4MVT


Conserved Protein Domain Family
SP-RING_PIAS3

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cd16820: SP-RING_PIAS3 
Click on image for an interactive view with Cn3D
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 DNA damage response (DDR) pathway through 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 the acidic C-terminal domain.
Statistics
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PSSM-Id: 319734
View PSSM: cd16820
Aligned: 5 rows
Threshold Bit Score: 100.91
Threshold Setting Gi: 550544742
Created: 22-Mar-2015
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:4MVT; Homo sapiens Sumo E3 Ligase Pias3 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                            # #                    #  #     
4MVT_A        231 SLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAP 281
gi 56405390   324 SLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAP 374
gi 465967303 1309 SLMCPLGKMRLIVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAP 1359
gi 147900500  331 SLMCPLGKMRLTVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAP 381
gi 556963626  331 SLMCPLGKMRLAVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAP 381

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