PIAS1

Functionⁱ

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. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).By similarity3 Publications

Pathwayⁱ: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	320 – 397	SP-RING-typePROSITE-ProRule annotationAdd BLAST		78

GO - Molecular functionⁱ

androgen receptor binding
Source: UniProtKB
Non-traceable author statementⁱ
- 15572661
DNA binding Source: UniProtKB-KW
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17087506
protein C-terminus binding Source: Ensembl
protein domain specific binding Source: Ensembl
SUMO ligase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 18579533
SUMO transferase activity
Source: Reactome
Inferred from experimentⁱ
transcription coactivator activity
Source: UniProtKB
Non-traceable author statementⁱ
- 15572661
transcription corepressor activity
Source: ProtInc
Traceable author statementⁱ
- 10805787
ubiquitin protein ligase binding Source: Ensembl
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

androgen receptor signaling pathway
Source: UniProtKB
Non-traceable author statementⁱ
- 15572661
fat cell differentiation Source: Ensembl
G1/S transition of mitotic cell cycle Source: Ensembl
JAK-STAT cascade
Source: ProtInc
Traceable author statementⁱ
- 10805787
negative regulation of apoptotic process Source: Ensembl
negative regulation of transcription by RNA polymerase II Source: Ensembl
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
positive regulation of protein sumoylation
Source: UniProtKB
Inferred from direct assayⁱ
- 17696781
- 21965678
positive regulation of smooth muscle cell differentiation Source: Ensembl
positive regulation of transcription, DNA-templated
Source: UniProtKB
Non-traceable author statementⁱ
- 15572661
protein-DNA complex assembly Source: Ensembl
protein sumoylation
Source: BHF-UCL
Inferred from direct assayⁱ
- 18579533
regulation of cell proliferation Source: UniProtKB
regulation of interferon-gamma-mediated signaling pathway Source: Reactome
spermatogenesis Source: Ensembl
visual learning Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Transferase
Biological process	Transcription, Transcription regulation, Ubl conjugation pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3108214 SUMOylation of DNA damage response and repair proteins R-HSA-3232118 SUMOylation of transcription factors R-HSA-3232142 SUMOylation of ubiquitinylation proteins R-HSA-3899300 SUMOylation of transcription cofactors R-HSA-4090294 SUMOylation of intracellular receptors R-HSA-4551638 SUMOylation of chromatin organization proteins R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-877312 Regulation of IFNG signaling
SignaLinkⁱ	O75925
SIGNORⁱ	O75925
UniPathwayⁱ	UPA00886

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: E3 SUMO-protein ligase PIAS1 (EC:2.3.2.-) Alternative name(s): DEAD/H box-binding protein 1 E3 SUMO-protein transferase PIAS1Curated Gu-binding protein Short name: GBP Protein inhibitor of activated STAT protein 1 RNA helicase II-binding protein
Gene namesⁱ	Name:PIAS1 Synonyms:DDXBP1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000033800.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:2752 PIAS1
MIMⁱ	603566 gene
neXtProtⁱ	NX_O75925

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	303	R → K: Partial loss of repression on STAT1 transcriptional activity. 1 Publication		1
Mutagenesisⁱ	351	C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8554
Open Targets More...OpenTargetsⁱ	ENSG00000033800
PharmGKBⁱ	PA33285

Polymorphism and mutation databases

BioMutaⁱ	PIAS1

BioMutaⁱ

PIAS1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000218974	2 – 651	E3 SUMO-protein ligase PIAS1Add BLAST		650

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources	1
Cross-linkⁱ	40	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	46	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	137	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	238	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	303	Asymmetric dimethylarginine; by PRMT11 Publication	1
Cross-linkⁱ	453	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	467	PhosphoserineCombined sources	1
Modified residueⁱ	468	PhosphoserineCombined sources	1
Modified residueⁱ	483	PhosphoserineBy similarity	1
Modified residueⁱ	485	PhosphoserineCombined sources	1
Modified residueⁱ	487	PhosphothreonineBy similarity	1
Modified residueⁱ	488	PhosphoserineCombined sources	1
Cross-linkⁱ	493	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	503	PhosphoserineCombined sources	1
Modified residueⁱ	510	PhosphoserineCombined sources	1
Modified residueⁱ	522	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Sumoylated.2 Publications

Dimethylated by PRMT1 at Arg-303 in the late phase of interferon gamma (IFN-gamma) signaling, leading to preferential interaction with STAT1 and thus resulting in release of STAT1 from its target gene.

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	O75925
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O75925
PaxDbⁱ	O75925
PeptideAtlas More...PeptideAtlasⁱ	O75925
PRIDEⁱ	O75925
ProteomicsDBⁱ	50293

PTM databases

iPTMnetⁱ	O75925
PhosphoSitePlusⁱ	O75925

Miscellaneous databases

PMAP-CutDBⁱ	O75925

PMAP-CutDBⁱ

O75925

Expressionⁱ

Tissue specificityⁱ

Gene expression databases

Bgeeⁱ	ENSG00000033800 Expressed in 235 organ(s), highest expression level in bone marrow
CleanExⁱ	HS_PIAS1
ExpressionAtlasⁱ	O75925 baseline and differential
Genevisibleⁱ	O75925 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB012304 HPA005743

HPAⁱ

CAB012304
HPA005743

Interactionⁱ

Subunit structureⁱ

Interacts with NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Interacts with DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G₁ phase. Interacts with STAT1. Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with PML (By similarity). Interacts with MTA1. Interacts with SUMO1P1/SUMO5 (PubMed:27211601).By similarity17 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P29991	3	EBI-629434,EBI-8826488	From Dengue virus type 2 (strain 16681-PDK53).
CASP8AP2	Q9UKL3	4	EBI-629434,EBI-2339650
MBD1	Q9UIS9	3	EBI-629434,EBI-867196
PRDM1	O75626	2	EBI-629434,EBI-948789
TP53	P04637	4	EBI-629434,EBI-366083

GO - Molecular functionⁱ

androgen receptor binding
Source: UniProtKB
Non-traceable author statementⁱ
- 15572661
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17087506
protein C-terminus binding Source: Ensembl
protein domain specific binding Source: Ensembl
ubiquitin protein ligase binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	114124, 106 interactors
Database of interacting proteins More...DIPⁱ	DIP-5970N
ELMⁱ	O75925
IntActⁱ	O75925, 53 interactors
Molecular INTeraction database More...MINTⁱ	O75925
STRINGⁱ	9606.ENSP00000249636

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 11	Combined sources	6
Helixⁱ	16 – 24	Combined sources	9
Helixⁱ	34 – 46	Combined sources	13
Helixⁱ	51 – 63	Combined sources	13

Show more details

3D structure databases

ProteinModelPortalⁱ	O75925
SMRⁱ	O75925
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O75925

EvolutionaryTraceⁱ

O75925

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	11 – 45	SAPPROSITE-ProRule annotationAdd BLAST	35
Domainⁱ	124 – 288	PINITPROSITE-ProRule annotationAdd BLAST	165
Repeatⁱ	520 – 523	1	4
Repeatⁱ	557 – 560	2	4
Repeatⁱ	598 – 601	3; approximate	4
Repeatⁱ	612 – 615	4; approximate	4

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	462 – 473	SUMO1-bindingBy similarityAdd BLAST		12
Regionⁱ	520 – 615	4 X 4 AA repeats of N-T-S-LAdd BLAST		96

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	19 – 23	LXXLL motif	5
Motifⁱ	56 – 64	Nuclear localization signalSequence analysis	9
Motifⁱ	368 – 380	Nuclear localization signalSequence analysisAdd BLAST	13

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	577 – 634	Ser-richAdd BLAST		58

Domainⁱ

The LXXLL motif is a transcriptional coregulator signature.

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

Sequence similaritiesⁱ

Belongs to the PIAS family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	320 – 397	SP-RING-typePROSITE-ProRule annotationAdd BLAST		78

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG2169 Eukaryota ENOG410XQ2E LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074410
HOGENOMⁱ	HOG000230594
HOVERGENⁱ	HBG053598
InParanoidⁱ	O75925
KEGG Orthology (KO) More...KOⁱ	K04706
OMAⁱ	NQHYNMV
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G08G5
PhylomeDBⁱ	O75925
TreeFamⁱ	TF323787

Family and domain databases

Gene3Dⁱ	1.10.720.30, 1 hit 2.60.120.780, 1 hit 3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR023321 PINIT IPR038654 PINIT_sf IPR003034 SAP_dom IPR036361 SAP_dom_sf IPR004181 Znf_MIZ IPR013083 Znf_RING/FYVE/PHD
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF14324 PINIT, 1 hit PF02891 zf-MIZ, 1 hit
SMARTⁱ	View protein in SMART SM00513 SAP, 1 hit
SUPFAMⁱ	SSF68906 SSF68906, 1 hit
PROSITEⁱ	View protein in PROSITE PS51466 PINIT, 1 hit PS50800 SAP, 1 hit PS51044 ZF_SP_RING, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: O75925-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS 
        60         70         80         90        100
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD 
       110        120        130        140        150
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 
       160        170        180        190        200
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 
       210        220        230        240        250
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 
       260        270        280        290        300
NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 
       310        320        330        340        350
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 
       360        370        380        390        400
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 
       410        420        430        440        450
DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS 
       460        470        480        490        500
SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH 
       510        520        530        540        550
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 
       560        570        580        590        600
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 
       610        620        630        640        650
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL 

D

Length:651

Mass (Da):71,836

Last modified:March 5, 2002 - v2

Checksum:ⁱAA69338221124119

GO

Isoform 2 (identifier: O75925-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-7: MADSAEL → MFTLQDSYV

« Hide

        10         20         30         40         50
MFTLQDSYVK QMVMSLRVSE LQVLLGYAGR NKHGRKHELL TKALHLLKAG 
        60         70         80         90        100
CSPAVQMKIK ELYRRRFPQK IMTPADLSIP NVHSSPMPAT LSPSTIPQLT 
       110        120        130        140        150
YDGHPASSPL LPVSLLGPKH ELELPHLTSA LHPVHPDIKL QKLPFYDLLD 
       160        170        180        190        200
ELIKPTSLAS DNSQRFRETC FAFALTPQQV QQISSSMDIS GTKCDFTVQV 
       210        220        230        240        250
QLRFCLSETS CPQEDHFPPN LCVKVNTKPC SLPGYLPPTK NGVEPKRPSR 
       260        270        280        290        300
PINITSLVRL STTVPNTIVV SWTAEIGRNY SMAVYLVKQL SSTVLLQRLR 
       310        320        330        340        350
AKGIRNPDHS RALIKEKLTA DPDSEIATTS LRVSLLCPLG KMRLTIPCRA 
       360        370        380        390        400
LTCSHLQCFD ATLYIQMNEK KPTWVCPVCD KKAPYEHLII DGLFMEILKY 
       410        420        430        440        450
CTDCDEIQFK EDGTWAPMRS KKEVQEVSAS YNGVDGCLSS TLEHQVASHH 
       460        470        480        490        500
QSSNKNKKVE VIDLTIDSSS DEEEEEPSAK RTCPSLSPTS PLNNKGILSL 
       510        520        530        540        550
PHQASPVSRT PSLPAVDTSY INTSLIQDYR HPFHMTPMPY DLQGLDFFPF 
       560        570        580        590        600
LSGDNQHYNT SLLAAAAAAV SDDQDLLHSS RFFPYTSSQM FLDQLSAGGS 
       610        620        630        640        650
TSLPTTNGSS SGSNSSLVSS NSLRESHSHT VTNRSSTDTA SIFGIIPDII 

SLD

Note: No experimental confirmation available.

Show »

Length:653

Mass (Da):72,203

Checksum:ⁱ585370DA0FBDC926

GO

Isoform 3 (identifier: O75925-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
312-325: IKEKLTADPDSEIA → STYDKLISLIQLFC
326-651: Missing.

« Hide

        10         20         30         40         50
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS 
        60         70         80         90        100
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD 
       110        120        130        140        150
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 
       160        170        180        190        200
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 
       210        220        230        240        250
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 
       260        270        280        290        300
NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 
       310        320 
GIRNPDHSRA LSTYDKLISL IQLFC

Show »

Length:325

Mass (Da):36,204

Checksum:ⁱF0A265377BDCADC2

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H3BSI8	H3BSI8_HUMAN	E3 SUMO-protein ligase PIAS1 E3 SUMO-protein ligase PIAS1	PIAS1	160	Annotation score:
H3BS65	H3BS65_HUMAN	E3 SUMO-protein ligase PIAS1 E3 SUMO-protein ligase PIAS1	PIAS1	64	Annotation score:
H3BUL7	H3BUL7_HUMAN	E3 SUMO-protein ligase PIAS1 E3 SUMO-protein ligase PIAS1	PIAS1	20	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	119	E → K in AAC36702 (PubMed:9724754).Curated	1
Sequence conflictⁱ	266 – 268	IVV → MC in AAC36702 (PubMed:9724754).Curated	3
Sequence conflictⁱ	613	S → T in AAB58488 (PubMed:15489334).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_056219	1 – 7	MADSAEL → MFTLQDSYV in isoform 2. 1 Publication	7
Alternative sequenceⁱVSP_057195	312 – 325	IKEKL…DSEIA → STYDKLISLIQLFC in isoform 3. 1 PublicationAdd BLAST	14
Alternative sequenceⁱVSP_057196	326 – 651	Missing in isoform 3. 1 PublicationAdd BLAST	326

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF077951 mRNA Translation: AAC36702.1 AF167160 mRNA Translation: AAD49722.1 FJ997900 mRNA Translation: ACR77525.1 AK094641 mRNA Translation: BAG52901.1 AK314515 mRNA Translation: BAG37114.1 AC107871 Genomic DNA No translation available. AC135628 Genomic DNA No translation available. BC118587 mRNA Translation: AAI18588.1 BC121797 mRNA Translation: AAI21798.1 U78524 mRNA Translation: AAB58488.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS45290.1 [O75925-1] CCDS81902.1 [O75925-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001307616.1, NM_001320687.1 [O75925-2] NP_057250.1, NM_016166.2 [O75925-1] XP_016878177.1, XM_017022688.1 [O75925-2]
UniGeneⁱ	Hs.162458 Hs.694796

Genome annotation databases

Ensemblⁱ	ENST00000249636; ENSP00000249636; ENSG00000033800 [O75925-1] ENST00000545237; ENSP00000438574; ENSG00000033800 [O75925-2]
GeneIDⁱ	8554
KEGGⁱ	hsa:8554
UCSC genome browser More...UCSCⁱ	uc002aqz.4 human [O75925-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O75925	Protein inhibitor of activated STAT 1		PONAB		683	UniRef100_O75925
E3 SUMO-protein ligase PIAS1		MACMU		651
PIAS1 isoform 2		PANTR		651
Testis cDNA clone: QtsA-10480, similar to human protein inhibitor of activated STAT, 1 (PIAS1)		MACFA		651
Uncharacterized protein		COLAP		651
+11

Protein	Similar proteins		Species	Score	Length	Source
O75925	E3 SUMO-protein ligase PIAS1		MOUSE		651	UniRef90_O75925
Protein inhibitor of activated STAT 1		PONAB		683
E3 SUMO-protein ligase PIAS1		MACMU		651
PIAS1 isoform 2		PANTR		651
Testis cDNA clone: QtsA-10480, similar to human protein inhibitor of activated STAT, 1 (PIAS1)		MACFA		651
+301

Protein	Similar proteins		Species	Score	Length	Source
O75925	Isoform PIAS2-alpha of E3 SUMO-protein ligase PIAS2		HUMAN		572	UniRef50_O75928-2
E3 SUMO-protein ligase PIAS3		MOUSE		628
E3 SUMO-protein ligase PIAS3		RAT		628
PIAS2 isoform 3		PANTR		572
E3 SUMO-protein ligase PIAS2		AMAAE		614
+1094
O75925-3	E3 SUMO-protein ligase PIAS2-like		ALLSI		371	UniRef50_O75925-3
UPI000523CF1A		TAUER		328
UPI0008DB75E8		SERCA		317
UPI000DF49D99		ORENI		299
UPI000C9F948E		OCTDE		388
+2

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF077951 mRNA Translation: AAC36702.1 AF167160 mRNA Translation: AAD49722.1 FJ997900 mRNA Translation: ACR77525.1 AK094641 mRNA Translation: BAG52901.1 AK314515 mRNA Translation: BAG37114.1 AC107871 Genomic DNA No translation available. AC135628 Genomic DNA No translation available. BC118587 mRNA Translation: AAI18588.1 BC121797 mRNA Translation: AAI21798.1 U78524 mRNA Translation: AAB58488.1
CCDSⁱ	CCDS45290.1 [O75925-1] CCDS81902.1 [O75925-2]
RefSeqⁱ	NP_001307616.1, NM_001320687.1 [O75925-2] NP_057250.1, NM_016166.2 [O75925-1] XP_016878177.1, XM_017022688.1 [O75925-2]
UniGeneⁱ	Hs.162458 Hs.694796

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1V66	NMR	-	A	1-65	[»]
ProteinModelPortalⁱ	O75925
SMRⁱ	O75925
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114124, 106 interactors
DIPⁱ	DIP-5970N
ELMⁱ	O75925
IntActⁱ	O75925, 53 interactors
MINTⁱ	O75925
STRINGⁱ	9606.ENSP00000249636

PTM databases

iPTMnetⁱ	O75925
PhosphoSitePlusⁱ	O75925

Polymorphism and mutation databases

BioMutaⁱ	PIAS1

BioMutaⁱ

PIAS1

Proteomic databases

EPDⁱ	O75925
MaxQBⁱ	O75925
PaxDbⁱ	O75925
PeptideAtlasⁱ	O75925
PRIDEⁱ	O75925
ProteomicsDBⁱ	50293

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000249636; ENSP00000249636; ENSG00000033800 [O75925-1] ENST00000545237; ENSP00000438574; ENSG00000033800 [O75925-2]
GeneIDⁱ	8554
KEGGⁱ	hsa:8554
UCSCⁱ	uc002aqz.4 human [O75925-1]

Organism-specific databases

CTDⁱ	8554
DisGeNETⁱ	8554
EuPathDBⁱ	HostDB:ENSG00000033800.13
GeneCardsⁱ	PIAS1
HGNCⁱ	HGNC:2752 PIAS1
HPAⁱ	CAB012304 HPA005743
MIMⁱ	603566 gene
neXtProtⁱ	NX_O75925
OpenTargetsⁱ	ENSG00000033800
PharmGKBⁱ	PA33285
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2169 Eukaryota ENOG410XQ2E LUCA
GeneTreeⁱ	ENSGT00550000074410
HOGENOMⁱ	HOG000230594
HOVERGENⁱ	HBG053598
InParanoidⁱ	O75925
KOⁱ	K04706
OMAⁱ	NQHYNMV
OrthoDBⁱ	EOG091G08G5
PhylomeDBⁱ	O75925
TreeFamⁱ	TF323787

Enzyme and pathway databases

UniPathwayⁱ	UPA00886
Reactomeⁱ	R-HSA-3108214 SUMOylation of DNA damage response and repair proteins R-HSA-3232118 SUMOylation of transcription factors R-HSA-3232142 SUMOylation of ubiquitinylation proteins R-HSA-3899300 SUMOylation of transcription cofactors R-HSA-4090294 SUMOylation of intracellular receptors R-HSA-4551638 SUMOylation of chromatin organization proteins R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-877312 Regulation of IFNG signaling
SignaLinkⁱ	O75925
SIGNORⁱ	O75925

Miscellaneous databases

ChiTaRSⁱ	PIAS1 human
EvolutionaryTraceⁱ	O75925
GeneWikiⁱ	PIAS1
GenomeRNAiⁱ	8554
PMAP-CutDBⁱ	O75925
Protein Ontology More...PROⁱ	PR:O75925
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000033800 Expressed in 235 organ(s), highest expression level in bone marrow
CleanExⁱ	HS_PIAS1
ExpressionAtlasⁱ	O75925 baseline and differential
Genevisibleⁱ	O75925 HS

Family and domain databases

Gene3Dⁱ	1.10.720.30, 1 hit 2.60.120.780, 1 hit 3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR023321 PINIT IPR038654 PINIT_sf IPR003034 SAP_dom IPR036361 SAP_dom_sf IPR004181 Znf_MIZ IPR013083 Znf_RING/FYVE/PHD
Pfamⁱ	View protein in Pfam PF14324 PINIT, 1 hit PF02891 zf-MIZ, 1 hit
SMARTⁱ	View protein in SMART SM00513 SAP, 1 hit
SUPFAMⁱ	SSF68906 SSF68906, 1 hit
PROSITEⁱ	View protein in PROSITE PS51466 PINIT, 1 hit PS50800 SAP, 1 hit PS51044 ZF_SP_RING, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PIAS1_HUMAN
Accessionⁱ	O75925Primary (citable) accession number: O75925 Secondary accession number(s): B2RB67 , B3KSY9, C5J4B4, Q147X4, Q99751, Q9UN02
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
	Last sequence update:	March 5, 2002
	Last modified:	November 7, 2018
	This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
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
Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM

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UniProtKB - O75925 (PIAS1_HUMAN)

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E3 SUMO-protein ligase PIAS1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Nucleus

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

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Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: protein sumoylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ