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O75925 (PIAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. 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.26

Subcellular location

Nucleus speckle. NucleusPML 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 processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Traceable author statement PubMed 10805787. Source: ProtInc

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of transcription, DNA-templated

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: Ensembl

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: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 14752048. Source: UniProtKB

   Molecular_functionDNA 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

enzyme binding

Inferred from physical interaction PubMed 17087506. 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.25
Chain2 – 651650E3 SUMO-protein ligase PIAS1
PRO_0000218974

Regions

Domain11 – 4535SAP
Domain124 – 288165PINIT
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 residue21N-acetylalanine Ref.25
Modified residue3031Asymmetric dimethylarginine; by PRMT1 Ref.22
Modified residue4851Phosphoserine By similarity
Modified residue4871Phosphothreonine By similarity
Modified residue5031Phosphoserine Ref.21 Ref.23 Ref.24
Modified residue5101Phosphoserine Ref.23
Modified residue5221Phosphoserine Ref.21

Experimental info

Mutagenesis3031R → K: Partial loss of repression on STAT1 transcriptional activity. Ref.22
Mutagenesis3511C → 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 conflict1191E → K in AAC36702. Ref.1
Sequence conflict266 – 2683IVV → MC in AAC36702. Ref.1
Sequence conflict6131S → T in AAB58488. Ref.5

Secondary structure

......... 651
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75925 [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] [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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[26]"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.
RefSeqNP_057250.1. NM_016166.1.
UniGeneHs.162458.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V66NMR-A1-65[»]
ProteinModelPortalO75925.
SMRO75925. Positions 1-65, 135-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114124. 83 interactions.
DIPDIP-5970N.
IntActO75925. 31 interactions.
MINTMINT-132657.
STRING9606.ENSP00000249636.

PTM databases

PhosphoSiteO75925.

Proteomic databases

PaxDbO75925.
PRIDEO75925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249636; ENSP00000249636; ENSG00000033800.
GeneID8554.
KEGGhsa:8554.
UCSCuc002aqz.3. human.

Organism-specific databases

CTD8554.
GeneCardsGC15P068346.
HGNCHGNC:2752. PIAS1.
HPACAB012304.
MIM603566. gene.
neXtProtNX_O75925.
PharmGKBPA33285.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG125513.
HOVERGENHBG053598.
InParanoidO75925.
KOK04706.
OrthoDBEOG7HF1JB.
PhylomeDBO75925.
TreeFamTF323787.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkO75925.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressO75925.
BgeeO75925.
CleanExHS_PIAS1.
GenevestigatorO75925.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75925.
GeneWikiPIAS1.
GenomeRNAi8554.
NextBio32053.
PMAP-CutDBO75925.
PROO75925.
SOURCESearch...

Entry information

Entry namePIAS1_HUMAN
AccessionPrimary (citable) accession number: O75925
Secondary accession number(s): B2RB67 expand/collapse secondary AC list , Q147X4, Q99751, Q9UN02
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 15

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