4FO9


Conserved Protein Domain Family
SP-RING_PIAS2

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cd16819: SP-RING_PIAS2 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 438468
Aligned: 6 rows
Threshold Bit Score: 121.351
Created: 22-Mar-2015
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding site
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: Zn binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:C H C CClick to see conserved feature residue pattern help
Evidence:
  • Structure:4FO9; Homo sapiens E3 Sumo Ligase Pias2 binds one Zn2+ ion through its SP-RING finger.
    View structure with Cn3D
  • Comment:The SP-RING finger is a variant of RING finger; it binds a single Zn ion and lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                # #                    #  #         
4FO9_A       210 TSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL 269 human
XP_007910053 337 TSLRVSLMCPLGKMRLTVPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKATYESL 396 elephant shark
NP_001025797 338 TSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL 397 chicken
NP_001072455 337 TSLRVSLMCPLGKMRLTIPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKASYESL 396 western clawed frog
KPP68565     372 TSLRVSLMCPLGKMRLIVPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL 431 Asian bonytongue
NP_001084972 337 TSLRVSLMCPLGKMRLSIPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKATYESL 396 African clawed frog

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