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P39687

- AN32A_HUMAN

UniProt

P39687 - AN32A_HUMAN

Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member A

Gene

ANP32A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.4 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. gene expression Source: Reactome
    2. intracellular signal transduction Source: ProtInc
    3. mRNA metabolic process Source: Reactome
    4. nucleocytoplasmic transport Source: UniProtKB
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. RNA metabolic process Source: Reactome
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_25218. HuR stabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acidic leucine-rich nuclear phosphoprotein 32 family member A
    Alternative name(s):
    Acidic nuclear phosphoprotein pp32
    Short name:
    pp32
    Leucine-rich acidic nuclear protein
    Short name:
    LANP
    Mapmodulin
    Potent heat-stable protein phosphatase 2A inhibitor I1PP2A
    Putative HLA-DR-associated protein I
    Short name:
    PHAPI
    Gene namesi
    Name:ANP32A
    Synonyms:C15orf1, LANP, MAPM, PHAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:13233. ANP32A.

    Subcellular locationi

    Nucleus. Cytoplasm. Endoplasmic reticulum
    Note: Translocates to the cytoplasm during the process of neuritogenesis By similarity. Shuttles between nucleus and cytoplasm.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24811.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249Acidic leucine-rich nuclear phosphoprotein 32 family member APRO_0000137592Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphothreonine1 Publication
    Modified residuei17 – 171Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on serine residues.1 Publication
    The N-terminus is blocked.
    Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39687.
    PaxDbiP39687.
    PRIDEiP39687.

    2D gel databases

    SWISS-2DPAGEP39687.

    PTM databases

    PhosphoSiteiP39687.

    Miscellaneous databases

    PMAP-CutDBP39687.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested. Highly expressed in kidney and skeletal muscle, moderate levels of expression in brain, placenta and pancreas, and weakly expressed in lung. Found in all regions of the brain examined (amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus), with highest levels in amygdala.1 Publication

    Gene expression databases

    ArrayExpressiP39687.
    BgeeiP39687.
    CleanExiHS_ANP32A.
    GenevestigatoriP39687.

    Organism-specific databases

    HPAiCAB005231.

    Interactioni

    Subunit structurei

    Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET. Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts with ELAVL1. Part of the INHAT (inhibitor of histone acetyltransferases) complex. Interacts with E4F1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXIN1O151692EBI-359234,EBI-710484
    E4F1Q66K893EBI-359234,EBI-1227043
    PPP2CAP677752EBI-359234,EBI-712311
    Ppp2caP633312EBI-359234,EBI-7050205From a different organism.

    Protein-protein interaction databases

    BioGridi113791. 41 interactions.
    IntActiP39687. 15 interactions.
    MINTiMINT-4999627.
    STRINGi9606.ENSP00000417864.

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119
    Helixi16 – 183
    Beta strandi20 – 234
    Beta strandi46 – 483
    Beta strandi68 – 703
    Helixi81 – 866
    Beta strandi92 – 943
    Helixi103 – 1064
    Helixi107 – 1115
    Beta strandi117 – 1193
    Helixi124 – 1274
    Helixi131 – 1388

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JE0X-ray2.40A/B/C/D/E/F1-149[»]
    2JE1X-ray2.69A/B/C/D1-149[»]
    ProteinModelPortaliP39687.
    SMRiP39687. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39687.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati18 – 3821LRR 11 PublicationAdd
    BLAST
    Repeati43 – 6422LRR 21 PublicationAdd
    BLAST
    Repeati65 – 8723LRR 31 PublicationAdd
    BLAST
    Repeati89 – 11022LRR 41 PublicationAdd
    BLAST
    Domaini123 – 16139LRRCTAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 17425Necessary for tumor-suppressive functionAdd
    BLAST
    Regioni165 – 24985Interaction with E4F1By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi168 – 24982Asp/Glu-rich (highly acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the ANP32 family.Curated
    Contains 4 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG322008.
    HOGENOMiHOG000007361.
    HOVERGENiHBG053102.
    InParanoidiP39687.
    OMAiFTFAVEL.
    OrthoDBiEOG7TJ3KH.
    PhylomeDBiP39687.
    TreeFamiTF317206.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view]
    SMARTiSM00446. LRRcap. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI    50
    NVGLTSIANL PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI 100
    KDLSTIEPLK KLENLKSLDL FNCEVTNLND YRENVFKLLP QLTYLDGYDR 150
    DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD EDAQVVEDEE DEDEEEEGEE 200
    EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD 249
    Length:249
    Mass (Da):28,585
    Last modified:February 1, 1995 - v1
    Checksum:iCA2D1A756FBAEA04
    GO

    Sequence cautioni

    The sequence BAD97000.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861V → A in BAD97000. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75090 mRNA. Translation: CAA52981.1.
    U60823 mRNA. Translation: AAC50570.1.
    U73477 mRNA. Translation: AAB39706.1.
    AF025684 mRNA. Translation: AAB91548.1.
    AY349171 mRNA. Translation: AAQ79832.1.
    BT007436 mRNA. Translation: AAP36104.1.
    AK223280 mRNA. Translation: BAD97000.1. Different initiation.
    AK312703 mRNA. Translation: BAG35581.1.
    CH471082 Genomic DNA. Translation: EAW77824.1.
    BC007200 mRNA. Translation: AAH07200.1.
    CCDSiCCDS45292.1.
    PIRiS36375.
    S43309.
    RefSeqiNP_006296.1. NM_006305.3.
    UniGeneiHs.458747.

    Genome annotation databases

    EnsembliENST00000465139; ENSP00000417864; ENSG00000140350.
    GeneIDi8125.
    KEGGihsa:8125.
    UCSCiuc002arl.3. human.

    Polymorphism databases

    DMDMi730318.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75090 mRNA. Translation: CAA52981.1 .
    U60823 mRNA. Translation: AAC50570.1 .
    U73477 mRNA. Translation: AAB39706.1 .
    AF025684 mRNA. Translation: AAB91548.1 .
    AY349171 mRNA. Translation: AAQ79832.1 .
    BT007436 mRNA. Translation: AAP36104.1 .
    AK223280 mRNA. Translation: BAD97000.1 . Different initiation.
    AK312703 mRNA. Translation: BAG35581.1 .
    CH471082 Genomic DNA. Translation: EAW77824.1 .
    BC007200 mRNA. Translation: AAH07200.1 .
    CCDSi CCDS45292.1.
    PIRi S36375.
    S43309.
    RefSeqi NP_006296.1. NM_006305.3.
    UniGenei Hs.458747.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JE0 X-ray 2.40 A/B/C/D/E/F 1-149 [» ]
    2JE1 X-ray 2.69 A/B/C/D 1-149 [» ]
    ProteinModelPortali P39687.
    SMRi P39687. Positions 1-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113791. 41 interactions.
    IntActi P39687. 15 interactions.
    MINTi MINT-4999627.
    STRINGi 9606.ENSP00000417864.

    PTM databases

    PhosphoSitei P39687.

    Polymorphism databases

    DMDMi 730318.

    2D gel databases

    SWISS-2DPAGE P39687.

    Proteomic databases

    MaxQBi P39687.
    PaxDbi P39687.
    PRIDEi P39687.

    Protocols and materials databases

    DNASUi 8125.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000465139 ; ENSP00000417864 ; ENSG00000140350 .
    GeneIDi 8125.
    KEGGi hsa:8125.
    UCSCi uc002arl.3. human.

    Organism-specific databases

    CTDi 8125.
    GeneCardsi GC15M069070.
    HGNCi HGNC:13233. ANP32A.
    HPAi CAB005231.
    MIMi 600832. gene.
    neXtProti NX_P39687.
    PharmGKBi PA24811.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322008.
    HOGENOMi HOG000007361.
    HOVERGENi HBG053102.
    InParanoidi P39687.
    OMAi FTFAVEL.
    OrthoDBi EOG7TJ3KH.
    PhylomeDBi P39687.
    TreeFami TF317206.

    Enzyme and pathway databases

    Reactomei REACT_25218. HuR stabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi ANP32A. human.
    EvolutionaryTracei P39687.
    GenomeRNAii 8125.
    NextBioi 30786.
    PMAP-CutDB P39687.
    PROi P39687.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39687.
    Bgeei P39687.
    CleanExi HS_ANP32A.
    Genevestigatori P39687.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view ]
    SMARTi SM00446. LRRcap. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII."
      Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N.
      Biol. Chem. Hoppe-Seyler 375:113-126(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-26; 29-47; 71-97 AND 100-161.
      Tissue: B-cell lymphoma.
    2. "Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A."
      Li M., Makkinje A., Damuni Z.
      Biochemistry 35:6998-7002(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-12 AND 29-44.
      Tissue: Kidney.
    3. "Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci."
      Chen T.-H., Brody J.R., Romantsev F.E., Yu J.-G., Kayler A.E., Voneiff E., Kuhajda F.P., Pasternack G.R.
      Mol. Biol. Cell 7:2045-2056(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1."
      Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.
      Nature 389:974-978(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau."
      Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.
      FEBS Lett. 579:363-372(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Synovium.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Lymph.
    11. "Identification of sequences required for inhibition of oncogene-mediated transformation by pp32."
      Brody J.R., Kadkol S.S., Mahmoud M.A., Rebel J.M., Pasternack G.R.
      J. Biol. Chem. 274:20053-20055(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein."
      Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.
      Cell 104:119-130(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE INHAT COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
      Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
      J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SET.
    14. "Tumor suppression and potentiation by manipulation of pp32 expression."
      Bai J., Brody J.R., Kadkol S.S., Pasternack G.R.
      Oncogene 20:2153-2160(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Delineation of mRNA export pathways by the use of cell-permeable peptides."
      Gallouzi I.-E., Steitz J.A.
      Science 294:1895-1901(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ELAVL1, SUBCELLULAR LOCATION.
    16. "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
      Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
      Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SET COMPLEX.
    17. "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
      Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
      Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "The Anp32 family of proteins containing leucine-rich repeats."
      Matilla A., Radrizzani M.
      Cerebellum 4:7-18(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    19. "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
      Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
      Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SET COMPLEX.
    20. "The role of LANP and ataxin 1 in E4F-mediated transcriptional repression."
      Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y., Opal P.
      EMBO Rep. 8:671-677(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH E4F1.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins."
      Huyton T., Wolberger C.
      Protein Sci. 16:1308-1315(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-149, LEUCINE-RICH REPEATS.

    Entry informationi

    Entry nameiAN32A_HUMAN
    AccessioniPrimary (citable) accession number: P39687
    Secondary accession number(s): B2R6T4
    , Q53FK4, Q5J8L8, Q7M4N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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