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O75925

- PIAS1_HUMAN

UniProt

O75925 - PIAS1_HUMAN

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Protein

E3 SUMO-protein ligase PIAS1

Gene
PIAS1, DDXBP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 39778SP-RING-typeAdd
BLAST

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. DNA binding Source: UniProtKB-KW
  3. enzyme binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. SUMO ligase activity Source: BHF-UCL
  6. transcription coactivator activity Source: UniProtKB
  7. transcription corepressor activity Source: ProtInc
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. cytokine-mediated signaling pathway Source: Reactome
  3. interferon-gamma-mediated signaling pathway Source: Reactome
  4. JAK-STAT cascade Source: ProtInc
  5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. positive regulation of protein sumoylation Source: UniProtKB
  8. positive regulation of smooth muscle cell differentiation Source: Ensembl
  9. positive regulation of transcription, DNA-templated Source: UniProtKB
  10. protein-DNA complex assembly Source: Ensembl
  11. protein sumoylation Source: UniProtKB
  12. regulation of cell proliferation Source: UniProtKB
  13. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  14. spermatogenesis Source: Ensembl
  15. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_24980. Regulation of IFNG signaling.
SignaLinkiO75925.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PIAS1
Synonyms:DDXBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:2752. PIAS1.

Subcellular locationi

Nucleus speckle. NucleusPML body By similarity
Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.3 Publications

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi303 – 3031R → K: Partial loss of repression on STAT1 transcriptional activity. 1 Publication
Mutagenesisi351 – 3511C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. 1 Publication

Organism-specific databases

PharmGKBiPA33285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 651650E3 SUMO-protein ligase PIAS1PRO_0000218974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei303 – 3031Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei485 – 4851Phosphoserine By similarity
Modified residuei487 – 4871Phosphothreonine By similarity
Modified residuei503 – 5031Phosphoserine3 Publications
Modified residuei510 – 5101Phosphoserine1 Publication
Modified residuei522 – 5221Phosphoserine1 Publication

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.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO75925.
PaxDbiO75925.
PRIDEiO75925.

PTM databases

PhosphoSiteiO75925.

Miscellaneous databases

PMAP-CutDBO75925.

Expressioni

Tissue specificityi

Expressed in numerous tissues with highest level in testis.2 Publications

Gene expression databases

ArrayExpressiO75925.
BgeeiO75925.
CleanExiHS_PIAS1.
GenevestigatoriO75925.

Organism-specific databases

HPAiCAB012304.

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.15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P299913EBI-629434,EBI-8826488From a different organism.
CASP8AP2Q9UKL34EBI-629434,EBI-2339650
MBD1Q9UIS93EBI-629434,EBI-867196
PRDM1O756262EBI-629434,EBI-948789
TP53P046373EBI-629434,EBI-366083

Protein-protein interaction databases

BioGridi114124. 86 interactions.
DIPiDIP-5970N.
IntActiO75925. 31 interactions.
MINTiMINT-132657.
STRINGi9606.ENSP00000249636.

Structurei

Secondary structure

1
651
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116
Helixi16 – 249
Helixi34 – 4613
Helixi51 – 6313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V66NMR-A1-65[»]
ProteinModelPortaliO75925.
SMRiO75925. Positions 1-65, 135-416.

Miscellaneous databases

EvolutionaryTraceiO75925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAPAdd
BLAST
Domaini124 – 288165PINITAdd
BLAST
Repeati520 – 52341
Repeati557 – 56042
Repeati598 – 60143; approximate
Repeati612 – 61544; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni462 – 47312SUMO1-binding By similarityAdd
BLAST
Regioni520 – 615964 X 4 AA repeats of N-T-S-LAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif
Motifi56 – 649Nuclear localization signal Reviewed prediction
Motifi368 – 38013Nuclear localization signal Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 63458Ser-richAdd
BLAST

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.
Contains 1 PINIT domain.
Contains 1 SAP domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 39778SP-RING-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG125513.
HOVERGENiHBG053598.
InParanoidiO75925.
KOiK04706.
OrthoDBiEOG7HF1JB.
PhylomeDBiO75925.
TreeFamiTF323787.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamiPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O75925-1 [UniParc]FASTAAdd to Basket

« Hide

MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS    50
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD 100
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 150
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 200
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 250
NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 300
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 350
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 400
DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS 450
SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH 500
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 550
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 600
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL 650
D 651
Length:651
Mass (Da):71,836
Last modified:March 5, 2002 - v2
Checksum:iAA69338221124119
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191E → K in AAC36702. 1 Publication
Sequence conflicti266 – 2683IVV → MC in AAC36702. 1 Publication
Sequence conflicti613 – 6131S → T in AAB58488. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45290.1.
RefSeqiNP_057250.1. NM_016166.1.
UniGeneiHs.162458.

Genome annotation databases

EnsembliENST00000249636; ENSP00000249636; ENSG00000033800.
GeneIDi8554.
KEGGihsa:8554.
UCSCiuc002aqz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS45290.1.
RefSeqi NP_057250.1. NM_016166.1.
UniGenei Hs.162458.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V66 NMR - A 1-65 [» ]
ProteinModelPortali O75925.
SMRi O75925. Positions 1-65, 135-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114124. 86 interactions.
DIPi DIP-5970N.
IntActi O75925. 31 interactions.
MINTi MINT-132657.
STRINGi 9606.ENSP00000249636.

PTM databases

PhosphoSitei O75925.

Proteomic databases

MaxQBi O75925.
PaxDbi O75925.
PRIDEi O75925.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249636 ; ENSP00000249636 ; ENSG00000033800 .
GeneIDi 8554.
KEGGi hsa:8554.
UCSCi uc002aqz.3. human.

Organism-specific databases

CTDi 8554.
GeneCardsi GC15P068346.
HGNCi HGNC:2752. PIAS1.
HPAi CAB012304.
MIMi 603566. gene.
neXtProti NX_O75925.
PharmGKBi PA33285.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG125513.
HOVERGENi HBG053598.
InParanoidi O75925.
KOi K04706.
OrthoDBi EOG7HF1JB.
PhylomeDBi O75925.
TreeFami TF323787.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_24980. Regulation of IFNG signaling.
SignaLinki O75925.

Miscellaneous databases

EvolutionaryTracei O75925.
GeneWikii PIAS1.
GenomeRNAii 8554.
NextBioi 32053.
PMAP-CutDB O75925.
PROi O75925.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75925.
Bgeei O75925.
CleanExi HS_PIAS1.
Genevestigatori O75925.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
InterProi IPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view ]
PANTHERi PTHR10782:SF11. PTHR10782:SF11. 1 hit.
Pfami PF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
[Graphical view ]
PROSITEi PS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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. 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.

Entry informationi

Entry nameiPIAS1_HUMAN
AccessioniPrimary (citable) accession number: O75925
Secondary accession number(s): B2RB67
, Q147X4, Q99751, Q9UN02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: September 3, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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