O75928 (PIAS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PIAS2
Synonyms:	PIASX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional 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'. Ref.14 Ref.15 Ref.20
Pathway	Protein modification; protein sumoylation.
Subunit structure	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). Ref.6 Ref.7 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20
Subcellular location	Nucleus speckle. Nucleus › PML body. Note: Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs). Ref.7 Ref.10 Ref.12 Ref.20
Tissue specificity	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. Ref.2 Ref.5 Ref.8
Developmental stage	Isoform 3 expression in adult testis is 14.2-fold stronger than in embryonic testis. Ref.2
Induction	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.
Domain	The LXXLL motif is a transcriptional coregulator signature.
Post-translational modification	Sumoylated. Ref.10 Ref.11
Sequence similarities	Belongs to the PIAS family. Contains 1 PINIT domain. Contains 1 SAP domain. Contains 1 SP-RING-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB negative regulation of androgen receptor signaling pathway Inferred from direct assay Ref.7. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement PubMed 15572661. Source: UniProtKB protein sumoylation Inferred from direct assay Ref.20. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.7PubMed 14752048. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW SUMO ligase activity Inferred from direct assay PubMed 18579533. Source: BHF-UCL androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB transcription coactivator activity Non-traceable author statement PubMed 15572661. Source: UniProtKB zinc ion binding Traceable author statement PubMed 9256341. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYC	P01106	4	EBI-348555,EBI-447544
RUFY1	Q96T51	3	EBI-348555,EBI-3941207
UBE2I	P63279	5	EBI-348555,EBI-80168

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform PIAS2-beta (identifier: O75928-1)

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.

Isoform PIAS2-alpha (identifier: O75928-2)

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.

Isoform 3 (identifier: O75928-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 621

621

E3 SUMO-protein ligase PIAS2

PRO_0000218976

Regions

Domain

11 – 45

35

SAP

Domain

134 – 299

166

PINIT

Zinc finger

331 – 408

78

SP-RING-type

Region

467 – 473

7

SUMO1-binding

Motif

19 – 23

5

LXXLL motif

Motif

484 – 492

9

Nuclear localization signal By similarity

Compositional bias

571 – 612

42

Ser-rich

Compositional bias

596 – 602

7

Poly-Ser

Amino acid modifications

Modified residue

476

1

Phosphoserine Ref.19

Modified residue

477

1

Phosphoserine Ref.19

Modified residue

478

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

1 – 8

8

MADFEELR → MNAGKQLQRTLH in isoform 3.

VSP_012196

Alternative sequence

402 – 621

220

Missing in isoform 3.

VSP_012197

Alternative sequence

551 – 572

22

LDFLS…FLDSL → EQRRNDINNELKLGTSSDTV QQ in isoform PIAS2-alpha.

VSP_050008

Alternative sequence

573 – 621

49

Missing in isoform PIAS2-alpha.

VSP_050009

Natural variant

207

1

V → A.
Corresponds to variant rs16940108 [ dbSNP | Ensembl ].

VAR_056693

Experimental info

Mutagenesis

362

1

C → S or A: Loss of MDM2 and TP53 sumoylation and of autosumoylation; no loss of JUN- and TP53-binding. Ref.10 Ref.11

Mutagenesis

467

1

V → A: Reduces affinity for SUMO1. Ref.21

Mutagenesis

469

1

V → A: Abolishes binding to SUMO1. Ref.21

Mutagenesis

470

1

I → A: Abolishes binding to SUMO1. Ref.21

Mutagenesis

472

1

L → A: Abolishes binding to SUMO1. Ref.21

Mutagenesis

473

1

T → A: Reduces affinity for SUMO1. Ref.21

Sequence conflict

144

1

P → L in AAK48938. Ref.2

Sequence conflict

616

1

D → E in AAC36705. Ref.1

Secondary structure

1

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621

Helix Strand Turn

Details...

Beta strand

154 – 165

12

Beta strand

173 – 181

9

Helix

185 – 192

8

Beta strand

195 – 197

3

Beta strand

203 – 215

13

Beta strand

231 – 234

4

Beta strand

237 – 239

3

Helix

264 – 266

3

Beta strand

271 – 273

3

Beta strand

275 – 282

8

Beta strand

289 – 298

10

Helix

301 – 309

9

Helix

316 – 327

12

Beta strand

340 – 345

6

Turn

347 – 349

3

Beta strand

354 – 359

6

Helix

370 – 379

10

Turn

386 – 388

3

Helix

394 – 396

3

Beta strand

397 – 400

4

Helix

401 – 407

7

Beta strand

415 – 418

4

Beta strand

469 – 471

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform PIAS2-beta (PIASx-beta) (Miz1) [UniParc]. Last modified May 5, 2009. Version 3. Checksum: 6422B383345AD883	FASTA	621	68,240
	10 20 30 40 50 60 MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL 70 80 90 100 110 120 YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG IHSLPSTSVT PHSPSSPVGS 130 140 150 160 170 180 VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI 190 200 210 220 230 240 FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP 250 260 270 280 290 300 LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 310 320 330 340 350 360 SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV 370 380 390 400 410 420 TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE 430 440 450 460 470 480 DGSWCPMRPK KEAMKVSSQP CTKIESSSVL SKPCSVTVAS EASKKKVDVI DLTIESSSDE 490 500 510 520 530 540 EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP 550 560 570 580 590 600 ISSMSSDLPG LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSSHE SSTHVSSSSS 610 620 RSETGVITSS GSNIPDIISL D
	Isoform PIAS2-alpha (PIASx-alpha) (ARIP3) [UniParc]. Checksum: 63106D68C585F0ED	FASTA	572	63,396
	10 20 30 40 50 60 MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL 70 80 90 100 110 120 YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG IHSLPSTSVT PHSPSSPVGS 130 140 150 160 170 180 VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI 190 200 210 220 230 240 FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP 250 260 270 280 290 300 LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 310 320 330 340 350 360 SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV 370 380 390 400 410 420 TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE 430 440 450 460 470 480 DGSWCPMRPK KEAMKVSSQP CTKIESSSVL SKPCSVTVAS EASKKKVDVI DLTIESSSDE 490 500 510 520 530 540 EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP 550 560 570 ISSMSSDLPG EQRRNDINNE LKLGTSSDTV QQ
	Isoform 3 [UniParc]. Checksum: 6C16003BCDB6384E	FASTA	405	45,057
	10 20 30 40 50 60 MNAGKQLQRT LHNMVSSFRV SELQVLLGFA GRNKSGRKHD LLMRALHLLK SGCSPAVQIK 70 80 90 100 110 120 IRELYRRRYP RTLEGLSDLS TIKSSVFSLD GGSSPVEPDL AVAGIHSLPS TSVTPHSPSS 130 140 150 160 170 180 PVGSVLLQDT KPTFEMQQPS PPIPPVHPDV QLKNLPFYDV LDVLIKPTSL VQSSIQRFQE 190 200 210 220 230 240 KFFIFALTPQ QVREICISRD FLPGGRRDYT VQVQLRLCLA ETSCPQEDNY PNSLCIKVNG 250 260 270 280 290 300 KLFPLPGYAP PPKNGIEQKR PGRPLNITSL VRLSSAVPNQ ISISWASEIG KNYSMSVYLV 310 320 330 340 350 360 RQLTSAMLLQ RLKMKGIRNP DHSRALIKEK LTADPDSEIA TTSLRVSLMC PLGKMRLTIP 370 380 390 400 CRAVTCTHLQ CFDAALYLQM NEKKPTWICP VCDKKAAYES LILDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inhibition of Stat1-mediated gene activation by PIAS1." Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K. Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (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]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005836.
IPI00244407.
IPI00477352.

RefSeq

NP_004662.2. NM_004671.3.
NP_775298.1. NM_173206.3.

UniGene

Hs.657844.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ASQ	NMR	-	B	466-488	[»]
4FO9	X-ray	2.39	A	147-488	[»]

ProteinModelPortal

O75928.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75928. 15 interactions.

MINT

MINT-1455373.

STRING

9606.ENSP00000381648.

PTM databases

PhosphoSite

O75928.

Proteomic databases

PaxDb

O75928.

PRIDE

O75928.

Protocols and materials databases

DNASU

9063.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324794; ENSP00000317163; ENSG00000078043.
ENST00000585916; ENSP00000465676; ENSG00000078043.
ENST00000592011; ENSP00000467733; ENSG00000078043.

GeneID

9063.

KEGG

hsa:9063.

UCSC

uc002lck.3. human.
uc002lcl.3. human.
uc002lcn.1. human.

Organism-specific databases

CTD

9063.

GeneCards

GC18M044392.

HGNC

HGNC:17311. PIAS2.

MIM

603567. gene.

neXtProt

NX_O75928.

PharmGKB

PA134933292.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG125513.

HOGENOM

HOG000230594.

HOVERGEN

HBG053598.

InParanoid

O75928.

KO

K16063.

OrthoDB

EOG4RNB85.

PhylomeDB

O75928.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_stat4pathway. IL12 signaling mediated by STAT4.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

SignaLink

O75928.

UniPathway

UPA00886.

Gene expression databases

ArrayExpress

O75928.

Bgee

O75928.

CleanEx

HS_PIAS2.

Genevestigator

O75928.

GermOnline

ENSG00000078043. Homo sapiens.

Family and domain databases

Gene3D

1.10.720.30. 1 hit.

InterPro

IPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]

PANTHER

PTHR10782:SF12. PTHR10782:SF12. 1 hit.

Pfam

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

SMART

SM00513. SAP. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

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EvolutionaryTrace

O75928.

GenomeRNAi

9063.

NextBio

33959.

SOURCE

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Entry information

Entry name

PIAS2_HUMAN

Accession

Primary (citable) accession number: O75928
Secondary accession number(s): O75927, Q96BT5, Q96KE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	May 5, 2009
Last modified:	May 29, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.