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P51693

- APLP1_HUMAN

UniProt

P51693 - APLP1_HUMAN

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Protein

Amyloid-like protein 1

Gene

APLP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini39 – 580542ExtracellularSequence AnalysisAdd
BLAST
Transmembranei581 – 60323HelicalSequence AnalysisAdd
BLAST
Topological domaini604 – 65047CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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...)1 Publication
Glycosylationi227 – 2271O-linked (GalNAc...)1 Publication
Glycosylationi228 – 2281O-linked (GalNAc...)1 Publication
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

BgeeiP51693.
CleanExiHS_APLP1.
ExpressionAtlasiP51693. baseline and differential.
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. 46 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 – 2986Combined sources
Helixi306 – 33732Combined sources
Turni338 – 3414Combined sources
Helixi344 – 39956Combined sources
Beta strandi401 – 4033Combined sources
Helixi406 – 43732Combined sources
Helixi439 – 4424Combined sources
Turni443 – 4453Combined sources
Helixi446 – 46722Combined sources
Helixi471 – 48515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00530000063252.
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

        10         20         30         40         50
MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA
60 70 80 90 100
PGSAQVAGLC GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP
110 120 130 140 150
ELQIARVEQA TQAIPMERWC GGSRSGSCAH PHHQVVPFRC LPGEFVSEAL
160 170 180 190 200
LVPEGCRFLH QERMDQCESS TRRHQEAQEA CSSQGLILHG SGMLLPCGSD
210 220 230 240 250
RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPPGSRVEGA EDEEEEESFP
260 270 280 290 300
QPVDDYFVEP PQAEEEEETV PPPSSHTLAV VGKVTPTPRP TDGVDIYFGM
310 320 330 340 350
PGEISEHEGF LRAKMDLEER RMRQINEVMR EWAMADNQSK NLPKADRQAL
360 370 380 390 400
NEHFQSILQT LEEQVSGERQ RLVETHATRV IALINDQRRA ALEGFLAALQ
410 420 430 440 450
ADPPQAERVL LALRRYLRAE QKEQRHTLRH YQHVAAVDPE KAQQMRFQVH
460 470 480 490 500
THLQVIEERV NQSLGLLDQN PHLAQELRPQ IQELLHSEHL GPSELEAPAP
510 520 530 540 550
GGSSEDKGGL QPPDSKDDTP MTLPKGSTEQ DAASPEKEKM NPLEQYERKV
560 570 580 590 600
NASVPRGFPF HSSEIQRDEL APAGTGVSRE AVSGLLIMGA GGGSLIVLSM
610 620 630 640 650
LLLRRKKPYG AISHGVVEVD PMLTLEEQQL RELQRHGYEN PTYRFLEERP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 46 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.
GeneTreei ENSGT00530000063252.
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

Bgeei P51693.
CleanExi HS_APLP1.
ExpressionAtlasi P51693. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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

Dasty 3