4FO9,3I2D


Conserved Protein Domain Family
SP-RING_PIAS_like

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cd16650: SP-RING_PIAS_like 
Click on image for an interactive view with Cn3D
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. 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. 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 and 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. All family members 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 RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers.
Statistics
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PSSM-Id: 319564
View PSSM: cd16650
Aligned: 28 rows
Threshold Bit Score: 68.0546
Threshold Setting Gi: 303271383
Created: 31-Jul-2013
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteSP-RING finger
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:4FO9; Homo sapiens E3 Sumo Ligase Pias2 binds one Zn2+ ion through its SP-RING finger.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
Feature 1                            # #                        #  #  
4FO9_A        215 SLMCPLGKMRLTIPcRAVTCTHLQCFDAALYLQMNek----kpTWICPVCDK 262
gi 163779467  310 SLKCPLSHKRISTPaRGEYCNHLQCFDALTYIQMNal----qcRWNCPICHR 357
gi 353233638  622 CLLCPLTRTRIDLPvRSFNCSHLQCFDLHSYLTINmr----rpRWSCPICSI 669
gi 672573773  201 KLLCPVTFMRIEVPcRGRACMHLQCYDLSGYLLVTrntkafntRWKCPECHL 252
gi 765555496  475 SLTCPLTLAVLRLPaRGVSCKHVQCFELETYISVCsr----qrTWICPICSQ 522
gi 934160617  187 SLLCPLSTLRIKIPaRSIKCEHINCFDLESFIKINdi----tpRWRCPICKI 234
gi 56470589   199 SLKCPISYQRIVIPaRGLNCSHLACFDLENYIRNStt----kqCFNCPICYK 246
gi 124396089  415 SLLCPITLQLINIPaRGRFCNHLQCFDLENFITAIddqk-dkkIWKCPICKL 465
gi 574978978  376 SLHCPFSLDRILIPcRGIMCSHIKCFDLKSFIDVTkktkafnnRWKCPICSF 427
gi 397585356 1360 SLLCPLTRMPIKTPvRGRDCKHLQCFDLLTYLHSNktv--tgsRWRCPVCND 1409

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