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Conserved domains on  [gi|157818035|ref|NP_001101715|]
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integrin beta-1-binding protein 2 [Rattus norvegicus]

Protein Classification

cysteine and histidine-rich domain-containing protein( domain architecture ID 10523069)

cysteine and histidine-rich domain (CHORD)-containing protein is a zinc-binding protein similar to Homo sapiens cysteine and histidine-rich domain-containing protein 1 (CHORDC1) and integrin beta-1-binding protein 2 (ITGB1BP2)

Gene Ontology:  GO:0008270

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
 218-304 4.29e-51

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


:

Pssm-ID: 107238  Cd Length: 87  Bit Score: 164.78  E-value: 4.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 218 CRHDWHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKADP 297
Cdd:cd06488    1 CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTKVEIKLRKAEP 80


                 ....*..
gi 157818035 298 GSWAQLE 304
Cdd:cd06488   81 GSWAKLE 87
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 3-64 3.26e-37

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


:

Pssm-ID: 461502  Cd Length: 62  Bit Score: 128.02  E-value: 3.26e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818035    3 LLCYNKGCGQHFDPNTNLPDSCRYHPGVPIFHDALKGWSCCRKRTVDFSEFLNIKGCTVGPH 64
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 148-208 1.54e-30

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


:

Pssm-ID: 461502  Cd Length: 62  Bit Score: 110.30  E-value: 1.54e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818035  148 SCQNPGCDAVYQGPESDATPCTYHPGAPRFHEGMKSWSCCGIQTLDFGAFLAQPGCRVGRH 208
Cdd:pfam04968   2 KCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
 
Name Accession Description Interval E-value
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
 218-304 4.29e-51

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


Pssm-ID: 107238  Cd Length: 87  Bit Score: 164.78  E-value: 4.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 218 CRHDWHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKADP 297
Cdd:cd06488    1 CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTKVEIKLRKAEP 80


                 ....*..
gi 157818035 298 GSWAQLE 304
Cdd:cd06488   81 GSWAKLE 87
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 3-64 3.26e-37

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 128.02  E-value: 3.26e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818035    3 LLCYNKGCGQHFDPNTNLPDSCRYHPGVPIFHDALKGWSCCRKRTVDFSEFLNIKGCTVGPH 64
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 148-208 1.54e-30

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 110.30  E-value: 1.54e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818035  148 SCQNPGCDAVYQGPESDATPCTYHPGAPRFHEGMKSWSCCGIQTLDFGAFLAQPGCRVGRH 208
Cdd:pfam04968   2 KCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 218-294 1.16e-13

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: 65.36  E-value: 1.16e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818035  218 CRHDWHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFqAQMKLWGVINVEQSSVSLMPSRVEISLVK 294
Cdd:pfam04969   1 PRYDWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYEL-IDGELFHPIDPEESSWTIEGKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 219-317 1.01e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 55.95  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 219 RHDWHQTDSLVVLTVYGQiPLPAfNWVKASQTE--LHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKAD 296
Cdd:PLN03088 158 RHEFYQKPEEVVVTVFAK-GVPA-ENVNVDFGEqiLSVVIEVPGEDAYHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAE 235

                         90       100
                 ....*....|....*....|.
gi 157818035 297 PGSWAQLEHPDSLAEKARAGV 317
Cdd:PLN03088 236 PITWASLEYGKGPAVLPKPNV 256
 
Name Accession Description Interval E-value
p23_melusin_like cd06488
p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related ...
 218-304 4.29e-51

p23_like domain similar to the C-terminal (tail) domain of vertebrate Melusin and related proteins. Melusin's tail domain interacts with the cytoplasmic domain of beta1-A and beta1-D isoforms of beta1 integrin, it does not bind other integrin beta subunits. Melusin is a muscle-specific protein expressed in skeletal and cardiac muscles but not in smooth muscle or other tissues. It is needed for heart hypertrophy following mechanical overload. The integrin-binding portion of this domain appears to be sequestered in the full length melusin protein, Ca2+ may modulate the protein's conformation exposing this binding site. This group includes Chordc1, also known as Chp-1, which is conserved from vertebrates to humans. Mammalian Chordc1 interacts with the heat shock protein (HSP) Hsp90 and is implicated in circadian and/or homeostatic mechanisms in the brain. The N-terminal portions of proteins belonging to this group contain two cysteine and histidine rich domain (CHORD) domains.


Pssm-ID: 107238  Cd Length: 87  Bit Score: 164.78  E-value: 4.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 218 CRHDWHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKADP 297
Cdd:cd06488    1 CRHDWHQTGSHVVVSVYAKNSNPELSVVEANSTVLTIHIVFEGNKEFQLDIELWGVIDVEKSSVNMLPTKVEIKLRKAEP 80


                 ....*..
gi 157818035 298 GSWAQLE 304
Cdd:cd06488   81 GSWAKLE 87
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 3-64 3.26e-37

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 128.02  E-value: 3.26e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157818035    3 LLCYNKGCGQHFDPNTNLPDSCRYHPGVPIFHDALKGWSCCRKRTVDFSEFLNIKGCTVGPH 64
Cdd:pfam04968   1 TKCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
CHORD pfam04968
CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene ...
 148-208 1.54e-30

CHORD; CHORD represents a Zn binding domain. Silencing of the C. elegans CHORD-containing gene results in semisterility and embryo lethality, suggesting an essential function of the wild-type gene in nematode development.


Pssm-ID: 461502  Cd Length: 62  Bit Score: 110.30  E-value: 1.54e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157818035  148 SCQNPGCDAVYQGPESDATPCTYHPGAPRFHEGMKSWSCCGIQTLDFGAFLAQPGCRVGRH 208
Cdd:pfam04968   2 KCKNKGCGKTFDEEENNDDACTYHPGAPIFHEGSKGWSCCKKRVLDFDEFLKIPGCTTGKH 62
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
 221-304 4.80e-29

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. 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. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 107.29  E-value: 4.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 221 DWHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKADPGSW 300
Cdd:cd06466    1 DWYQTDTSVTVTIYAKNVDKEDVKVEFNEQSLSVSIILPGGSEYQLELDLFGPIDPEQSKVSVLPTKVEITLKKAEPGSW 80


                 ....
gi 157818035 301 AQLE 304
Cdd:cd06466   81 PSLE 84
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
 222-304 2.37e-16

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: 73.09  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 222 WHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKADPG-SW 300
Cdd:cd06463    1 WYQTLDEVTITIPLKDVTKKDVKVEFTPKSLTVSVKGGGGKEYLLEGELFGPIDPEESKWTVEDRKIEITLKKKEPGeWW 80


                 ....
gi 157818035 301 AQLE 304
Cdd:cd06463   81 PRLE 84
CS pfam04969
CS domain; The CS and CHORD (pfam04968) are fused into a single polypeptide chain in metazoans ...
 218-294 1.16e-13

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: 65.36  E-value: 1.16e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157818035  218 CRHDWHQTDSLVVLTVYGQIPLPAFNWVKASQTELHVHIVFDGNRVFqAQMKLWGVINVEQSSVSLMPSRVEISLVK 294
Cdd:pfam04969   1 PRYDWYQTLDEVTITIPVKGAGIKKKDVKVNIKPRSLKVKIKGGYEL-IDGELFHPIDPEESSWTIEGKKVEITLKK 76
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 219-317 1.01e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 55.95  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 219 RHDWHQTDSLVVLTVYGQiPLPAfNWVKASQTE--LHVHIVFDGNRVFQAQMKLWGVINVEQSSVSLMPSRVEISLVKAD 296
Cdd:PLN03088 158 RHEFYQKPEEVVVTVFAK-GVPA-ENVNVDFGEqiLSVVIEVPGEDAYHLQPRLFGKIIPDKCKYEVLSTKIEIRLAKAE 235

                         90       100
                 ....*....|....*....|.
gi 157818035 297 PGSWAQLEHPDSLAEKARAGV 317
Cdd:PLN03088 236 PITWASLEYGKGPAVLPKPNV 256
p23_CS_hSgt1_like cd06489
p23_like domain similar to the C-terminal CS (CHORD-SGT1) domain of human (h) Sgt1 and related ...
 221-304 1.77e-05

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: 42.75  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 221 DWHQTDSLVVLTVYgqiplpafnwVKASQTElHVHIVFDGNRVfQAQMK------------LWGVINVEQSSVSLMPSRV 288
Cdd:cd06489    1 DWYQTESQVVITIL----------IKNVKPE-DVSVEFEKREL-SATVKlpsgndyslklhLLHPIVPEQSSYKILSTKI 68

                         90
                 ....*....|....*.
gi 157818035 289 EISLVKADPGSWAQLE 304
Cdd:cd06489   69 EIKLKKTEAIRWSKLE 84
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 222-294 3.34e-04

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and 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).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 38.72  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 222 WHQTDSLVVLTVYgqipLPAFNW----VKASQTELHVHIVFD-------GNRVFQAQMKLWGVINVEQSSVSLMPSRVEI 290
Cdd:cd00298    1 WYQTDDEVVVTVD----LPGVKKedikVEVEDNVLTISGKREeeeererSYGEFERSFELPEDVDPEKSKASLENGVLEI 76


                 ....
gi 157818035 291 SLVK 294
Cdd:cd00298   77 TLPK 80
p23_CacyBP cd06468
p23_like domain found in proteins similar to Calcyclin-Binding Protein(CacyBP) ...
 220-304 2.32e-03

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: 36.86  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818035 220 HDWHQTDSLVvlTVYgqIPLPAFNWVKASQT---------ELHVHIVFDGNRVFQAQmKLWGVINVEQSSVSLMPSRVEI 290
Cdd:cd06468    4 YAWDQSDKFV--KIY--ITLKGVHQLPKENIqveftersfELKVHDLNGKNYRFTIN-RLLKKIDPEKSSFKVKTDRIVI 78

                         90
                 ....*....|....
gi 157818035 291 SLVKADPGSWAQLE 304
Cdd:cd06468   79 TLAKKKEKKWESLT 92
 
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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