GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)

 DP13A_HUMAN             Reviewed;         709 AA.
Q9UKG1; Q9P2B9;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
13-FEB-2019, entry version 161.
RecName: Full=DCC-interacting protein 13-alpha {ECO:0000305};
Short=Dip13-alpha {ECO:0000303|PubMed:12011067};
AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 1 {ECO:0000305};
Name=APPL1 {ECO:0000312|HGNC:HGNC:24035};
Synonyms=APPL {ECO:0000312|EMBL:AAH28599.1}, DIP13A,
KIAA1428 {ECO:0000312|EMBL:BAA92666.2};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF04012.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INTERACTION WITH AKT2 AND PIK3CA.
PubMed=10490823; DOI=10.1038/sj.onc.1203080;
Mitsuuchi Y., Johnson S.W., Sonoda G., Tanno S., Golemis E.A.,
Testa J.R.;
"Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an
adaptor molecule that interacts with the oncoprotein-serine/threonine
kinase AKT2.";
Oncogene 18:4891-4898(1999).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL17835.1}
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH DCC.
PubMed=12011067; DOI=10.1074/jbc.M204679200;
Liu J., Yao F., Wu R., Morgan M., Thorburn A., Finley R.L. Jr.,
Chen Y.Q.;
"Mediation of the DCC apoptotic signal by DIP13 alpha.";
J. Biol. Chem. 277:26281-26285(2002).
[3] {ECO:0000312|EMBL:BAA92666.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:BAA92666.2};
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5] {ECO:0000312|EMBL:AAH28599.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis {ECO:0000312|EMBL:AAH28599.1};
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).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND NURD/MECP1
COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15016378; DOI=10.1016/S0092-8674(04)00117-5;
Miaczynska M., Christoforidis S., Giner A., Shevchenko A.,
Uttenweiler-Joseph S., Habermann B., Wilm M., Parton R.G., Zerial M.;
"APPL proteins link Rab5 to nuclear signal transduction via an
endosomal compartment.";
Cell 116:445-456(2004).
[7]
INTERACTION WITH OCRL, F&H MOTIF, PHOSPHORYLATION AT SER-410, AND
MUTAGENESIS OF SER-410.
PubMed=17765681; DOI=10.1016/j.devcel.2007.08.004;
Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S.,
Modregger J., Biemesderfer D., Toomre D., De Camilli P.;
"A role of the Lowe syndrome protein OCRL in early steps of the
endocytic pathway.";
Dev. Cell 13:377-390(2007).
[8]
INTERACTION WITH APPL2.
PubMed=17030088; DOI=10.1016/j.mce.2006.08.014;
Nechamen C.A., Thomas R.M., Dias J.A.;
"APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential
signaling complex.";
Mol. Cell. Endocrinol. 260:93-99(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
SUBUNIT, INTERACTION WITH APPL2, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=18034774; DOI=10.1111/j.1600-0854.2007.00680.x;
Chial H.J., Wu R., Ustach C.V., McPhail L.C., Mobley W.C., Chen Y.Q.;
"Membrane targeting by APPL1 and APPL2: dynamic scaffolds that
oligomerize and bind phosphoinositides.";
Traffic 9:215-229(2008).
[12]
FUNCTION, AND INTERACTION WITH APPL2.
PubMed=19661063; DOI=10.1074/jbc.M109.010355;
Wang C., Xin X., Xiang R., Ramos F.J., Liu M., Lee H.J., Chen H.,
Mao X., Kikani C.K., Liu F., Dong L.Q.;
"Yin-Yang regulation of adiponectin signaling by APPL isoforms in
muscle cells.";
J. Biol. Chem. 284:31608-31615(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
INTERACTION WITH RUVBL2; CTNNB1; APPL2; HDAC1 AND HDAC2, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=19433865; DOI=10.1074/jbc.M109.007237;
Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B.,
Miaczynska M.;
"Endosomal adaptor proteins APPL1 and APPL2 are novel activators of
beta-catenin/TCF-mediated transcription.";
J. Biol. Chem. 284:18115-18128(2009).
[15]
INTERACTION WITH OCRL, AND SUBCELLULAR LOCATION.
PubMed=20133602; DOI=10.1073/pnas.0914658107;
Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
"Two closely related endocytic proteins that share a common OCRL-
binding motif with APPL1.";
Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INTERACTION WITH OCRL.
PubMed=21233288; DOI=10.1091/mbc.E10-08-0730;
Noakes C.J., Lee G., Lowe M.;
"The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling
in the endocytic pathway.";
Mol. Biol. Cell 22:606-623(2011).
[19]
INTERACTION WITH OCRL AND INPP5B, AND F&H MOTIF.
PubMed=21666675; DOI=10.1038/nsmb.2071;
Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.;
"Recognition of the F&H motif by the Lowe syndrome protein OCRL.";
Nat. Struct. Mol. Biol. 18:789-795(2011).
[20]
INTERACTION WITH ANXA2, AND SUBCELLULAR LOCATION.
PubMed=21645192; DOI=10.1111/j.1600-0854.2011.01226.x;
Urbanska A., Sadowski L., Kalaidzidis Y., Miaczynska M.;
"Biochemical characterization of APPL endosomes: the role of annexin
A2 in APPL membrane recruitment.";
Traffic 12:1227-1241(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
FUNCTION.
PubMed=24879834; DOI=10.2337/db14-0337;
Cheng K.K., Zhu W., Chen B., Wang Y., Wu D., Sweeney G., Wang B.,
Lam K.S., Xu A.;
"The adaptor protein APPL2 inhibits insulin-stimulated glucose uptake
by interacting with TBC1D1 in skeletal muscle.";
Diabetes 63:3748-3758(2014).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
FUNCTION, INVOLVEMENT IN MODY14, VARIANT MODY14 ASN-94, AND
CHARACTERIZATION OF VARIANT MODY14 ASN-94.
PubMed=26073777; DOI=10.1016/j.ajhg.2015.05.011;
Prudente S., Jungtrakoon P., Marucci A., Ludovico O.,
Buranasupkajorn P., Mazza T., Hastings T., Milano T., Morini E.,
Mercuri L., Bailetti D., Mendonca C., Alberico F., Basile G.,
Romani M., Miccinilli E., Pizzuti A., Carella M., Barbetti F.,
Pascarella S., Marchetti P., Trischitta V., Di Paola R., Doria A.;
"Loss-of-function mutations in APPL1 in familial diabetes mellitus.";
Am. J. Hum. Genet. 97:177-185(2015).
[26]
INTERACTION WITH TGFBR1 AND PRKCZ, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=26583432; DOI=10.18632/oncotarget.6346;
Song J., Mu Y., Li C., Bergh A., Miaczynska M., Heldin C.H.,
Landstroem M.;
"APPL proteins promote TGFbeta-induced nuclear transport of the
TGFbeta type I receptor intracellular domain.";
Oncotarget 7:279-292(2016).
[27]
VARIANT [LARGE SCALE ANALYSIS] GLN-643.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Multifunctional adapter protein that binds to various
membrane receptors, nuclear factors and signaling proteins to
regulate many processes, such as cell proliferation, immune
response, endosomal trafficking and cell metabolism
(PubMed:26583432, PubMed:15016378, PubMed:26073777,
PubMed:19661063, PubMed:10490823). Regulates signaling pathway
leading to cell proliferation through interaction with RAB5A and
subunits of the NuRD/MeCP1 complex (PubMed:15016378). Functions as
a positive regulator of innate immune response via activation of
AKT1 signaling pathway by forming a complex with APPL1 and PIK3R1
(By similarity). Inhibits Fc-gamma receptor-mediated phagocytosis
through PI3K/Akt signaling in macrophages (By similarity).
Regulates TLR4 signaling in activated macrophages (By similarity).
Involved in trafficking of the TGFBR1 from the endosomes to the
nucleus via microtubules in a TRAF6-dependent manner
(PubMed:26583432). Plays a role in cell metabolism by regulating
adiponecting and insulin signaling pathways (PubMed:26073777,
PubMed:19661063, PubMed:24879834). Required for fibroblast
migration through HGF cell signaling (By similarity). Positive
regulator of beta-catenin/TCF-dependent transcription through
direct interaction with RUVBL2/reptin resulting in the relief of
RUVBL2-mediated repression of beta-catenin/TCF target genes by
modulating the interactions within the beta-catenin-reptin-HDAC
complex (PubMed:19433865). {ECO:0000250|UniProtKB:Q8K3H0,
ECO:0000269|PubMed:10490823, ECO:0000269|PubMed:15016378,
ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19661063,
ECO:0000269|PubMed:24879834, ECO:0000269|PubMed:26073777,
ECO:0000269|PubMed:26583432}.
-!- SUBUNIT: Homodimer (PubMed:18034774). Binds RAB5A/Rab5 through an
N-terminal domain. This interaction is essential for its
recruitment to endosomal membranes as well as its role in cell
proliferation (PubMed:15016378). Binds DCC and the catalytic
domain of the inactive form of AKT2 through its PID domain
(PubMed:10490823, PubMed:12011067). Binds PIK3CA and subunits of
the NuRD/MeCP1 complex (PubMed:10490823, PubMed:15016378).
Interacts with OCRL and INPP5B (PubMed:21666675, PubMed:17765681,
PubMed:20133602, PubMed:21233288). Interacts with NTRK2 (By
similarity). Interacts with APPL2; interaction is independent of
follicle stimulating hormone stimulation; interaction is decreased
by adiponectin in a time-dependent manner (PubMed:17030088,
PubMed:18034774, PubMed:19661063). Forms a complex with APPL2 and
RUVBL2 (PubMed:19433865). Forms a complex comprising APPL2,
RUVBL2, CTNNB1, HDAC1 and HDAC2; interaction reduces interaction
between CTNNB1, HDAC1, HDAC2 and RUVBL2 leading to the decrease of
deacetylase activity of this complex; affects the recruitment of
repressive complexes to the Wnt target genes (PubMed:19433865).
Interacts with ANXA2 (PubMed:21645192). Interacts with TGFBR1;
interaction is TGF beta dependent; mediates trafficking of the
TGFBR1 from the endosomes to the nucleus via microtubules in a
TRAF6-dependent manner (PubMed:26583432). Interacts with PRKCZ
(PubMed:26583432). Interacts with PIK3R1 and APPL2 (By
similarity). Interacts with ADIPOR1; ADIPOQ enhances this
interaction; inhibites adiponectin-stimulated binding of APPL2 to
ADIPOR1 (By similarity). {ECO:0000250|UniProtKB:Q8K3H0,
ECO:0000269|PubMed:10490823, ECO:0000269|PubMed:12011067,
ECO:0000269|PubMed:15016378, ECO:0000269|PubMed:17030088,
ECO:0000269|PubMed:17765681, ECO:0000269|PubMed:18034774,
ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19661063,
ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21233288,
ECO:0000269|PubMed:21645192, ECO:0000269|PubMed:21666675,
ECO:0000269|PubMed:26583432}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-741243, EBI-741243;
P35609:ACTN2; NbExp=2; IntAct=EBI-741243, EBI-77797;
Q96A54:ADIPOR1; NbExp=6; IntAct=EBI-741243, EBI-1632076;
Q91VH1:Adipor1 (xeno); NbExp=3; IntAct=EBI-741243, EBI-992398;
Q86V24:ADIPOR2; NbExp=3; IntAct=EBI-741243, EBI-1769445;
P31749:AKT1; NbExp=2; IntAct=EBI-741243, EBI-296087;
Q8NEU8:APPL2; NbExp=9; IntAct=EBI-741243, EBI-741261;
Q03001:DST; NbExp=3; IntAct=EBI-741243, EBI-310758;
O75923:DYSF; NbExp=2; IntAct=EBI-741243, EBI-2799016;
P00533:EGFR; NbExp=2; IntAct=EBI-741243, EBI-297353;
O95363:FARS2; NbExp=5; IntAct=EBI-741243, EBI-2513774;
Q13547:HDAC1; NbExp=2; IntAct=EBI-741243, EBI-301834;
O15379:HDAC3; NbExp=2; IntAct=EBI-741243, EBI-607682;
P43362:MAGEA9B; NbExp=3; IntAct=EBI-741243, EBI-10209139;
P50221:MEOX1; NbExp=3; IntAct=EBI-741243, EBI-2864512;
Q9UL25:RAB21; NbExp=10; IntAct=EBI-741243, EBI-1056039;
P20339:RAB5A; NbExp=20; IntAct=EBI-741243, EBI-399437;
Q8TAI7:RHEBL1; NbExp=3; IntAct=EBI-741243, EBI-746555;
Q9Y3I0:RTCB; NbExp=3; IntAct=EBI-741243, EBI-2107208;
Q8WXH0:SYNE2; NbExp=3; IntAct=EBI-741243, EBI-2372294;
Q12933:TRAF2; NbExp=2; IntAct=EBI-741243, EBI-355744;
Q9C0C9:UBE2O; NbExp=5; IntAct=EBI-741243, EBI-2339946;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:15016378, ECO:0000269|PubMed:20133602,
ECO:0000269|PubMed:21645192}; Peripheral membrane protein
{ECO:0000269|PubMed:15016378}. Nucleus
{ECO:0000269|PubMed:15016378, ECO:0000269|PubMed:19433865,
ECO:0000269|PubMed:26583432}. Cytoplasm
{ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19661063}.
Endosome {ECO:0000269|PubMed:26583432}. Cell projection, ruffle
{ECO:0000250|UniProtKB:Q8K3H0}. Cytoplasmic vesicle, phagosome
{ECO:0000250|UniProtKB:Q8K3H0}. Note=Early endosomal membrane-
bound and nuclear. Translocated into the nucleus upon release from
endosomal membranes following internalization of EGF.
{ECO:0000269|PubMed:15016378}.
-!- TISSUE SPECIFICITY: High levels in heart, ovary, pancreas and
skeletal muscle. {ECO:0000269|PubMed:10490823}.
-!- DOMAIN: Overexpression of an N-terminal domain (residues 1-319) or
a C-terminal region (residues 273-709) has a proapoptotic effect.
{ECO:0000269|PubMed:15016378}.
-!- DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence
centered around Phe and His residues, is essential for binding to
OCRL and INPP5B. {ECO:0000269|PubMed:21666675}.
-!- PTM: Phosphorylation at Ser-410 by PKA severely impairs binding to
OCRL. {ECO:0000269|PubMed:17765681}.
-!- DISEASE: Maturity-onset diabetes of the young 14 (MODY14)
[MIM:616511]: A form of diabetes that is characterized by an
autosomal dominant mode of inheritance, onset in childhood or
early adulthood (usually before 25 years of age), a primary defect
in insulin secretion and frequent insulin-independence at the
beginning of the disease. {ECO:0000269|PubMed:26073777}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF169797; AAF04012.1; -; mRNA.
EMBL; AF424738; AAL17835.1; -; mRNA.
EMBL; AB037849; BAA92666.2; -; mRNA.
EMBL; BC028599; AAH28599.1; -; mRNA.
CCDS; CCDS2882.1; -.
RefSeq; NP_036228.1; NM_012096.2.
UniGene; Hs.476415; -.
PDB; 2EJ8; X-ray; 1.84 A; A/B=492-644.
PDB; 2ELA; X-ray; 2.00 A; A/B=493-646.
PDB; 2ELB; X-ray; 2.60 A; A=1-376.
PDB; 2Q12; X-ray; 1.79 A; A=5-265.
PDB; 2Q13; X-ray; 2.05 A; A=5-385.
PDB; 2Z0N; X-ray; 1.95 A; A=1-275.
PDB; 2Z0O; X-ray; 2.58 A; A=1-385.
PDB; 5C5B; X-ray; 2.90 A; A/C=5-375.
PDBsum; 2EJ8; -.
PDBsum; 2ELA; -.
PDBsum; 2ELB; -.
PDBsum; 2Q12; -.
PDBsum; 2Q13; -.
PDBsum; 2Z0N; -.
PDBsum; 2Z0O; -.
PDBsum; 5C5B; -.
ProteinModelPortal; Q9UKG1; -.
SMR; Q9UKG1; -.
BioGrid; 117522; 76.
CORUM; Q9UKG1; -.
DIP; DIP-29322N; -.
ELM; Q9UKG1; -.
IntAct; Q9UKG1; 88.
MINT; Q9UKG1; -.
STRING; 9606.ENSP00000288266; -.
MoonDB; Q9UKG1; Curated.
iPTMnet; Q9UKG1; -.
PhosphoSitePlus; Q9UKG1; -.
BioMuta; APPL1; -.
DMDM; 61213025; -.
EPD; Q9UKG1; -.
jPOST; Q9UKG1; -.
MaxQB; Q9UKG1; -.
PaxDb; Q9UKG1; -.
PeptideAtlas; Q9UKG1; -.
PRIDE; Q9UKG1; -.
ProteomicsDB; 84785; -.
Ensembl; ENST00000288266; ENSP00000288266; ENSG00000157500.
Ensembl; ENST00000650354; ENSP00000498115; ENSG00000157500.
GeneID; 26060; -.
KEGG; hsa:26060; -.
UCSC; uc003dio.4; human.
CTD; 26060; -.
DisGeNET; 26060; -.
EuPathDB; HostDB:ENSG00000157500.10; -.
GeneCards; APPL1; -.
GeneReviews; APPL1; -.
HGNC; HGNC:24035; APPL1.
HPA; HPA011138; -.
HPA; HPA073477; -.
MalaCards; APPL1; -.
MIM; 604299; gene.
MIM; 616511; phenotype.
neXtProt; NX_Q9UKG1; -.
OpenTargets; ENSG00000157500; -.
Orphanet; 552; MODY.
PharmGKB; PA162376755; -.
eggNOG; KOG0521; Eukaryota.
eggNOG; KOG3536; Eukaryota.
eggNOG; ENOG410ZWZQ; LUCA.
GeneTree; ENSGT00940000156624; -.
HOGENOM; HOG000285988; -.
HOVERGEN; HBG051394; -.
InParanoid; Q9UKG1; -.
KO; K08733; -.
OMA; SDVETMQ; -.
OrthoDB; 253010at2759; -.
PhylomeDB; Q9UKG1; -.
TreeFam; TF328669; -.
Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
SignaLink; Q9UKG1; -.
SIGNOR; Q9UKG1; -.
ChiTaRS; APPL1; human.
EvolutionaryTrace; Q9UKG1; -.
GeneWiki; APPL1; -.
GenomeRNAi; 26060; -.
PRO; PR:Q9UKG1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000157500; Expressed in 219 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; Q9UKG1; baseline and differential.
Genevisible; Q9UKG1; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0097708; C:intracellular vesicle; IDA:UniProtKB.
GO; GO:0044354; C:macropinosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0012506; C:vesicle membrane; IDA:BHF-UCL.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043422; F:protein kinase B binding; IPI:BHF-UCL.
GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISS:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:1905450; P:negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; ISS:UniProtKB.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; IMP:UniProtKB.
GO; GO:1905303; P:positive regulation of macropinocytosis; ISS:UniProtKB.
GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
GO; GO:0010762; P:regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:0046324; P:regulation of glucose import; IMP:BHF-UCL.
GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0034143; P:regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
GO; GO:0023052; P:signaling; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
CDD; cd07631; BAR_APPL1; 1.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR037929; APPL1_BAR.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR006020; PTB/PI_dom.
Pfam; PF00169; PH; 1.
Pfam; PF00640; PID; 1.
SMART; SM00233; PH; 1.
SMART; SM00462; PTB; 1.
SUPFAM; SSF103657; SSF103657; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS01179; PID; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Diabetes mellitus;
Disease mutation; Endosome; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 709 DCC-interacting protein 13-alpha.
/FTId=PRO_0000079985.
DOMAIN 3 268 BAR. {ECO:0000255|PROSITE-
ProRule:PRU00361}.
DOMAIN 277 375 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 496 656 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 1 428 Required for RAB5A binding.
COILED 215 259 {ECO:0000255}.
COILED 621 673 {ECO:0000255}.
MOTIF 403 414 F&H.
MOD_RES 399 399 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 410 410 Phosphoserine; by PKA.
{ECO:0000269|PubMed:17765681}.
MOD_RES 693 693 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K3H0}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K3H0}.
VARIANT 94 94 D -> N (in MODY14; no effect on protein
abundance; loss of function in insulin
receptor signaling pathway;
dbSNP:rs796065047).
{ECO:0000269|PubMed:26073777}.
/FTId=VAR_075857.
VARIANT 108 108 A -> V (in dbSNP:rs4381906).
/FTId=VAR_050958.
VARIANT 643 643 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035909.
VARIANT 700 700 E -> G (in dbSNP:rs11544593).
/FTId=VAR_050959.
MUTAGEN 410 410 S->D: Decreased interaction with OCRL.
{ECO:0000269|PubMed:17765681}.
HELIX 9 11 {ECO:0000244|PDB:2Q13}.
TURN 12 14 {ECO:0000244|PDB:2Q13}.
HELIX 16 66 {ECO:0000244|PDB:2Q12}.
HELIX 67 70 {ECO:0000244|PDB:2Q12}.
HELIX 81 110 {ECO:0000244|PDB:2Q12}.
HELIX 112 120 {ECO:0000244|PDB:2Q12}.
HELIX 122 151 {ECO:0000244|PDB:2Q12}.
STRAND 152 154 {ECO:0000244|PDB:2Q13}.
HELIX 157 217 {ECO:0000244|PDB:2Q12}.
HELIX 220 257 {ECO:0000244|PDB:2Q12}.
HELIX 259 261 {ECO:0000244|PDB:2Q13}.
STRAND 262 265 {ECO:0000244|PDB:2Q13}.
TURN 268 270 {ECO:0000244|PDB:2Q13}.
STRAND 281 286 {ECO:0000244|PDB:2Q13}.
STRAND 298 305 {ECO:0000244|PDB:2Q13}.
STRAND 308 312 {ECO:0000244|PDB:2Q13}.
STRAND 320 324 {ECO:0000244|PDB:2Q13}.
STRAND 329 333 {ECO:0000244|PDB:2Q13}.
STRAND 339 345 {ECO:0000244|PDB:2Q13}.
STRAND 348 350 {ECO:0000244|PDB:2ELB}.
STRAND 354 356 {ECO:0000244|PDB:5C5B}.
HELIX 360 374 {ECO:0000244|PDB:2Q13}.
STRAND 499 512 {ECO:0000244|PDB:2EJ8}.
HELIX 519 534 {ECO:0000244|PDB:2EJ8}.
STRAND 542 555 {ECO:0000244|PDB:2EJ8}.
TURN 557 559 {ECO:0000244|PDB:2EJ8}.
STRAND 562 567 {ECO:0000244|PDB:2EJ8}.
HELIX 568 570 {ECO:0000244|PDB:2EJ8}.
STRAND 571 577 {ECO:0000244|PDB:2EJ8}.
STRAND 580 590 {ECO:0000244|PDB:2EJ8}.
STRAND 600 610 {ECO:0000244|PDB:2EJ8}.
HELIX 612 629 {ECO:0000244|PDB:2EJ8}.
HELIX 634 643 {ECO:0000244|PDB:2ELA}.
SEQUENCE 709 AA; 79663 MW; 4CABECFCF4BB110D CRC64;
MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA QNELSAATHL
TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH AVLSTQLADA MMFPITQFKE
RDLKEILTLK EVFQIASNDH DAAINRYSRL SKKRENDKVK YEVTEDVYTS RKKQHQTMMH
YFCALNTLQY KKKIALLEPL LGYMQAQISF FKMGSENLNE QLEEFLANIG TSVQNVRREM
DSDIETMQQT IEDLEVASDP LYVPDPDPTK FPVNRNLTRK AGYLNARNKT GLVSSTWDRQ
FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK KSSILQAESK
KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP SPSFQQRHES LRPAAGQSRP
PTARTSSSGS LGSESTNLAA LSLDSLVAPD TPIQFDIISP VCEDQPGQAK AFGQGGRRTN
PFGESGGSTK SETEDSILHQ LFIVRFLGSM EVKSDDHPDV VYETMRQILA ARAIHNIFRM
TESHLLVTCD CLKLIDPQTQ VTRLTFPLPC VVLYATHQEN KRLFGFVLRT SSGRSESNLS
SVCYIFESNN EGEKICDSVG LAKQIALHAE LDRRASEKQK EIERVKEKQQ KELNKQKQIE
KDLEEQSRLI AASSRPNQAS SEGQFVVLSS SQSEESDLGE GGKKRESEA


Related products :

Catalog number Product name Quantity
EIAAB11722 Adapter protein containing PH domain, PTB domain and leucine zipper motif 1,Appl1,DCC-interacting protein 13-alpha,Dip13a,Dip13-alpha,Kiaa1428,Mouse,Mus musculus
EIAAB11723 Adapter protein containing PH domain, PTB domain and leucine zipper motif 1,APPL,APPL1,DCC-interacting protein 13-alpha,DIP13A,Dip13-alpha,Homo sapiens,Human,KIAA1428
EIAAB11725 Adapter protein containing PH domain, PTB domain and leucine zipper motif 2,Appl2,DCC-interacting protein 13-beta,Dip13b,Dip13-beta,Dip3b,Mouse,Mus musculus
EIAAB11724 Adapter protein containing PH domain, PTB domain and leucine zipper motif 2,APPL2,DCC-interacting protein 13-beta,DIP13B,Dip13-beta,Homo sapiens,Human
EIAAB37300 Homo sapiens,Human,KIAA0524,SAM domain-containing protein 2,SAMD2,SARM,SARM1,Sterile alpha and Armadillo repeat protein,Sterile alpha and TIR motif-containing protein 1,Sterile alpha motif domain-cont
EIAAB37228 Major retinal SAM domain-containing protein,Mouse,Mr-s,Mus musculus,SAM domain-containing protein 11,Samd11,Sterile alpha motif domain-containing protein 11
EIAAB05866 Brain leucine zipper domain-containing protein,BRLZ,CCDC88B,Coiled-coil domain-containing protein 88B,HkRP3,Homo sapiens,Hook-related protein 3,Human
EIAAB41080 Dsip1,Dsipi,Gilz,Glucocorticoid-induced leucine zipper protein,Mouse,Mus musculus,Tilz3,TSC22 domain family protein 3,Tsc22d3,TSC22-related-inducible leucine zipper 3
EIAAB41674 Mouse,Mus musculus,Ticam1,TICAM-1,TIR domain-containing adapter molecule 1,TIR domain-containing adapter protein inducing IFN-beta,Toll-interleukin-1 receptor domain-containing adapter protein inducin
EIAAB37254 Homo sapiens,Human,SAM domain-containing protein 8,SAMD8,SMSr,Sphingomyelin synthase-related protein 1,Sterile alpha motif domain-containing protein 8
ABP-Ri-VAsiD26 DIP13-alpha (DCC interacting protein) 5OD (12.5nmol)
EIAAB38192 FceRI gamma-chain-interacting protein SH2-B,Rat,Rattus norvegicus,SH2 domain-containing protein 1B,Sh2-b,SH2B adapter protein 1,SH2-B PH domain-containing signaling mediator 1,Sh2b1,Sh2bpsm1
25-468 LDOC1 contains a leucine zipper-like motif and a proline-rich region that shares marked similarity with an SH3-binding domain. The protein localizes to the nucleus and is down-regulated in some cancer 0.05 mg
EIAAB37245 Atherin,Oryctolagus cuniculus,Rabbit,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37246 Atherin,Homo sapiens,Human,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37231 Homo sapiens,HSD42,HSD-42,Human,SAM domain-containing protein 13,SAMD13,Sterile alpha motif domain-containing protein 13
EIAAB37249 Homo sapiens,Human,SAM domain-containing protein 5,SAMD5,SAMDC1,Sterile alpha motif domain-containing protein 5
EIAAB37225 C20orf136,Homo sapiens,Human,SAM domain-containing protein 10,SAMD10,Sterile alpha motif domain-containing protein 10
EIAAB42483 Adaptor protein Wyatt,Homo sapiens,Human,MAL,MyD88 adapter-like protein,TIR domain-containing adapter protein,TIRAP,Toll_interleukin-1 receptor domain-containing adapter protein
EIAAB37235 C14orf174,FAM15A,Homo sapiens,Human,SAM domain-containing protein 15,SAMD15,Sterile alpha motif domain-containing protein 15
EIAAB37227 Homo sapiens,Human,SAM domain-containing protein 11,SAMD11,Sterile alpha motif domain-containing protein 11
EIAAB37248 Gm623,Mouse,Mus musculus,SAM domain-containing protein 3,Samd3,Sterile alpha motif domain-containing protein 3
EIAAB37253 Homo sapiens,Human,SAM domain-containing protein 7,SAMD7,Sterile alpha motif domain-containing protein 7
EIAAB37247 Homo sapiens,Human,SAM domain-containing protein 3,SAMD3,Sterile alpha motif domain-containing protein 3
EIAAB37234 Homo sapiens,Human,SAM domain-containing protein 14,SAMD14,Sterile alpha motif domain-containing protein 14

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1689: Porphyrin and chlorophyll metabolism
WP210: Cytoplasmic Ribosomal Proteins
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP1003: Ovarian Infertility Genes
WP1047: TNF-alpha NF-kB Signaling Pathway
WP1049: G Protein Signaling Pathways
WP1120: Ovarian Infertility Genes
WP1163: TNF-alpha NF-kB Signaling Pathway
WP1165: G Protein Signaling Pathways
WP1209: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1340: Ovarian Infertility Genes
WP1369: TNF-alpha NF-kB Signaling Pathway
WP1371: G Protein Signaling Pathways
WP1434: Osteopontin Signaling
WP1438: Influenza A virus infection
WP1487: TNF-alpha and mucus production in lung epythelium
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1571: EBV LMP1 signaling
WP1584: Type II diabetes mellitus

Related Genes :
[APPL1 APPL DIP13A KIAA1428] DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)
[Appl1 Dip13a Kiaa1428] DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)
[APPL2 DIP13B] DCC-interacting protein 13-beta (Dip13-beta) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)
[Appl2 Dip13b Dip3b] DCC-interacting protein 13-beta (Dip13-beta) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)
[Appl2] DCC-interacting protein 13-beta (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)
[MAP3K20 MLTK ZAK HCCS4] Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)
[AP2A2 ADTAB CLAPA2 HIP9 HYPJ KIAA0899] AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Huntingtin yeast partner J) (Huntingtin-interacting protein 9) (HIP-9) (Huntingtin-interacting protein J) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)
[PHLPP1 KIAA0606 PHLPP PLEKHE1 SCOP] PH domain leucine-rich repeat-containing protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein) (hSCOP)
[Ap2a1 Adtaa Clapa1] AP-2 complex subunit alpha-1 (100 kDa coated vesicle protein A) (Adaptor protein complex AP-2 subunit alpha-1) (Adaptor-related protein complex 2 subunit alpha-1) (Alpha-adaptin A) (Alpha1-adaptin) (Clathrin assembly protein complex 2 alpha-A large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit)
[APP A4 AD1] Amyloid-beta precursor protein (APP) (ABPP) (APPI) (Alzheimer disease amyloid protein) (Amyloid precursor protein) (Amyloid-beta A4 protein) (Cerebral vascular amyloid peptide) (CVAP) (PreA4) (Protease nexin-II) (PN-II) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Amyloid intracellular domain 59) (AICD-59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Amyloid intracellular domain 57) (AICD-57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AICD-50) (AID(50)) (Gamma-CTF(50)); C31]
[App] Amyloid-beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Amyloid-beta precursor protein) (Amyloidogenic glycoprotein) (AG) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (APP-C99) (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (APP-C59) (Amyloid intracellular domain 59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (APP-C57) (Amyloid intracellular domain 57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AID(50)) (Gamma-CTF(50)); C31]
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[AP2A1 ADTAA CLAPA1] AP-2 complex subunit alpha-1 (100 kDa coated vesicle protein A) (Adaptor protein complex AP-2 subunit alpha-1) (Adaptor-related protein complex 2 subunit alpha-1) (Alpha-adaptin A) (Alpha1-adaptin) (Clathrin assembly protein complex 2 alpha-A large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[PLEKHO1 CKIP1 OC120 HQ0024c] Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) (C-Jun-binding protein) (JBP) (Casein kinase 2-interacting protein 1) (CK2-interacting protein 1) (CKIP-1) (Osteoclast maturation-associated gene 120 protein)
[PHLPP2 KIAA0931 PHLPPL] PH domain leucine-rich repeat-containing protein phosphatase 2 (EC 3.1.3.16) (PH domain leucine-rich repeat-containing protein phosphatase-like) (PHLPP-like)
[Sh2b1 Sh2bpsm1] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[NCKIPSD AF3P21 SPIN90] NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (54 kDa vimentin-interacting protein) (VIP54) (90 kDa SH3 protein interacting with Nck) (AF3p21) (Dia-interacting protein 1) (DIP-1) (Diaphanous protein-interacting protein) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-interacting protein)
[Ap2a2 Adtab] AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)
[CREB3 LZIP] Cyclic AMP-responsive element-binding protein 3 (CREB-3) (cAMP-responsive element-binding protein 3) (Leucine zipper protein) (Luman) (Transcription factor LZIP-alpha) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3 (N-terminal Luman) (Transcriptionally active form)]
[Tsc22d3 Dsip1 Dsipi Gilz] TSC22 domain family protein 3 (Glucocorticoid-induced leucine zipper protein) (TSC22-related-inducible leucine zipper 3) (Tilz3)
[APBA1 MINT1 X11] Amyloid-beta A4 precursor protein-binding family A member 1 (Adapter protein X11alpha) (Neuron-specific X11 protein) (Neuronal Munc18-1-interacting protein 1) (Mint-1)
[PLEKHM1 KIAA0356] Pleckstrin homology domain-containing family M member 1 (PH domain-containing family M member 1) (162 kDa adapter protein) (AP162)
[HIF1A BHLHE78 MOP1 PASD8] Hypoxia-inducible factor 1-alpha (HIF-1-alpha) (HIF1-alpha) (ARNT-interacting protein) (Basic-helix-loop-helix-PAS protein MOP1) (Class E basic helix-loop-helix protein 78) (bHLHe78) (Member of PAS protein 1) (PAS domain-containing protein 8)
[HAT5 ATHB-1 At3g01470 F4P13.2] Homeobox-leucine zipper protein HAT5 (HD-ZIP protein ATHB-1) (Homeodomain transcription factor ATHB-1) (Homeodomain-leucine zipper protein HAT5) (HD-ZIP protein 5)
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[LINGO1 LERN1 LRRN6A UNQ201/PRO227] Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 (Leucine-rich repeat and immunoglobulin domain-containing protein 1) (Leucine-rich repeat neuronal protein 1) (Leucine-rich repeat neuronal protein 6A)
[SNTA1 SNT1] Alpha-1-syntrophin (59 kDa dystrophin-associated protein A1 acidic component 1) (Pro-TGF-alpha cytoplasmic domain-interacting protein 1) (TACIP1) (Syntrophin-1)
[SH2B1 KIAA1299 SH2B] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)
[Chuk Ikka] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA)

Bibliography :