSQkkaelLDNEKPAAVVAPITTGYTV 73
Cdd:pfam09032   1 STLEELQLDLEELKSLLEKATRKRVQDLLTIEIRKLETELlrlkelqANKAQQKSQ-----LENEKPSAKVAPITKGYTV 75


                  ..
gi 7656952     74 KI 75
Cdd:pfam09032  76 KI 77
SGS super family cl38174
SGS domain; This domain was thought to be unique to the SGT1-like proteins, but is also found ...
 182-217 1.83e-03

SGS domain; This domain was thought to be unique to the SGT1-like proteins, but is also found in calcyclin binding proteins.


The actual alignment was detected with superfamily member pfam05002:

Pssm-ID: 461514 [Multi-domain]  Cd Length: 81  Bit Score: 36.00  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7656952    182 DTETDPSEGLMNVL-KKIYEDGDDDMKRTINKAWVES 217
Cdd:pfam05002  15 KEEKDGGDAALNAFfQKIYADADEDTRRAMMKSFVES 51
 
Name Accession Description Interval E-value
p23_CacyBP cd06468
p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP) ...
 75-167 1.48e-38

p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP)/Siah-1-interacting protein (SIP). CacyBP/SIP interacts with S100A6 (calcyclin), with some other members of the S100 family, with tubulin, and with Siah-1 and Skp-1. The latter two are components of the ubiquitin ligase that regulates beta-catenin degradation. The beta-catenin gene is an oncogene participating in tumorigenesis in many different cancers. Overexpression of CacyBP/SIP, in part through its effect on the expression of beta-catenin, inhibits the proliferation, tumorigenicity, and invasion of gastric cancer cells. CacyBP/SIP is abundant in neurons and neuroblastoma NB2a cells. An extensive re-organization of microtubules accompanies the differentiation of NB2a cells. CacyBP/SIP may contribute to NB2a cell differentiation through binding to and increasing the oligomerization of tubulin. CacyBP/SIP is also implicated in differentiation of erythroid cells, rat neonatal cardiomyocytes, in mouse endometrial events, and in thymocyte development.


Pssm-ID: 107225  Cd Length: 92  Bit Score: 128.92  E-value: 1.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   75 ISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKSYSMIVNNLLKPISVEGSSKKVKTDTVLILC 154
Cdd:cd06468   1 ITKYAWDQSDKFVKIYITLKGVHQLPKENIQVEFTERSFELKVHDLNGKNYRFTINRLLKKIDPEKSSFKVKTDRIVITL 80

                        90
                ....*....|...
gi 7656952  155 RKKvENTRWDYLT 167
Cdd:cd06468  81 AKK-KEKKWESLT 92
Siah-Interact_N pfam09032
Siah interacting protein, N terminal; The N terminal domain of Siah interacting protein (SIP) ...
 1-75 5.00e-27

Siah interacting protein, N terminal; The N terminal domain of Siah interacting protein (SIP) adopts a helical hairpin structure with a hydrophobic core stabilized by a classic knobs-and-holes arrangement of side chains contributed by the two amphipathic helices. Little is known about this domain's function, except that it is crucial for interactions with Siah. It has also been hypothesized that SIP can dimerize through this N terminal domain.


Pssm-ID: 462660  Cd Length: 77  Bit Score: 98.98  E-value: 5.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952      1 MASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEI-------KNKMQQKSQkkaelLDNEKPAAVVAPITTGYTV 73
Cdd:pfam09032   1 STLEELQLDLEELKSLLEKATRKRVQDLLTIEIRKLETELlrlkelqANKAQQKSQ-----LENEKPSAKVAPITKGYTV 75


                  ..
gi 7656952     74 KI 75
Cdd:pfam09032  76 KI 77
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 77-156 3.04e-11

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 57.27  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952     77 NYGWDQSDKFVKIYITLTGVHqVPTENVQVHFTERSfdLLVKNLNGKSYsmIVNNLLKPISVEGSSKKVKTDTVLILCRK 156
Cdd:pfam04969   2 RYDWYQTLDEVTITIPVKGAG-IKKKDVKVNIKPRS--LKVKIKGGYEL--IDGELFHPIDPEESSWTIEGKKVEITLKK 76
SGT1 COG5091
Suppressor of G2 allele of skp1 and related proteins [General function prediction only];
8-217 2.49e-04

Suppressor of G2 allele of skp1 and related proteins [General function prediction only];


Pssm-ID: 227422 [Multi-domain]  Cd Length: 368  Bit Score: 41.23  E-value: 2.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952    8 KDLEEVKVLLEKATRKRVRDALTAEKSKIETE--IKNKMQQKSQKKAELL---------DNEKPAAVVAP--ITTGYTVK 74
Cdd:COG5091  93 KDYELAQSYFKKAKNLYVDDTLPLWEDRLETKlnKKNKKQKDSTNKHTIKpvesienrgDNNSSHSPISPlkIETAPQES 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   75 ISN-YGWDQSDKFVKIYITLTGVhQVPTENVQVHFTERSFDLLVKNLNGKSYSMIVNNLLKPISVEGSSKKVKTDTVLIL 153
Cdd:COG5091 173 PKMeIAYDFSETSDTAIIFIYRP-PVGDEQVSPVLEGNTLSISYQPRRLRLWNDITISLYKEVYPDIRSIKSFSKRVEVH 251

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952  154 CRKkVENTRW-----DYLTQVEKECKEKEKPSY-------------------DTETDPSEGLMNVLKKIYEDGDDDMKRT 209
Cdd:COG5091 252 LRK-VEMVRWgglngRPADESSRLSDEGKNSDSatpksskkqddwkelmvedSGDEENPSVMDSLFQKLYQRADDDTRRA 330


                ....*...
gi 7656952  210 INKAWVES 217
Cdd:COG5091 331 MMKSFYES 338
SGS pfam05002
SGS domain; This domain was thought to be unique to the SGT1-like proteins, but is also found ...
 182-217 1.83e-03

SGS domain; This domain was thought to be unique to the SGT1-like proteins, but is also found in calcyclin binding proteins.


Pssm-ID: 461514 [Multi-domain]  Cd Length: 81  Bit Score: 36.00  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7656952    182 DTETDPSEGLMNVL-KKIYEDGDDDMKRTINKAWVES 217
Cdd:pfam05002  15 KEEKDGGDAALNAFfQKIYADADEDTRRAMMKSFVES 51
PTZ00121 PTZ00121
MAEBL; Provisional
 3-63 5.62e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 5.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7656952      3 SEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEIKNKMQQ---KSQKKAELLDNEKPAAV 63
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlkkEEEKKAEEIRKEKEAVI 1781
 
Name Accession Description Interval E-value
p23_CacyBP cd06468
p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP) ...
 75-167 1.48e-38

p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP)/Siah-1-interacting protein (SIP). CacyBP/SIP interacts with S100A6 (calcyclin), with some other members of the S100 family, with tubulin, and with Siah-1 and Skp-1. The latter two are components of the ubiquitin ligase that regulates beta-catenin degradation. The beta-catenin gene is an oncogene participating in tumorigenesis in many different cancers. Overexpression of CacyBP/SIP, in part through its effect on the expression of beta-catenin, inhibits the proliferation, tumorigenicity, and invasion of gastric cancer cells. CacyBP/SIP is abundant in neurons and neuroblastoma NB2a cells. An extensive re-organization of microtubules accompanies the differentiation of NB2a cells. CacyBP/SIP may contribute to NB2a cell differentiation through binding to and increasing the oligomerization of tubulin. CacyBP/SIP is also implicated in differentiation of erythroid cells, rat neonatal cardiomyocytes, in mouse endometrial events, and in thymocyte development.


Pssm-ID: 107225  Cd Length: 92  Bit Score: 128.92  E-value: 1.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   75 ISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKSYSMIVNNLLKPISVEGSSKKVKTDTVLILC 154
Cdd:cd06468   1 ITKYAWDQSDKFVKIYITLKGVHQLPKENIQVEFTERSFELKVHDLNGKNYRFTINRLLKKIDPEKSSFKVKTDRIVITL 80

                        90
                ....*....|...
gi 7656952  155 RKKvENTRWDYLT 167
Cdd:cd06468  81 AKK-KEKKWESLT 92
Siah-Interact_N pfam09032
Siah interacting protein, N terminal; The N terminal domain of Siah interacting protein (SIP) ...
 1-75 5.00e-27

Siah interacting protein, N terminal; The N terminal domain of Siah interacting protein (SIP) adopts a helical hairpin structure with a hydrophobic core stabilized by a classic knobs-and-holes arrangement of side chains contributed by the two amphipathic helices. Little is known about this domain's function, except that it is crucial for interactions with Siah. It has also been hypothesized that SIP can dimerize through this N terminal domain.


Pssm-ID: 462660  Cd Length: 77  Bit Score: 98.98  E-value: 5.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952      1 MASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEI-------KNKMQQKSQkkaelLDNEKPAAVVAPITTGYTV 73
Cdd:pfam09032   1 STLEELQLDLEELKSLLEKATRKRVQDLLTIEIRKLETELlrlkelqANKAQQKSQ-----LENEKPSAKVAPITKGYTV 75


                  ..
gi 7656952     74 KI 75
Cdd:pfam09032  76 KI 77
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 80-167 1.29e-13

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 63.84  E-value: 1.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   80 WDQSDKFVKIYITLTGVHqvpTENVQVHFTERSFDLLVKNLNGKSYSMIVNnLLKPISVEGSSKKVKTDTVLILCRKKVE 159
Cdd:cd06463   1 WYQTLDEVTITIPLKDVT---KKDVKVEFTPKSLTVSVKGGGGKEYLLEGE-LFGPIDPEESKWTVEDRKIEITLKKKEP 76


                ....*...
gi 7656952  160 NTRWDYLT 167
Cdd:cd06463  77 GEWWPRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 77-156 3.04e-11

CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans but are found in separate proteins in plants; this is thought to be indicative of an interaction between CS and CHORD. It has been suggested that the CS domain is a binding module for HSP90, implying that CS domain-containing proteins are involved in recruiting heat shock proteins to multiprotein assemblies. Two CS domains are found at the N-terminus of Ubiquitin carboxyl-terminal hydrolase 19 (USP19), these domains may play a role in the interaction of USP19 with cellular inhibitor of apoptosis 2.


Pssm-ID: 461503  Cd Length: 76  Bit Score: 57.27  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952     77 NYGWDQSDKFVKIYITLTGVHqVPTENVQVHFTERSfdLLVKNLNGKSYsmIVNNLLKPISVEGSSKKVKTDTVLILCRK 156
Cdd:pfam04969   2 RYDWYQTLDEVTITIPVKGAG-IKKKDVKVNIKPRS--LKVKIKGGYEL--IDGELFHPIDPEESSWTIEGKKVEITLKK 76
SGT1 COG5091
Suppressor of G2 allele of skp1 and related proteins [General function prediction only];
8-217 2.49e-04

Suppressor of G2 allele of skp1 and related proteins [General function prediction only];


Pssm-ID: 227422 [Multi-domain]  Cd Length: 368  Bit Score: 41.23  E-value: 2.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952    8 KDLEEVKVLLEKATRKRVRDALTAEKSKIETE--IKNKMQQKSQKKAELL---------DNEKPAAVVAP--ITTGYTVK 74
Cdd:COG5091  93 KDYELAQSYFKKAKNLYVDDTLPLWEDRLETKlnKKNKKQKDSTNKHTIKpvesienrgDNNSSHSPISPlkIETAPQES 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   75 ISN-YGWDQSDKFVKIYITLTGVhQVPTENVQVHFTERSFDLLVKNLNGKSYSMIVNNLLKPISVEGSSKKVKTDTVLIL 153
Cdd:COG5091 173 PKMeIAYDFSETSDTAIIFIYRP-PVGDEQVSPVLEGNTLSISYQPRRLRLWNDITISLYKEVYPDIRSIKSFSKRVEVH 251

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952  154 CRKkVENTRW-----DYLTQVEKECKEKEKPSY-------------------DTETDPSEGLMNVLKKIYEDGDDDMKRT 209
Cdd:COG5091 252 LRK-VEMVRWgglngRPADESSRLSDEGKNSDSatpksskkqddwkelmvedSGDEENPSVMDSLFQKLYQRADDDTRRA 330


                ....*...
gi 7656952  210 INKAWVES 217
Cdd:COG5091 331 MMKSFYES 338
SGS pfam05002
SGS domain; This domain was thought to be unique to the SGT1-like proteins, but is also found ...
 182-217 1.83e-03

SGS domain; This domain was thought to be unique to the SGT1-like proteins, but is also found in calcyclin binding proteins.


Pssm-ID: 461514 [Multi-domain]  Cd Length: 81  Bit Score: 36.00  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7656952    182 DTETDPSEGLMNVL-KKIYEDGDDDMKRTINKAWVES 217
Cdd:pfam05002  15 KEEKDGGDAALNAFfQKIYADADEDTRRAMMKSFVES 51
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
 80-167 2.73e-03

p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related proteins. hSgt1 is a co-chaperone which has been shown to be elevated in HEp-2 cells as a result of stress conditions such as heat shock. It interacts with the heat shock proteins (HSPs) Hsp70 and Hsp90, and it expression pattern is synchronized with these two Hsps. The interaction with HSP90 has been shown to involve the hSgt1_CS domain, and appears to be required for correct kinetochore assembly and efficient cell division. Some proteins in this subgroup contain a tetratricopeptide repeat (TPR) HSP-binding domain N-terminal to this CS domain, and most proteins in this subgroup contain a Sgt1-specific (SGS) domain C-terminal to the CS domain. The SGS domain interacts with some S100 family proteins. Studies suggest that S100A6 modulates in a Ca2+ dependent manner the interactions of hSgt1 with Hsp90 and Hsp70. The yeast Sgt1 CS domain is not found in this subgroup.


Pssm-ID: 107239  Cd Length: 84  Bit Score: 35.82  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   80 WDQSDKFVKIYITLTGVHQvptENVQVHFTERSFDLLVKNLNGKSYSMIVnNLLKPISVEGSSKKVKTDTVLILCrKKVE 159
Cdd:cd06489   2 WYQTESQVVITILIKNVKP---EDVSVEFEKRELSATVKLPSGNDYSLKL-HLLHPIVPEQSSYKILSTKIEIKL-KKTE 76


                ....*...
gi 7656952  160 NTRWDYLT 167
Cdd:cd06489  77 AIRWSKLE 84
PTZ00121 PTZ00121
MAEBL; Provisional
 3-63 5.62e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 5.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7656952      3 SEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEIKNKMQQ---KSQKKAELLDNEKPAAV 63
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlkkEEEKKAEEIRKEKEAVI 1781
p23_hB-ind1_like cd06465
p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. ...
 80-168 7.44e-03

p23_like domain found in human (h) butyrate-induced transcript 1 (B-ind1) and similar proteins. hB-ind1 participates in signaling by the small GTPase Rac1. It binds to Rac1 and enhances different Rac1 effects including activation of nuclear factor (NF) kappaB and activation of c-Jun N-terminal kinase (JNK). hB-ind1 also plays a part in the RNA replication and particle production of Hepatitis C virus (HCV) through its interaction with heat shock protein Hsp90, HCV nonstructural protein 5A (NS5A), and the immunophilin FKBP8. hB-ind1 is upregulated in the outer layer of Chinese hamster V79 cells grown as multicell spheroids, versus in the same cells grown as monolayers. This group includes the Saccharomyces cerevisiae Sba1, a co-chaperone of the Hsp90. Sba1 has been shown to be is required for telomere length maintenance, and may modulate telomerase DNA-binding activity.


Pssm-ID: 107222 [Multi-domain]  Cd Length: 108  Bit Score: 35.26  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7656952   80 WDQSDKFvkIYITLtgvhQVP-TENVQVHFTERSFDLLVKN-LNGKSYSMIVNnLLKPISVEGSSKKVKTDTVLILCRKK 157
Cdd:cd06465   5 WAQRSDV--VYLTI----ELPdAKDPKIKLEPTSLSFKAKGgGGGKKYEFDLE-FYKEIDPEESKYKVTGRQIEFVLRKK 77

                        90
                ....*....|.
gi 7656952  158 VENTRWDYLTQ 168
Cdd:cd06465  78 EAGEYWPRLTK 88
 
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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