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O75928 (PIAS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional 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. NucleusPML 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 processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen 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 from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

protein sumoylation

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.7PubMed 14752048. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

SUMO ligase activity

Inferred from direct assay PubMed 18579533. Source: BHF-UCL

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 9256341. Source: ProtInc

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621E3 SUMO-protein ligase PIAS2
PRO_0000218976

Regions

Domain11 – 4535SAP
Domain134 – 299166PINIT
Zinc finger331 – 40878SP-RING-type
Region467 – 4737SUMO1-binding
Motif19 – 235LXXLL motif
Motif484 – 4929Nuclear localization signal By similarity
Compositional bias571 – 61242Ser-rich
Compositional bias596 – 6027Poly-Ser

Amino acid modifications

Modified residue4761Phosphoserine Ref.19
Modified residue4771Phosphoserine Ref.19
Modified residue4781Phosphoserine Ref.19

Natural variations

Alternative sequence1 – 88MADFEELR → MNAGKQLQRTLH in isoform 3.
VSP_012196
Alternative sequence402 – 621220Missing in isoform 3.
VSP_012197
Alternative sequence551 – 57222LDFLS…FLDSL → EQRRNDINNELKLGTSSDTV QQ in isoform PIAS2-alpha.
VSP_050008
Alternative sequence573 – 62149Missing in isoform PIAS2-alpha.
VSP_050009
Natural variant2071V → A.
Corresponds to variant rs16940108 [ dbSNP | Ensembl ].
VAR_056693

Experimental info

Mutagenesis3621C → S or A: Loss of MDM2 and TP53 sumoylation and of autosumoylation; no loss of JUN- and TP53-binding. Ref.10 Ref.11
Mutagenesis4671V → A: Reduces affinity for SUMO1. Ref.21
Mutagenesis4691V → A: Abolishes binding to SUMO1. Ref.21
Mutagenesis4701I → A: Abolishes binding to SUMO1. Ref.21
Mutagenesis4721L → A: Abolishes binding to SUMO1. Ref.21
Mutagenesis4731T → A: Reduces affinity for SUMO1. Ref.21
Sequence conflict1441P → L in AAK48938. Ref.2
Sequence conflict6161D → E in AAC36705. Ref.1

Secondary structure

............................................. 621
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PIAS2-beta (PIASx-beta) (Miz1) [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: 6422B383345AD883

FASTA62168,240
        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 

« Hide

Isoform PIAS2-alpha (PIASx-alpha) (ARIP3) [UniParc].

Checksum: 63106D68C585F0ED
Show »

FASTA57263,396
Isoform 3 [UniParc].

Checksum: 6C16003BCDB6384E
Show »

FASTA40545,057

References

« Hide 'large scale' references
[1]"Inhibition of Stat1-mediated gene activation by PIAS1."
Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K.
Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (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. expand/collapse author list , 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, 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.
+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.
RefSeqNP_004662.2. NM_004671.3.
NP_775298.1. NM_173206.3.
UniGeneHs.657844.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASQNMR-B466-488[»]
4FO9X-ray2.39A147-488[»]
ProteinModelPortalO75928.
SMRO75928. Positions 1-65, 147-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114523. 59 interactions.
IntActO75928. 23 interactions.
MINTMINT-1455373.
STRING9606.ENSP00000381648.

PTM databases

PhosphoSiteO75928.

Proteomic databases

PaxDbO75928.
PRIDEO75928.

Protocols and materials databases

DNASU9063.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324794; ENSP00000317163; ENSG00000078043. [O75928-2]
ENST00000585916; ENSP00000465676; ENSG00000078043. [O75928-1]
GeneID9063.
KEGGhsa:9063.
UCSCuc002lck.3. human. [O75928-1]
uc002lcl.3. human. [O75928-2]
uc002lcn.1. human. [O75928-3]

Organism-specific databases

CTD9063.
GeneCardsGC18M044392.
HGNCHGNC:17311. PIAS2.
MIM603567. gene.
neXtProtNX_O75928.
PharmGKBPA134933292.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG125513.
HOGENOMHOG000230594.
HOVERGENHBG053598.
InParanoidO75928.
KOK16063.
OMAICISRDF.
OrthoDBEOG7HF1JB.
PhylomeDBO75928.

Enzyme and pathway databases

SignaLinkO75928.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressO75928.
BgeeO75928.
CleanExHS_PIAS2.
GenevestigatorO75928.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERPTHR10782:SF12. PTHR10782:SF12. 1 hit.
PfamPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75928.
GeneWikiProtein_inhibitor_of_activated_STAT2.
GenomeRNAi9063.
NextBio33959.
PROO75928.
SOURCESearch...

Entry information

Entry namePIAS2_HUMAN
AccessionPrimary (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: March 19, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM