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Amyloid-beta A4 precursor protein-binding family B member 1 (Protein Fe65)

 APBB1_HUMAN             Reviewed;         710 AA.
O00213; A1E379; A6NH82; A6NL69; B7Z1J5; B7Z1J6; B7Z2Y0; D3DQT2;
Q7Z324; Q96A93; V9GYK0; V9GYT4;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 2.
18-JUL-2018, entry version 173.
RecName: Full=Amyloid-beta A4 precursor protein-binding family B member 1;
AltName: Full=Protein Fe65;
Name=APBB1; Synonyms=FE65, RIR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8894693; DOI=10.1093/hmg/5.10.1589;
Bressler S.L., Gray M.D., Sopher B.L., Hu Q., Hearn M.G., Pham D.G.,
Dinulos M.B., Fukuchi K., Sisodia S.S., Miller M.A., Disteche C.M.,
Martin G.M.;
"cDNA cloning and chromosome mapping of the human Fe65 gene:
interaction of the conserved cytoplasmic domains of the human beta-
amyloid precursor protein and its homologues with the mouse Fe65
protein.";
Hum. Mol. Genet. 5:1589-1598(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9799084; DOI=10.1007/s004390050820;
Hu Q., Kukull W.A., Bressler S.L., Gray M.D., Cam J.A., Larson E.B.,
Martin G.M., Deeb S.S.;
"The human FE65 gene: genomic structure and an intronic biallelic
polymorphism associated with sporadic dementia of the Alzheimer
type.";
Hum. Genet. 103:295-303(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=21824145; DOI=10.1111/j.1471-4159.2011.07420.x;
Domingues S.C., Henriques A.G., Fardilha M., da Cruz E Silva E.F.,
da Cruz E Silva O.A.;
"Identification and characterization of a neuronal enriched novel
transcript encoding the previously described p60Fe65 isoform.";
J. Neurochem. 119:1086-1098(2011).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6).
TISSUE=Caudate nucleus, and Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, INTERACTION WITH ABL1, SUBCELLULAR LOCATION, PHOSPHORYLATION
AT TYR-547 BY ABL1, AND MUTAGENESIS OF TYR-117; TYR-234; TYR-269;
TYR-270; TYR-403; TYR-467; 269-TYR--TRP-271; TYR-546 AND TYR-547.
PubMed=15031292; DOI=10.1074/jbc.M311479200;
Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L.,
Ward M., McLoughlin D.M., Miller C.C.;
"The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to
stimulate Fe65/amyloid precursor protein nuclear signaling.";
J. Biol. Chem. 279:22084-22091(2004).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH NEK6.
PubMed=17512906; DOI=10.1016/j.bbrc.2007.04.203;
Lee E.J., Hyun S.H., Chun J., Kang S.S.;
"Human NIMA-related kinase 6 is one of the Fe65 WW domain binding
proteins.";
Biochem. Biophys. Res. Commun. 358:783-788(2007).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH APP.
PubMed=18468999; DOI=10.1074/jbc.M801827200;
Nakaya T., Kawai T., Suzuki T.;
"Regulation of FE65 nuclear translocation and function by amyloid
beta-protein precursor in osmotically stressed cells.";
J. Biol. Chem. 283:19119-19131(2008).
[12]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-547,
INTERACTION WITH RASD1, AND MUTAGENESIS OF TYR-547.
PubMed=18922798; DOI=10.1074/jbc.M801874200;
Lau K.-F., Chan W.-M., Perkinton M.S., Tudor E.L., Chang R.C.C.,
Chan H.-Y., McLoughlin D.M., Miller C.C.J.;
"Dexras1 interacts with FE65 to regulate FE65-amyloid precursor
protein-dependent transcription.";
J. Biol. Chem. 283:34728-34737(2008).
[13]
FUNCTION, AND INTERACTION WITH H2AX AND MAPK8.
PubMed=19234442; DOI=10.1038/nature07849;
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.;
"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival
decisions.";
Nature 458:591-596(2009).
[14]
FUNCTION, INTERACTION WITH SET AND TSHZ3, IDENTIFICATION IN A TRIMERIC
COMPLEX WITH HDAC1 AND TSHZ3, CHROMATIN-BINDING, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=19343227; DOI=10.1371/journal.pone.0005071;
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
"FE65 binds Teashirt, inhibiting expression of the primate-specific
caspase-4.";
PLoS ONE 4:E5071-E5071(2009).
[15]
INTERACTION WITH RNF157, UBIQUITINATION BY RNF157, AND FUNCTION.
PubMed=25342469; DOI=10.1038/cdd.2014.163;
Matz A., Lee S.J., Schwedhelm-Domeyer N., Zanini D., Holubowska A.,
Kannan M., Farnworth M., Jahn O., Goepfert M.C., Stegmueller J.;
"Regulation of neuronal survival and morphology by the E3 ubiquitin
ligase RNF157.";
Cell Death Differ. 22:626-642(2015).
[16]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 253-289 IN COMPLEX WITH
ENAH.
PubMed=17686488; DOI=10.1016/j.jmb.2007.06.064;
Meiyappan M., Birrane G., Ladias J.A.A.;
"Structural basis for polyproline recognition by the FE65 WW domain.";
J. Mol. Biol. 372:970-980(2007).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 534-667 IN COMPLEX WITH APP.
PubMed=18833287; DOI=10.1038/embor.2008.188;
Radzimanowski J., Simon B., Sattler M., Beyreuther K., Sinning I.,
Wild K.;
"Structure of the intracellular domain of the amyloid precursor
protein in complex with Fe65-PTB2.";
EMBO Rep. 9:1134-1140(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 366-505.
PubMed=18550529; DOI=10.1074/jbc.M800861200;
Radzimanowski J., Ravaud S., Schlesinger S., Koch J., Beyreuther K.,
Sinning I., Wild K.;
"Crystal structure of the human Fe65-PTB1 domain.";
J. Biol. Chem. 283:23113-23120(2008).
-!- FUNCTION: Transcription coregulator that can have both coactivator
and corepressor functions. Adapter protein that forms a
transcriptionally active complex with the gamma-secretase-derived
amyloid precursor protein (APP) intracellular domain. Plays a
central role in the response to DNA damage by translocating to the
nucleus and inducing apoptosis. May act by specifically
recognizing and binding histone H2AX phosphorylated on 'Tyr-142'
(H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-
apoptosis factors such as MAPK8/JNK1. Required for histone H4
acetylation at double-strand breaks (DSBs). Its ability to
specifically bind modified histones and chromatin modifying
enzymes such as KAT5/TIP60, probably explains its transcription
activation activity. Function in association with TSHZ3, SET and
HDAC factors as a transcriptional repressor, that inhibits the
expression of CASP4. Associates with chromatin in a region
surrounding the CASP4 transcriptional start site(s).
{ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999,
ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19234442,
ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:25342469}.
-!- SUBUNIT: Component of a complex, at least composed of APBB1,
RASD1/DEXRAS1 and APP. Interacts (via PID domain 2) with APP (with
the intracellular domain of the amyloid-beta precursor protein).
Interacts (via PID domain 2) with RASD1/DEXRAS1; impairs the
transcription activation activity. Interacts (via PID domain 1)
with KAT5/TIP60. Interacts (via the WW domain) with the proline-
rich region of APBB1IP. Interacts with TSHZ1 and TSHZ2 (By
similarity). Interacts (via the WW domain) with histone H2AX (when
phosphorylated on 'Tyr-142') and the proline-rich region of ENAH.
Interacts with MAPK8. Interacts (via PID domain 1) with TSHZ3 (via
homeobox domain). Interacts with SET. Found in a trimeric complex
with HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is
mediated by TSHZ3. Interacts (via WWW domain) with NEK6. Interacts
(via WWW domain) with ABL1. Interacts with RNF157
(PubMed:25342469). {ECO:0000250, ECO:0000269|PubMed:15031292,
ECO:0000269|PubMed:17512906, ECO:0000269|PubMed:17686488,
ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18833287,
ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19234442,
ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:25342469}.
-!- INTERACTION:
P05067:APP; NbExp=5; IntAct=EBI-81694, EBI-77613;
P05067-4:APP; NbExp=2; IntAct=EBI-81694, EBI-302641;
P00533:EGFR; NbExp=4; IntAct=EBI-81694, EBI-297353;
P04626:ERBB2; NbExp=2; IntAct=EBI-81694, EBI-641062;
Q07954:LRP1; NbExp=3; IntAct=EBI-81694, EBI-1046087;
-!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus. Cell
projection, growth cone {ECO:0000250}. Nucleus speckle.
Note=Colocalizes with TSHZ3 in axonal growth cone (By similarity).
In normal conditions, it mainly localizes to the cytoplasm, while
a small fraction is tethered to the cell membrane via its
interaction with APP. Following exposure to DNA damaging agents,
it is released from cell membrane and translocates to the nucleus.
Nuclear translocation is under the regulation of APP. Colocalizes
with TSHZ3 in the nucleus. Colocalizes with NEK6 at the nuclear
speckles. Phosphorylation at Ser-610 by SGK1 promotes its
localization to the nucleus (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=O00213-1; Sequence=Displayed;
Name=2;
IsoId=O00213-2; Sequence=VSP_011658;
Name=3;
IsoId=O00213-3; Sequence=VSP_045326, VSP_045327, VSP_011658;
Name=4; Synonyms=p60Fe65;
IsoId=O00213-4; Sequence=VSP_047459;
Note=Expressed preferentially in the brain.;
Name=5;
IsoId=O00213-5; Sequence=VSP_045326, VSP_045327;
Note=No experimental confirmation available.;
Name=6;
IsoId=O00213-6; Sequence=VSP_054709;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain; strongly reduced in
post-mortem elderly subjects with Alzheimer disease.
{ECO:0000269|PubMed:19343227}.
-!- PTM: Polyubiquitination by RNF157 leads to degradation by the
proteasome (PubMed:25342469). {ECO:0000269|PubMed:25342469}.
-!- PTM: Phosphorylation at Ser-610 by SGK1 promotes its localization
to the nucleus (By similarity). Phosphorylated following nuclear
translocation. Phosphorylation at Tyr-547 by ABL1 enhances
transcriptional activation activity and reduces the affinity for
RASD1/DEXRAS1. {ECO:0000250, ECO:0000269|PubMed:15031292,
ECO:0000269|PubMed:18922798}.
-!- SEQUENCE CAUTION:
Sequence=CAD98057.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L77864; AAB93631.1; -; mRNA.
EMBL; AF029234; AAC79942.1; -; Genomic_DNA.
EMBL; AF047835; AAC79942.1; JOINED; Genomic_DNA.
EMBL; EF103274; ABL07489.3; -; mRNA.
EMBL; AK293550; BAH11531.1; -; mRNA.
EMBL; AK293554; BAH11532.1; -; mRNA.
EMBL; AK293643; BAH11554.1; -; mRNA.
EMBL; AK295241; BAH12016.1; -; mRNA.
EMBL; BX538185; CAD98057.1; ALT_INIT; mRNA.
EMBL; AC068733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68723.1; -; Genomic_DNA.
EMBL; CH471064; EAW68724.1; -; Genomic_DNA.
EMBL; BC010854; AAH10854.1; -; mRNA.
CCDS; CCDS31410.1; -. [O00213-2]
CCDS; CCDS58114.1; -. [O00213-3]
CCDS; CCDS66015.1; -. [O00213-4]
CCDS; CCDS66016.1; -. [O00213-6]
CCDS; CCDS66017.1; -. [O00213-5]
CCDS; CCDS66018.1; -. [O00213-1]
RefSeq; NP_001155.1; NM_001164.4. [O00213-1]
RefSeq; NP_001244248.1; NM_001257319.2. [O00213-5]
RefSeq; NP_001244249.1; NM_001257320.2. [O00213-4]
RefSeq; NP_001244250.1; NM_001257321.2. [O00213-4]
RefSeq; NP_001244252.1; NM_001257323.2. [O00213-3]
RefSeq; NP_001244254.1; NM_001257325.2. [O00213-6]
RefSeq; NP_001244255.1; NM_001257326.2. [O00213-4]
RefSeq; NP_663722.1; NM_145689.2. [O00213-2]
RefSeq; XP_011518342.1; XM_011520040.2. [O00213-4]
RefSeq; XP_016873130.1; XM_017017641.1. [O00213-2]
UniGene; Hs.372840; -.
PDB; 2E45; NMR; -; A=241-290.
PDB; 2HO2; X-ray; 1.33 A; A=253-289.
PDB; 2IDH; X-ray; 2.28 A; A/B/C/D/E/F/G/H=253-289.
PDB; 2OEI; X-ray; 1.35 A; A=253-289.
PDB; 3D8D; X-ray; 2.20 A; A/B=366-505.
PDB; 3D8E; X-ray; 2.80 A; A/B/C/D=366-505.
PDB; 3D8F; X-ray; 2.70 A; A/B/C/D=366-505.
PDB; 3DXC; X-ray; 2.10 A; A/C=534-667.
PDB; 3DXD; X-ray; 2.20 A; A/C=534-667.
PDB; 3DXE; X-ray; 2.00 A; A/C=534-667.
PDB; 5NQH; X-ray; 2.60 A; A/B/C/D=534-667.
PDBsum; 2E45; -.
PDBsum; 2HO2; -.
PDBsum; 2IDH; -.
PDBsum; 2OEI; -.
PDBsum; 3D8D; -.
PDBsum; 3D8E; -.
PDBsum; 3D8F; -.
PDBsum; 3DXC; -.
PDBsum; 3DXD; -.
PDBsum; 3DXE; -.
PDBsum; 5NQH; -.
ProteinModelPortal; O00213; -.
SMR; O00213; -.
BioGrid; 106819; 99.
CORUM; O00213; -.
DIP; DIP-30903N; -.
ELM; O00213; -.
IntAct; O00213; 17.
MINT; O00213; -.
STRING; 9606.ENSP00000299402; -.
iPTMnet; O00213; -.
PhosphoSitePlus; O00213; -.
EPD; O00213; -.
MaxQB; O00213; -.
PaxDb; O00213; -.
PeptideAtlas; O00213; -.
PRIDE; O00213; -.
ProteomicsDB; 47783; -.
ProteomicsDB; 47784; -. [O00213-2]
DNASU; 322; -.
Ensembl; ENST00000299402; ENSP00000299402; ENSG00000166313. [O00213-2]
Ensembl; ENST00000311051; ENSP00000311912; ENSG00000166313. [O00213-2]
Ensembl; ENST00000530885; ENSP00000433338; ENSG00000166313. [O00213-3]
Ensembl; ENST00000608394; ENSP00000476442; ENSG00000166313. [O00213-4]
Ensembl; ENST00000608645; ENSP00000476646; ENSG00000166313. [O00213-4]
Ensembl; ENST00000608655; ENSP00000476846; ENSG00000166313. [O00213-5]
Ensembl; ENST00000608704; ENSP00000476871; ENSG00000166313. [O00213-4]
Ensembl; ENST00000609331; ENSP00000477069; ENSG00000166313. [O00213-6]
Ensembl; ENST00000609360; ENSP00000477213; ENSG00000166313. [O00213-1]
GeneID; 322; -.
KEGG; hsa:322; -.
UCSC; uc001mdb.4; human. [O00213-1]
CTD; 322; -.
DisGeNET; 322; -.
EuPathDB; HostDB:ENSG00000166313.18; -.
GeneCards; APBB1; -.
H-InvDB; HIX0009398; -.
HGNC; HGNC:581; APBB1.
HPA; CAB022104; -.
HPA; HPA038521; -.
HPA; HPA038522; -.
MIM; 602709; gene.
neXtProt; NX_O00213; -.
OpenTargets; ENSG00000166313; -.
PharmGKB; PA24873; -.
eggNOG; ENOG410IEKA; Eukaryota.
eggNOG; ENOG410YEVS; LUCA.
GeneTree; ENSGT00390000000002; -.
HOGENOM; HOG000033983; -.
HOVERGEN; HBG050524; -.
InParanoid; O00213; -.
KO; K04529; -.
PhylomeDB; O00213; -.
TreeFam; TF314331; -.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
SignaLink; O00213; -.
SIGNOR; O00213; -.
ChiTaRS; APBB1; human.
EvolutionaryTrace; O00213; -.
GeneWiki; APBB1; -.
GenomeRNAi; 322; -.
PRO; PR:O00213; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166313; -.
CleanEx; HS_APBB1; -.
ExpressionAtlas; O00213; baseline and differential.
Genevisible; O00213; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:1990812; C:growth cone filopodium; IEA:Ensembl.
GO; GO:1990761; C:growth cone lamellipodium; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0044304; C:main axon; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0050760; P:negative regulation of thymidylate synthase biosynthetic process; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:ARUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00201; WW; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00640; PID; 2.
Pfam; PF00397; WW; 1.
SMART; SM00462; PTB; 2.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS01179; PID; 2.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Apoptosis;
Cell membrane; Cell projection; Chromatin regulator;
Complete proteome; Cytoplasm; DNA damage; Membrane; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 710 Amyloid-beta A4 precursor protein-binding
family B member 1.
/FTId=PRO_0000076049.
DOMAIN 253 285 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 370 509 PID 1. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 542 699 PID 2. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
COMPBIAS 158 171 Glu-rich.
MOD_RES 517 517 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXJ1}.
MOD_RES 547 547 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:15031292,
ECO:0000269|PubMed:18922798}.
MOD_RES 610 610 Phosphoserine; by SGK1.
{ECO:0000250|UniProtKB:P46933}.
VAR_SEQ 1 259 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:21824145}.
/FTId=VSP_047459.
VAR_SEQ 1 240 MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQ
ATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAAT
AHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELS
AHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDD
DDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKS
ASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDT -> MT
QMR (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054709.
VAR_SEQ 1 213 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_045326.
VAR_SEQ 214 240 NSAASDEDSSWATLSQGSPSYGSPEDT -> MSAMFSQDFF
LAIILQDSSA (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_045327.
VAR_SEQ 462 463 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011658.
VARIANT 327 327 M -> V (in dbSNP:rs1800423).
/FTId=VAR_014444.
VARIANT 396 396 N -> S (in dbSNP:rs1800425).
/FTId=VAR_014445.
MUTAGEN 117 117 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 234 234 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 269 271 YYW->AAA: Impairs transcriptional
activation and inhibits binding to ABL1.
{ECO:0000269|PubMed:15031292}.
MUTAGEN 269 269 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 270 270 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 403 403 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 467 467 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 546 546 Y->F: No effect on phosphorylation by
ABL1. {ECO:0000269|PubMed:15031292}.
MUTAGEN 547 547 Y->F: Abrogates phosphorylation and
stimulation of transcription by ABL1, and
increases the interaction with
RASD1/DEXRAS1.
{ECO:0000269|PubMed:15031292,
ECO:0000269|PubMed:18922798}.
MUTAGEN 658 658 Y->F: No effect on phosphorylation by
ABL1.
CONFLICT 367 367 I -> T (in Ref. 4; BAH11532).
{ECO:0000305}.
CONFLICT 493 493 T -> A (in Ref. 4; BAH11532).
{ECO:0000305}.
STRAND 259 263 {ECO:0000244|PDB:2HO2}.
STRAND 268 272 {ECO:0000244|PDB:2HO2}.
TURN 273 275 {ECO:0000244|PDB:2HO2}.
STRAND 278 281 {ECO:0000244|PDB:2HO2}.
STRAND 368 379 {ECO:0000244|PDB:3D8D}.
HELIX 382 385 {ECO:0000244|PDB:3D8D}.
TURN 387 389 {ECO:0000244|PDB:3D8D}.
HELIX 390 401 {ECO:0000244|PDB:3D8D}.
STRAND 421 427 {ECO:0000244|PDB:3D8D}.
STRAND 430 434 {ECO:0000244|PDB:3D8D}.
TURN 436 438 {ECO:0000244|PDB:3D8D}.
STRAND 441 446 {ECO:0000244|PDB:3D8D}.
HELIX 447 449 {ECO:0000244|PDB:3D8D}.
STRAND 452 455 {ECO:0000244|PDB:3D8D}.
STRAND 458 460 {ECO:0000244|PDB:3D8F}.
STRAND 464 470 {ECO:0000244|PDB:3D8D}.
TURN 472 474 {ECO:0000244|PDB:3D8D}.
STRAND 477 486 {ECO:0000244|PDB:3D8D}.
HELIX 488 504 {ECO:0000244|PDB:3D8D}.
STRAND 544 554 {ECO:0000244|PDB:3DXE}.
HELIX 559 571 {ECO:0000244|PDB:3DXE}.
HELIX 575 577 {ECO:0000244|PDB:3DXE}.
STRAND 579 585 {ECO:0000244|PDB:3DXE}.
STRAND 587 594 {ECO:0000244|PDB:3DXE}.
TURN 595 597 {ECO:0000244|PDB:3DXE}.
STRAND 600 605 {ECO:0000244|PDB:3DXE}.
HELIX 606 608 {ECO:0000244|PDB:3DXE}.
STRAND 609 614 {ECO:0000244|PDB:3DXE}.
STRAND 620 628 {ECO:0000244|PDB:3DXE}.
STRAND 631 641 {ECO:0000244|PDB:3DXE}.
HELIX 644 665 {ECO:0000244|PDB:3DXE}.
SEQUENCE 710 AA; 77244 MW; FD4A2EF7E8D8E884 CRC64;
MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL RSAMGEGGGP
EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEPEMAPLGP KGLIHLYSEL
ELSAHNAANR GLRGPGLIIS TQEQGPDEGE EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP
EPLESVEAPP RPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT
DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL
TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP LPQEEEKLPP
RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMSGGWGEGK
DLLLQLEDET LKLVEPQSQA LLHAQPIISI RVWGVGRDSG RERDFAYVAR DKLTQMLKCH
VFRCEAPAKN IATSLHEICS KIMAERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV
QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV
LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK
CLDARSQAST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGAHTP


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