LOCUS       NP_057250                651 aa            linear   PRI 12-JUN-2025
DEFINITION  E3 SUMO-protein ligase PIAS1 isoform 2 [Homo sapiens].
ACCESSION   NP_057250
VERSION     NP_057250.1
DBSOURCE    REFSEQ: accession NM_016166.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Zhang,X.Y., Li,S.S., Gu,Y.R., Xiao,L.X., Ma,X.Y., Chen,X.R.,
            Wang,J.L., Liao,C.H., Lin,B.L., Huang,Y.H. and Lian,Y.F.
  TITLE     CircPIAS1 promotes hepatocellular carcinoma progression by
            inhibiting ferroptosis via the miR-455-3p/NUPR1/FTH1 axis
  JOURNAL   Mol Cancer 23 (1), 113 (2024)
   PUBMED   38802795
  REMARK    GeneRIF: CircPIAS1 promotes hepatocellular carcinoma progression by
            inhibiting ferroptosis via the miR-455-3p/NUPR1/FTH1 axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Ho,P.J., Kweon,J., Blumensaadt,L.A., Neely,A.E., Kalika,E.,
            Leon,D.B., Oh,S., Stringer,C.W.P., Lloyd,S.M., Ren,Z. and Bao,X.
  TITLE     Multi-omics integration identifies cell-state-specific repression
            by PBRM1-PIAS1 cooperation
  JOURNAL   Cell Genom 4 (1), 100471 (2024)
   PUBMED   38190100
  REMARK    GeneRIF: Multi-omics integration identifies cell-state-specific
            repression by PBRM1-PIAS1 cooperation.
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Wang,L., Zeng,W., Wang,C., Lu,Y., Xiong,X., Chen,S., Huang,Q.,
            Yan,F. and Huang,Q.
  TITLE     SUMOylation and coupling of eNOS mediated by PIAS1 contribute to
            maintenance of vascular homeostasis
  JOURNAL   FASEB J 38 (1), e23362 (2024)
   PUBMED   38102979
  REMARK    GeneRIF: SUMOylation and coupling of eNOS mediated by PIAS1
            contribute to maintenance of vascular homeostasis.
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Wu,C., Zhu,X., Dai,Q., Chu,Z., Yang,S. and Dong,Z.
  TITLE     SUMOylation of SMAD4 by PIAS1 in Conjunction with Vimentin
            Upregulation Promotes Migration Potential in Non-Small Cell Lung
            Cancer
  JOURNAL   Front Biosci (Landmark Ed) 28 (8), 192 (2023)
   PUBMED   37664931
  REMARK    GeneRIF: SUMOylation of SMAD4 by PIAS1 in Conjunction with Vimentin
            Upregulation Promotes Migration Potential in Non-Small Cell Lung
            Cancer.
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Belaguli,N.S., Zhang,M., Garcia,A.H. and Berger,D.H.
  TITLE     PIAS1 is a GATA4 SUMO ligase that regulates GATA4-dependent
            intestinal promoters independent of SUMO ligase activity and GATA4
            sumoylation
  JOURNAL   PLoS One 7 (4), e35717 (2012)
   PUBMED   22539995
  REMARK    GeneRIF: PIAS1 is a SUMO ligase for GATA4 that differentially
            regulates GATA4 transcriptional activity independent of SUMO ligase
            activity and GATA4 sumoylation.
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Liao,J., Fu,Y. and Shuai,K.
  TITLE     Distinct roles of the NH2- and COOH-terminal domains of the protein
            inhibitor of activated signal transducer and activator of
            transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1
            interaction
  JOURNAL   Proc Natl Acad Sci U S A 97 (10), 5267-5272 (2000)
   PUBMED   10805787
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Gatei,M., Young,D., Cerosaletti,K.M., Desai-Mehta,A., Spring,K.,
            Kozlov,S., Lavin,M.F., Gatti,R.A., Concannon,P. and Khanna,K.
  TITLE     ATM-dependent phosphorylation of nibrin in response to radiation
            exposure
  JOURNAL   Nat Genet 25 (1), 115-119 (2000)
   PUBMED   10802669
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Tan,J., Hall,S.H., Hamil,K.G., Grossman,G., Petrusz,P., Liao,J.,
            Shuai,K. and French,F.S.
  TITLE     Protein inhibitor of activated STAT-1 (signal transducer and
            activator of transcription-1) is a nuclear receptor coregulator
            expressed in human testis
  JOURNAL   Mol Endocrinol 14 (1), 14-26 (2000)
   PUBMED   10628744
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Liu,B., Liao,J., Rao,X., Kushner,S.A., Chung,C.D., Chang,D.D. and
            Shuai,K.
  TITLE     Inhibition of Stat1-mediated gene activation by PIAS1
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10626-10631 (1998)
   PUBMED   9724754
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Valdez,B.C., Henning,D., Perlaky,L., Busch,R.K. and Busch,H.
  TITLE     Cloning and characterization of Gu/RH-II binding protein
  JOURNAL   Biochem Biophys Res Commun 234 (2), 335-340 (1997)
   PUBMED   9177271
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF167160.1, AC107871.10 and
            AA837658.1.
            
            Summary: This gene encodes a member of the protein inhibitor of
            activated STAT (PIAS) family. PIAS proteins function as SUMO E3
            ligases and play important roles in many cellular processes by
            mediating the sumoylation of target proteins. This protein plays a
            central role as a transcriptional coregulator of numerous cellular
            pathways includign the STAT1 and nuclear factor kappaB pathways.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) uses an alternate 5' structure
            which results in a distinct 5' UTR and 5' coding region compared to
            variant 1. The encoded isoform (2) is shorter and has a distinct
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.10216.1,
                                           SRR1803616.31761.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249636.11/ ENSP00000249636.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..651
                     /product="E3 SUMO-protein ligase PIAS1 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="AR interacting protein; zinc finger, MIZ-type
                     containing 3; DEAD/H (Asp-Glu-Ala-Asp/His) box binding
                     protein 1; E3 SUMO-protein ligase PIAS1; gu-binding
                     protein; RNA helicase II-binding protein; DEAD/H
                     box-binding protein 1; protein inhibitor of activated STAT
                     protein 1; E3 SUMO-protein transferase PIAS1"
                     /calculated_mol_wt=71705
     Region          2..200
                     /region_name="Required for interaction with MSX1.
                     /evidence=ECO:0000250|UniProtKB:O88907"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Region          11..45
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Region          19..23
                     /region_name="LXXLL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Region          56..64
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Site            100
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-6 and -8.
                     /evidence=ECO:0000269|PubMed:29262325; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Region          140..286
                     /region_name="PINIT"
                     /note="PINIT domain; pfam14324"
                     /db_xref="CDD:464136"
     Region          327..386
                     /region_name="SP-RING_PIAS1"
                     /note="SP-RING finger found in protein inhibitor of
                     activated STAT protein 1 (PIAS1) and similar proteins;
                     cd16818"
                     /db_xref="CDD:438467"
     Region          368..380
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Site            433
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3, -6, and -8.
                     /evidence=ECO:0000269|PubMed:29262325; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Region          462..473
                     /region_name="SUMO1-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Region          465..511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88907; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88907; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Region          520..615
                     /region_name="4 X 4 AA repeats of N-T-S-L"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75925.2)"
     Region          599..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75925.2)"
     CDS             1..651
                     /gene="PIAS1"
                     /gene_synonym="DDXBP1; GBP; GU/RH-II; ZMIZ3"
                     /coded_by="NM_016166.3:13..1968"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45290.1"
                     /db_xref="GeneID:8554"
                     /db_xref="HGNC:HGNC:2752"
                     /db_xref="MIM:603566"
ORIGIN      
        1 madsaelkqm vmslrvselq vllgyagrnk hgrkhelltk alhllkagcs pavqmkikel
       61 yrrrfpqkim tpadlsipnv hsspmpatls pstipqltyd ghpasspllp vsllgpkhel
      121 elphltsalh pvhpdiklqk lpfydlldel ikptslasdn sqrfretcfa faltpqqvqq
      181 isssmdisgt kcdftvqvql rfclsetscp qedhfppnlc vkvntkpcsl pgylpptkng
      241 vepkrpsrpi nitslvrlst tvpntivvsw taeigrnysm avylvkqlss tvllqrlrak
      301 girnpdhsra likekltadp dseiattslr vsllcplgkm rltipcralt cshlqcfdat
      361 lyiqmnekkp twvcpvcdkk apyehliidg lfmeilkyct dcdeiqfked gtwapmrskk
      421 evqevsasyn gvdgclsstl ehqvashhqs snknkkvevi dltidsssde eeeepsakrt
      481 cpslsptspl nnkgilslph qaspvsrtps lpavdtsyin tsliqdyrhp fhmtpmpydl
      541 qgldffpfls gdnqhyntsl laaaaaavsd dqdllhssrf fpytssqmfl dqlsaggsts
      601 lpttngsssg snsslvssns lreshshtvt nrsstdtasi fgiipdiisl d
//
