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 A4_CAVPO                Reviewed;         770 AA.
Q60495; Q60496;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 2.
22-NOV-2017, entry version 141.
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;
AltName: Full=Beta-secretase C-terminal fragment;
Short=Beta-CTF;
AltName: Full=CTF-beta;
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;
AltName: Full=Alpha-secretase C-terminal fragment;
Short=Alpha-CTF;
AltName: Full=CTF-alpha;
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=Amyloid intracellular domain 50;
Short=AICD-50;
Short=AID(50);
AltName: Full=Gamma-CTF(50);
Contains:
RecName: Full=C31;
Flags: Precursor;
Name=APP;
Cavia porcellus (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10141;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain, and Liver;
PubMed=9116031; DOI=10.1016/S0167-4781(96)00232-1;
Beck M., Mueller D., Bigl V.;
"Amyloid precursor protein in Guinea pigs -- complete cDNA sequence
and alternative splicing.";
Biochim. Biophys. Acta 1351:17-21(1997).
[2]
INTERACTION OF APP40-BETA WITH APOE.
PubMed=9349544;
Martel C.L., Mackic J.B., Matsubara E., Governale S., Miguel C.,
Miao W., McComb J.G., Frangione B., Ghiso J., Zlokovic B.V.;
"Isoform-specific effects of apolipoproteins E2, E3, and E4 on
cerebral capillary sequestration and blood-brain barrier transport of
circulating Alzheimer's amyloid beta.";
J. Neurochem. 69:1995-2004(1997).
[3]
PROTEOLYTIC PROCESSING.
PubMed=10619481; DOI=10.1016/S0306-4522(99)00390-5;
Beck M., Brueckner M.K., Holzer M., Kaap S., Pannicke T., Arendt T.,
Bigl V.;
"Guinea-pig primary cell cultures provide a model to study expression
and amyloidogenic processing of endogenous amyloid precursor
protein.";
Neuroscience 95:243-254(2000).
[4]
PROTEOLYTIC PROCESSING BY GAMMA-SECRETASE.
PubMed=11035007; DOI=10.1074/jbc.M005968200;
Pinnix I., Musunuru U., Tun H., Sridharan A., Golde T., Eckman C.,
Ziani-Cherif C., Onstead L., Sambamurti K.;
"A novel gamma-secretase assay based on detection of the putative C-
terminal fragment-gamma of amyloid beta protein precursor.";
J. Biol. Chem. 276:481-487(2001).
-!- 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 (By similarity). 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 (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. Amyloid-beta peptides bind to lipoproteins
and apolipoproteins E and J in the CSF and to HDL particles in
plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Also
bind GPC1 in lipid rafts (By similarity). {ECO:0000250}.
-!- FUNCTION: Appicans elicit adhesion of neural cells to the
extracellular matrix and may regulate neurite outgrowth in the
brain. {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, SHC1, NUMB and DAB1. CTF-alpha product of APP
interacts with GSAP (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), APPBP2 (via BaSS) and DDB1 (By similarity). Associates
with microtubules in the presence of ATP and in a kinesin-
dependent manner (By similarity). Soluble amyloid-beta protein 40
binds all three isoforms of APOE, in vitro and in vivo. When
lipidated, ApoE3 appears to be the preferred amyloid binding
isoform, while the apoE4 isoform-amyloid-beta protein 40 complex
is capable of being transported across the blood-brain barrier.
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). 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 (By similarity). During
maturation, the immature APP (N-glycosylated in the endoplasmic
reticulum) moves to the Golgi complex where complete maturation
occurs (O-glycosylated and sulfated) (By similarity). After alpha-
secretase cleavage, soluble APP is released into the extracellular
space and the C-terminal is internalized to endosomes and lysomes
Some APP accumulates in secretory transport vesicles leaving the
late Golgi compartment and returns to the cell surface. APP sorts
to the basolateral surface in epithelial cells. Associates with
GPC1 in perinuclear compartments (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms, missing exons 7,8 and 15, seem to
exist. The L-isoforms, missing exon 15, are referred to as
appicans.;
Name=APP770;
IsoId=Q60495-1; Sequence=Displayed;
Name=APP695;
IsoId=Q60495-2; Sequence=VSP_007221, VSP_007222;
-!- TISSUE SPECIFICITY: Isoform APP695 is the major isoform found in
brain. The longer isoforms containing the BPTI domain are
predominantly expressed in peripheral organs such as muscle and
liver.
-!- INDUCTION: Increased levels during neuronal differentiation.
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for
sorting of membrane proteins to the basolateral surface of
epithelial cells.
-!- 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 (By similarity). The NPXY site is also involved in
clathrin-mediated endocytosis. {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 caspase-3 during neuronal
apoptosis. {ECO:0000250}.
-!- PTM: N- and O-glycosylated. O-linkage of chondroitin sulfate to
the L-APP isoforms produces the APP proteoglycan core proteins,
the appicans (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
serine residues is neuron-specific (By similarity).
Phosphorylation can affect APP processing, neuronal
differentiation and interaction with other proteins. {ECO:0000250,
ECO:0000269|PubMed:10619481, ECO:0000269|PubMed:11035007}.
-!- PTM: Extracellular binding and reduction of copper, results in a
corresponding oxidation of Cys-144 and Cys-158, and the formation
of a disulfide bond. {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.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X97631; CAA66230.1; -; mRNA.
EMBL; X99198; CAA67589.1; -; mRNA.
ProteinModelPortal; Q60495; -.
SMR; Q60495; -.
STRING; 10141.ENSCPOP00000001291; -.
MEROPS; I02.015; -.
eggNOG; KOG3540; Eukaryota.
eggNOG; ENOG410ZTKC; LUCA.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; Q60495; -.
Proteomes; UP000005447; Unassembled WGS sequence.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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: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: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:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
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:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
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; IPR036669; Amyloid_Cu-bd_sf.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
InterPro; IPR037071; Amyloid_glyco_Abeta_sf.
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; IPR036454; Amyloid_glyco_heparin-bd_sf.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR036176; E2_sf.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103; PTHR23103; 1.
PANTHER; PTHR23103:SF7; PTHR23103:SF7; 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.
1: Evidence at protein level;
Alternative splicing; 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|UniProtKB:P05067}.
CHAIN 18 770 Amyloid-beta A4 protein.
/FTId=PRO_0000000076.
CHAIN 18 687 Soluble APP-alpha. {ECO:0000250}.
/FTId=PRO_0000000077.
CHAIN 18 671 Soluble APP-beta. {ECO:0000250}.
/FTId=PRO_0000000078.
CHAIN 18 286 N-APP. {ECO:0000250}.
/FTId=PRO_0000381965.
CHAIN 672 770 C99. {ECO:0000250}.
/FTId=PRO_0000000079.
CHAIN 672 713 Amyloid-beta protein 42. {ECO:0000250}.
/FTId=PRO_0000000080.
CHAIN 672 711 Amyloid-beta protein 40. {ECO:0000250}.
/FTId=PRO_0000000081.
CHAIN 688 770 C83. {ECO:0000250}.
/FTId=PRO_0000000082.
PEPTIDE 688 713 P3(42). {ECO:0000250}.
/FTId=PRO_0000000083.
PEPTIDE 688 711 P3(40). {ECO:0000250}.
/FTId=PRO_0000000084.
CHAIN 691 770 C80.
/FTId=PRO_0000384573.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
{ECO:0000250}.
/FTId=PRO_0000000085.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
{ECO:0000250}.
/FTId=PRO_0000000086.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
{ECO:0000250}.
/FTId=PRO_0000442140.
CHAIN 740 770 C31. {ECO:0000250}.
/FTId=PRO_0000000087.
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 135 155 Copper-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.
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 713 714 Cleavage; by gamma-secretase.
{ECO:0000250}.
SITE 739 740 Cleavage; by caspase-3. {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}.
CARBOHYD 656 656 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000250}.
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}.
VAR_SEQ 289 289 E -> V (in isoform APP695).
{ECO:0000305}.
/FTId=VSP_007221.
VAR_SEQ 290 364 Missing (in isoform APP695).
{ECO:0000305}.
/FTId=VSP_007222.
SEQUENCE 770 AA; 86883 MW; 0AFD36C90F0D8B6C CRC64;
MLPSLALLLL TTWTARALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWEPDPSGTK
TCIGSKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR SRKQCKTHPH FVIPYRCLVG
EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDNIDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVADVEEE
EADDDEDVED GDEVEEEAEE PYEEATEKTT SIATTTTTTT ESVEEVVREV CSEQAETGPC
RSMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSVMSQNLL KTSGEPVSQG
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 WHPFGVDSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN
IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN


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52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur