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DCC-interacting protein 13-beta (Dip13-beta) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 2)

 DP13B_HUMAN             Reviewed;         664 AA.
Q8NEU8; B7Z411; B7Z4B0; F5GZG0; F8W1P5; Q8N4R7; Q9NVL2;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
23-MAY-2018, entry version 144.
RecName: Full=DCC-interacting protein 13-beta;
Short=Dip13-beta;
AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 2;
Name=APPL2; Synonyms=DIP13B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000312|EMBL:AAM55530.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Chen Y.Q.;
"Identification of DIP13 beta, a novel protein related to the DCC-
interacting protein 13 alpha (DIP13alpha).";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANT VAL-433.
TISSUE=Colon, and Teratocarcinoma;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4] {ECO:0000312|EMBL:AAH33731.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-433.
TISSUE=Brain {ECO:0000312|EMBL:AAH33731.1};
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).
[5] {ECO:0000305}
CHROMOSOMAL TRANSLOCATION WITH SHANK3, AND TISSUE SPECIFICITY.
PubMed=11431708; DOI=10.1086/321293;
Bonaglia M.C., Giorda R., Borgatti R., Felisari G., Gagliardi C.,
Selicorni A., Zuffardi O.;
"Disruption of the ProSAP2 gene in a t(12;22)(q24.1;q13.3) is
associated with the 22q13.3 deletion syndrome.";
Am. J. Hum. Genet. 69:261-268(2001).
[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]
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).
-!- FUNCTION: Required for the regulation of cell proliferation in
response to extracellular signals mediated by an early endosomal
compartment. Links Rab5 to nuclear signal transduction.
{ECO:0000269|PubMed:15016378}.
-!- SUBUNIT: 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. Binds
subunits of the NuRD/MeCP1 complex.
-!- INTERACTION:
Q9UKG1:APPL1; NbExp=9; IntAct=EBI-741261, EBI-741243;
P78560:CRADD; NbExp=3; IntAct=EBI-741261, EBI-520375;
Q9UPY8:MAPRE3; NbExp=3; IntAct=EBI-741261, EBI-726739;
Q9UL26:RAB22A; NbExp=6; IntAct=EBI-741261, EBI-399456;
P51148:RAB5C; NbExp=5; IntAct=EBI-741261, EBI-1054923;
Q9H5I1:SUV39H2; NbExp=4; IntAct=EBI-741261, EBI-723127;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:15016378}; Peripheral membrane protein
{ECO:0000269|PubMed:15016378}. Nucleus
{ECO:0000269|PubMed:15016378}. Note=Early endosomal membrane-bound
and nuclear. Translocated into the nucleus upon release from
endosomal membranes following internalization of EGF.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8NEU8-1; Sequence=Displayed;
Name=2;
IsoId=Q8NEU8-2; Sequence=VSP_044771;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8NEU8-3; Sequence=VSP_044772;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High levels in brain, heart, kidney and
skeletal muscle. {ECO:0000269|PubMed:11431708}.
-!- DISEASE: Note=A chromosomal aberration involving APPL2/DIP13B is
found in patients with chromosome 22q13.3 deletion syndrome.
Translocation t(12;22)(q24.1;q13.3) with SHANK3/PSAP2
(PubMed:11431708). {ECO:0000269|PubMed:11431708}.
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EMBL; AY113704; AAM55530.1; -; mRNA.
EMBL; AK001521; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK296610; BAH12397.1; -; mRNA.
EMBL; AK297100; BAH12496.1; -; mRNA.
EMBL; AC016257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033731; AAH33731.1; -; mRNA.
CCDS; CCDS58275.1; -. [Q8NEU8-2]
CCDS; CCDS58276.1; -. [Q8NEU8-3]
CCDS; CCDS9101.1; -. [Q8NEU8-1]
RefSeq; NP_001238833.1; NM_001251904.1. [Q8NEU8-3]
RefSeq; NP_001238834.1; NM_001251905.1. [Q8NEU8-2]
RefSeq; NP_060641.2; NM_018171.3. [Q8NEU8-1]
RefSeq; XP_016875041.1; XM_017019552.1. [Q8NEU8-2]
RefSeq; XP_016875042.1; XM_017019553.1. [Q8NEU8-2]
UniGene; Hs.506603; -.
PDB; 4H8S; X-ray; 3.50 A; A/B/C/D=2-384.
PDB; 5C5B; X-ray; 2.90 A; B/D=1-375.
PDBsum; 4H8S; -.
PDBsum; 5C5B; -.
ProteinModelPortal; Q8NEU8; -.
SMR; Q8NEU8; -.
BioGrid; 120495; 32.
IntAct; Q8NEU8; 35.
MINT; Q8NEU8; -.
STRING; 9606.ENSP00000258530; -.
iPTMnet; Q8NEU8; -.
PhosphoSitePlus; Q8NEU8; -.
BioMuta; APPL2; -.
DMDM; 160419148; -.
EPD; Q8NEU8; -.
MaxQB; Q8NEU8; -.
PaxDb; Q8NEU8; -.
PeptideAtlas; Q8NEU8; -.
PRIDE; Q8NEU8; -.
DNASU; 55198; -.
Ensembl; ENST00000258530; ENSP00000258530; ENSG00000136044. [Q8NEU8-1]
Ensembl; ENST00000539978; ENSP00000444472; ENSG00000136044. [Q8NEU8-2]
Ensembl; ENST00000551662; ENSP00000446917; ENSG00000136044. [Q8NEU8-3]
GeneID; 55198; -.
KEGG; hsa:55198; -.
UCSC; uc001tlf.2; human. [Q8NEU8-1]
CTD; 55198; -.
DisGeNET; 55198; -.
EuPathDB; HostDB:ENSG00000136044.11; -.
GeneCards; APPL2; -.
H-InvDB; HIX0010948; -.
HGNC; HGNC:18242; APPL2.
HPA; HPA039688; -.
HPA; HPA043925; -.
MIM; 606231; gene.
neXtProt; NX_Q8NEU8; -.
OpenTargets; ENSG00000136044; -.
PharmGKB; PA164741199; -.
eggNOG; KOG0521; Eukaryota.
eggNOG; KOG3536; Eukaryota.
eggNOG; ENOG410ZISK; LUCA.
GeneTree; ENSGT00710000106752; -.
HOGENOM; HOG000285988; -.
HOVERGEN; HBG051394; -.
InParanoid; Q8NEU8; -.
KO; K20132; -.
OMA; CQPRGAV; -.
OrthoDB; EOG091G08AV; -.
PhylomeDB; Q8NEU8; -.
TreeFam; TF328669; -.
ChiTaRS; APPL2; human.
GeneWiki; APPL2; -.
GenomeRNAi; 55198; -.
PRO; PR:Q8NEU8; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000136044; -.
CleanEx; HS_APPL2; -.
ExpressionAtlas; Q8NEU8; baseline and differential.
Genevisible; Q8NEU8; HS.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR027267; AH/BAR_dom_sf.
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; Alternative splicing; Cell cycle;
Chromosomal rearrangement; Complete proteome; Endosome; Membrane;
Nucleus; Polymorphism; Reference proteome.
CHAIN 1 664 DCC-interacting protein 13-beta.
/FTId=PRO_0000079987.
DOMAIN 277 375 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 488 637 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 1 428 Required for RAB5A binding.
{ECO:0000250}.
SITE 234 235 Breakpoint for chromosomal translocation.
{ECO:0000269|PubMed:11431708}.
VAR_SEQ 1 43 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044771.
VAR_SEQ 138 138 N -> NDVCLFL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044772.
VARIANT 433 433 A -> V (in dbSNP:rs2272495).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_021505.
CONFLICT 295 295 T -> A (in Ref. 2). {ECO:0000305}.
CONFLICT 448 448 T -> A (in Ref. 2). {ECO:0000305}.
CONFLICT 528 528 N -> S (in Ref. 2; BAH12496).
{ECO:0000305}.
CONFLICT 575 575 L -> P (in Ref. 2; BAH12397).
{ECO:0000305}.
HELIX 9 11 {ECO:0000244|PDB:5C5B}.
TURN 12 14 {ECO:0000244|PDB:5C5B}.
HELIX 17 70 {ECO:0000244|PDB:5C5B}.
HELIX 80 110 {ECO:0000244|PDB:5C5B}.
HELIX 112 148 {ECO:0000244|PDB:5C5B}.
STRAND 152 154 {ECO:0000244|PDB:5C5B}.
HELIX 157 217 {ECO:0000244|PDB:5C5B}.
HELIX 220 254 {ECO:0000244|PDB:5C5B}.
HELIX 259 261 {ECO:0000244|PDB:5C5B}.
HELIX 266 269 {ECO:0000244|PDB:5C5B}.
STRAND 281 288 {ECO:0000244|PDB:5C5B}.
STRAND 291 293 {ECO:0000244|PDB:5C5B}.
STRAND 296 305 {ECO:0000244|PDB:5C5B}.
STRAND 308 312 {ECO:0000244|PDB:5C5B}.
STRAND 320 324 {ECO:0000244|PDB:5C5B}.
STRAND 329 333 {ECO:0000244|PDB:5C5B}.
STRAND 341 345 {ECO:0000244|PDB:5C5B}.
STRAND 351 356 {ECO:0000244|PDB:5C5B}.
HELIX 360 373 {ECO:0000244|PDB:5C5B}.
SEQUENCE 664 AA; 74493 MW; 359404B1CBA813DB CRC64;
MPAVDKLLLE EALQDSPQTR SLLSVFEEDA GTLTDYTNQL LQAMQRVYGA QNEMCLATQQ
LSKQLLAYEK QNFALGKGDE EVISTLHYFS KVVDELNLLH TELAKQLADT MVLPIIQFRE
KDLTEVSTLK DLFGLASNEH DLSMAKYSRL PKKKENEKVK TEVGKEVAAA RRKQHLSSLQ
YYCALNALQY RKQMAMMEPM IGFAHGQINF FKKGAEMFSK RMDSFLSSVA DMVQSIQVEL
EAEAEKMRVS QQELLSVDES VYTPDSDVAA PQINRNLIQK AGYLNLRNKT GLVTTTWERL
YFFTQGGNLM CQPRGAVAGG LIQDLDNCSV MAVDCEDRRY CFQITTPNGK SGIILQAESR
KENEEWICAI NNISRQIYLT DNPEAVAIKL NQTALQAVTP ITSFGKKQES SCPSQNLKNS
EMENENDKIV PKATASLPEA EELIAPGTPI QFDIVLPATE FLDQNRGSRR TNPFGETEDE
SFPEAEDSLL QQMFIVRFLG SMAVKTDSTT EVIYEAMRQV LAARAIHNIF RMTESHLMVT
SQSLRLIDPQ TQVSRANFEL TSVTQFAAHQ ENKRLVGFVI RVPESTGEES LSTYIFESNS
EGEKICYAIN LGKEIIEVQK DPEALAQLML SIPLTNDGKY VLLNDQPDDD DGNPNEHRGA
ESEA


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U1600m CLIA Bash,B-cell adapter containing a SH2 domain protein,B-cell adapter containing a Src homology 2 domain protein,B-cell linker protein,Blnk,Cytoplasmic adapter protein,Ly57,Lymphocyte antigen 57,Mou 96T
28-968 CORO1A is a novel actin-binding protein with a WD repeat and a leucine zipper motif. CORO1A forms homodimers, that the association is mediated by the leucine zipper structure in the C-terminal region, 0.1 mg
28-967 CORO1A is a novel actin-binding protein with a WD repeat and a leucine zipper motif. CORO1A forms homodimers, that the association is mediated by the leucine zipper structure in the C-terminal region, 0.1 mg
EIAAB38183 Homo sapiens,Human,SCAP,SH2 domain-containing adapter protein,SH2 domain-containing protein 2A,SH2D2A,T cell-specific adapter protein,TSAd,TSAD,VEGF receptor-associated protein,VRAP
BZW1_RAT Rat ELISA Kit FOR Basic leucine zipper and W2 domain-containing protein 1 96T
28-082 LIM domain only 6 is a three LIM domain-containing protein. The LIM domain is a cysteine-rich sequence motif that binds zinc atoms to form a specific protein-binding interface for protein-protein inte 0.05 mg


 

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