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Conserved domains on  [gi|1003088814|ref|NP_001307616|]
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E3 SUMO-protein ligase PIAS1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PINIT pfam14324
PINIT domain; The PINIT domain is a protein domain that is found in PIAS proteins. The PINIT ...
142-288 6.59e-38

PINIT domain; The PINIT domain is a protein domain that is found in PIAS proteins. The PINIT domain is about 180 amino acids in length.


:

Pssm-ID: 464136  Cd Length: 137  Bit Score: 137.33  E-value: 6.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 142 KLPFYDLLDELIKPTSLasDNSQRFRETC-FAFALTPQQVQQISSSmdisgtkcDFTVQVQLrFCL-----SETSCPQED 215
Cdd:pfam14324   2 PSPFYKILELLLSPTEL--PAPSQGRNTVsFSFTLTPDQVQLLAKS--------DRSYQLRL-FCAasdtqSETSGEQDI 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003088814 216 HFPPNLCVKVNTKPCslpgylPPTKNGVEPKR-PSRPINITSLVRLSTTVPNTIVVSWtAEIGRNYSMAVYLVK 288
Cdd:pfam14324  71 EFPPPLEIKVNGKQV------KANLRGLKNKPgTTRPVDITPYLRLSPGYPNTIEITY-ALTKKKYYLVVYLVK 137
SP-RING_PIAS1 cd16818
SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar ...
329-388 3.06e-34

SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar proteins; PIAS1, also known as DEAD/H box-binding protein 1, Gu-binding protein (GBP), or RNA helicase II-binding protein, was initially identified as an inhibitor of STAT1 that blocks the DNA-binding activity of STAT1 and specifically inhibits STAT1-mediated gene transcription in response to cytokine stimulation. It selectively inhibits interferon-inducible gene expression and plays an important role in the IFN-gamma- or IFN-beta-mediated innate immune response through negative regulation of STAT1. It also regulates the activity of other transcription factors to regulate immune response, such as NF-kappaB and Smad4. Moreover, PIAS1 functions as an E3 small ubiquitin-like modifier (SUMO)-protein ligase specifying target proteins for SUMO conjugation by Ubc9. The sumoylation activity of PIAS1 can suppress cytokine transforming growth factor beta (TGFbeta)-induced epithelial mesenchymal transition (EMT) in non-transformed epithelial cells to promote activation of the matrix metalloproteinase 2 (MMP2). It thus regulates TGFbeta-induced cancer cell invasion and metastasis. PIAS1 may also be involved in spatial learning and memory formation through its SUMOylation of cAMP-responsive element binding protein (CREB). In addition, PIAS1 is the E3 ligase responsible for SUMOylation of High mobility group nucleosomal binding domain 2 (HMGN2), which is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair, as well as antimicrobial activity, cell homing, and regulating cytokine release. Furthermore, PIAS1 is a genuine chromatin-bound androgen receptor (AR) co-regulator that functions in a target gene selective fashion to regulate prostate cancer cell growth. It also mediates the SUMOylation of c-Myc, which is the most frequently overexpressed oncogene in tumors, including breast cancer, colon cancer, and lung cancer. Necdin, a pleiotropic protein that promotes differentiation and survival of mammalian neurons, can suppress PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PIAS1 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and the acidic C-terminal domain. The SP-RING finger mediates the interaction of PIAS1 with the SUMO E2 conjugating enzyme Ubc9. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


:

Pssm-ID: 438467  Cd Length: 60  Bit Score: 124.40  E-value: 3.06e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 388
Cdd:cd16818     1 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 60
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
13-47 1.04e-05

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


:

Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 42.47  E-value: 1.04e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1003088814   13 VMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLL 47
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
 
Name Accession Description Interval E-value
PINIT pfam14324
PINIT domain; The PINIT domain is a protein domain that is found in PIAS proteins. The PINIT ...
142-288 6.59e-38

PINIT domain; The PINIT domain is a protein domain that is found in PIAS proteins. The PINIT domain is about 180 amino acids in length.


Pssm-ID: 464136  Cd Length: 137  Bit Score: 137.33  E-value: 6.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 142 KLPFYDLLDELIKPTSLasDNSQRFRETC-FAFALTPQQVQQISSSmdisgtkcDFTVQVQLrFCL-----SETSCPQED 215
Cdd:pfam14324   2 PSPFYKILELLLSPTEL--PAPSQGRNTVsFSFTLTPDQVQLLAKS--------DRSYQLRL-FCAasdtqSETSGEQDI 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003088814 216 HFPPNLCVKVNTKPCslpgylPPTKNGVEPKR-PSRPINITSLVRLSTTVPNTIVVSWtAEIGRNYSMAVYLVK 288
Cdd:pfam14324  71 EFPPPLEIKVNGKQV------KANLRGLKNKPgTTRPVDITPYLRLSPGYPNTIEITY-ALTKKKYYLVVYLVK 137
SP-RING_PIAS1 cd16818
SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar ...
329-388 3.06e-34

SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar proteins; PIAS1, also known as DEAD/H box-binding protein 1, Gu-binding protein (GBP), or RNA helicase II-binding protein, was initially identified as an inhibitor of STAT1 that blocks the DNA-binding activity of STAT1 and specifically inhibits STAT1-mediated gene transcription in response to cytokine stimulation. It selectively inhibits interferon-inducible gene expression and plays an important role in the IFN-gamma- or IFN-beta-mediated innate immune response through negative regulation of STAT1. It also regulates the activity of other transcription factors to regulate immune response, such as NF-kappaB and Smad4. Moreover, PIAS1 functions as an E3 small ubiquitin-like modifier (SUMO)-protein ligase specifying target proteins for SUMO conjugation by Ubc9. The sumoylation activity of PIAS1 can suppress cytokine transforming growth factor beta (TGFbeta)-induced epithelial mesenchymal transition (EMT) in non-transformed epithelial cells to promote activation of the matrix metalloproteinase 2 (MMP2). It thus regulates TGFbeta-induced cancer cell invasion and metastasis. PIAS1 may also be involved in spatial learning and memory formation through its SUMOylation of cAMP-responsive element binding protein (CREB). In addition, PIAS1 is the E3 ligase responsible for SUMOylation of High mobility group nucleosomal binding domain 2 (HMGN2), which is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair, as well as antimicrobial activity, cell homing, and regulating cytokine release. Furthermore, PIAS1 is a genuine chromatin-bound androgen receptor (AR) co-regulator that functions in a target gene selective fashion to regulate prostate cancer cell growth. It also mediates the SUMOylation of c-Myc, which is the most frequently overexpressed oncogene in tumors, including breast cancer, colon cancer, and lung cancer. Necdin, a pleiotropic protein that promotes differentiation and survival of mammalian neurons, can suppress PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PIAS1 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and the acidic C-terminal domain. The SP-RING finger mediates the interaction of PIAS1 with the SUMO E2 conjugating enzyme Ubc9. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438467  Cd Length: 60  Bit Score: 124.40  E-value: 3.06e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 388
Cdd:cd16818     1 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 60
zf-MIZ pfam02891
MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity ...
333-381 1.67e-20

MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organization.


Pssm-ID: 460741  Cd Length: 50  Bit Score: 85.01  E-value: 1.67e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1003088814 333 VSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDK 381
Cdd:pfam02891   1 VSLKCPISYLRISIPVRGRFCKHLQCFDLLSYLESNERTPTWNCPVCDK 49
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
13-47 1.04e-05

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 42.47  E-value: 1.04e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1003088814   13 VMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLL 47
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
315-399 3.97e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 43.20  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 315 KEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDAtlyIQMNEKKPTWVCPVCDKKapyeHLIIDGLF 394
Cdd:COG5222   255 TKAVAEIPDQVYKMQPPNISLKCPLCHCLLRNPMKTPCCGHTFCDEC---IGTALLDSDFKCPNCSRK----DVLLDGLT 327

                  ....*
gi 1003088814 395 MEILK 399
Cdd:COG5222   328 PDIDK 332
 
Name Accession Description Interval E-value
PINIT pfam14324
PINIT domain; The PINIT domain is a protein domain that is found in PIAS proteins. The PINIT ...
142-288 6.59e-38

PINIT domain; The PINIT domain is a protein domain that is found in PIAS proteins. The PINIT domain is about 180 amino acids in length.


Pssm-ID: 464136  Cd Length: 137  Bit Score: 137.33  E-value: 6.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 142 KLPFYDLLDELIKPTSLasDNSQRFRETC-FAFALTPQQVQQISSSmdisgtkcDFTVQVQLrFCL-----SETSCPQED 215
Cdd:pfam14324   2 PSPFYKILELLLSPTEL--PAPSQGRNTVsFSFTLTPDQVQLLAKS--------DRSYQLRL-FCAasdtqSETSGEQDI 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1003088814 216 HFPPNLCVKVNTKPCslpgylPPTKNGVEPKR-PSRPINITSLVRLSTTVPNTIVVSWtAEIGRNYSMAVYLVK 288
Cdd:pfam14324  71 EFPPPLEIKVNGKQV------KANLRGLKNKPgTTRPVDITPYLRLSPGYPNTIEITY-ALTKKKYYLVVYLVK 137
SP-RING_PIAS1 cd16818
SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar ...
329-388 3.06e-34

SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar proteins; PIAS1, also known as DEAD/H box-binding protein 1, Gu-binding protein (GBP), or RNA helicase II-binding protein, was initially identified as an inhibitor of STAT1 that blocks the DNA-binding activity of STAT1 and specifically inhibits STAT1-mediated gene transcription in response to cytokine stimulation. It selectively inhibits interferon-inducible gene expression and plays an important role in the IFN-gamma- or IFN-beta-mediated innate immune response through negative regulation of STAT1. It also regulates the activity of other transcription factors to regulate immune response, such as NF-kappaB and Smad4. Moreover, PIAS1 functions as an E3 small ubiquitin-like modifier (SUMO)-protein ligase specifying target proteins for SUMO conjugation by Ubc9. The sumoylation activity of PIAS1 can suppress cytokine transforming growth factor beta (TGFbeta)-induced epithelial mesenchymal transition (EMT) in non-transformed epithelial cells to promote activation of the matrix metalloproteinase 2 (MMP2). It thus regulates TGFbeta-induced cancer cell invasion and metastasis. PIAS1 may also be involved in spatial learning and memory formation through its SUMOylation of cAMP-responsive element binding protein (CREB). In addition, PIAS1 is the E3 ligase responsible for SUMOylation of High mobility group nucleosomal binding domain 2 (HMGN2), which is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair, as well as antimicrobial activity, cell homing, and regulating cytokine release. Furthermore, PIAS1 is a genuine chromatin-bound androgen receptor (AR) co-regulator that functions in a target gene selective fashion to regulate prostate cancer cell growth. It also mediates the SUMOylation of c-Myc, which is the most frequently overexpressed oncogene in tumors, including breast cancer, colon cancer, and lung cancer. Necdin, a pleiotropic protein that promotes differentiation and survival of mammalian neurons, can suppress PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PIAS1 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and the acidic C-terminal domain. The SP-RING finger mediates the interaction of PIAS1 with the SUMO E2 conjugating enzyme Ubc9. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438467  Cd Length: 60  Bit Score: 124.40  E-value: 3.06e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 388
Cdd:cd16818     1 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 60
SP-RING_PIAS3 cd16820
SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar ...
329-390 5.47e-31

SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar proteins; PIAS3 is an E3 SUMO-protein ligase that was initially identified as an interleukin-6 (IL-6)-dependent repressor of signal transducer and activator of transcription 3 (STAT3) and has anti-proliferative properties. It binds specifically to phosphorylated STAT3 and inhibits its transcriptional activity by blocking its binding to DNA. It regulates STAT3-mediated induction of Snail expression, as well as suppresses acute graft-versus-host disease (GVHD) by modulating effector T and B cell subsets through inhibition of STAT3 activation. It activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status. When overexpressed, it can interact with STAT5 to regulate prolactin-induced STAT5-mediated gene expression. Moreover, PIAS3 binds to and activates Smad3 transcriptional activity, resulting in the enhancement of transforming growth factor-beta (TGF-beta) signaling. It functions as a transcriptional corepressor of Erythroid Kruppel-like factor (EKLF or KLF1) and thus plays an important role in erythropoiesis. It also plays a significant role in the DNA damage response (DDR) pathway by promoting homologous recombination (HR)- and non-homologous end joining (NHEJ)-mediated DNA double-strand break (DSB) repair. Furthermore, PIAS3 preferentially interacts with and enhances the SUMOylation of TAK1-binding protein 2 (TAB2), an upstream adaptor protein in the IL-1 signaling pathway. It also promotes SUMOylation and nuclear sequestration of ErbB4 receptor tyrosine kinase. In addition, PIAS3 may form a complex with microphthalmia-associated transcription factor, nuclear factor-kappaB, Smad, and estrogen receptor. Its other transcription factor binding partners include: ETS, EGR1, NR1I2, and GATA1. PIAS3 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438469  Cd Length: 62  Bit Score: 115.14  E-value: 5.47e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLII 390
Cdd:cd16820     1 TSLRVSLMCPLGKMRLTVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAPYESLII 62
SP-RING_PIAS2 cd16819
SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar ...
329-388 1.54e-30

SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar proteins; PIAS2, also known as androgen receptor-interacting protein 3 (ARIP3), DAB2-interacting protein (DIP), Msx-interacting zinc finger protein (Miz1), PIAS-NY protein, protein inhibitor of activated STAT x, protein inhibitor of activated STAT2, is an E3 SUMO-protein ligase highly expressed in the testis. It functions as a transcriptional activator of BCL2 and is essential for blocking c-MYC-induced apoptosis. It also acts as a negative regulator of cell proliferation, induces expression of the cell-cycle inhibitors p15(Ink4b) and p21(Cip1), and activates transcription of the p21(Cip1) gene in response to UV irradiation. Moreover, PIAS2 associates with topoisomerase II binding protein 1 (TopBP1), an essential activator of the Atr kinase. It thus affects the activity of the Atr checkpoint. Receptor of activated C kinase 1 (RACK1), glucocorticoid receptor (GR)-interacting protein 1 (GRIP1), friend leukemia integration-I (FLI-1), and ubiquitously expressed transcript (UXT) are binding partners of PIAS2. The interaction between UXT and PIAS2 may be important for the transcriptional activation of androgen receptor (AR). PIAS2 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus, and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438468  Cd Length: 60  Bit Score: 114.03  E-value: 1.54e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 388
Cdd:cd16819     1 TSLRVSLMCPLGKMRLTIPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL 60
SP-RING_PIAS cd16790
SP-RING finger found in protein inhibitor of activated signal transducer and activator of ...
334-381 5.52e-29

SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins; The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. It consists of four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS1, PIAS2, and PIAS3 interact with STAT1, STAT3, and STAT4, respectively. In addition, PIAS4 is associated with STAT1. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. PIAS proteins contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, which is required for the trans-repression of STAT1 activity by PIAS2, a PINT motif, which is essential for nuclear retention of PIAS3L (the long form of PIAS3), a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity, and the acidic C-terminal domain, which is involved in binding of PIAS3 to the nuclear coactivator TIF2. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438444  Cd Length: 48  Bit Score: 109.13  E-value: 5.52e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1003088814 334 SLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDK 381
Cdd:cd16790     1 SLMCPLGKMRLTIPCRALTCSHLQCFDAALYLQMNEKKPTWICPVCDK 48
SP-RING_PIAS4 cd16821
SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar ...
329-386 1.50e-28

SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar proteins; PIAS4, also known as PIASy or protein inhibitor of activated STAT protein gamma (PIAS-gamma), is an E3 SUMO-protein ligase that interacts with the androgen receptor (AR) and is involved in ubiquitin signaling pathways. It is associated with macro/microcephaly in the novel interstitial 19p13.3 microdeletion/microduplication syndrome. It also regulates the hypoxia signalling pathway by interacting with the tumor suppressor von Hippel-Lindau (VHL), which leads to VHL sumoylation, oligomerization, and impaired function during growth of pancreatic cancer cells. Moreover, PIAS4 acts as a direct binding partner for vitamin D receptor (VDR) and facilitates its modification with SUMO2. The process of SUMOylation modulates VDR-mediated signaling. As components of the DNA-damage response (DDR), PIAS4 together with PIAS1 promote responses to DNA double-strand breaks (DSBs). They are required for effective ubiquitin-adduct formation mediated by RNF8, RNF168, and BRCA1 at sites of DNA damage. PIAS4 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438470  Cd Length: 58  Bit Score: 108.22  E-value: 1.50e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYE 386
Cdd:cd16821     1 TGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWTCPVCDKPAPYD 58
SP-RING_PIAS-like cd16650
SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING ...
334-381 1.18e-21

SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. PIAS proteins modulate the activity of several transcription factors and act as E3 ubiquitin ligases in the sumoylation pathway. There are four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7) were initially identified in humans as androgen receptor (AR) interacting proteins that function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. SIZ1 proteins from plants and fungi are also founding members of this family. SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. Yeast SIZ proteins are SUMO E3 ligases involved in a novel pathway of chromosome maintenance. They enhance SUMO modification to many substrates in vivo, but also exhibit unique substrate specificity. PIAS proteins contain a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity. The SP-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438312  Cd Length: 48  Bit Score: 88.10  E-value: 1.18e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1003088814 334 SLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDK 381
Cdd:cd16650     1 SLRCPLSLKRIKTPARGKHCKHLQCFDLDSYLEFNKRKPTWKCPICDK 48
zf-MIZ pfam02891
MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity ...
333-381 1.67e-20

MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organization.


Pssm-ID: 460741  Cd Length: 50  Bit Score: 85.01  E-value: 1.67e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1003088814 333 VSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDK 381
Cdd:pfam02891   1 VSLKCPISYLRISIPVRGRFCKHLQCFDLLSYLESNERTPTWNCPVCDK 49
SP-RING_Siz-like cd16792
SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar ...
334-381 5.16e-20

SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar proteins; SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. AtSIZ1 negatively regulates abscisic acid (ABA) signaling through the sumoylation of bZIP transcripton factor ABI5. It also mediates sumoylation of bromodomain GTE proteins. Moreover, AtSIZ1 regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affecting on FLOWERING LOCUS C (FLC) chromatin structure. It also plays a role in drought stress response likely through the regulation of gene expression. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box, a plant homeodomain (PHD) finger, and a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438446  Cd Length: 50  Bit Score: 83.61  E-value: 5.16e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1003088814 334 SLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDK 381
Cdd:cd16792     1 SLKCPLSYSRIKVPCRSIKCTHIQCFDLDSFLQLNEQTPSWQCPICNK 48
SP-RING_ZMIZ2 cd16823
SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar ...
329-386 7.52e-14

SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar proteins; Zmiz2, also known as PIAS-like protein Zimp7 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 7), is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It interacts with beta-catenin and enhances Wnt/beta-catenin-mediated transcription. It also associates with BRG1 and BAF57, components of the ATP-dependent mammalian SWI/SNF-like BAF chromatin-remodeling complexes, and thus plays a potential role in modulation of AR and/or other nuclear receptor-mediated transcription. For instance, it can increase the effects of BRG1 on AR-mediated transcriptional activity. Moreover, Zmiz2 physically interacts with PIAS proteins, especially PIAS3. Through this interaction, PIAS3 augments Zmiz2-mediated transcription, suggesting PIAS proteins may play a regulatory role in Zmiz-mediated transcription. Furthermore, Zmiz2 is involved in transcriptional regulation of factors essential for patterning in the dorsoventral axis. It is required for the restriction of the zebrafish organizer and mesoderm development. Zmiz2 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438472  Cd Length: 61  Bit Score: 66.61  E-value: 7.52e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1003088814 329 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYE 386
Cdd:cd16823     3 TAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLE 60
SP-RING_ZMIZ1 cd16822
SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar ...
332-391 8.99e-14

SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar proteins; Zmiz1, also known as PIAS-like protein Zimp10 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 10) or retinoic acid-induced protein 17, is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It co-localizes with AR and small ubiquitin-like modifier SUMO-1, forms a protein complex at replication foci in the nucleus, and augments AR-mediated transcription. It also functions as a transcriptional co-activator of the p53 tumor suppressor that plays a critical role in cell cycle progression, DNA repair, and apoptosis. Moreover, Zmiz1 dysfunction may be associated with multiple autoimmune diseases and it has been implicated in the development, function, and survival of melanocytes. Zmiz1 also interacts with Smad3/4 proteins and augments Smad-mediated transcription, suggesting it is important in the regulation of the transforming growth factor beta (TGF-beta)/Smad signaling pathway and may have an inhibitory effect on the immune system. Zmiz1 is overexpressed in a significant percentage of human cutaneous squamous cell carcinoma (SCC), breast, ovarian, and colon cancers, suggesting it may play a broader role in epithelial cancers. It functionally interacts with NOTCH1 to promote C-MYC transcription and activity, and thus is involved in a variety of C-MYC-driven cancers. Zmiz1 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a putative nuclear localization sequence (NLS), as well as a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438471  Cd Length: 64  Bit Score: 66.24  E-value: 8.99e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 332 RVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIID 391
Cdd:cd16822     1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVD 60
SP-RING_ZMIZ cd16791
SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar ...
334-381 1.81e-13

SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar proteins; This subfamily includes Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7), both initially identified in humans as androgen receptor (AR) interacting proteins which function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors, such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. This subfamily also includes tonalli (Tna), an ortholog identified in Drosophila. It genetically interacts with the ATP-dependent SWI/SNF and Mediator complexes, suggesting a potential role for the Zmiz proteins in chromatin remodeling. Zmiz proteins contain a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong transactivation domain within the C-terminus. The SP-RING/Miz domain is highly conserved in members of the PIAS family and confers SUMO-conjugating activity. It is a variant of the RING finger, and lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers. The strong intrinsic transactivation domain facilitates Zmiz proteins to augment the transcriptional activity of nuclear hormone receptors and other transcriptional factors. They may act as transcriptional co-regulators.


Pssm-ID: 438445  Cd Length: 48  Bit Score: 64.83  E-value: 1.81e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1003088814 334 SLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDK 381
Cdd:cd16791     1 SLKCPITFRRITLPARGHDCKHIQCFDLESYLQLNCERGTWRCPVCNK 48
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
335-380 3.13e-11

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 58.42  E-value: 3.13e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1003088814 335 LLCPLGKMRLTIPCRALTCSHlqCFDATLYIQMNEK-KPTWVCPVCD 380
Cdd:cd16452     1 LKCPITQKRMKDPVRGKHCGH--CFDLEAILQYLKRrKKKWKCPVCS 45
SP-RING_ScSiz-like cd16793
SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and ...
330-379 1.11e-09

SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and similar proteins; Saccharomyces cerevisiae SIZ proteins, also known as SAP and Miz-finger domain-containing proteins, are Siz/PIAS RING (SP-RING) family SUMO E3 ligases, and may be involved in a novel pathway of chromosome maintenance. They enhance SUMO modification with many substrates in vivo, but also exhibit unique substrate specificity. SIZ1, also known as ubiquitin-like protein ligase 1 (Ull1), modifies both cytoplasmic and nuclear proteins. It functions as an E3 factor specific for septin components. SIZ1-dependent substrates include Cdc3 and Cdc11 (septin subunits), Prp45 (a splicing factor), and the proliferating cell nuclear antigen (PCNA). SIZ2, also known as NFI1, interacts with Smt3, SUMO/Smt3 conjugating enzyme Ubc9, and a septin component Cdc3. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438447  Cd Length: 56  Bit Score: 54.30  E-value: 1.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1003088814 330 SLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVC 379
Cdd:cd16793     1 STIMSLQCPISYTRMKYPSKSINCKHLQCFDALWFLHSQLQIPTWQCPVC 50
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
13-47 1.04e-05

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 42.47  E-value: 1.04e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1003088814   13 VMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLL 47
Cdd:smart00513   1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLLEAL 35
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
315-399 3.97e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 43.20  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1003088814 315 KEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDAtlyIQMNEKKPTWVCPVCDKKapyeHLIIDGLF 394
Cdd:COG5222   255 TKAVAEIPDQVYKMQPPNISLKCPLCHCLLRNPMKTPCCGHTFCDEC---IGTALLDSDFKCPNCSRK----DVLLDGLT 327

                  ....*
gi 1003088814 395 MEILK 399
Cdd:COG5222   328 PDIDK 332
 
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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