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Q8WUF5 (IASPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RelA-associated inhibitor
Alternative name(s):
Inhibitor of ASPP protein
Short name=Protein iASPP
NFkB-interacting protein 1
PPP1R13B-like protein
Gene names
Name:PPP1R13L
Synonyms:IASPP, NKIP1, PPP1R13BL, RAI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis. Ref.1 Ref.5 Ref.6 Ref.7

Subunit structure

Interacts with RELA NF-kappa-B subunit and with SP1 via its C-terminus part. Interacts with p53/TP53, TP63 and TP73. Ref.1 Ref.5 Ref.6 Ref.7 Ref.16

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic but also nuclear. Ref.1 Ref.5

Tissue specificity

Highly expressed in heart, placenta and prostate. Weakly expressed in brain, liver, skeletal muscle, testis and peripheral blood leukocyte. Ref.5

Domain

Isoform 1N-terminal region is required for cytoplasmic localization.

Sequence similarities

Belongs to the ASPP family.

Contains 2 ANK repeats.

Contains 1 SH3 domain.

Sequence caution

The sequence AAD27004.1 differs from that shown. Reason: Frameshift at positions 439, 483, 562 and 591.

The sequence AAD27005.1 differs from that shown. Reason: Frameshift at positions 483, 562 and 591.

The sequence AAD27005.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainANK repeat
Repeat
SH3 domain
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

cardiac right ventricle morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye development

Inferred from electronic annotation. Source: Ensembl

hair cycle

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

multicellular organismal homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ventricular cardiac muscle tissue development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Traceable author statement Ref.5. Source: ProtInc

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 23623661. Source: IntAct

protein binding

Inferred from physical interaction PubMed 17906639PubMed 18985028PubMed 21513714PubMed 21998301PubMed 22321011PubMed 23623661. Source: IntAct

transcription corepressor activity

Traceable author statement Ref.5. Source: ProtInc

transcription factor binding

Traceable author statement Ref.5. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 828828RelA-associated inhibitor
PRO_0000066966

Regions

Repeat659 – 69133ANK 1
Repeat692 – 72433ANK 2
Domain758 – 82063SH3
Compositional bias54 – 602549Pro-rich
Compositional bias407 – 44438Gln-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue1021Phosphoserine Ref.11
Modified residue1101Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue1131Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue1191Phosphoserine Ref.11
Modified residue1201Phosphoserine Ref.11
Modified residue1231Phosphothreonine Ref.11
Modified residue1341Phosphoserine Ref.11
Modified residue1831Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue1871Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue2031Phosphoserine Ref.11
Modified residue2801Phosphoserine Ref.13
Modified residue3161Phosphoserine Ref.11
Modified residue3321Phosphoserine Ref.11
Modified residue5261Phosphoserine Ref.11
Modified residue5671Phosphoserine Ref.8 Ref.10 Ref.11 Ref.13
Modified residue5971Phosphoserine Ref.11

Experimental info

Sequence conflict1981P → S in AAH64913. Ref.4
Sequence conflict2231L → I in AAW51146. Ref.2
Sequence conflict317 – 3182PL → AA in AAD27004. Ref.5
Sequence conflict3211D → T in AAD27004. Ref.5
Sequence conflict3691P → S in AAW51146. Ref.2
Sequence conflict3721Missing in AAW51146. Ref.2
Sequence conflict4261P → Q in AAD27004. Ref.5
Sequence conflict439 – 4402PQ → HP in AAD27004. Ref.5
Sequence conflict7471Y → S in AAW51146. Ref.2

Secondary structure

.............................. 828
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WUF5 [UniParc].

Last modified April 4, 2006. Version 4.
Checksum: 7BEEF239B7CA9C70

FASTA82889,091
        10         20         30         40         50         60 
MDSEAFQSAR DFLDMNFQSL AMKHMDLKQM ELDTAAAKVD ELTKQLESLW SDSPAPPGPQ 

        70         80         90        100        110        120 
AGPPSRPPRY SSSSIPEPFG SRGSPRKAAT DGADTPFGRS ESAPTLHPYS PLSPKGRPSS 

       130        140        150        160        170        180 
PRTPLYLQPD AYGSLDRATS PRPRAFDGAG SSLGRAPSPR PGPGPLRQQG PPTPFDFLGR 

       190        200        210        220        230        240 
AGSPRGSPLA EGPQAFFPER GPSPRPPATA YDAPASAFGS SLLGSGGSAF APPLRAQDDL 

       250        260        270        280        290        300 
TLRRRPPKAW NESDLDVAYE KKPSQTASYE RLDVFARPAS PSLQLLPWRE SSLDGLGGTG 

       310        320        330        340        350        360 
KDNLTSATLP RNYKVSPLAS DRRSDAGSYR RSLGSAGPSG TLPRSWQPVS RIPMPPSSPQ 

       370        380        390        400        410        420 
PRGAPRQRPI PLSMIFKLQN AFWEHGASRA MLPGSPLFTR APPPKLQPQP QPQPQPQSQP 

       430        440        450        460        470        480 
QPQLPPQPQT QPQTPTPAPQ HPQQTWPPVN EGPPKPPTEL EPEPEIEGLL TPVLEAGDVD 

       490        500        510        520        530        540 
EGPVARPLSP TRLQPALPPE AQSVPELEEV ARVLAEIPRP LKRRGSMEQA PAVALPPTHK 

       550        560        570        580        590        600 
KQYQQIISRL FHRHGGPGPG GPEPELSPIT EGSEARAGPP APAPPAPIPP PAPSQSSPPE 

       610        620        630        640        650        660 
QPQSMEMRSV LRKAGSPRKA RRARLNPLVL LLDAALTGEL EVVQQAVKEM NDPSQPNEEG 

       670        680        690        700        710        720 
ITALHNAICG ANYSIVDFLI TAGANVNSPD SHGWTPLHCA ASCNDTVICM ALVQHGAAIF 

       730        740        750        760        770        780 
ATTLSDGATA FEKCDPYREG YADCATYLAD VEQSMGLMNS GAVYALWDYS AEFGDELSFR 

       790        800        810        820 
EGESVTVLRR DGPEETDWWW AALHGQEGYV PRNYFGLFPR VKPQRSKV 

« Hide

References

« Hide 'large scale' references
[1]"The N-terminus of a novel isoform of human iASPP is required for its cytoplasmic localization."
Slee E.A., Gillotin S., Bergamaschi D., Royer C., Llanos S., Ali S., Jin B., Trigiante G., Lu X.
Oncogene 23:9007-9016(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53.
[2]Herron B.J., Rao C., Beier D.R.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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].
Tissue: Liver, Placenta and Testis.
[5]"Identification of a novel inhibitor of nuclear factor-kappaB, RelA-associated inhibitor."
Yang J.-P., Hori M., Sanda T., Okamoto T.
J. Biol. Chem. 274:15662-15670(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 317-828, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RELA.
Tissue: Placenta.
[6]"RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions."
Takada N., Sanda T., Okamoto H., Yang J.-P., Asamitsu K., Sarol L., Kimura G., Uranishi H., Tetsuka T., Okamoto T.
J. Virol. 76:8019-8030(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SP1.
[7]"iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human."
Bergamaschi D., Samuels Y., O'Neil N.J., Trigiante G., Crook T., Hsieh J.-K., O'Connor D.J., Zhong S., Campargue I., Tomlinson M.L., Kuwabara P.E., Lu X.
Nat. Genet. 33:162-167(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-113; SER-183 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-110; SER-113; SER-119; SER-120; THR-123; SER-134; SER-203; SER-316; SER-332; SER-526; SER-567 AND SER-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-183 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-110; SER-113; SER-183; SER-187; SER-280 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Biochemical and structural studies of ASPP proteins reveal differential binding to p53, p63, and p73."
Robinson R.A., Lu X., Jones E.Y., Siebold C.
Structure 16:259-268(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 607-828, INTERACTION WITH TP53/P53; TP63 AND TP73.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ888472 mRNA. Translation: CAI60219.1.
AY869712 mRNA. Translation: AAW51146.1.
DQ314886 Genomic DNA. Translation: ABC40745.1.
BC001475 mRNA. Translation: AAH01475.1.
BC020589 mRNA. Translation: AAH20589.1.
BC032298 mRNA. Translation: AAH32298.1.
BC064913 mRNA. Translation: AAH64913.1.
AF078036 mRNA. Translation: AAD27004.1. Frameshift.
AF078037 mRNA. Translation: AAD27005.1. Sequence problems.
CCDSCCDS33050.1.
RefSeqNP_001135974.1. NM_001142502.1.
NP_006654.2. NM_006663.3.
UniGeneHs.466937.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VGEX-ray2.10A607-828[»]
ProteinModelPortalQ8WUF5.
SMRQ8WUF5. Positions 616-822.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116059. 5 interactions.
DIPDIP-29586N.
IntActQ8WUF5. 8 interactions.
MINTMINT-7034564.
STRING9606.ENSP00000354218.

PTM databases

PhosphoSiteQ8WUF5.

Polymorphism databases

DMDM92090607.

Proteomic databases

MaxQBQ8WUF5.
PaxDbQ8WUF5.
PRIDEQ8WUF5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360957; ENSP00000354218; ENSG00000104881.
ENST00000418234; ENSP00000403902; ENSG00000104881.
GeneID10848.
KEGGhsa:10848.
UCSCuc002pbn.3. human.

Organism-specific databases

CTD10848.
GeneCardsGC19M045883.
HGNCHGNC:18838. PPP1R13L.
HPACAB005016.
HPA041231.
MIM607463. gene.
neXtProtNX_Q8WUF5.
PharmGKBPA34195.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237939.
HOVERGENHBG055210.
InParanoidQ8WUF5.
OMAYEKKSSQ.
OrthoDBEOG7WDN20.
PhylomeDBQ8WUF5.
TreeFamTF105545.

Gene expression databases

ArrayExpressQ8WUF5.
BgeeQ8WUF5.
CleanExHS_PPP1R13L.
GenevestigatorQ8WUF5.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR028320. iASPP.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR24164. PTHR24164. 1 hit.
PfamPF12796. Ank_2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00248. ANK. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8WUF5.
GeneWikiPPP1R13L.
GenomeRNAi10848.
NextBio41185.
PMAP-CutDBQ8WUF5.
PROQ8WUF5.
SOURCESearch...

Entry information

Entry nameIASPP_HUMAN
AccessionPrimary (citable) accession number: Q8WUF5
Secondary accession number(s): Q2PNZ9 expand/collapse secondary AC list , Q5DU71, Q5I1X4, Q6P1R7, Q6PKF8, Q9Y290
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 119 of the entry and version 4 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

MIM cross-references

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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM