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Q8WUF5

- IASPP_HUMAN

UniProt

Q8WUF5 - IASPP_HUMAN

Protein

RelA-associated inhibitor

Gene

PPP1R13L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 4 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    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.4 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. transcription corepressor activity Source: ProtInc
    4. transcription factor binding Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cardiac muscle contraction Source: Ensembl
    3. cardiac right ventricle morphogenesis Source: Ensembl
    4. embryonic camera-type eye development Source: Ensembl
    5. hair cycle Source: Ensembl
    6. multicellular organismal homeostasis Source: Ensembl
    7. multicellular organism growth Source: Ensembl
    8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. post-embryonic development Source: Ensembl
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. ventricular cardiac muscle tissue development Source: Ensembl

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RelA-associated inhibitor
    Alternative name(s):
    Inhibitor of ASPP protein
    Short name:
    Protein iASPP
    NFkB-interacting protein 1
    PPP1R13B-like protein
    Gene namesi
    Name:PPP1R13L
    Synonyms:IASPP, NKIP1, PPP1R13BL, RAI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:18838. PPP1R13L.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic but also nuclear.

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. cytoplasm Source: HPA
    3. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34195.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 828828RelA-associated inhibitorPRO_0000066966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei102 – 1021Phosphoserine1 Publication
    Modified residuei110 – 1101Phosphoserine3 Publications
    Modified residuei113 – 1131Phosphoserine3 Publications
    Modified residuei119 – 1191Phosphoserine1 Publication
    Modified residuei120 – 1201Phosphoserine1 Publication
    Modified residuei123 – 1231Phosphothreonine1 Publication
    Modified residuei134 – 1341Phosphoserine1 Publication
    Modified residuei183 – 1831Phosphoserine3 Publications
    Modified residuei187 – 1871Phosphoserine3 Publications
    Modified residuei203 – 2031Phosphoserine1 Publication
    Modified residuei280 – 2801Phosphoserine1 Publication
    Modified residuei316 – 3161Phosphoserine1 Publication
    Modified residuei332 – 3321Phosphoserine1 Publication
    Modified residuei526 – 5261Phosphoserine1 Publication
    Modified residuei567 – 5671Phosphoserine4 Publications
    Modified residuei597 – 5971Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8WUF5.
    PaxDbiQ8WUF5.
    PRIDEiQ8WUF5.

    PTM databases

    PhosphoSiteiQ8WUF5.

    Miscellaneous databases

    PMAP-CutDBQ8WUF5.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, placenta and prostate. Weakly expressed in brain, liver, skeletal muscle, testis and peripheral blood leukocyte.1 Publication

    Gene expression databases

    ArrayExpressiQ8WUF5.
    BgeeiQ8WUF5.
    CleanExiHS_PPP1R13L.
    GenevestigatoriQ8WUF5.

    Organism-specific databases

    HPAiCAB005016.
    HPA041231.

    Interactioni

    Subunit structurei

    Interacts with RELA NF-kappa-B subunit and with SP1 via its C-terminus part. Interacts with p53/TP53, TP63 and TP73.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-5550163,EBI-5550163
    Q9WMX22EBI-5550163,EBI-6863748From a different organism.
    EP300Q094722EBI-5550163,EBI-447295
    PPP1CAP621364EBI-5550163,EBI-357253
    TP53P0463711EBI-5550163,EBI-366083

    Protein-protein interaction databases

    BioGridi116059. 5 interactions.
    DIPiDIP-29586N.
    IntActiQ8WUF5. 8 interactions.
    MINTiMINT-7034564.
    STRINGi9606.ENSP00000354218.

    Structurei

    Secondary structure

    1
    828
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi627 – 63711
    Helixi640 – 64910
    Helixi663 – 6697
    Helixi673 – 6819
    Helixi696 – 7027
    Helixi706 – 7138
    Turni714 – 7163
    Helixi731 – 7333
    Helixi741 – 75414
    Turni755 – 7573
    Helixi759 – 7613
    Beta strandi762 – 7676
    Beta strandi784 – 7918
    Beta strandi796 – 8038
    Beta strandi806 – 8116
    Helixi812 – 8143
    Beta strandi815 – 8184

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VGEX-ray2.10A607-828[»]
    ProteinModelPortaliQ8WUF5.
    SMRiQ8WUF5. Positions 616-822.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WUF5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati659 – 69133ANK 1Add
    BLAST
    Repeati692 – 72433ANK 2Add
    BLAST
    Domaini758 – 82063SH3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi54 – 602549Pro-richAdd
    BLAST
    Compositional biasi407 – 44438Gln-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the ASPP family.Curated
    Contains 2 ANK repeats.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG237939.
    HOVERGENiHBG055210.
    InParanoidiQ8WUF5.
    OMAiYEKKSSQ.
    OrthoDBiEOG7WDN20.
    PhylomeDBiQ8WUF5.
    TreeFamiTF105545.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR028320. iASPP.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR24164. PTHR24164. 1 hit.
    PfamiPF12796. Ank_2. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00248. ANK. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8WUF5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSEAFQSAR DFLDMNFQSL AMKHMDLKQM ELDTAAAKVD ELTKQLESLW    50
    SDSPAPPGPQ AGPPSRPPRY SSSSIPEPFG SRGSPRKAAT DGADTPFGRS 100
    ESAPTLHPYS PLSPKGRPSS PRTPLYLQPD AYGSLDRATS PRPRAFDGAG 150
    SSLGRAPSPR PGPGPLRQQG PPTPFDFLGR AGSPRGSPLA EGPQAFFPER 200
    GPSPRPPATA YDAPASAFGS SLLGSGGSAF APPLRAQDDL TLRRRPPKAW 250
    NESDLDVAYE KKPSQTASYE RLDVFARPAS PSLQLLPWRE SSLDGLGGTG 300
    KDNLTSATLP RNYKVSPLAS DRRSDAGSYR RSLGSAGPSG TLPRSWQPVS 350
    RIPMPPSSPQ PRGAPRQRPI PLSMIFKLQN AFWEHGASRA MLPGSPLFTR 400
    APPPKLQPQP QPQPQPQSQP QPQLPPQPQT QPQTPTPAPQ HPQQTWPPVN 450
    EGPPKPPTEL EPEPEIEGLL TPVLEAGDVD EGPVARPLSP TRLQPALPPE 500
    AQSVPELEEV ARVLAEIPRP LKRRGSMEQA PAVALPPTHK KQYQQIISRL 550
    FHRHGGPGPG GPEPELSPIT EGSEARAGPP APAPPAPIPP PAPSQSSPPE 600
    QPQSMEMRSV LRKAGSPRKA RRARLNPLVL LLDAALTGEL EVVQQAVKEM 650
    NDPSQPNEEG ITALHNAICG ANYSIVDFLI TAGANVNSPD SHGWTPLHCA 700
    ASCNDTVICM ALVQHGAAIF ATTLSDGATA FEKCDPYREG YADCATYLAD 750
    VEQSMGLMNS GAVYALWDYS AEFGDELSFR EGESVTVLRR DGPEETDWWW 800
    AALHGQEGYV PRNYFGLFPR VKPQRSKV 828
    Length:828
    Mass (Da):89,091
    Last modified:April 4, 2006 - v4
    Checksum:i7BEEF239B7CA9C70
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti198 – 1981P → S in AAH64913. (PubMed:15489334)Curated
    Sequence conflicti223 – 2231L → I in AAW51146. 1 PublicationCurated
    Sequence conflicti317 – 3182PL → AA in AAD27004. (PubMed:10336463)Curated
    Sequence conflicti321 – 3211D → T in AAD27004. (PubMed:10336463)Curated
    Sequence conflicti369 – 3691P → S in AAW51146. 1 PublicationCurated
    Sequence conflicti372 – 3721Missing in AAW51146. 1 PublicationCurated
    Sequence conflicti426 – 4261P → Q in AAD27004. (PubMed:10336463)Curated
    Sequence conflicti439 – 4402PQ → HP in AAD27004. (PubMed:10336463)Curated
    Sequence conflicti747 – 7471Y → S in AAW51146. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33050.1.
    RefSeqiNP_001135974.1. NM_001142502.1.
    NP_006654.2. NM_006663.3.
    UniGeneiHs.466937.

    Genome annotation databases

    EnsembliENST00000360957; ENSP00000354218; ENSG00000104881.
    ENST00000418234; ENSP00000403902; ENSG00000104881.
    GeneIDi10848.
    KEGGihsa:10848.
    UCSCiuc002pbn.3. human.

    Polymorphism databases

    DMDMi92090607.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS33050.1.
    RefSeqi NP_001135974.1. NM_001142502.1.
    NP_006654.2. NM_006663.3.
    UniGenei Hs.466937.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VGE X-ray 2.10 A 607-828 [» ]
    ProteinModelPortali Q8WUF5.
    SMRi Q8WUF5. Positions 616-822.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116059. 5 interactions.
    DIPi DIP-29586N.
    IntActi Q8WUF5. 8 interactions.
    MINTi MINT-7034564.
    STRINGi 9606.ENSP00000354218.

    PTM databases

    PhosphoSitei Q8WUF5.

    Polymorphism databases

    DMDMi 92090607.

    Proteomic databases

    MaxQBi Q8WUF5.
    PaxDbi Q8WUF5.
    PRIDEi Q8WUF5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360957 ; ENSP00000354218 ; ENSG00000104881 .
    ENST00000418234 ; ENSP00000403902 ; ENSG00000104881 .
    GeneIDi 10848.
    KEGGi hsa:10848.
    UCSCi uc002pbn.3. human.

    Organism-specific databases

    CTDi 10848.
    GeneCardsi GC19M045883.
    HGNCi HGNC:18838. PPP1R13L.
    HPAi CAB005016.
    HPA041231.
    MIMi 607463. gene.
    neXtProti NX_Q8WUF5.
    PharmGKBi PA34195.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237939.
    HOVERGENi HBG055210.
    InParanoidi Q8WUF5.
    OMAi YEKKSSQ.
    OrthoDBi EOG7WDN20.
    PhylomeDBi Q8WUF5.
    TreeFami TF105545.

    Miscellaneous databases

    EvolutionaryTracei Q8WUF5.
    GeneWikii PPP1R13L.
    GenomeRNAii 10848.
    NextBioi 41185.
    PMAP-CutDB Q8WUF5.
    PROi Q8WUF5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WUF5.
    Bgeei Q8WUF5.
    CleanExi HS_PPP1R13L.
    Genevestigatori Q8WUF5.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR028320. iASPP.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR24164. PTHR24164. 1 hit.
    Pfami PF12796. Ank_2. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00248. ANK. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 2 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. 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.

    Entry informationi

    Entry nameiIASPP_HUMAN
    AccessioniPrimary (citable) accession number: Q8WUF5
    Secondary accession number(s): Q2PNZ9
    , Q5DU71, Q5I1X4, Q6P1R7, Q6PKF8, Q9Y290
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 120 of the entry and version 4 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3