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Amyloid beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Beta-amyloid precursor protein) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99; Beta-amyloid protein 42 (Beta-APP42); Beta-amyloid protein 40 (Beta-APP40); C83; P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Gamma-CTF(50)); C31]

 A4_PANTR                Reviewed;         770 AA.
Q5IS80;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
27-SEP-2017, entry version 114.
RecName: Full=Amyloid-beta A4 protein;
AltName: Full=ABPP;
Short=APP;
AltName: Full=Alzheimer disease amyloid A4 protein homolog;
AltName: Full=Amyloid precursor protein {ECO:0000305};
AltName: Full=Amyloid-beta precursor protein {ECO:0000305};
Contains:
RecName: Full=N-APP;
Contains:
RecName: Full=Soluble APP-alpha;
Short=S-APP-alpha;
Contains:
RecName: Full=Soluble APP-beta;
Short=S-APP-beta;
Contains:
RecName: Full=C99;
Contains:
RecName: Full=Amyloid-beta protein 42;
Short=Abeta42;
AltName: Full=Beta-APP42;
Contains:
RecName: Full=Amyloid-beta protein 40;
Short=Abeta40;
AltName: Full=Beta-APP40;
Contains:
RecName: Full=C83;
Contains:
RecName: Full=P3(42);
Contains:
RecName: Full=P3(40);
Contains:
RecName: Full=C80;
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 59;
AltName: Full=Gamma-CTF(59);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 57;
AltName: Full=Gamma-CTF(57);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 50;
AltName: Full=Gamma-CTF(50);
Contains:
RecName: Full=C31;
Flags: Precursor;
Name=APP;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
"Accelerated evolution of nervous system genes in the origin of Homo
sapiens.";
Cell 119:1027-1040(2004).
-!- FUNCTION: Functions as a cell surface receptor and performs
physiological functions on the surface of neurons relevant to
neurite growth, neuronal adhesion and axonogenesis. Involved in
cell mobility and transcription regulation through protein-protein
interactions (By similarity). Can promote transcription activation
through binding to APBB1-KAT5 and inhibit Notch signaling through
interaction with Numb (By similarity). Couples to apoptosis-
inducing pathways such as those mediated by G(O) and JIP (By
similarity). Inhibits G(o) alpha ATPase activity (By similarity).
Acts as a kinesin I membrane receptor, mediating the axonal
transport of beta-secretase and presenilin 1 (By similarity). May
be involved in copper homeostasis/oxidative stress through copper
ion reduction. In vitro, copper-metallated APP induces neuronal
death directly or is potentiated through Cu(2+)-mediated low-
density lipoprotein oxidation (By similarity). Can regulate
neurite outgrowth through binding to components of the
extracellular matrix such as heparin and collagen I and IV (By
similarity). The splice isoforms that contain the BPTI domain
possess protease inhibitor activity. Induces a AGER-dependent
pathway that involves activation of p38 MAPK, resulting in
internalization of amyloid-beta peptide and leading to
mitochondrial dysfunction in cultured cortical neurons. Provides
Cu(2+) ions for GPC1 which are required for release of nitric
oxide (NO) and subsequent degradation of the heparan sulfate
chains on GPC1 (By similarity). {ECO:0000250}.
-!- FUNCTION: Amyloid-beta peptides are lipophilic metal chelators
with metal-reducing activity. Binds transient metals such as
copper, zinc and iron (By similarity). {ECO:0000250}.
-!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved
peptides, including C31, are potent enhancers of neuronal
apoptosis. {ECO:0000250}.
-!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and
degeneration of both neuronal cell bodies (via caspase-3) and
axons (via caspase-6). {ECO:0000250}.
-!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several
cytoplasmic proteins, including APBB family members, the APBA
family, MAPK8IP1, and SHC1, NUMB and DAB1 (By similarity). Binding
to Dab1 inhibits its serine phosphorylation (By similarity).
Interacts (via NPXY motif) with DAB2 (via PID domain); the
interaction is impaired by tyrosine phosphorylation of the NPXY
motif. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1,
IB1, KNS2 (via its TPR domains) (By similarity), APPBP2 (via BaSS)
and DDB1. In vitro, it binds MAPT via the MT-binding domains (By
similarity). Associates with microtubules in the presence of ATP
and in a kinesin-dependent manner (By similarity). Interacts with
CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with
ITM2B. Interacts with ITM2C. Interacts with IDE. Can form
homodimers; this is promoted by heparin binding (By similarity).
Amyloid-beta protein 40 interacts with S100A9 (By similarity).
CTF-alpha product of APP interacts with GSAP (By similarity).
Interacts with SORL1 (By similarity). Interacts with PLD3 (By
similarity). Interacts with VDAC1 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P05067}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Membrane, clathrin-coated pit
{ECO:0000250}. Note=Cell surface protein that rapidly becomes
internalized via clathrin-coated pits. During maturation, the
immature APP (N-glycosylated in the endoplasmic reticulum) moves
to the Golgi complex where complete maturation occurs (O-
glycosylated and sulfated). After alpha-secretase cleavage,
soluble APP is released into the extracellular space and the C-
terminal is internalized to endosomes and lysosomes. Some APP
accumulates in secretory transport vesicles leaving the late Golgi
compartment and returns to the cell surface. Gamma-CTF(59) peptide
is located to both the cytoplasm and nuclei of neurons. Associates
with GPC1 in perinuclear compartments (By similarity).
{ECO:0000250}.
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for
sorting of membrane proteins to the basolateral surface of
epithelial cells. {ECO:0000250}.
-!- DOMAIN: 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 PID domain-containing proteins which bind APP
require the YENPTY motif for full interaction. These interactions
are independent of phosphorylation on the terminal tyrosine
residue. The NPXY site is also involved in clathrin-mediated
endocytosis (By similarity). {ECO:0000250}.
-!- PTM: Proteolytically processed under normal cellular conditions.
Cleavage either by alpha-secretase, beta-secretase or theta-
secretase leads to generation and extracellular release of soluble
APP peptides, S-APP-alpha and S-APP-beta, and the retention of
corresponding membrane-anchored C-terminal fragments, C80, C83 and
C99. Subsequent processing of C80 and C83 by gamma-secretase
yields P3 peptides. This is the major secretory pathway and is
non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated
gamma-secretase processing of C99 releases the amyloid-beta
proteins, amyloid-beta protein 40 and amyloid-beta protein 42,
major components of amyloid plaques, and the cytotoxic C-terminal
fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59) (By
similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved by caspases during neuronal
apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9
results in the production of the neurotoxic C31 peptide and the
increased production of amyloid-beta peptides. {ECO:0000250}.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
serine residues is neuron-specific. Phosphorylation can affect APP
processing, neuronal differentiation and interaction with other
proteins (By similarity). {ECO:0000250}.
-!- PTM: Trophic-factor deprivation triggers the cleavage of surface
APP by beta-secretase to release sAPP-beta which is further
cleaved to release an N-terminal fragment of APP (N-APP).
{ECO:0000250}.
-!- PTM: Amyloid-beta peptides are degraded by IDE. {ECO:0000250}.
-!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and
zinc, can induce histidine-bridging between amyloid-beta molecules
resulting in amyloid-beta-metal aggregates. Extracellular zinc-
binding increases binding of heparin to APP and inhibits collagen-
binding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000305}.
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EMBL; AY665248; AAV74286.1; -; mRNA.
RefSeq; NP_001013036.1; NM_001013018.1.
UniGene; Ptr.762; -.
ProteinModelPortal; Q5IS80; -.
SMR; Q5IS80; -.
STRING; 9598.ENSPTRP00000023795; -.
MEROPS; I02.015; -.
PaxDb; Q5IS80; -.
PRIDE; Q5IS80; -.
Ensembl; ENSPTRT00000025781; ENSPTRP00000023795; ENSPTRG00000013811.
GeneID; 473931; -.
KEGG; ptr:473931; -.
CTD; 351; -.
eggNOG; KOG3540; Eukaryota.
eggNOG; ENOG410ZTKC; LUCA.
GeneTree; ENSGT00530000063252; -.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; Q5IS80; -.
KO; K04520; -.
OMA; REVCSEQ; -.
OrthoDB; EOG091G0UW4; -.
TreeFam; TF317274; -.
Proteomes; UP000002277; Unplaced.
Bgee; ENSPTRG00000013811; -.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0051233; C:spindle midzone; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
GO; GO:0002265; P:astrocyte activation involved in immune response; IEA:Ensembl.
GO; GO:0008088; P:axo-dendritic transport; ISS:UniProtKB.
GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB.
GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0007617; P:mating behavior; ISS:UniProtKB.
GO; GO:0014005; P:microglia development; IEA:Ensembl.
GO; GO:0090647; P:modulation of age-related behavioral decline; IEA:Ensembl.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IEA:Ensembl.
GO; GO:0032640; P:tumor necrosis factor production; IEA:Ensembl.
GO; GO:0008542; P:visual learning; ISS:UniProtKB.
CDD; cd00109; KU; 1.
Gene3D; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
Gene3D; 4.10.230.10; -; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
InterPro; IPR011178; Amyloid_glyco_Cu-bd.
InterPro; IPR024329; Amyloid_glyco_E2_domain.
InterPro; IPR008154; Amyloid_glyco_extra.
InterPro; IPR019744; Amyloid_glyco_extracell_CS.
InterPro; IPR015849; Amyloid_glyco_heparin-bd.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103:SF17; PTHR23103:SF17; 1.
Pfam; PF10515; APP_amyloid; 1.
Pfam; PF12924; APP_Cu_bd; 1.
Pfam; PF12925; APP_E2; 1.
Pfam; PF02177; APP_N; 1.
Pfam; PF03494; Beta-APP; 1.
Pfam; PF00014; Kunitz_BPTI; 1.
PRINTS; PR00203; AMYLOIDA4.
PRINTS; PR00759; BASICPTASE.
PRINTS; PR00204; BETAAMYLOID.
SMART; SM00006; A4_EXTRA; 1.
SMART; SM00131; KU; 1.
SUPFAM; SSF109843; SSF109843; 1.
SUPFAM; SSF56491; SSF56491; 1.
SUPFAM; SSF57362; SSF57362; 1.
SUPFAM; SSF89811; SSF89811; 1.
PROSITE; PS00319; A4_EXTRA; 1.
PROSITE; PS00320; A4_INTRA; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
2: Evidence at transcript level;
Amyloid; Apoptosis; Cell adhesion; Coated pit; Complete proteome;
Copper; Disulfide bond; Endocytosis; Glycoprotein; Heparin-binding;
Iron; Isopeptide bond; Membrane; Metal-binding;
Notch signaling pathway; Phosphoprotein; Protease inhibitor;
Proteoglycan; Reference proteome; Serine protease inhibitor; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
SIGNAL 1 17 {ECO:0000250}.
CHAIN 18 770 Amyloid-beta A4 protein.
/FTId=PRO_0000000127.
CHAIN 18 687 Soluble APP-alpha. {ECO:0000255}.
/FTId=PRO_0000000128.
CHAIN 18 671 Soluble APP-beta. {ECO:0000255}.
/FTId=PRO_0000000129.
CHAIN 18 286 N-APP. {ECO:0000250}.
/FTId=PRO_0000381969.
CHAIN 672 770 C99. {ECO:0000255}.
/FTId=PRO_0000000130.
CHAIN 672 713 Amyloid-beta protein 42. {ECO:0000255}.
/FTId=PRO_0000000131.
CHAIN 672 711 Amyloid-beta protein 40. {ECO:0000255}.
/FTId=PRO_0000000132.
CHAIN 688 770 C83. {ECO:0000255}.
/FTId=PRO_0000000133.
PEPTIDE 688 713 P3(42). {ECO:0000255}.
/FTId=PRO_0000000134.
PEPTIDE 688 711 P3(40). {ECO:0000255}.
/FTId=PRO_0000000135.
CHAIN 691 770 C80.
/FTId=PRO_0000384577.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
{ECO:0000255}.
/FTId=PRO_0000000136.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
{ECO:0000255}.
/FTId=PRO_0000000137.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
{ECO:0000255}.
/FTId=PRO_0000000138.
CHAIN 740 770 C31. {ECO:0000255}.
/FTId=PRO_0000000139.
TOPO_DOM 18 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 723 Helical. {ECO:0000255}.
TOPO_DOM 724 770 Cytoplasmic. {ECO:0000255}.
DOMAIN 291 341 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 96 110 Heparin-binding. {ECO:0000250}.
REGION 181 188 Zinc-binding. {ECO:0000250}.
REGION 391 423 Heparin-binding. {ECO:0000250}.
REGION 491 522 Heparin-binding. {ECO:0000250}.
REGION 523 540 Collagen-binding. {ECO:0000250}.
REGION 732 751 Interaction with G(o)-alpha.
{ECO:0000250}.
MOTIF 724 734 Basolateral sorting signal.
{ECO:0000250}.
MOTIF 759 762 NPXY motif; contains endocytosis signal.
COMPBIAS 230 260 Asp/Glu-rich (acidic).
COMPBIAS 274 280 Poly-Thr.
METAL 147 147 Copper 1. {ECO:0000250}.
METAL 151 151 Copper 1. {ECO:0000250}.
METAL 168 168 Copper 1. {ECO:0000250}.
METAL 677 677 Copper or zinc 2. {ECO:0000250}.
METAL 681 681 Copper or zinc 2. {ECO:0000250}.
METAL 684 684 Copper or zinc 2. {ECO:0000250}.
METAL 685 685 Copper or zinc 2. {ECO:0000250}.
SITE 144 144 Required for Cu(2+) reduction.
{ECO:0000250}.
SITE 301 302 Reactive bond. {ECO:0000250}.
SITE 671 672 Cleavage; by beta-secretase.
{ECO:0000250}.
SITE 672 673 Cleavage; by caspase-6. {ECO:0000250}.
SITE 687 688 Cleavage; by alpha-secretase.
{ECO:0000250|UniProtKB:P08592}.
SITE 690 691 Cleavage; by theta-secretase.
{ECO:0000250|UniProtKB:P08592}.
SITE 704 704 Implicated in free radical propagation.
{ECO:0000250}.
SITE 711 712 Cleavage; by gamma-secretase; site 1.
{ECO:0000250|UniProtKB:P08592}.
SITE 713 714 Cleavage; by gamma-secretase; site 2.
{ECO:0000250}.
SITE 720 721 Cleavage; by gamma-secretase; site 3.
{ECO:0000250}.
SITE 739 740 Cleavage; by caspase-6, caspase-8 or
caspase-9. {ECO:0000250}.
MOD_RES 198 198 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 206 206 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 497 497 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 729 729 Phosphothreonine.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 730 730 Phosphoserine; by APP-kinase I.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10.
{ECO:0000250|UniProtKB:P05067}.
MOD_RES 757 757 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:P12023}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 62 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 73 117 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 98 105 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 133 187 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 144 174 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 158 186 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 291 341 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 300 324 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 316 337 {ECO:0000255|PROSITE-ProRule:PRU00031}.
CROSSLNK 763 763 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08592}.
SEQUENCE 770 AA; 86971 MW; 08EBAAFE7E4930A9 CRC64;
MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK
TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG
EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE
EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC
RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQSLL KTTQEPLARD
PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA
KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL
QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER
MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET
KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN
IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN


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