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O75928

- PIAS2_HUMAN

UniProt

O75928 - PIAS2_HUMAN

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Protein
E3 SUMO-protein ligase PIAS2
Gene
PIAS2, PIASX
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 coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'.3 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri331 – 40878SP-RING-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. negative regulation of androgen receptor signaling pathway Source: UniProtKB
  3. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. protein sumoylation Source: UniProtKB
  6. regulation of osteoblast differentiation Source: Ensembl
  7. 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

SignaLinkiO75928.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS2 (EC:6.3.2.-)
Alternative name(s):
Androgen receptor-interacting protein 3
Short name:
ARIP3
DAB2-interacting protein
Short name:
DIP
Msx-interacting zinc finger protein
Short name:
Miz1
PIAS-NY protein
Protein inhibitor of activated STAT x
Protein inhibitor of activated STAT2
Gene namesi
Name:PIAS2
Synonyms:PIASX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:17311. PIAS2.

Subcellular locationi

Nucleus speckle. NucleusPML body
Note: Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs).4 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi362 – 3621C → S or A: Loss of MDM2 and TP53 sumoylation and of autosumoylation; no loss of JUN- and TP53-binding. 2 Publications
Mutagenesisi467 – 4671V → A: Reduces affinity for SUMO1. 1 Publication
Mutagenesisi469 – 4691V → A: Abolishes binding to SUMO1. 1 Publication
Mutagenesisi470 – 4701I → A: Abolishes binding to SUMO1. 1 Publication
Mutagenesisi472 – 4721L → A: Abolishes binding to SUMO1. 1 Publication
Mutagenesisi473 – 4731T → A: Reduces affinity for SUMO1. 1 Publication

Organism-specific databases

PharmGKBiPA134933292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621E3 SUMO-protein ligase PIAS2
PRO_0000218976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei476 – 4761Phosphoserine1 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei478 – 4781Phosphoserine1 Publication

Post-translational modificationi

Sumoylated.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO75928.
PaxDbiO75928.
PRIDEiO75928.

PTM databases

PhosphoSiteiO75928.

Expressioni

Tissue specificityi

Mainly expressed in testis. Isoform 3 is expressed predominantly in adult testis, weakly in pancreas, embryonic testis and sperm, and at very low levels in other organs.3 Publications

Developmental stagei

Isoform 3 expression in adult testis is 14.2-fold stronger than in embryonic testis.1 Publication

Inductioni

Up-regulated transiently during myeloid differentiation in various cells lines, such as HL-60, U-937, K-562, induced by either phorbol ester (TPA) or retinoic acid.

Gene expression databases

ArrayExpressiO75928.
BgeeiO75928.
CleanExiHS_PIAS2.
GenevestigatoriO75928.

Interactioni

Subunit structurei

Binds SUMO1 and UBE2I. Interacts with AXIN1, JUN, MDM2, PARK7, TP53 and TP73 isoform alpha, but not TP73 isoform beta. Interacts with STAT4 following IL12 and IFN-alpha stimulation of T-cells. Interacts also with GTF2I, GTF2IRD1, IKFZ1, DAB2 and MSX2, as well as with several steroid receptors, including ESR1, ESR2, NR3C1, PGR, AR, and with NCOA2 By similarity. Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with PLAG1. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase. PIAS2-beta interacts with IFIH1/MDA5. Isoform PIAS2-alpha interacts with PML (isoform PML-12).10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GNB2L1P632442EBI-348555,EBI-296739
MYCP011064EBI-348555,EBI-447544
RUFY1Q96T513EBI-348555,EBI-3941207
UBE2IP632795EBI-348555,EBI-80168

Protein-protein interaction databases

BioGridi114523. 59 interactions.
IntActiO75928. 23 interactions.
MINTiMINT-1455373.
STRINGi9606.ENSP00000381648.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi154 – 16512
Beta strandi173 – 1819
Helixi185 – 1928
Beta strandi195 – 1973
Beta strandi203 – 21513
Beta strandi231 – 2344
Beta strandi237 – 2393
Helixi264 – 2663
Beta strandi271 – 2733
Beta strandi275 – 2828
Beta strandi289 – 29810
Helixi301 – 3099
Helixi316 – 32712
Beta strandi340 – 3456
Turni347 – 3493
Beta strandi354 – 3596
Helixi370 – 37910
Turni386 – 3883
Helixi394 – 3963
Beta strandi397 – 4004
Helixi401 – 4077
Beta strandi415 – 4184
Beta strandi469 – 4713

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASQNMR-B466-488[»]
4FO9X-ray2.39A147-488[»]
ProteinModelPortaliO75928.
SMRiO75928. Positions 1-65, 147-426.

Miscellaneous databases

EvolutionaryTraceiO75928.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAP
Add
BLAST
Domaini134 – 299166PINIT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni467 – 4737SUMO1-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif
Motifi484 – 4929Nuclear localization signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi571 – 61242Ser-rich
Add
BLAST
Compositional biasi596 – 6027Poly-Ser

Domaini

The LXXLL motif is a transcriptional coregulator signature.

Sequence similaritiesi

Belongs to the PIAS family.
Contains 1 PINIT domain.
Contains 1 SAP domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG125513.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO75928.
KOiK16063.
OMAiPHESSTH.
OrthoDBiEOG7HF1JB.
PhylomeDBiO75928.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF12. PTHR10782:SF12. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform PIAS2-beta (identifier: O75928-1) [UniParc]FASTAAdd to Basket

Also known as: PIASx-beta, Miz1

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

MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS    50
PAVQIKIREL YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG 100
IHSLPSTSVT PHSPSSPVGS VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN 150
LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI FALTPQQVRE ICISRDFLPG 200
GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP LPGYAPPPKN 250
GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 300
SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK 350
MRLTIPCRAV TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD 400
GLFMEILNDC SDVDEIKFQE DGSWCPMRPK KEAMKVSSQP CTKIESSSVL 450
SKPCSVTVAS EASKKKVDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP 500
TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP ISSMSSDLPG 550
LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSSHE SSTHVSSSSS 600
RSETGVITSS GSNIPDIISL D 621
Length:621
Mass (Da):68,240
Last modified:May 5, 2009 - v3
Checksum:i6422B383345AD883
GO
Isoform PIAS2-alpha (identifier: O75928-2) [UniParc]FASTAAdd to Basket

Also known as: PIASx-alpha, ARIP3

The sequence of this isoform differs from the canonical sequence as follows:
     551-572: LDFLSLIPVDPQYCPPMFLDSL → EQRRNDINNELKLGTSSDTVQQ
     573-621: Missing.

Show »
Length:572
Mass (Da):63,396
Checksum:i63106D68C585F0ED
GO
Isoform 3 (identifier: O75928-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MADFEELR → MNAGKQLQRTLH
     402-621: Missing.

Note: No experimental confirmation available.

Show »
Length:405
Mass (Da):45,057
Checksum:i6C16003BCDB6384E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071V → A.
Corresponds to variant rs16940108 [ dbSNP | Ensembl ].
VAR_056693

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88MADFEELR → MNAGKQLQRTLH in isoform 3.
VSP_012196
Alternative sequencei402 – 621220Missing in isoform 3.
VSP_012197Add
BLAST
Alternative sequencei551 – 57222LDFLS…FLDSL → EQRRNDINNELKLGTSSDTV QQ in isoform PIAS2-alpha.
VSP_050008Add
BLAST
Alternative sequencei573 – 62149Missing in isoform PIAS2-alpha.
VSP_050009Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441P → L in AAK48938. 1 Publication
Sequence conflicti616 – 6161D → E in AAC36705. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077953 mRNA. Translation: AAC36704.1.
AF077954 mRNA. Translation: AAC36705.1.
AF361054 mRNA. Translation: AAK48938.1.
AC090241 Genomic DNA. No translation available.
AC090373 Genomic DNA. No translation available.
BC015190 mRNA. Translation: AAH15190.1.
CCDSiCCDS32824.1. [O75928-1]
CCDS32825.1. [O75928-2]
RefSeqiNP_004662.2. NM_004671.3. [O75928-1]
NP_775298.1. NM_173206.3. [O75928-2]
UniGeneiHs.657844.

Genome annotation databases

EnsembliENST00000324794; ENSP00000317163; ENSG00000078043. [O75928-2]
ENST00000585916; ENSP00000465676; ENSG00000078043. [O75928-1]
GeneIDi9063.
KEGGihsa:9063.
UCSCiuc002lck.3. human. [O75928-1]
uc002lcl.3. human. [O75928-2]
uc002lcn.1. human. [O75928-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077953 mRNA. Translation: AAC36704.1 .
AF077954 mRNA. Translation: AAC36705.1 .
AF361054 mRNA. Translation: AAK48938.1 .
AC090241 Genomic DNA. No translation available.
AC090373 Genomic DNA. No translation available.
BC015190 mRNA. Translation: AAH15190.1 .
CCDSi CCDS32824.1. [O75928-1 ]
CCDS32825.1. [O75928-2 ]
RefSeqi NP_004662.2. NM_004671.3. [O75928-1 ]
NP_775298.1. NM_173206.3. [O75928-2 ]
UniGenei Hs.657844.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ASQ NMR - B 466-488 [» ]
4FO9 X-ray 2.39 A 147-488 [» ]
ProteinModelPortali O75928.
SMRi O75928. Positions 1-65, 147-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114523. 59 interactions.
IntActi O75928. 23 interactions.
MINTi MINT-1455373.
STRINGi 9606.ENSP00000381648.

PTM databases

PhosphoSitei O75928.

Proteomic databases

MaxQBi O75928.
PaxDbi O75928.
PRIDEi O75928.

Protocols and materials databases

DNASUi 9063.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324794 ; ENSP00000317163 ; ENSG00000078043 . [O75928-2 ]
ENST00000585916 ; ENSP00000465676 ; ENSG00000078043 . [O75928-1 ]
GeneIDi 9063.
KEGGi hsa:9063.
UCSCi uc002lck.3. human. [O75928-1 ]
uc002lcl.3. human. [O75928-2 ]
uc002lcn.1. human. [O75928-3 ]

Organism-specific databases

CTDi 9063.
GeneCardsi GC18M044392.
HGNCi HGNC:17311. PIAS2.
MIMi 603567. gene.
neXtProti NX_O75928.
PharmGKBi PA134933292.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG125513.
HOGENOMi HOG000230594.
HOVERGENi HBG053598.
InParanoidi O75928.
KOi K16063.
OMAi PHESSTH.
OrthoDBi EOG7HF1JB.
PhylomeDBi O75928.

Enzyme and pathway databases

UniPathwayi UPA00886 .
SignaLinki O75928.

Miscellaneous databases

EvolutionaryTracei O75928.
GeneWikii Protein_inhibitor_of_activated_STAT2.
GenomeRNAii 9063.
NextBioi 33959.
PROi O75928.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75928.
Bgeei O75928.
CleanExi HS_PIAS2.
Genevestigatori O75928.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
InterProi IPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view ]
PANTHERi PTHR10782:SF12. PTHR10782:SF12. 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] (ISOFORMS PIAS2-ALPHA AND PIAS2-BETA).
    Tissue: B-cell.
  2. "Molecular cloning and characterization of a novel splicing variant of PIASx."
    Zheng Y., Zhou Z.-M., Yin L.-L., Li J.-M., Sha J.-H.
    Acta Pharmacol. Sin. 25:1058-1064(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM PIAS2-ALPHA).
    Tissue: Brain.
  5. "A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins."
    Moilanen A.-M., Karvonen U., Poukka H., Yan W., Toppari J., Jaenne O.A., Palvimo J.J.
    J. Biol. Chem. 274:3700-3704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif."
    Minty A., Dumont X., Kaghad M., Caput D.
    J. Biol. Chem. 275:36316-36323(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUMO1; TP73 AND TP53.
  7. "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."
    Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    J. Biol. Chem. 276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARK7, SUBCELLULAR LOCATION.
  8. "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.
  9. "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.
  10. "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, MUTAGENESIS OF CYS-362.
  11. "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; TP53 AND UBE2I, SUMOYLATION, MUTAGENESIS OF CYS-362.
  12. "PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4."
    Arora T., Liu B., He H., Kim J., Murphy T.L., Murphy K.M., Modlin R.L., Shuai K.
    J. Biol. Chem. 278:21327-21330(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT4, SUBCELLULAR LOCATION.
  13. "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.
  14. "PIASx acts as an Elk-1 coactivator by facilitating derepression."
    Yang S.-H., Sharrocks A.D.
    EMBO J. 24:2161-2171(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ELK1.
  15. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
    Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PARK7 SUMOYLATION.
  16. "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.
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "MDA5 is SUMOylated by PIAS2? in the upregulation of type I interferon signaling."
    Fu J., Xiong Y., Xu Y., Cheng G., Tang H.
    Mol. Immunol. 48:415-422(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFIH1/MDA5.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-477 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
    Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
    Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
  21. "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation."
    Song J., Zhang Z., Hu W., Chen Y.
    J. Biol. Chem. 280:40122-40129(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 466-488 IN COMPLEX WITH SUMO1, MUTAGENESIS OF VAL-467; VAL-469; ILE-470; LEU-472 AND THR-473.

Entry informationi

Entry nameiPIAS2_HUMAN
AccessioniPrimary (citable) accession number: O75928
Secondary accession number(s): O75927, Q96BT5, Q96KE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 136 of the entry and version 3 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 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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