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Reviewed, UniProtKB/Swiss-Prot O75925 (PIAS1_HUMAN)

Last modified November 25, 2008. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    E3 SUMO-protein ligase PIAS1
Alternative name(s):
    Protein inhibitor of activated STAT protein 1
    Gu-binding protein
      Short name=GBP
    RNA helicase II-binding protein
    DEAD/H box-binding protein 1
Gene names
Name: PIAS1
Synonyms: DDXBP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context.

Pathway

Protein modification; protein sumoylation.

Subunit structure

Binds SUMO1 and UBE2I. Interacts with AR, CSRP2, JUN, MDM2, NCOA2, TP53, RNA helicase II and STAT1 dimers, following IFN-alpha-stimulation. Interacts with SP3, preferentially when SUMO-modified. Binds preferentially AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) By similarity. Interacts with PLAG1.

Subcellular location

Nucleus speckle. Note= Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.

Tissue specificity

Expressed in numerous tissues with highest level in testis.

Domain

The LXXLL motif is a transcriptional coregulator signature.

The SP-RING-type domain is required for promoting EKLF sumoylation By similarity.

Post-translational modification

Sumoylated.

Sequence similarities

Belongs to the PIAS family.

Contains 1 SAP domain.

Contains 1 SP-RING-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPN1P180311EBI-629434,EBI-968788
TP53P046371EBI-629434,EBI-366083

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651E3 SUMO-protein ligase PIAS1
PRO_0000218974

Regions

Domain11 – 4535SAP
Repeat520 – 52341
Repeat557 – 56042
Repeat598 – 60143; approximate
Repeat612 – 61544; approximate
Zinc finger320 – 39778SP-RING-type
Region462 – 47312SUMO1-binding By similarity
Region520 – 615964 X 4 AA repeats of N-T-S-L
Motif19 – 235LXXLL motif
Motif56 – 649Nuclear localization signal Potential
Motif368 – 38013Nuclear localization signal Potential
Compositional bias577 – 63458Ser-rich

Amino acid modifications

Modified residue4661Phosphoserine
Modified residue4671Phosphoserine
Modified residue4681Phosphoserine
Modified residue4831Phosphoserine By similarity
Modified residue4851Phosphoserine By similarity
Modified residue4871Phosphothreonine By similarity

Experimental info

Mutagenesis3511C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding
Sequence conflict1191E → K in AAC36702. Ref.1
Sequence conflict266 – 2683IVV → MC in AAC36702. Ref.1
Sequence conflict6131S → T in AAB58488. Ref.4

Secondary structure

......... 651
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75925-1 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: AA69338221124119

FASTA65171,836
        10         20         30         40         50         60 
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL 

        70         80         90        100        110        120 
YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL 

       130        140        150        160        170        180 
ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ 

       190        200        210        220        230        240 
ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG 

       250        260        270        280        290        300 
VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 

       310        320        330        340        350        360 
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT 

       370        380        390        400        410        420 
LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GTWAPMRSKK 

       430        440        450        460        470        480 
EVQEVSASYN GVDGCLSSTL EHQVASHHQS SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT 

       490        500        510        520        530        540 
CPSLSPTSPL NNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL 

       550        560        570        580        590        600 
QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 

       610        620        630        640        650 
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL D 

« Hide

References

« Hide 'large scale' references
[1]"Inhibition of Stat1-mediated gene activation by PIAS1."
Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K.
Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998) [PubMed: 9724754] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STAT1.
Tissue: B-cell.
[2]"Protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1) is a nuclear receptor coregulator expressed in human testis."
Tan J., Hall S.H., Hamil K.G., Grossman G., Petrusz P., Liao J., Shuai K., French F.S.
Mol. Endocrinol. 14:14-26(2000) [PubMed: 10628744] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning and characterization of Gu/RH-II binding protein."
Valdez B.C., Henning D., Perlaky L., Busch R.K., Busch H.
Biochem. Biophys. Res. Commun. 234:335-340(1997) [PubMed: 9177271] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-651, INTERACTION WITH RNA HELICASE II, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: B-cell.
[5]"LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1."
Weiskirchen R., Moser M., Weiskirchen S., Erdel M., Dahmen S., Buettner R., Gressner A.M.
Biochem. J. 359:485-496(2001) [PubMed: 11672422] [Abstract]
Cited for: INTERACTION WITH CSRP2.
[6]"Involvement of PIAS1 in the sumoylation of tumor suppressor p53."
Kahyo T., Nishida T., Yasuda H.
Mol. Cell 8:713-718(2001) [PubMed: 11583632] [Abstract]
Cited for: INTERACTION WITH UBE2I; SUMO1 AND TP53, MUTAGENESIS OF CYS-351.
[7]"Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells."
Gross M., Liu B., Tan J.-A., French F.S., Carey M., Shuai K.
Oncogene 20:3880-3887(2001) [PubMed: 11439351] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes."
Miyauchi Y., Yogosawa S., Honda R., Nishida T., Yasuda H.
J. Biol. Chem. 277:50131-50136(2002) [PubMed: 12393906] [Abstract]
Cited for: SUMOYLATION OF MDM2, SUBCELLULAR LOCATION.
[9]"Transcription factor Sp3 is silenced through SUMO modification by PIAS1."
Sapetschnig A., Rischitor G., Braun H., Doll A., Schergaut M., Melchior F., Suske G.
EMBO J. 21:5206-5215(2002) [PubMed: 12356736] [Abstract]
Cited for: INTERACTION WITH SP3 AND UBE2I.
[10]"Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity."
Schmidt D., Mueller S.
Proc. Natl. Acad. Sci. U.S.A. 99:2872-2877(2002) [PubMed: 11867732] [Abstract]
Cited for: INTERACTION WITH JUN AND TP53, SUMOYLATION.
[11]"Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation."
Van Dyck F., Delvaux E.L.D., Van de Ven W.J.M., Chavez M.V.
J. Biol. Chem. 279:36121-36131(2004) [PubMed: 15208321] [Abstract]
Cited for: INTERACTION WITH PLAG1.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-467 AND SER-468, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers."
Okubo S., Hara F., Tsuchida Y., Shimotakahara S., Suzuki S., Hatanaka H., Yokoyama S., Tanaka H., Yasuda H., Shindo H.
J. Biol. Chem. 279:31455-31461(2004) [PubMed: 15133049] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-65, INTERACTION WITH TP53 AND DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF077951 mRNA. Translation: AAC36702.1.
AF167160 mRNA. Translation: AAD49722.1.
BC118587 mRNA. Translation: AAI18588.1.
BC121797 mRNA. Translation: AAI21798.1.
U78524 mRNA. Translation: AAB58488.1.
RefSeqNP_057250.1.
UniGeneHs.162458

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1V66NMR-A1-65[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO75925.

PTM databases

PhosphoSiteO75925.

Genome annotation databases

EnsemblENSG00000033800. Homo sapiens. [Contig view]
GeneID8554.
KEGGhsa:8554.

Organism-specific databases

H-InvDBHIX0012374.
HGNCHGNC:2752. PIAS1.
HPACAB012304.
HPA005743.
MIM603566. gene.
PharmGKBPA33285.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO75925.
HOVERGENO75925.

Gene expression databases

ArrayExpressO75925.
CleanExHS_PIAS1.
GermOnlineENSG00000033800. Homo sapiens.

Family and domain databases

InterProIPR003034. SAP_DNA_bd.
IPR004181. Znf_MIZ.
[Graphical view]
PfamPF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio32053.
SOURCESearch...

Entry information

Entry namePIAS1_HUMAN
AccessionPrimary (citable) accession number: O75925
Secondary accession number(s): Q147X4, Q99751, Q9UN02
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: November 25, 2008
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents