E3 SUMO-protein ligase PIAS1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot O75925 (PIAS1_HUMAN)

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

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

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Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	651 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	JAK-STAT cascade Traceable author statement. Source: ProtInc androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW androgen receptor binding Non-traceable author statement. Source: UniProtKB transcription coactivator activity Non-traceable author statement. Source: UniProtKB transcription corepressor activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPN1	P18031	1	EBI-629434,EBI-968788
TP53	P04637	1	EBI-629434,EBI-366083

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 651

651

E3 SUMO-protein ligase PIAS1

PRO_0000218974

Regions

Domain

11 – 45

SAP

Repeat

520 – 523

Repeat

557 – 560

Repeat

598 – 601

3; approximate

Repeat

612 – 615

4; approximate

Zinc finger

320 – 397

SP-RING-type

Region

462 – 473

SUMO1-binding By similarity

Region

520 – 615

4 X 4 AA repeats of N-T-S-L

Motif

19 – 23

LXXLL motif

Motif

56 – 64

Nuclear localization signal Potential

Motif

368 – 380

Nuclear localization signal Potential

Compositional bias

577 – 634

Ser-rich

Amino acid modifications

Modified residue

466

Phosphoserine

Modified residue

467

Phosphoserine

Modified residue

468

Phosphoserine

Modified residue

483

Phosphoserine By similarity

Modified residue

485

Phosphoserine By similarity

Modified residue

487

Phosphothreonine By similarity

Experimental info

Mutagenesis

351

C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding

Sequence conflict

119

E → K in AAC36702. Ref.1

Sequence conflict

266 – 268

IVV → MC in AAC36702. Ref.1

Sequence conflict

613

S → T in AAB58488. Ref.4

Secondary structure

651

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O75925-1 [UniParc].

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

651

71,836

        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

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References

	« Hide 'large scale' referencesShow '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.

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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.

RefSeq

NP_057250.1.

UniGene

Hs.162458

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V66	NMR	-	A	1-65	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O75925.

PTM databases

PhosphoSite

O75925.

Genome annotation databases

Ensembl

ENSG00000033800. Homo sapiens. [Contig view]

GeneID

8554.

KEGG

hsa:8554.

Organism-specific databases

H-InvDB

HIX0012374.

HGNC

HGNC:2752. PIAS1.

HPA

CAB012304.
HPA005743.

MIM

603566. gene.

PharmGKB

PA33285.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

O75925.

HOVERGEN

O75925.

Gene expression databases

ArrayExpress

O75925.

CleanEx

HS_PIAS1.

GermOnline

ENSG00000033800. Homo sapiens.

Family and domain databases

InterPro

IPR003034. SAP_DNA_bd.
IPR004181. Znf_MIZ.
[Graphical view]

Pfam

PF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]

SMART

SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32053.

SOURCE

Search...

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Entry information

Entry name

PIAS1_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents