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

Ankyrin repeat and sterile alpha motif domain-containing protein 1B (Amyloid-beta protein intracellular domain-associated protein 1) (AIDA-1) (E2A-PBX1-associated protein) (EB-1)

 ANS1B_HUMAN             Reviewed;        1248 AA.
Q7Z6G8; A5PKY5; A7E259; A8K153; A8MSN4; B4DFP6; B4DH98; F8VPM3;
F8VZR9; F8WC27; Q5XLJ0; Q6IVB5; Q6NUS4; Q7Z6G6; Q7Z6G7; Q8TAP3;
Q9NRX7; Q9Y5K9;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
03-MAY-2011, sequence version 2.
22-NOV-2017, entry version 127.
RecName: Full=Ankyrin repeat and sterile alpha motif domain-containing protein 1B;
AltName: Full=Amyloid-beta protein intracellular domain-associated protein 1;
Short=AIDA-1;
AltName: Full=E2A-PBX1-associated protein;
Short=EB-1;
Name=ANKS1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 4), INTERACTION WITH
APP, AND SUBCELLULAR LOCATION.
TISSUE=Fetal brain;
PubMed=15004329;
Ghersi E., Vito P., Lopez P., Abdallah M., D'Adamio L.;
"The intracellular localization of amyloid beta protein precursor
(AbetaPP) intracellular domain associated protein-1 (AIDA-1) is
regulated by AbetaPP and alternative splicing.";
J. Alzheimers Dis. 6:67-78(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
COIL, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=15862129; DOI=10.1186/1471-2121-6-23;
Xu H., Hebert M.D.;
"A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body
protein coilin.";
BMC Cell Biol. 6:23-23(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9 AND 10).
TISSUE=Amygdala, and Brain;
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 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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5; 7 AND 8).
TISSUE=Brain, and Hippocampus;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 294-1248 (ISOFORM 1), INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=10490826; DOI=10.1038/sj.onc.1202874;
Fu X., McGrath S., Pasillas M., Nakazawa S., Kamps M.P.;
"EB-1, a tyrosine kinase signal transduction gene, is
transcriptionally activated in the t(1;19) subset of pre-B ALL, which
express oncoprotein E2a-Pbx1.";
Oncogene 18:4920-4929(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 425-1192 (ISOFORM 1), FUNCTION,
INTERACTION WITH APP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15347684; DOI=10.1074/jbc.M405329200;
Ghersi E., Noviello C., D'Adamio L.;
"Amyloid-beta protein precursor (AbetaPP) intracellular domain-
associated protein-1 proteins bind to AbetaPP and modulate its
processing in an isoform-specific manner.";
J. Biol. Chem. 279:49105-49112(2004).
[9]
INDUCTION.
PubMed=16769578;
Casagrande G., te Kronnie G., Basso G.;
"The effects of siRNA-mediated inhibition of E2A-PBX1 on EB-1 and
Wnt16b expression in the 697 pre-B leukemia cell line.";
Haematologica 91:765-771(2006).
[10]
INTERACTION WITH EPHA8.
PubMed=17875921; DOI=10.1128/MCB.00794-07;
Shin J., Gu C., Park E., Park S.;
"Identification of phosphotyrosine binding domain-containing proteins
as novel downstream targets of the EphA8 signaling function.";
Mol. Cell. Biol. 27:8113-8126(2007).
[11]
STRUCTURE BY NMR OF 813-947, SUBCELLULAR LOCATION, AND NUCLEAR
LOCALIZATION SIGNAL.
PubMed=19666031; DOI=10.1016/j.jmb.2009.08.004;
Kurabi A., Brener S., Mobli M., Kwan J.J., Donaldson L.W.;
"A nuclear localization signal at the SAM-SAM domain interface of
AIDA-1 suggests a requirement for domain uncoupling prior to nuclear
import.";
J. Mol. Biol. 392:1168-1177(2009).
-!- FUNCTION: Isoform 2 may participate in the regulation of
nucleoplasmic coilin protein interactions in neuronal and
transformed cells.
-!- FUNCTION: Isoform 3 can regulate global protein synthesis by
altering nucleolar numbers. {ECO:0000250,
ECO:0000269|PubMed:15347684, ECO:0000269|PubMed:15862129}.
-!- FUNCTION: Isoform 4 may play a role as a modulator of APP
processing. Overexpression can down-regulate APP processing.
-!- SUBUNIT: Isoform 3 interacts with DLG4 (By similarity). Interacts
with EPHA8. Isoform 2 interacts with COIL. Isoform 4 interacts
with APP and EPHA8. Isoform 6 interacts with EPHA8. {ECO:0000250,
ECO:0000269|PubMed:15004329, ECO:0000269|PubMed:15347684,
ECO:0000269|PubMed:15862129, ECO:0000269|PubMed:17875921}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15004329,
ECO:0000269|PubMed:15347684, ECO:0000269|PubMed:15862129,
ECO:0000269|PubMed:19666031}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density. Cell projection,
dendritic spine. Nucleus. Nucleus, Cajal body. Note=The synaptic
localization requires DLG4 interaction. Translocation to the
nucleus in response to stimulation of NMDA receptors (NMDARs) in a
calcium-independent manner (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus. Note=The interaction
with APP causes its partial exclusion from the nucleus, when APP
is overexpressed.
-!- SUBCELLULAR LOCATION: Isoform 6: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1; Synonyms=AIDA-1b;
IsoId=Q7Z6G8-1; Sequence=Displayed;
Name=2; Synonyms=AIDA-1c;
IsoId=Q7Z6G8-2; Sequence=VSP_032702, VSP_032704, VSP_032707,
VSP_032710;
Name=3;
IsoId=Q7Z6G8-3; Sequence=VSP_032702, VSP_032704, VSP_032709,
VSP_032710;
Name=4; Synonyms=AIDA-1a;
IsoId=Q7Z6G8-4; Sequence=VSP_032702, VSP_032704, VSP_032711;
Name=5;
IsoId=Q7Z6G8-5; Sequence=VSP_032702, VSP_032704, VSP_032708,
VSP_032710;
Name=6; Synonyms=AIDA-1bDeltaAnk;
IsoId=Q7Z6G8-6; Sequence=VSP_032703, VSP_032705, VSP_032707;
Name=7;
IsoId=Q7Z6G8-7; Sequence=VSP_032702, VSP_032704, VSP_032707;
Name=8;
IsoId=Q7Z6G8-8; Sequence=VSP_032701, VSP_032706, VSP_032712;
Note=Ref.6 (AAH68451) sequence is in conflict in position:
325:P->R. {ECO:0000305};
Name=9;
IsoId=Q7Z6G8-9; Sequence=VSP_046414;
Note=No experimental confirmation available.;
Name=10;
IsoId=Q7Z6G8-10; Sequence=VSP_046415, VSP_032707, VSP_032712;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in marrow from patients with
pre-B ALL associated with the t(1;19) translocation. Strongly
expressed in brain and testis. Expressed in fetal brain. Isoform 4
is highly expressed in brain (at protein level). Isoform 6 is
expressed in brain and several cancer cell lines.
{ECO:0000269|PubMed:10490826, ECO:0000269|PubMed:15347684}.
-!- INDUCTION: Transcriptionally up-regulated in t(1:19) pre-B cell
acute lymphocytic leukemia by the chimeric TCF3-PBX1. Not
expressed in pre-B cell that lack this translocation.
{ECO:0000269|PubMed:10490826, ECO:0000269|PubMed:16769578}.
-!- PTM: Isoform 3 nuclear translocation requires an NMDAR-dependent
proteolytic cleavage. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAP38184.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY281131; AAP37612.1; -; mRNA.
EMBL; AY281132; AAP37613.1; -; mRNA.
EMBL; AY283057; AAP38184.2; ALT_INIT; mRNA.
EMBL; AY753193; AAV28691.1; -; mRNA.
EMBL; AF164792; AAF80756.1; -; mRNA.
EMBL; AK289768; BAF82457.1; -; mRNA.
EMBL; AK294191; BAG57507.1; -; mRNA.
EMBL; AK294994; BAG58059.1; -; mRNA.
EMBL; AC008126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC021653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC048330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC069437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC117377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC141554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC141555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC141556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC026313; AAH26313.2; -; mRNA.
EMBL; BC068451; AAH68451.1; -; mRNA.
EMBL; BC142669; AAI42670.1; -; mRNA.
EMBL; BC150204; AAI50205.1; -; mRNA.
EMBL; AF145204; AAD33951.1; -; mRNA.
EMBL; AY620824; AAT39519.1; -; mRNA.
CCDS; CCDS55864.1; -. [Q7Z6G8-9]
CCDS; CCDS55865.1; -. [Q7Z6G8-8]
CCDS; CCDS55866.1; -. [Q7Z6G8-7]
CCDS; CCDS55867.1; -. [Q7Z6G8-2]
CCDS; CCDS55868.1; -. [Q7Z6G8-5]
CCDS; CCDS55869.1; -. [Q7Z6G8-4]
CCDS; CCDS55870.1; -. [Q7Z6G8-3]
CCDS; CCDS55871.1; -. [Q7Z6G8-10]
CCDS; CCDS55872.1; -. [Q7Z6G8-1]
RefSeq; NP_001190994.1; NM_001204065.1.
RefSeq; NP_001190995.1; NM_001204066.1. [Q7Z6G8-8]
RefSeq; NP_001190996.1; NM_001204067.1. [Q7Z6G8-10]
RefSeq; NP_001190997.1; NM_001204068.1. [Q7Z6G8-4]
RefSeq; NP_001190998.1; NM_001204069.1. [Q7Z6G8-5]
RefSeq; NP_001190999.1; NM_001204070.1. [Q7Z6G8-2]
RefSeq; NP_001191008.1; NM_001204079.1.
RefSeq; NP_001191009.1; NM_001204080.1.
RefSeq; NP_001191010.1; NM_001204081.1. [Q7Z6G8-9]
RefSeq; NP_064525.1; NM_020140.3. [Q7Z6G8-7]
RefSeq; NP_690001.3; NM_152788.4. [Q7Z6G8-1]
RefSeq; NP_858056.2; NM_181670.3. [Q7Z6G8-3]
UniGene; Hs.506458; -.
PDB; 2EAM; NMR; -; A=808-874.
PDB; 2KE7; NMR; -; A=808-893.
PDB; 2KIV; NMR; -; A=812-946.
PDB; 2M38; NMR; -; A=1042-1194.
PDBsum; 2EAM; -.
PDBsum; 2KE7; -.
PDBsum; 2KIV; -.
PDBsum; 2M38; -.
ProteinModelPortal; Q7Z6G8; -.
SMR; Q7Z6G8; -.
BioGrid; 121229; 9.
DIP; DIP-41406N; -.
IntAct; Q7Z6G8; 5.
MINT; MINT-258807; -.
STRING; 9606.ENSP00000449629; -.
iPTMnet; Q7Z6G8; -.
PhosphoSitePlus; Q7Z6G8; -.
SwissPalm; Q7Z6G8; -.
BioMuta; ANKS1B; -.
DMDM; 332278155; -.
EPD; Q7Z6G8; -.
MaxQB; Q7Z6G8; -.
PaxDb; Q7Z6G8; -.
PeptideAtlas; Q7Z6G8; -.
PRIDE; Q7Z6G8; -.
DNASU; 56899; -.
Ensembl; ENST00000341752; ENSP00000345510; ENSG00000185046. [Q7Z6G8-9]
Ensembl; ENST00000546568; ENSP00000448205; ENSG00000185046. [Q7Z6G8-2]
Ensembl; ENST00000546960; ENSP00000447839; ENSG00000185046. [Q7Z6G8-4]
Ensembl; ENST00000547010; ENSP00000448512; ENSG00000185046. [Q7Z6G8-6]
Ensembl; ENST00000547446; ENSP00000450015; ENSG00000185046. [Q7Z6G8-10]
Ensembl; ENST00000547776; ENSP00000449629; ENSG00000185046. [Q7Z6G8-1]
Ensembl; ENST00000549025; ENSP00000447312; ENSG00000185046. [Q7Z6G8-8]
Ensembl; ENST00000549493; ENSP00000448203; ENSG00000185046. [Q7Z6G8-3]
Ensembl; ENST00000549558; ENSP00000448993; ENSG00000185046. [Q7Z6G8-7]
Ensembl; ENST00000550693; ENSP00000447999; ENSG00000185046. [Q7Z6G8-5]
GeneID; 56899; -.
KEGG; hsa:56899; -.
UCSC; uc001tgd.3; human. [Q7Z6G8-1]
CTD; 56899; -.
DisGeNET; 56899; -.
EuPathDB; HostDB:ENSG00000185046.18; -.
GeneCards; ANKS1B; -.
HGNC; HGNC:24600; ANKS1B.
HPA; HPA044628; -.
MIM; 607815; gene.
neXtProt; NX_Q7Z6G8; -.
OpenTargets; ENSG00000185046; -.
PharmGKB; PA128394692; -.
eggNOG; KOG0507; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00530000063104; -.
HOGENOM; HOG000007214; -.
HOVERGEN; HBG050506; -.
InParanoid; Q7Z6G8; -.
KO; K21413; -.
OMA; RNGDQWV; -.
OrthoDB; EOG091G00YV; -.
TreeFam; TF320582; -.
ChiTaRS; ANKS1B; human.
EvolutionaryTrace; Q7Z6G8; -.
GeneWiki; ANKS1B; -.
GenomeRNAi; 56899; -.
PRO; PR:Q7Z6G8; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000185046; -.
ExpressionAtlas; Q7Z6G8; baseline and differential.
Genevisible; Q7Z6G8; HS.
GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:1900383; P:regulation of synaptic plasticity by receptor localization to synapse; IEA:InterPro.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR033635; ANKS1.
InterPro; IPR033636; ANKS1B.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
PANTHER; PTHR24174; PTHR24174; 1.
PANTHER; PTHR24174:SF3; PTHR24174:SF3; 1.
Pfam; PF12796; Ank_2; 3.
Pfam; PF00640; PID; 1.
Pfam; PF00536; SAM_1; 2.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SMART; SM00462; PTB; 1.
SMART; SM00454; SAM; 2.
SUPFAM; SSF47769; SSF47769; 2.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS01179; PID; 1.
PROSITE; PS50105; SAM_DOMAIN; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse.
CHAIN 1 1248 Ankyrin repeat and sterile alpha motif
domain-containing protein 1B.
/FTId=PRO_0000327259.
REPEAT 2 31 ANK 1.
REPEAT 58 87 ANK 2.
REPEAT 91 120 ANK 3.
REPEAT 127 156 ANK 4.
REPEAT 160 189 ANK 5.
REPEAT 193 222 ANK 6.
REPEAT 225 254 ANK 7.
DOMAIN 810 876 SAM 1. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 884 949 SAM 2. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 1056 1213 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
MOTIF 935 938 Nuclear localization signal.
{ECO:0000269|PubMed:19666031}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000250|UniProtKB:P0C6S7}.
MOD_RES 503 503 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 773 773 Phosphothreonine.
{ECO:0000250|UniProtKB:P0C6S7}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000250|UniProtKB:P0C6S7}.
MOD_RES 901 901 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 974 974 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 1007 1007 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
VAR_SEQ 1 994 Missing (in isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046414.
VAR_SEQ 1 831 Missing (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032701.
VAR_SEQ 1 774 Missing (in isoform 3, isoform 4, isoform
5, isoform 2 and isoform 7).
{ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15004329,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15862129}.
/FTId=VSP_032702.
VAR_SEQ 1 420 Missing (in isoform 6).
{ECO:0000303|PubMed:15004329}.
/FTId=VSP_032703.
VAR_SEQ 3 807 Missing (in isoform 10).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046415.
VAR_SEQ 775 807 SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR -> MMWQ
CHLSAQDYRYYPVDGYSLLKRFPLHPLTG (in isoform
3, isoform 4, isoform 5, isoform 2 and
isoform 7). {ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15004329,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15862129}.
/FTId=VSP_032704.
VAR_SEQ 804 807 Missing (in isoform 6).
{ECO:0000303|PubMed:15004329}.
/FTId=VSP_032705.
VAR_SEQ 927 1022 VLKINLIGHRKRILASLGDRLHDDPPQKPPRSITLREPSGN
HTPPQLSPSLSQSTYTTGGSLDVPHIIMQGDARRRRNENYF
DDIPRSKLERQMAQ -> QSSVCEIWTNQNAGFPFSAIHQV
HN (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032706.
VAR_SEQ 963 1022 Missing (in isoform 2, isoform 6, isoform
7 and isoform 10).
{ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15004329,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15862129}.
/FTId=VSP_032707.
VAR_SEQ 963 1022 EPSGNHTPPQLSPSLSQSTYTTGGSLDVPHIIMQGDARRRR
NENYFDDIPRSKLERQMAQ -> SSVCEIWTNQNAGFPFSA
IHQVHN (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032708.
VAR_SEQ 1022 1022 Q -> QSSVCEIWTNQNAGFPFSAIHQVHN (in
isoform 3). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_032709.
VAR_SEQ 1225 1248 DLLHASHTGQEPSERHTEEALRKF -> QIDPSEQKTLANL
PWIVEPGQEAKRGINTKYETTIF (in isoform 3,
isoform 5 and isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15862129}.
/FTId=VSP_032710.
VAR_SEQ 1225 1248 DLLHASHTGQEPSERHTEEALRKF -> PFCFKADRPI
(in isoform 4).
{ECO:0000303|PubMed:15004329}.
/FTId=VSP_032711.
VAR_SEQ 1225 1247 DLLHASHTGQEPSERHTEEALRK -> IDPSEQKTLANLPW
IVEPGQEAKRGINTKYETTI (in isoform 8 and
isoform 10).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_032712.
CONFLICT 290 291 RS -> KYA (in Ref. 1; AAP37612).
{ECO:0000305}.
CONFLICT 813 813 Q -> L (in Ref. 4; BAF82457).
{ECO:0000305}.
CONFLICT 854 854 E -> G (in Ref. 6; AAI42670).
{ECO:0000305}.
CONFLICT 1160 1160 C -> R (in Ref. 4; BAG57507).
{ECO:0000305}.
CONFLICT 1167 1167 D -> G (in Ref. 4; BAG58059).
{ECO:0000305}.
HELIX 815 822 {ECO:0000244|PDB:2EAM}.
HELIX 825 827 {ECO:0000244|PDB:2EAM}.
HELIX 828 833 {ECO:0000244|PDB:2EAM}.
TURN 834 837 {ECO:0000244|PDB:2KIV}.
TURN 839 841 {ECO:0000244|PDB:2EAM}.
STRAND 842 847 {ECO:0000244|PDB:2EAM}.
HELIX 851 854 {ECO:0000244|PDB:2EAM}.
HELIX 860 872 {ECO:0000244|PDB:2EAM}.
HELIX 889 894 {ECO:0000244|PDB:2KIV}.
TURN 895 897 {ECO:0000244|PDB:2KIV}.
HELIX 901 908 {ECO:0000244|PDB:2KIV}.
HELIX 913 916 {ECO:0000244|PDB:2KIV}.
HELIX 921 927 {ECO:0000244|PDB:2KIV}.
HELIX 933 943 {ECO:0000244|PDB:2KIV}.
TURN 1056 1058 {ECO:0000244|PDB:2M38}.
STRAND 1059 1074 {ECO:0000244|PDB:2M38}.
HELIX 1078 1091 {ECO:0000244|PDB:2M38}.
STRAND 1094 1097 {ECO:0000244|PDB:2M38}.
STRAND 1104 1110 {ECO:0000244|PDB:2M38}.
STRAND 1113 1121 {ECO:0000244|PDB:2M38}.
STRAND 1124 1128 {ECO:0000244|PDB:2M38}.
HELIX 1130 1132 {ECO:0000244|PDB:2M38}.
STRAND 1133 1138 {ECO:0000244|PDB:2M38}.
STRAND 1145 1150 {ECO:0000244|PDB:2M38}.
TURN 1153 1155 {ECO:0000244|PDB:2M38}.
STRAND 1156 1167 {ECO:0000244|PDB:2M38}.
HELIX 1168 1186 {ECO:0000244|PDB:2M38}.
SEQUENCE 1248 AA; 138066 MW; EC3921C45083426D CRC64;
MGKDQELLEA ARTGNVALVE KLLSGRKGGI LGGGSGPLPL SNLLSIWRGP NVNCTDSSGY
TALHHAALNG HKDIVLKLLQ YEASTNVADN KGYFPIHLAA WKGDVEIVKI LIHHGPSHSR
VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPTIRNSK LETPLDLAAL YGRLRVVKMI
ISAHPNLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEAALFGKVD
VVRVLLETGI DANIKDSLGR TVLDILKEHP SQKSLQIATL LQEYLEGVGR STVLEEPVQE
DATQETHISS PVESPSQKTK SETVTGELSK LLDEIKLCQE KDYSFEDLCH TISDHYLDNL
SKISEEELGK NGSQSVRTSS TINLSPGEVE EEDDDENTCG PSGLWEALTP CNGCRNLGFP
MLAQESYPKK RNYTMEIVPS ASLDTFPSEN ENFLCDLMDT AVTKKPCSLE IARAPSPRTD
NASEVAVTTP GTSNHRNSST GPTPDCSPPS PDTALKNIVK VIRPQPKQRT SIVSSLDFHR
MNHNQEYFEI NTSTGCTSFT ASPPASPPTS SVGTTEVKNE GTNHTDDLSR QDDNDPPKEY
DPGQFAGLLH GSSPACESPE NPFHLYGKRE QCEKGQDEVS LANSPLPFKQ SPIENNSEPL
VKKIKPKVVS RTIFHKKSNQ LENHTIVGTR STRSGSRNGD QWVMNAGGFV ERACTLGRIR
SLPKALIDMH LSKSVSKSDS DLIAYPSNEK TSRVNWSESS TAEHSSKGNS ERTPSFTSEW
EEIDKIMSSI DVGINNELKE MNGETTRPRC PVQTVGQWLE SIGLPQYENH LMANGFDNVQ
FMGSNVMEDQ DLLEIGILNS GHRQRILQAI QLLPKMRPIG HDGYHPTSVA EWLDSIELGD
YTKAFLINGY TSMDLLKKIW EVELINVLKI NLIGHRKRIL ASLGDRLHDD PPQKPPRSIT
LREPSGNHTP PQLSPSLSQS TYTTGGSLDV PHIIMQGDAR RRRNENYFDD IPRSKLERQM
AQTGDWGEPS ITLRPPNEAT ASTPVQYWQH HPEKLIFQSC DYKAFYLGSM LIKELRGTES
TQDACAKMRA NCQKSTEQMK KVPTIILSVS YKGVKFIDAT NKNIIAEHEI RNISCAAQDP
EDLSTFAYIT KDLKSNHHYC HVFTAFDVNL AYEIILTLGQ AFEVAYQLAL QARKGGHSST
LPESFENKPS KPIPKPRVSI RKSVDLLHAS HTGQEPSERH TEEALRKF


Related products :

Catalog number Product name Quantity
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
ANS1B_MOUSE Mouse ELISA Kit FOR Ankyrin repeat and sterile alpha motif domain-containing protein 1B 96T
CSB-EL001805RA Rat Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit 96T
CSB-EL001805RA Rat Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit SpeciesRat 96T
CSB-EL001805MO Mouse Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit 96T
CSB-EL001805HU Human Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit 96T
CSB-EL001805MO Mouse Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit SpeciesMouse 96T
CSB-EL001805HU Human Ankyrin repeat and sterile alpha motif domain-containing protein 1B(ANKS1B) ELISA kit SpeciesHuman 96T
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
EIAAB37254 Homo sapiens,Human,SAM domain-containing protein 8,SAMD8,SMSr,Sphingomyelin synthase-related protein 1,Sterile alpha motif domain-containing protein 8
EIAAB38727 Homo sapiens,hSmaug2,Human,Protein Smaug homolog 2,SAM domain-containing protein 4B,SAMD4B,Smaug 2,SMAUG2,Sterile alpha motif domain-containing protein 4B
EIAAB38725 Homo sapiens,hSmaug1,Human,KIAA1053,Protein Smaug homolog 1,SAM domain-containing protein 4A,SAMD4,SAMD4A,Smaug 1,SMAUG1,Sterile alpha motif domain-containing protein 4A
EIAAB37246 Atherin,Homo sapiens,Human,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37225 C20orf136,Homo sapiens,Human,SAM domain-containing protein 10,SAMD10,Sterile alpha motif domain-containing protein 10
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
EIAAB37245 Atherin,Oryctolagus cuniculus,Rabbit,SAM domain-containing protein 1,SAMD1,Sterile alpha motif domain-containing protein 1
EIAAB37235 C14orf174,FAM15A,Homo sapiens,Human,SAM domain-containing protein 15,SAMD15,Sterile alpha motif domain-containing protein 15
EIAAB37229 Homo sapiens,Human,SAM domain-containing protein 12,SAMD12,Sterile alpha motif domain-containing protein 12
EIAAB37247 Homo sapiens,Human,SAM domain-containing protein 3,SAMD3,Sterile alpha motif domain-containing protein 3
EIAAB37240 Kiaa2005,Mouse,Mus musculus,SAM domain-containing protein 9-like,Samd9l,Sterile alpha motif domain-containing protein 9-like
EIAAB37248 Gm623,Mouse,Mus musculus,SAM domain-containing protein 3,Samd3,Sterile alpha motif domain-containing protein 3
EIAAB37227 Homo sapiens,Human,SAM domain-containing protein 11,SAMD11,Sterile alpha motif domain-containing protein 11
EIAAB37234 Homo sapiens,Human,SAM domain-containing protein 14,SAMD14,Sterile alpha motif domain-containing protein 14
EIAAB37253 Homo sapiens,Human,SAM domain-containing protein 7,SAMD7,Sterile alpha motif domain-containing protein 7


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
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