ANS1B_HUMAN
ID ANS1B_HUMAN Reviewed; 1248 AA.
AC Q7Z6G8; A5PKY5; A7E259; A8K153; A8MSN4; B4DFP6; B4DH98; F8VPM3; F8VZR9;
AC F8WC27; Q5XLJ0; Q6IVB5; Q6NUS4; Q7Z6G6; Q7Z6G7; Q8TAP3; Q9NRX7; Q9Y5K9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ankyrin repeat and sterile alpha motif domain-containing protein 1B;
DE AltName: Full=Amyloid-beta protein intracellular domain-associated protein 1;
DE Short=AIDA-1;
DE AltName: Full=E2A-PBX1-associated protein;
DE Short=EB-1;
GN Name=ANKS1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 4), INTERACTION WITH APP, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=15004329; DOI=10.3233/jad-2004-6108;
RA Ghersi E., Vito P., Lopez P., Abdallah M., D'Adamio L.;
RT "The intracellular localization of amyloid beta protein precursor (AbetaPP)
RT intracellular domain associated protein-1 (AIDA-1) is regulated by AbetaPP
RT and alternative splicing.";
RL J. Alzheimers Dis. 6:67-78(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH COIL,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=15862129; DOI=10.1186/1471-2121-6-23;
RA Xu H., Hebert M.D.;
RT "A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body
RT protein coilin.";
RL BMC Cell Biol. 6:23-23(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9 AND 10).
RC TISSUE=Amygdala, and Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5; 7 AND 8).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-1248 (ISOFORM 1), INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10490826; DOI=10.1038/sj.onc.1202874;
RA Fu X., McGrath S., Pasillas M., Nakazawa S., Kamps M.P.;
RT "EB-1, a tyrosine kinase signal transduction gene, is transcriptionally
RT activated in the t(1;19) subset of pre-B ALL, which express oncoprotein
RT E2a-Pbx1.";
RL Oncogene 18:4920-4929(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-1192 (ISOFORM 1), FUNCTION, INTERACTION
RP WITH APP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15347684; DOI=10.1074/jbc.m405329200;
RA Ghersi E., Noviello C., D'Adamio L.;
RT "Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated
RT protein-1 proteins bind to AbetaPP and modulate its processing in an
RT isoform-specific manner.";
RL J. Biol. Chem. 279:49105-49112(2004).
RN [9]
RP INDUCTION.
RX PubMed=16769578;
RA Casagrande G., te Kronnie G., Basso G.;
RT "The effects of siRNA-mediated inhibition of E2A-PBX1 on EB-1 and Wnt16b
RT expression in the 697 pre-B leukemia cell line.";
RL Haematologica 91:765-771(2006).
RN [10]
RP INTERACTION WITH EPHA8.
RX PubMed=17875921; DOI=10.1128/mcb.00794-07;
RA Shin J., Gu C., Park E., Park S.;
RT "Identification of phosphotyrosine binding domain-containing proteins as
RT novel downstream targets of the EphA8 signaling function.";
RL Mol. Cell. Biol. 27:8113-8126(2007).
RN [11]
RP STRUCTURE BY NMR OF 813-947, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION
RP SIGNAL.
RX PubMed=19666031; DOI=10.1016/j.jmb.2009.08.004;
RA Kurabi A., Brener S., Mobli M., Kwan J.J., Donaldson L.W.;
RT "A nuclear localization signal at the SAM-SAM domain interface of AIDA-1
RT suggests a requirement for domain uncoupling prior to nuclear import.";
RL J. Mol. Biol. 392:1168-1177(2009).
CC -!- FUNCTION: Isoform 2 may participate in the regulation of nucleoplasmic
CC coilin protein interactions in neuronal and transformed cells.
CC -!- FUNCTION: Isoform 3 can regulate global protein synthesis by altering
CC nucleolar numbers. {ECO:0000250, ECO:0000269|PubMed:15347684,
CC ECO:0000269|PubMed:15862129}.
CC -!- FUNCTION: Isoform 4 may play a role as a modulator of APP processing.
CC Overexpression can down-regulate APP processing.
CC -!- SUBUNIT: Isoform 3 interacts with DLG4 (By similarity). Interacts with
CC EPHA8. Isoform 2 interacts with COIL. Isoform 4 interacts with APP and
CC EPHA8. Isoform 6 interacts with EPHA8. {ECO:0000250,
CC ECO:0000269|PubMed:15004329, ECO:0000269|PubMed:15347684,
CC ECO:0000269|PubMed:15862129, ECO:0000269|PubMed:17875921}.
CC -!- INTERACTION:
CC Q7Z6G8-1; P38432: COIL; NbExp=3; IntAct=EBI-20771343, EBI-945751;
CC Q7Z6G8-2; P38432: COIL; NbExp=3; IntAct=EBI-20771303, EBI-945751;
CC Q7Z6G8-3; Q9NQ75-2: CASS4; NbExp=3; IntAct=EBI-17714371, EBI-12270182;
CC Q7Z6G8-3; O75031: HSF2BP; NbExp=3; IntAct=EBI-17714371, EBI-7116203;
CC Q7Z6G8-3; O43639: NCK2; NbExp=3; IntAct=EBI-17714371, EBI-713635;
CC Q7Z6G8-3; P61586: RHOA; NbExp=3; IntAct=EBI-17714371, EBI-446668;
CC Q7Z6G8-3; Q13671: RIN1; NbExp=3; IntAct=EBI-17714371, EBI-366017;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15004329,
CC ECO:0000269|PubMed:15347684, ECO:0000269|PubMed:15862129,
CC ECO:0000269|PubMed:19666031}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Postsynaptic density. Cell
CC projection, dendritic spine. Nucleus. Nucleus, Cajal body. Note=The
CC synaptic localization requires DLG4 interaction. Translocation to the
CC nucleus in response to stimulation of NMDA receptors (NMDARs) in a
CC calcium-independent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus. Note=The interaction with
CC APP causes its partial exclusion from the nucleus, when APP is
CC overexpressed.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=AIDA-1b;
CC IsoId=Q7Z6G8-1; Sequence=Displayed;
CC Name=2; Synonyms=AIDA-1c;
CC IsoId=Q7Z6G8-2; Sequence=VSP_032702, VSP_032704, VSP_032707,
CC VSP_032710;
CC Name=3;
CC IsoId=Q7Z6G8-3; Sequence=VSP_032702, VSP_032704, VSP_032709,
CC VSP_032710;
CC Name=4; Synonyms=AIDA-1a;
CC IsoId=Q7Z6G8-4; Sequence=VSP_032702, VSP_032704, VSP_032711;
CC Name=5;
CC IsoId=Q7Z6G8-5; Sequence=VSP_032702, VSP_032704, VSP_032708,
CC VSP_032710;
CC Name=6; Synonyms=AIDA-1bDeltaAnk;
CC IsoId=Q7Z6G8-6; Sequence=VSP_032703, VSP_032705, VSP_032707;
CC Name=7;
CC IsoId=Q7Z6G8-7; Sequence=VSP_032702, VSP_032704, VSP_032707;
CC Name=8;
CC IsoId=Q7Z6G8-8; Sequence=VSP_032701, VSP_032706, VSP_032712;
CC Name=9;
CC IsoId=Q7Z6G8-9; Sequence=VSP_046414;
CC Name=10;
CC IsoId=Q7Z6G8-10; Sequence=VSP_046415, VSP_032707, VSP_032712;
CC -!- TISSUE SPECIFICITY: Highly expressed in marrow from patients with pre-B
CC ALL associated with the t(1;19) translocation. Strongly expressed in
CC brain and testis. Expressed in fetal brain. Isoform 4 is highly
CC expressed in brain (at protein level). Isoform 6 is expressed in brain
CC and several cancer cell lines. {ECO:0000269|PubMed:10490826,
CC ECO:0000269|PubMed:15347684}.
CC -!- INDUCTION: Transcriptionally up-regulated in t(1:19) pre-B cell acute
CC lymphocytic leukemia by the chimeric TCF3-PBX1. Not expressed in pre-B
CC cell that lack this translocation. {ECO:0000269|PubMed:10490826,
CC ECO:0000269|PubMed:16769578}.
CC -!- PTM: Isoform 3 nuclear translocation requires an NMDAR-dependent
CC proteolytic cleavage. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP38184.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY281131; AAP37612.1; -; mRNA.
DR EMBL; AY281132; AAP37613.1; -; mRNA.
DR EMBL; AY283057; AAP38184.2; ALT_INIT; mRNA.
DR EMBL; AY753193; AAV28691.1; -; mRNA.
DR EMBL; AF164792; AAF80756.1; -; mRNA.
DR EMBL; AK289768; BAF82457.1; -; mRNA.
DR EMBL; AK294191; BAG57507.1; -; mRNA.
DR EMBL; AK294994; BAG58059.1; -; mRNA.
DR EMBL; AC008126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC021653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC048330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026313; AAH26313.2; -; mRNA.
DR EMBL; BC068451; AAH68451.1; -; mRNA.
DR EMBL; BC142669; AAI42670.1; -; mRNA.
DR EMBL; BC150204; AAI50205.1; -; mRNA.
DR EMBL; AF145204; AAD33951.1; -; mRNA.
DR EMBL; AY620824; AAT39519.1; -; mRNA.
DR CCDS; CCDS55864.1; -. [Q7Z6G8-9]
DR CCDS; CCDS55865.1; -. [Q7Z6G8-8]
DR CCDS; CCDS55866.1; -. [Q7Z6G8-7]
DR CCDS; CCDS55867.1; -. [Q7Z6G8-2]
DR CCDS; CCDS55868.1; -. [Q7Z6G8-5]
DR CCDS; CCDS55869.1; -. [Q7Z6G8-4]
DR CCDS; CCDS55870.1; -. [Q7Z6G8-3]
DR CCDS; CCDS55871.1; -. [Q7Z6G8-10]
DR CCDS; CCDS55872.1; -. [Q7Z6G8-1]
DR RefSeq; NP_001190994.1; NM_001204065.1.
DR RefSeq; NP_001190995.1; NM_001204066.1. [Q7Z6G8-8]
DR RefSeq; NP_001190996.1; NM_001204067.1. [Q7Z6G8-10]
DR RefSeq; NP_001190997.1; NM_001204068.1. [Q7Z6G8-4]
DR RefSeq; NP_001190998.1; NM_001204069.1. [Q7Z6G8-5]
DR RefSeq; NP_001190999.1; NM_001204070.1. [Q7Z6G8-2]
DR RefSeq; NP_001191008.1; NM_001204079.1.
DR RefSeq; NP_001191009.1; NM_001204080.1.
DR RefSeq; NP_001191010.1; NM_001204081.1. [Q7Z6G8-9]
DR RefSeq; NP_064525.1; NM_020140.3. [Q7Z6G8-7]
DR RefSeq; NP_690001.3; NM_152788.4. [Q7Z6G8-1]
DR RefSeq; NP_858056.2; NM_181670.3. [Q7Z6G8-3]
DR PDB; 2EAM; NMR; -; A=808-874.
DR PDB; 2KE7; NMR; -; A=808-893.
DR PDB; 2KIV; NMR; -; A=812-946.
DR PDB; 2M38; NMR; -; A=1042-1194.
DR PDBsum; 2EAM; -.
DR PDBsum; 2KE7; -.
DR PDBsum; 2KIV; -.
DR PDBsum; 2M38; -.
DR AlphaFoldDB; Q7Z6G8; -.
DR SMR; Q7Z6G8; -.
DR BioGRID; 121229; 23.
DR DIP; DIP-41406N; -.
DR IntAct; Q7Z6G8; 13.
DR MINT; Q7Z6G8; -.
DR STRING; 9606.ENSP00000449629; -.
DR iPTMnet; Q7Z6G8; -.
DR PhosphoSitePlus; Q7Z6G8; -.
DR SwissPalm; Q7Z6G8; -.
DR BioMuta; ANKS1B; -.
DR DMDM; 332278155; -.
DR EPD; Q7Z6G8; -.
DR jPOST; Q7Z6G8; -.
DR MassIVE; Q7Z6G8; -.
DR MaxQB; Q7Z6G8; -.
DR PaxDb; Q7Z6G8; -.
DR PeptideAtlas; Q7Z6G8; -.
DR PRIDE; Q7Z6G8; -.
DR ProteomicsDB; 28297; -.
DR ProteomicsDB; 29375; -.
DR ProteomicsDB; 31007; -.
DR ProteomicsDB; 69401; -. [Q7Z6G8-1]
DR ProteomicsDB; 69402; -. [Q7Z6G8-2]
DR ProteomicsDB; 69403; -. [Q7Z6G8-3]
DR ProteomicsDB; 69404; -. [Q7Z6G8-4]
DR ProteomicsDB; 69405; -. [Q7Z6G8-5]
DR ProteomicsDB; 69406; -. [Q7Z6G8-6]
DR ProteomicsDB; 69407; -. [Q7Z6G8-7]
DR ProteomicsDB; 69408; -. [Q7Z6G8-8]
DR Antibodypedia; 57828; 157 antibodies from 21 providers.
DR DNASU; 56899; -.
DR Ensembl; ENST00000341752.11; ENSP00000345510.6; ENSG00000185046.20. [Q7Z6G8-9]
DR Ensembl; ENST00000546568.5; ENSP00000448205.1; ENSG00000185046.20. [Q7Z6G8-2]
DR Ensembl; ENST00000546960.5; ENSP00000447839.1; ENSG00000185046.20. [Q7Z6G8-4]
DR Ensembl; ENST00000547010.5; ENSP00000448512.1; ENSG00000185046.20. [Q7Z6G8-6]
DR Ensembl; ENST00000547446.5; ENSP00000450015.1; ENSG00000185046.20. [Q7Z6G8-10]
DR Ensembl; ENST00000547776.6; ENSP00000449629.2; ENSG00000185046.20. [Q7Z6G8-1]
DR Ensembl; ENST00000549025.6; ENSP00000447312.2; ENSG00000185046.20. [Q7Z6G8-8]
DR Ensembl; ENST00000549493.6; ENSP00000448203.2; ENSG00000185046.20. [Q7Z6G8-3]
DR Ensembl; ENST00000549558.6; ENSP00000448993.2; ENSG00000185046.20. [Q7Z6G8-7]
DR Ensembl; ENST00000550693.6; ENSP00000447999.2; ENSG00000185046.20. [Q7Z6G8-5]
DR GeneID; 56899; -.
DR KEGG; hsa:56899; -.
DR UCSC; uc001tgd.3; human. [Q7Z6G8-1]
DR CTD; 56899; -.
DR DisGeNET; 56899; -.
DR GeneCards; ANKS1B; -.
DR HGNC; HGNC:24600; ANKS1B.
DR HPA; ENSG00000185046; Group enriched (brain, skeletal muscle).
DR MIM; 607815; gene.
DR neXtProt; NX_Q7Z6G8; -.
DR OpenTargets; ENSG00000185046; -.
DR PharmGKB; PA128394692; -.
DR VEuPathDB; HostDB:ENSG00000185046; -.
DR eggNOG; KOG0507; Eukaryota.
DR GeneTree; ENSGT00940000154572; -.
DR HOGENOM; CLU_010379_0_0_1; -.
DR InParanoid; Q7Z6G8; -.
DR OrthoDB; 549581at2759; -.
DR TreeFam; TF320582; -.
DR PathwayCommons; Q7Z6G8; -.
DR SignaLink; Q7Z6G8; -.
DR SIGNOR; Q7Z6G8; -.
DR BioGRID-ORCS; 56899; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; ANKS1B; human.
DR EvolutionaryTrace; Q7Z6G8; -.
DR GeneWiki; ANKS1B; -.
DR GenomeRNAi; 56899; -.
DR Pharos; Q7Z6G8; Tbio.
DR PRO; PR:Q7Z6G8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z6G8; protein.
DR Bgee; ENSG00000185046; Expressed in Brodmann (1909) area 23 and 143 other tissues.
DR ExpressionAtlas; Q7Z6G8; baseline and differential.
DR Genevisible; Q7Z6G8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1900383; P:regulation of synaptic plasticity by receptor localization to synapse; IEA:InterPro.
DR CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR033636; ANKS1B.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041880; SAM_ANKS1_repeat1.
DR InterPro; IPR041882; SAM_ANKS1_repeat2.
DR PANTHER; PTHR24174:SF3; PTHR24174:SF3; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00454; SAM; 2.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cell projection; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1248
FT /note="Ankyrin repeat and sterile alpha motif domain-
FT containing protein 1B"
FT /id="PRO_0000327259"
FT REPEAT 2..31
FT /note="ANK 1"
FT REPEAT 58..87
FT /note="ANK 2"
FT REPEAT 91..120
FT /note="ANK 3"
FT REPEAT 127..156
FT /note="ANK 4"
FT REPEAT 160..189
FT /note="ANK 5"
FT REPEAT 193..222
FT /note="ANK 6"
FT REPEAT 225..254
FT /note="ANK 7"
FT DOMAIN 810..876
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 884..949
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1056..1213
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 296..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 935..938
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:19666031"
FT COMPBIAS 297..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6S7"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 773
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0C6S7"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6S7"
FT MOD_RES 901
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 1007
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT VAR_SEQ 1..994
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046414"
FT VAR_SEQ 1..831
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032701"
FT VAR_SEQ 1..774
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15004329,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15862129"
FT /id="VSP_032702"
FT VAR_SEQ 1..420
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15004329"
FT /id="VSP_032703"
FT VAR_SEQ 3..807
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046415"
FT VAR_SEQ 775..807
FT /note="SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR -> MMWQCHLSAQDYRYY
FT PVDGYSLLKRFPLHPLTG (in isoform 3, isoform 4, isoform 5,
FT isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15004329,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15862129"
FT /id="VSP_032704"
FT VAR_SEQ 804..807
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15004329"
FT /id="VSP_032705"
FT VAR_SEQ 927..1022
FT /note="VLKINLIGHRKRILASLGDRLHDDPPQKPPRSITLREPSGNHTPPQLSPSLS
FT QSTYTTGGSLDVPHIIMQGDARRRRNENYFDDIPRSKLERQMAQ -> QSSVCEIWTNQ
FT NAGFPFSAIHQVHN (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032706"
FT VAR_SEQ 963..1022
FT /note="Missing (in isoform 2, isoform 6, isoform 7 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15004329,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15862129"
FT /id="VSP_032707"
FT VAR_SEQ 963..1022
FT /note="EPSGNHTPPQLSPSLSQSTYTTGGSLDVPHIIMQGDARRRRNENYFDDIPRS
FT KLERQMAQ -> SSVCEIWTNQNAGFPFSAIHQVHN (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032708"
FT VAR_SEQ 1022
FT /note="Q -> QSSVCEIWTNQNAGFPFSAIHQVHN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032709"
FT VAR_SEQ 1225..1248
FT /note="DLLHASHTGQEPSERHTEEALRKF -> QIDPSEQKTLANLPWIVEPGQEAK
FT RGINTKYETTIF (in isoform 3, isoform 5 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15862129"
FT /id="VSP_032710"
FT VAR_SEQ 1225..1248
FT /note="DLLHASHTGQEPSERHTEEALRKF -> PFCFKADRPI (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15004329"
FT /id="VSP_032711"
FT VAR_SEQ 1225..1247
FT /note="DLLHASHTGQEPSERHTEEALRK -> IDPSEQKTLANLPWIVEPGQEAKRG
FT INTKYETTI (in isoform 8 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032712"
FT CONFLICT 290..291
FT /note="RS -> KYA (in Ref. 1; AAP37612)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="Q -> L (in Ref. 4; BAF82457)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="E -> G (in Ref. 6; AAI42670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160
FT /note="C -> R (in Ref. 4; BAG57507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="D -> G (in Ref. 4; BAG58059)"
FT /evidence="ECO:0000305"
FT HELIX 815..822
FT /evidence="ECO:0007829|PDB:2EAM"
FT HELIX 825..827
FT /evidence="ECO:0007829|PDB:2EAM"
FT HELIX 828..833
FT /evidence="ECO:0007829|PDB:2EAM"
FT TURN 834..837
FT /evidence="ECO:0007829|PDB:2KIV"
FT TURN 839..841
FT /evidence="ECO:0007829|PDB:2EAM"
FT STRAND 842..847
FT /evidence="ECO:0007829|PDB:2EAM"
FT HELIX 851..854
FT /evidence="ECO:0007829|PDB:2EAM"
FT HELIX 860..872
FT /evidence="ECO:0007829|PDB:2EAM"
FT HELIX 889..894
FT /evidence="ECO:0007829|PDB:2KIV"
FT TURN 895..897
FT /evidence="ECO:0007829|PDB:2KIV"
FT HELIX 901..908
FT /evidence="ECO:0007829|PDB:2KIV"
FT HELIX 913..916
FT /evidence="ECO:0007829|PDB:2KIV"
FT HELIX 921..927
FT /evidence="ECO:0007829|PDB:2KIV"
FT HELIX 933..943
FT /evidence="ECO:0007829|PDB:2KIV"
FT TURN 1056..1058
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1059..1074
FT /evidence="ECO:0007829|PDB:2M38"
FT HELIX 1078..1091
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1094..1097
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1104..1110
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1113..1121
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1124..1128
FT /evidence="ECO:0007829|PDB:2M38"
FT HELIX 1130..1132
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1133..1138
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1145..1150
FT /evidence="ECO:0007829|PDB:2M38"
FT TURN 1153..1155
FT /evidence="ECO:0007829|PDB:2M38"
FT STRAND 1156..1167
FT /evidence="ECO:0007829|PDB:2M38"
FT HELIX 1168..1186
FT /evidence="ECO:0007829|PDB:2M38"
FT CONFLICT Q7Z6G8-8:325
FT /note="P -> R (in Ref. 6; AAH68451)"
FT /evidence="ECO:0000305"
SQ 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
