O75925 (PIAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 SUMO-protein ligase PIAS1
EC=6.3.2.-

Alternative name(s):
DEAD/H box-binding protein 1
Gu-binding protein
Short name=GBP
Protein inhibitor of activated STAT protein 1
RNA helicase II-binding protein

Gene names

Name:	PIAS1
Synonyms:	DDXBP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	651 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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. Ref.15 Ref.22
Pathway	Protein modification; protein sumoylation.
Subunit structure	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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.25
Subcellular location	Nucleus speckle. Nucleus › PML body By similarity. Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton. Ref.6 Ref.11 Ref.22
Tissue specificity	Expressed in numerous tissues with highest level in testis. Ref.6 Ref.9
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. Ref.11 Ref.13 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. Ref.22
Sequence similarities	Belongs to the PIAS family. Contains 1 PINIT domain. Contains 1 SAP domain. Contains 1 SP-RING-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Traceable author statement PubMed 10805787. Source: ProtInc androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein sumoylation Inferred from direct assay PubMed 17696781. Source: UniProtKB positive regulation of smooth muscle cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Non-traceable author statement PubMed 15572661. Source: UniProtKB protein sumoylation Inferred from sequence or structural similarity. Source: UniProtKB protein-DNA complex assembly Inferred from electronic annotation. Source: Compara regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB regulation of interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome spermatogenesis Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO ligase activity Inferred from direct assay PubMed 18579533. Source: BHF-UCL androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB transcription coactivator activity Non-traceable author statement PubMed 15572661. Source: UniProtKB transcription corepressor activity Traceable author statement PubMed 10805787. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP8AP2	Q9UKL3	4	EBI-629434,EBI-2339650
TP53	P04637	3	EBI-629434,EBI-366083

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

35

SAP

Domain

124 – 288

165

PINIT

Repeat

520 – 523

4

1

Repeat

557 – 560

4

2

Repeat

598 – 601

4

3; approximate

Repeat

612 – 615

4

4; approximate

Zinc finger

320 – 397

78

SP-RING-type

Region

462 – 473

12

SUMO1-binding By similarity

Region

520 – 615

96

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

Motif

19 – 23

5

LXXLL motif

Motif

56 – 64

9

Nuclear localization signal Potential

Motif

368 – 380

13

Nuclear localization signal Potential

Compositional bias

577 – 634

58

Ser-rich

Amino acid modifications

Modified residue

303

1

Asymmetric dimethylarginine; by PRMT1 Ref.22

Modified residue

483

1

Phosphoserine By similarity

Modified residue

485

1

Phosphoserine By similarity

Modified residue

487

1

Phosphothreonine By similarity

Modified residue

503

1

Phosphoserine Ref.21 Ref.23 Ref.24

Modified residue

510

1

Phosphoserine Ref.23

Modified residue

522

1

Phosphoserine Ref.21

Experimental info

Mutagenesis

303

1

R → K: Partial loss of repression on STAT1 transcriptional activity. Ref.22

Mutagenesis

351

1

C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. Ref.8

Sequence conflict

119

1

E → K in AAC36702. Ref.1

Sequence conflict

266 – 268

3

IVV → MC in AAC36702. Ref.1

Sequence conflict

613

1

S → T in AAB58488. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

651

Helix Strand Turn

Details...

Helix

6 – 11

6

Helix

16 – 24

9

Helix

34 – 46

13

Helix

51 – 63

13

Sequences

	Sequence		Length	Mass (Da)
	O75925 [UniParc]. Last modified March 5, 2002. Version 2. Checksum: AA69338221124119	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

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[4]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-651, INTERACTION WITH DDX21, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: B-cell.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSRP2.
[8]	"Involvement of PIAS1 in the sumoylation of tumor suppressor p53." Kahyo T., Nishida T., Yasuda H. Mol. Cell 8:713-718(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBE2I; SUMO1 AND TP53, MUTAGENESIS OF CYS-351.
[9]	"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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling." Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C. J. Biol. Chem. 277:42981-42986(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AXIN1.
[11]	"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] [Europe PMC] [Abstract] Cited for: SUMOYLATION OF MDM2, SUBCELLULAR LOCATION.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SP3 AND UBE2I.
[13]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JUN AND TP53, SUMOYLATION.
[14]	"SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression." Dobreva G., Dambacher J., Grosschedl R. Genes Dev. 17:3048-3061(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SATB2.
[15]	"PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation." Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M., Boutterin M.C., Girault J.A. J. Biol. Chem. 278:47434-47440(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1.
[16]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLAG1.
[17]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[18]	"Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation." Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L., Zhao J. J. Biol. Chem. 281:16664-16671(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KLF8.
[19]	"Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of PIAS1 to restrict inflammation and immunity." Liu B., Yang Y., Chernishof V., Loo R.R., Jang H., Tahk S., Yang R., Mink S., Shultz D., Bellone C.J., Loo J.A., Shuai K. Cell 129:903-914(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHUK.
[20]	"SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1." Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V. Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX5.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-522, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling." Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M. Genes Dev. 23:118-132(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH STAT1, METHYLATION AT ARG-303 BY PRMT1, MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-303.
[23]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-510, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-65, INTERACTION WITH TP53 AND DNA-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF077951 mRNA. Translation: AAC36702.1.
AF167160 mRNA. Translation: AAD49722.1.
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.

IPI

IPI01011206.

RefSeq

NP_057250.1. NM_016166.1.

UniGene

Hs.162458.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

O75925.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5970N.

IntAct

O75925. 18 interactions.

MINT

MINT-132657.

STRING

9606.ENSP00000249636.

PTM databases

PhosphoSite

O75925.

Proteomic databases

PaxDb

O75925.

PRIDE

O75925.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000249636; ENSP00000249636; ENSG00000033800.

GeneID

8554.

KEGG

hsa:8554.

UCSC

uc002aqz.3. human.

Organism-specific databases

CTD

8554.

GeneCards

GC15P068346.

HGNC

HGNC:2752. PIAS1.

HPA

CAB012304.

MIM

603566. gene.

neXtProt

NX_O75925.

PharmGKB

PA33285.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG125513.

HOVERGEN

HBG053598.

InParanoid

O75925.

KO

K04706.

OrthoDB

EOG4G1MG3.

PhylomeDB

O75925.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
ifngpathway. IFN-gamma pathway.
il6_7pathway. IL6-mediated signaling events.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_6900. Immune System.

UniPathway

UPA00886.

Gene expression databases

ArrayExpress

O75925.

Bgee

O75925.

CleanEx

HS_PIAS1.

Genevestigator

O75925.

GermOnline

ENSG00000033800. Homo sapiens.

Family and domain databases

Gene3D

1.10.720.30. 1 hit.

InterPro

IPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]

PANTHER

PTHR10782:SF11. PTHR10782:SF11. 1 hit.

Pfam

PF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]

SMART

SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

PS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75925.

GenomeRNAi

8554.

NextBio

32053.

PMAP-CutDB

O75925.

SOURCE

Search...

Entry information

Entry name

PIAS1_HUMAN

Accession

Primary (citable) accession number: O75925
Secondary accession number(s): B2RB67 , Q147X4, Q99751, Q9UN02

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 5, 2002
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.