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Protein

E3 SUMO-protein ligase PIAS2

Gene

Pias2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and 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 PIASx-beta, but not isoform PIASx-alpha, promotes MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation. Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than isoform PIASx-alpha (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity).By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri331 – 40878SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. androgen receptor binding Source: MGI
  2. DNA binding Source: MGI
  3. ligase activity Source: UniProtKB-KW
  4. SUMO transferase activity Source: MGI
  5. ubiquitin protein ligase binding Source: BHF-UCL
  6. zinc ion binding Source: InterPro

GO - Biological processi

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

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
Protein inhibitor of activated STAT x
Protein inhibitor of activated STAT2
Gene namesi
Name:Pias2
Synonyms:Miz1, Piasx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1096566. Pias2.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621E3 SUMO-protein ligase PIAS2PRO_0000218977Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8C5D8.
PaxDbiQ8C5D8.
PRIDEiQ8C5D8.

PTM databases

PhosphoSiteiQ8C5D8.

Expressioni

Gene expression databases

BgeeiQ8C5D8.
CleanExiMM_PIAS2.
ExpressionAtlasiQ8C5D8. baseline and differential.
GenevestigatoriQ8C5D8.

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. Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Interacts with PLAG1 (By similarity). Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase (By similarity). Interacts with IFIH1/MDA5 (By similarity). Interacts with PML (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab2P980782EBI-6305825,EBI-1391846
Dab2P98078-33EBI-6305825,EBI-6305891
Egr2P081525EBI-8064899,EBI-7070449

Protein-protein interaction databases

BioGridi201429. 11 interactions.
IntActiQ8C5D8. 5 interactions.
MINTiMINT-1782012.

Structurei

3D structure databases

ProteinModelPortaliQ8C5D8.
SMRiQ8C5D8. Positions 1-65, 147-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 299166PINITPROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif
Motifi484 – 4929Nuclear localization signal1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi571 – 61040Ser-richAdd
BLAST
Compositional biasi596 – 6027Poly-Ser

Domaini

The LXXLL motif is a transcriptional coregulator signature.

Sequence similaritiesi

Belongs to the PIAS family.Curated
Contains 1 PINIT domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri331 – 40878SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG125513.
GeneTreeiENSGT00550000074410.
HOVERGENiHBG053598.
InParanoidiQ8C5D8.
KOiK16063.
OMAiPHESSTH.
OrthoDBiEOG7HF1JB.
PhylomeDBiQ8C5D8.
TreeFamiTF323787.

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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C5D8-1) [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

        10         20         30         40         50
MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS
60 70 80 90 100
PAVQIKIREL YRRRYPRTLE GLCDLSTIKS SVFSLDGSSS PVEPDLPVAG
110 120 130 140 150
IHSLPSTSIT PHSPSSPVGS VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN
160 170 180 190 200
LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI FALTPQQVRE ICISRDFLPG
210 220 230 240 250
GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP LPGYAPPPKN
260 270 280 290 300
GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT
310 320 330 340 350
SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK
360 370 380 390 400
MRLTIPCRAV TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD
410 420 430 440 450
GLFMEILNDC SDVDEIKFQE DGSWCPMRPK KEAMKVTSQP CTKVESSSVF
460 470 480 490 500
SKPCSVTVAS DASKKKIDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP
510 520 530 540 550
TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP VSSMSSDLPG
560 570 580 590 600
LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSPHE SSTHVSSSSS
610 620
RSETGVITSS GRNIPDIISL D
Length:621
Mass (Da):68,426
Last modified:December 7, 2004 - v2
Checksum:iE980B834C2A9C58E
GO
Isoform 2 (identifier: Q8C5D8-2) [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 → EQRRNDINNEVQLGASSDTVQQ
     573-621: Missing.

Show »
Length:572
Mass (Da):63,458
Checksum:i70668C1CEB3702EE
GO
Isoform 3 (identifier: Q8C5D8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
     551-572: LDFLSLIPVDPQYCPPMFLDSL → EQRRNDINNEVQLGASSDTVQQ
     573-621: Missing.

Note: No experimental confirmation available.

Show »
Length:563
Mass (Da):62,352
Checksum:i25D6D636E852AA07
GO
Isoform 4 (identifier: Q8C5D8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     563-580: YCPPMFLDSLTSPLTASS → SHLTLNSKQYVCHHHQPP
     581-621: Missing.

Note: No experimental confirmation available.

Show »
Length:580
Mass (Da):64,421
Checksum:i4461E5438EC68633
GO
Isoform 5 (identifier: Q8C5D8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Note: No experimental confirmation available.

Show »
Length:612
Mass (Da):67,320
Checksum:i98EA1B83556CDE86
GO

Sequence cautioni

The sequence AAB96678.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB29594.1 differs from that shown. Reason: Frameshift at position 34. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731C → S in AAF12825 (PubMed:11104669).Curated
Sequence conflicti97 – 971P → A in AAF12825 (PubMed:11104669).Curated
Sequence conflicti110 – 1101T → A in AAF12825 (PubMed:11104669).Curated
Sequence conflicti119 – 1191G → E in AAF12825 (PubMed:11104669).Curated
Sequence conflicti150 – 1501N → T in AAF12825 (PubMed:11104669).Curated
Sequence conflicti158 – 1581D → E in AAF12825 (PubMed:11104669).Curated
Sequence conflicti173 – 1731R → G in BAC26579 (PubMed:16141072).Curated
Sequence conflicti243 – 2431G → A in AAF12825 (PubMed:11104669).Curated
Sequence conflicti288 – 2881N → Q in AAF12825 (PubMed:11104669).Curated
Sequence conflicti320 – 3201R → K in AAF12825 (PubMed:11104669).Curated
Sequence conflicti327 – 3271L → P in AAF12825 (PubMed:11104669).Curated
Sequence conflicti375 – 3751Q → R in AAF12825 (PubMed:11104669).Curated
Sequence conflicti413 – 4131V → A in AAF12825 (PubMed:11104669).Curated
Sequence conflicti438 – 4381S → I in BAC37407 (PubMed:16141072).Curated
Sequence conflicti458 – 4581V → G in AAF12825 (PubMed:11104669).Curated
Sequence conflicti464 – 4663KKK → GTR in AAF12825 (PubMed:11104669).Curated
Isoform 2 (identifier: Q8C5D8-2)
Sequence conflicti555 – 5551N → T in AAF12825 (PubMed:11104669).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99Missing in isoform 3 and isoform 5. 1 PublicationVSP_012198
Alternative sequencei551 – 57222LDFLS…FLDSL → EQRRNDINNEVQLGASSDTV QQ in isoform 2 and isoform 3. 3 PublicationsVSP_012199Add
BLAST
Alternative sequencei563 – 58018YCPPM…LTASS → SHLTLNSKQYVCHHHQPP in isoform 4. 1 PublicationVSP_012200Add
BLAST
Alternative sequencei573 – 62149Missing in isoform 2 and isoform 3. 3 PublicationsVSP_012201Add
BLAST
Alternative sequencei581 – 62141Missing in isoform 4. 1 PublicationVSP_012202Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF201391 mRNA. Translation: AAF12825.1.
AK029716 mRNA. Translation: BAC26579.1.
AK014871 mRNA. Translation: BAB29594.1. Frameshift.
AK078813 mRNA. Translation: BAC37407.1.
AK086653 mRNA. Translation: BAC39710.1.
BC005596 mRNA. Translation: AAH05596.1.
BC034711 mRNA. Translation: AAH34711.1.
AF039567 mRNA. Translation: AAB96678.1. Different initiation.
CCDSiCCDS37866.1. [Q8C5D8-1]
RefSeqiNP_001157639.1. NM_001164167.1. [Q8C5D8-4]
NP_001157640.1. NM_001164168.1.
NP_001157641.1. NM_001164169.1. [Q8C5D8-2]
NP_001157642.1. NM_001164170.1.
NP_032628.3. NM_008602.4. [Q8C5D8-1]
UniGeneiMm.6370.

Genome annotation databases

EnsembliENSMUST00000114777; ENSMUSP00000110425; ENSMUSG00000025423. [Q8C5D8-1]
GeneIDi17344.
KEGGimmu:17344.
UCSCiuc008frb.1. mouse. [Q8C5D8-2]
uc008frc.2. mouse. [Q8C5D8-1]
uc012bfb.1. mouse. [Q8C5D8-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF201391 mRNA. Translation: AAF12825.1.
AK029716 mRNA. Translation: BAC26579.1.
AK014871 mRNA. Translation: BAB29594.1. Frameshift.
AK078813 mRNA. Translation: BAC37407.1.
AK086653 mRNA. Translation: BAC39710.1.
BC005596 mRNA. Translation: AAH05596.1.
BC034711 mRNA. Translation: AAH34711.1.
AF039567 mRNA. Translation: AAB96678.1. Different initiation.
CCDSiCCDS37866.1. [Q8C5D8-1]
RefSeqiNP_001157639.1. NM_001164167.1. [Q8C5D8-4]
NP_001157640.1. NM_001164168.1.
NP_001157641.1. NM_001164169.1. [Q8C5D8-2]
NP_001157642.1. NM_001164170.1.
NP_032628.3. NM_008602.4. [Q8C5D8-1]
UniGeneiMm.6370.

3D structure databases

ProteinModelPortaliQ8C5D8.
SMRiQ8C5D8. Positions 1-65, 147-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201429. 11 interactions.
IntActiQ8C5D8. 5 interactions.
MINTiMINT-1782012.

PTM databases

PhosphoSiteiQ8C5D8.

Proteomic databases

MaxQBiQ8C5D8.
PaxDbiQ8C5D8.
PRIDEiQ8C5D8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114777; ENSMUSP00000110425; ENSMUSG00000025423. [Q8C5D8-1]
GeneIDi17344.
KEGGimmu:17344.
UCSCiuc008frb.1. mouse. [Q8C5D8-2]
uc008frc.2. mouse. [Q8C5D8-1]
uc012bfb.1. mouse. [Q8C5D8-4]

Organism-specific databases

CTDi9063.
MGIiMGI:1096566. Pias2.

Phylogenomic databases

eggNOGiNOG125513.
GeneTreeiENSGT00550000074410.
HOVERGENiHBG053598.
InParanoidiQ8C5D8.
KOiK16063.
OMAiPHESSTH.
OrthoDBiEOG7HF1JB.
PhylomeDBiQ8C5D8.
TreeFamiTF323787.

Enzyme and pathway databases

UniPathwayiUPA00886.

Miscellaneous databases

ChiTaRSiPias2. mouse.
NextBioi291922.
PROiQ8C5D8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C5D8.
CleanExiMM_PIAS2.
ExpressionAtlasiQ8C5D8. baseline and differential.
GenevestigatoriQ8C5D8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p67 isoform of mouse disabled 2 protein acts as a transcriptional activator during the differentiation of F9 cells."
    Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S.
    Biochem. J. 352:645-650(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH DAB2.
    Strain: 129.
    Tissue: Teratocarcinoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
    Strain: C57BL/6J.
    Tissue: Embryonic lung and Testis.
  3. "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] (ISOFORMS 3 AND 5).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA."
    Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R.
    Mech. Dev. 65:3-17(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-621 (ISOFORM 1), INTERACTION WITH MSX2.
    Tissue: Embryo.
  5. Erratum
    Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R.
    Mech. Dev. 69:219-219(1997)
  6. "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta/Siz2 is a transcriptional cofactor for TFII-I."
    Tussie-Luna M.I., Michel B., Hakre S., Roy A.L.
    J. Biol. Chem. 277:43185-43193(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH GTF2I AND GTF2IRD1.
  7. "PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases."
    Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.
    Mol. Cell. Biol. 22:5222-5234(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION.
  8. Cited for: INTERACTION WITH IKFZ1.

Entry informationi

Entry nameiPIAS2_MOUSE
AccessioniPrimary (citable) accession number: Q8C5D8
Secondary accession number(s): O54987
, Q8C384, Q8CDQ8, Q8K208, Q99JX5, Q9D5W7, Q9QZ63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: March 4, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.