Details for: PIAS2
Associated with
Other Information
Genular Protein ID: 2662652399
Symbol: PIAS2_HUMAN
Name: E3 SUMO-protein ligase PIAS2
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9724754
Title: Inhibition of Stat1-mediated gene activation by PIAS1.
PubMed ID: 9724754
PubMed ID: 15301740
Title: Molecular cloning and characterization of a novel splicing variant of PIASx.
PubMed ID: 15301740
PubMed ID: 16177791
Title: DNA sequence and analysis of human chromosome 18.
PubMed ID: 16177791
DOI: 10.1038/nature03983
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 9920921
Title: A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins.
PubMed ID: 9920921
PubMed ID: 10961991
Title: Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif.
PubMed ID: 10961991
PubMed ID: 11477070
Title: DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor.
PubMed ID: 11477070
PubMed ID: 11439351
Title: Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells.
PubMed ID: 11439351
PubMed ID: 12223491
Title: SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling.
PubMed ID: 12223491
PubMed ID: 12393906
Title: Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes.
PubMed ID: 12393906
PubMed ID: 11867732
Title: Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity.
PubMed ID: 11867732
PubMed ID: 12716907
Title: PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4.
PubMed ID: 12716907
PubMed ID: 15208321
Title: Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation.
PubMed ID: 15208321
PubMed ID: 15920481
Title: PIASx acts as an Elk-1 coactivator by facilitating derepression.
PubMed ID: 15920481
PubMed ID: 15976810
Title: Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities.
PubMed ID: 15976810
PubMed ID: 16617055
Title: Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation.
PubMed ID: 16617055
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21156324
Title: MDA5 is SUMOylated by PIAS2? in the upregulation of type I interferon signaling.
PubMed ID: 21156324
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22406621
Title: The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA.
PubMed ID: 22406621
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 28842558
Title: HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells.
PubMed ID: 28842558
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 16204249
Title: Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation.
PubMed ID: 16204249
Sequence Information:
- Length: 621
- Mass: 68240
- Checksum: 6422B383345AD883
- Sequence:
MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG IHSLPSTSVT PHSPSSPVGS VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE DGSWCPMRPK KEAMKVSSQP CTKIESSSVL SKPCSVTVAS EASKKKVDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP ISSMSSDLPG LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSSHE SSTHVSSSSS RSETGVITSS GSNIPDIISL D
Genular Protein ID: 1768235984
Symbol: Q2TA77_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
Sequence Information:
- Length: 507
- Mass: 56391
- Checksum: DC1F1B1EE7CBA99A
- Sequence:
MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG IHSLPSTSVT PHSPSSPVGS VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE DGSWCPMRPK KEAMKVSSQP CTKIESSSVL SKPCSVTVAS EASKKKVDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP TKGFVNL
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.