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P51693

- APLP1_HUMAN

UniProt

P51693 - APLP1_HUMAN

Protein

Amyloid-like protein 1

Gene

APLP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (22 Feb 2003)
      Previous versions | rss
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    Functioni

    May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding By similarity. Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I.By similarity
    The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei167 – 1671Required for Cu(2+) reductionBy similarity
    Sitei620 – 6212Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    1. alpha-2A adrenergic receptor binding Source: BHF-UCL
    2. alpha-2B adrenergic receptor binding Source: BHF-UCL
    3. alpha-2C adrenergic receptor binding Source: BHF-UCL
    4. heparin binding Source: UniProtKB-KW
    5. identical protein binding Source: IntAct
    6. protein binding Source: IntAct
    7. transition metal ion binding Source: InterPro

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: BHF-UCL
    2. apoptotic process Source: UniProtKB-KW
    3. cell adhesion Source: UniProtKB-KW
    4. cellular response to norepinephrine stimulus Source: BHF-UCL
    5. endocytosis Source: UniProtKB-KW
    6. extracellular matrix organization Source: Ensembl
    7. forebrain development Source: Ensembl
    8. mRNA polyadenylation Source: Ensembl
    9. negative regulation of cAMP biosynthetic process Source: BHF-UCL
    10. nervous system development Source: ProtInc
    11. organ morphogenesis Source: ProtInc
    12. regulation of translation Source: Ensembl

    Keywords - Biological processi

    Apoptosis, Cell adhesion, Endocytosis

    Keywords - Ligandi

    Copper, Heparin-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amyloid-like protein 1
    Short name:
    APLP
    Short name:
    APLP-1
    Cleaved into the following chain:
    Gene namesi
    Name:APLP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:597. APLP1.

    Subcellular locationi

    Peptide C30 : Cytoplasm
    Note: C-terminally processed in the Golgi complex.

    GO - Cellular componenti

    1. basement membrane Source: ProtInc
    2. Golgi apparatus Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. perinuclear region of cytoplasm Source: BHF-UCL
    5. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi426 – 4261H → A: Reduced affinity for heparin. Reduces homodimerization. 1 Publication
    Mutagenesisi429 – 4291R → A: Strongly reduced affinity for heparin. Strongly reduced homodimerization. 1 Publication
    Mutagenesisi433 – 4331H → A: Reduced affinity for heparin. Reduces homodimerization. 1 Publication

    Keywords - Diseasei

    Neurodegeneration

    Organism-specific databases

    PharmGKBiPA24884.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 650612Amyloid-like protein 1PRO_0000000203Add
    BLAST
    Peptidei621 – 65030C30By similarityPRO_0000000204Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi215 – 2151O-linked (GalNAc...)2 Publications
    Glycosylationi227 – 2271O-linked (GalNAc...)2 Publications
    Glycosylationi228 – 2281O-linked (GalNAc...)2 Publications
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-620 by caspase-3 By similarity.By similarity
    N- and O-glycosylated. O-glycosylation with core 1 or possibly core 8 glycans. Glycosylation on Ser-227 is the preferred site to Thr-228.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP51693.
    PRIDEiP51693.

    PTM databases

    PhosphoSiteiP51693.

    Expressioni

    Tissue specificityi

    Expressed in the cerebral cortex where it is localized to the postsynaptic density (PSD).1 Publication

    Gene expression databases

    ArrayExpressiP51693.
    BgeeiP51693.
    CleanExiHS_APLP1.
    GenevestigatoriP51693.

    Organism-specific databases

    HPAiHPA028971.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Heparin binding promotes homodimerization. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB and APBA family members, MAPK8IP1 and Dab1 By similarity. Binding to Dab1 inhibits its serine phosphorylation By similarity. Interacts with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts (via NPXY motif) with DAB1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-74648,EBI-74648
    APLP2Q064812EBI-74648,EBI-79306
    APPP05067-42EBI-74648,EBI-302641
    MED12Q930742EBI-74648,EBI-394357
    ZNF24P170282EBI-74648,EBI-707773

    Protein-protein interaction databases

    BioGridi106830. 45 interactions.
    DIPiDIP-30846N.
    IntActiP51693. 42 interactions.
    MINTiMINT-1395075.
    STRINGi9606.ENSP00000221891.

    Structurei

    Secondary structure

    1
    650
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi293 – 2986
    Helixi306 – 33732
    Turni338 – 3414
    Helixi344 – 39956
    Beta strandi401 – 4033
    Helixi406 – 43732
    Helixi439 – 4424
    Turni443 – 4453
    Helixi446 – 46722
    Helixi471 – 48515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PMRX-ray2.11A/B285-499[»]
    3Q7GX-ray2.30A/B285-494[»]
    3Q7LX-ray2.20A/B285-494[»]
    3QMKX-ray2.21A/B285-494[»]
    ProteinModelPortaliP51693.
    SMRiP51693. Positions 55-211, 292-489.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51693.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini39 – 580542ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini604 – 65047CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei581 – 60323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni158 – 17821Copper-bindingBy similarityAdd
    BLAST
    Regioni204 – 2118Zinc-binding
    Regioni285 – 30521O-glycosylated at three sitesAdd
    BLAST
    Regioni310 – 34233Heparin-bindingBy similarityAdd
    BLAST
    Regioni410 – 44132Heparin-bindingBy similarityAdd
    BLAST
    Regioni442 – 45918Collagen-bindingBy similarityAdd
    BLAST
    Regioni632 – 64918Interaction with DAB1By similarityAdd
    BLAST
    Regioni636 – 65015Interaction with DAB2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi604 – 61512Basolateral sorting signalBy similarityAdd
    BLAST
    Motifi640 – 6434Clathrin-bindingSequence Analysis
    Motifi640 – 6434NPXY motif; contains endocytosis signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi241 – 2477Poly-Glu
    Compositional biasi264 – 2685Poly-Glu

    Domaini

    The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The NPXY site is also involved in clathrin-mediated endocytosis.

    Sequence similaritiesi

    Belongs to the APP family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG289770.
    HOGENOMiHOG000232190.
    HOVERGENiHBG000051.
    InParanoidiP51693.
    KOiK05639.
    OMAiMLLPCGS.
    PhylomeDBiP51693.
    TreeFamiTF317274.

    Family and domain databases

    Gene3Di3.30.1490.140. 1 hit.
    3.90.570.10. 1 hit.
    InterProiIPR008155. Amyloid_glyco.
    IPR011178. Amyloid_glyco_Cu-bd.
    IPR024329. Amyloid_glyco_E2_domain.
    IPR008154. Amyloid_glyco_extra.
    IPR019744. Amyloid_glyco_extracell_CS.
    IPR015849. Amyloid_glyco_heparin-bd.
    IPR019745. Amyloid_glyco_intracell_CS.
    IPR019543. APP_amyloid_C.
    [Graphical view]
    PfamiPF10515. APP_amyloid. 1 hit.
    PF12924. APP_Cu_bd. 1 hit.
    PF12925. APP_E2. 1 hit.
    PF02177. APP_N. 1 hit.
    [Graphical view]
    PRINTSiPR00203. AMYLOIDA4.
    SMARTiSM00006. A4_EXTRA. 1 hit.
    [Graphical view]
    SUPFAMiSSF109843. SSF109843. 1 hit.
    SSF56491. SSF56491. 1 hit.
    SSF89811. SSF89811. 1 hit.
    PROSITEiPS00319. A4_EXTRA. 1 hit.
    PS00320. A4_INTRA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51693-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA    50
    PGSAQVAGLC GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP 100
    ELQIARVEQA TQAIPMERWC GGSRSGSCAH PHHQVVPFRC LPGEFVSEAL 150
    LVPEGCRFLH QERMDQCESS TRRHQEAQEA CSSQGLILHG SGMLLPCGSD 200
    RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPPGSRVEGA EDEEEEESFP 250
    QPVDDYFVEP PQAEEEEETV PPPSSHTLAV VGKVTPTPRP TDGVDIYFGM 300
    PGEISEHEGF LRAKMDLEER RMRQINEVMR EWAMADNQSK NLPKADRQAL 350
    NEHFQSILQT LEEQVSGERQ RLVETHATRV IALINDQRRA ALEGFLAALQ 400
    ADPPQAERVL LALRRYLRAE QKEQRHTLRH YQHVAAVDPE KAQQMRFQVH 450
    THLQVIEERV NQSLGLLDQN PHLAQELRPQ IQELLHSEHL GPSELEAPAP 500
    GGSSEDKGGL QPPDSKDDTP MTLPKGSTEQ DAASPEKEKM NPLEQYERKV 550
    NASVPRGFPF HSSEIQRDEL APAGTGVSRE AVSGLLIMGA GGGSLIVLSM 600
    LLLRRKKPYG AISHGVVEVD PMLTLEEQQL RELQRHGYEN PTYRFLEERP 650
    Length:650
    Mass (Da):72,176
    Last modified:February 22, 2003 - v3
    Checksum:iB95F0F4D1C5CBAC7
    GO
    Isoform 2 (identifier: P51693-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         517-517: D → DA

    Show »
    Length:651
    Mass (Da):72,247
    Checksum:iEEF2FB97BDDF6A66
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481A → P in AAB96331. (PubMed:9428684)Curated
    Sequence conflicti78 – 781P → S in BC013850. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei517 – 5171D → DA in isoform 2. 1 PublicationVSP_039100

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48437 mRNA. Translation: AAB96331.1.
    AD000864 Genomic DNA. Translation: AAB50173.1.
    BC012889 mRNA. Translation: AAH12889.1.
    BC013850 mRNA. No translation available.
    CCDSiCCDS32997.1. [P51693-2]
    RefSeqiNP_001019978.1. NM_001024807.1. [P51693-2]
    NP_005157.1. NM_005166.3. [P51693-1]
    UniGeneiHs.74565.

    Genome annotation databases

    EnsembliENST00000221891; ENSP00000221891; ENSG00000105290. [P51693-2]
    GeneIDi333.
    KEGGihsa:333.
    UCSCiuc002oce.3. human. [P51693-1]
    uc002ocf.3. human. [P51693-2]

    Polymorphism databases

    DMDMi28558769.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48437 mRNA. Translation: AAB96331.1 .
    AD000864 Genomic DNA. Translation: AAB50173.1 .
    BC012889 mRNA. Translation: AAH12889.1 .
    BC013850 mRNA. No translation available.
    CCDSi CCDS32997.1. [P51693-2 ]
    RefSeqi NP_001019978.1. NM_001024807.1. [P51693-2 ]
    NP_005157.1. NM_005166.3. [P51693-1 ]
    UniGenei Hs.74565.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PMR X-ray 2.11 A/B 285-499 [» ]
    3Q7G X-ray 2.30 A/B 285-494 [» ]
    3Q7L X-ray 2.20 A/B 285-494 [» ]
    3QMK X-ray 2.21 A/B 285-494 [» ]
    ProteinModelPortali P51693.
    SMRi P51693. Positions 55-211, 292-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106830. 45 interactions.
    DIPi DIP-30846N.
    IntActi P51693. 42 interactions.
    MINTi MINT-1395075.
    STRINGi 9606.ENSP00000221891.

    PTM databases

    PhosphoSitei P51693.

    Polymorphism databases

    DMDMi 28558769.

    Proteomic databases

    PaxDbi P51693.
    PRIDEi P51693.

    Protocols and materials databases

    DNASUi 333.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221891 ; ENSP00000221891 ; ENSG00000105290 . [P51693-2 ]
    GeneIDi 333.
    KEGGi hsa:333.
    UCSCi uc002oce.3. human. [P51693-1 ]
    uc002ocf.3. human. [P51693-2 ]

    Organism-specific databases

    CTDi 333.
    GeneCardsi GC19P036359.
    HGNCi HGNC:597. APLP1.
    HPAi HPA028971.
    MIMi 104775. gene.
    neXtProti NX_P51693.
    PharmGKBi PA24884.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289770.
    HOGENOMi HOG000232190.
    HOVERGENi HBG000051.
    InParanoidi P51693.
    KOi K05639.
    OMAi MLLPCGS.
    PhylomeDBi P51693.
    TreeFami TF317274.

    Miscellaneous databases

    ChiTaRSi APLP1. human.
    EvolutionaryTracei P51693.
    GeneWikii APLP1.
    GenomeRNAii 333.
    NextBioi 1377.
    PROi P51693.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51693.
    Bgeei P51693.
    CleanExi HS_APLP1.
    Genevestigatori P51693.

    Family and domain databases

    Gene3Di 3.30.1490.140. 1 hit.
    3.90.570.10. 1 hit.
    InterProi IPR008155. Amyloid_glyco.
    IPR011178. Amyloid_glyco_Cu-bd.
    IPR024329. Amyloid_glyco_E2_domain.
    IPR008154. Amyloid_glyco_extra.
    IPR019744. Amyloid_glyco_extracell_CS.
    IPR015849. Amyloid_glyco_heparin-bd.
    IPR019745. Amyloid_glyco_intracell_CS.
    IPR019543. APP_amyloid_C.
    [Graphical view ]
    Pfami PF10515. APP_amyloid. 1 hit.
    PF12924. APP_Cu_bd. 1 hit.
    PF12925. APP_E2. 1 hit.
    PF02177. APP_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00203. AMYLOIDA4.
    SMARTi SM00006. A4_EXTRA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109843. SSF109843. 1 hit.
    SSF56491. SSF56491. 1 hit.
    SSF89811. SSF89811. 1 hit.
    PROSITEi PS00319. A4_EXTRA. 1 hit.
    PS00320. A4_INTRA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human amyloid precursor-like protein 1 -- cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid."
      Paliga K., Peraus G., Kreger S., Duwrrwang U., Hesse L., Multhaup G., Masters C.L., Beyreuther K., Weidemann A.
      Eur. J. Biochem. 250:354-363(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure of the human amyloid-precursor-like protein gene APLP1 at 19q13.1."
      Lenkkeri U., Kestila M., Lamerdin J.E., McCready P., Adamson A., Olsen A., Tryggvason K.
      Hum. Genet. 102:192-196(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Ovary.
    5. "Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density."
      Kim T.-W., Wu K., Xu J.-L., McAuliffe G., Tanzi R.E., Wasco W., Black I.B.
      Brain Res. Mol. Brain Res. 32:36-44(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE FUNCTION, TISSUE SPECIFICITY.
    6. "The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily."
      Bush A.I., Pettingell W.H. Jr., de Paradis M., Tanzi R.E., Wasco W.
      J. Biol. Chem. 269:26618-26621(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEPARIN AND ZINC-BINDING.
    7. "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein."
      Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., Sakiyama S., Kirino Y., Suzuki T.
      J. Biol. Chem. 274:2243-2254(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APBA2.
    8. Cited for: EXTRACELLULAR COPPER-BINDING.
    9. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-215; SER-227 AND THR-228, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    10. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "The E2 Domains of APP and APLP1 Share a Conserved Mode of Dimerization."
      Lee S., Xue Y., Hu J., Wang Y., Liu X., Demeler B., Ha Y.
      Biochemistry 50:5453-5464(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 285-499, HEPARIN-BINDING, MUTAGENESIS OF HIS-426; ARG-429 AND HIS-433, SUBUNIT.

    Entry informationi

    Entry nameiAPLP1_HUMAN
    AccessioniPrimary (citable) accession number: P51693
    Secondary accession number(s): O00113, Q96A92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: February 22, 2003
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 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

    Miscellaneous

    Binds zinc and copper in the extracellular domain. Zinc-binding increases heparin binding. No Cu2+ reducing activity with copper-binding.

    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

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