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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_RAT               Reviewed;        1260 AA.
P0C6S7;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 1.
25-OCT-2017, entry version 75.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION
WITH DLG4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
935-HIS--ARG-938, AND PROTEOLYTIC CLEAVAGE.
TISSUE=Brain;
PubMed=17334360; DOI=10.1038/nn1867;
Jordan B.A., Fernholz B.D., Khatri L., Ziff E.B.;
"Activity-dependent AIDA-1 nuclear signaling regulates nucleolar
numbers and protein synthesis in neurons.";
Nat. Neurosci. 10:427-435(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 3), AND SUBCELLULAR
LOCATION.
PubMed=15169875; DOI=10.1074/mcp.M400045-MCP200;
Jordan B.A., Fernholz B.D., Boussac M., Xu C., Grigorean G.,
Ziff E.B., Neubert T.A.;
"Identification and verification of novel rodent postsynaptic density
proteins.";
Mol. Cell. Proteomics 3:857-871(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; THR-773 AND
SER-775, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Isoform 2 may participate in the regulation of
nucleoplasmic coilin protein interactions in neuronal and
transformed cells. {ECO:0000269|PubMed:17334360}.
-!- FUNCTION: Isoform 3 can regulate global protein synthesis by
altering nucleolar numbers. {ECO:0000269|PubMed:17334360}.
-!- SUBUNIT: Interacts with EPHA8 (By similarity). Isoform 2 interacts
with COIL. Isoform 3 interacts with DLG4. {ECO:0000250,
ECO:0000269|PubMed:17334360}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P0C6S7-1; Sequence=Displayed;
Name=2; Synonyms=AIDA-1e;
IsoId=P0C6S7-2; Sequence=VSP_032720, VSP_032721, VSP_032723;
Name=3; Synonyms=AIDA-1d;
IsoId=P0C6S7-3; Sequence=VSP_032720, VSP_032721, VSP_032722;
-!- TISSUE SPECIFICITY: Isoform 3 is brain specific and highly
enriched in the postsynaptic densities (PSDs), especially in
cortical, striatal and hippocampal PSDs.
{ECO:0000269|PubMed:17334360}.
-!- PTM: Nuclear translocation of isoform 3 requires an NMDAR-
dependent proteolytic cleavage. A 35 kDa N-terminal form shuttles
to the nucleus. {ECO:0000269|PubMed:17334360}.
-----------------------------------------------------------------------
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EMBL; AABR03061338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03058184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03058315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03059811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03060233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03056177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03057703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03056626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03056332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03055414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03055479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03055359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03058062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_006241311.1; XM_006241249.3. [P0C6S7-2]
UniGene; Rn.147770; -.
ProteinModelPortal; P0C6S7; -.
SMR; P0C6S7; -.
BioGrid; 260815; 1.
iPTMnet; P0C6S7; -.
PhosphoSitePlus; P0C6S7; -.
SwissPalm; P0C6S7; -.
PaxDb; P0C6S7; -.
PRIDE; P0C6S7; -.
GeneID; 314721; -.
CTD; 56899; -.
RGD; 1565556; Anks1b.
eggNOG; ENOG410JDN1; Eukaryota.
eggNOG; ENOG41119JC; LUCA.
HOGENOM; HOG000033973; -.
HOVERGEN; HBG050506; -.
InParanoid; P0C6S7; -.
PhylomeDB; P0C6S7; -.
PRO; PR:P0C6S7; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0097120; P:receptor localization to synapse; IMP:MGI.
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_dom-like.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
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;
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 1260 Ankyrin repeat and sterile alpha motif
domain-containing protein 1B.
/FTId=PRO_0000327261.
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:0000250}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 504 504 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 739 739 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIZ1}.
MOD_RES 773 773 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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 1 771 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:17334360}.
/FTId=VSP_032720.
VAR_SEQ 772 807 RTPSFTSEWEEIDKIMNSIDVGINSELEGMNGEATR -> M
MWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:17334360}.
/FTId=VSP_032721.
VAR_SEQ 963 1022 Missing (in isoform 2).
{ECO:0000303|PubMed:17334360}.
/FTId=VSP_032723.
VAR_SEQ 1022 1022 Q -> QSSVCEIWTNQNAGFPFSAIHQVHN (in
isoform 3).
{ECO:0000303|PubMed:17334360}.
/FTId=VSP_032722.
MUTAGEN 935 938 HRKR->AAAA: Does not shuttle to the
nucleus in response to NMDA stimulation.
{ECO:0000269|PubMed:17334360}.
MUTAGEN 1000 1003 RRRR->AAAA: Shuttles to the nucleus is
irrespective of NMDA stimulation.
SEQUENCE 1260 AA; 139207 MW; C7C71F67C349C50D CRC64;
MGKDQELLEA ARTGNVALVE KLLSGRKGGI LGGGSGPLPL SNLLSIWRGP NVNCTDSSGY
TALHHAALNG HKDIVLKLLQ FEASTNVADN KGYFPIHLAA WKGDVEIVKI LIHHGPSHSR
VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPTIRNSK LETPLDLAAL YGRLRVVKMI
ISAHPNLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEAALFGKVD
VVRVLLETGI DANIKDSLGR TVLDILKEHP SQKSLQIATL LQDYLEGVGR SVVLEEEHAQ
EDTAQETRLS SPAQSPSQKT KSETVTGELS KLLDEIKLCQ EKDYSFEDLC HTISDHYLDN
LSKISEEELG KNGSQSVRTS STINLSPGEV EDEEEDPNSC GPTGLWEALT PCNGCRNLGF
PMLAQESYPK KRNYPMEIVP SASLDTFPSE NENFLCELVD TAVTKKPCSL EIARAPSPRT
DNASEVAITA PGTGHHRNSS TGPTPDCSPP SPDTALKNIV KVIRPQPKQR TSIVSSLDFQ
RMNHNQEYFE ISTSTGCTSF TSSPPVSPPT SSVETTEIKN EGAEHTDDLS QQEDDEPPKE
YDAGQFAGLL HGSSPACEAP ENPFHLYGKR NQGEDGQEEA SLANSPLPFK QTPIENNPEP
SVKKIKPKVV SRTIFHKRSH QLENHTIVGT RMSRGGSRNG DQWGVNPGGF VERACTLGRI
RSLPKALIDM HLSKNVSKSD SDLIAYPSKD KARVNWSKSS TAERSSKDNS ERTPSFTSEW
EEIDKIMNSI DVGINSELEG MNGEATRPRC PVQTVGQWLE SIGLPQYENH LTANGFDNVQ
FMGSNVMEDQ DLLEIGILNS GHRQRILQAI QLLPKMRPIG HDGYHPTSVA EWLDSIELGD
YTKAFLINGY TSMDLLKKIW ELELINVLKI SLIGHRKRIL ASLGDRLHED PPQKPPRSIT
LREPSGNHTP PQLSPSLSQS TYTTGGSLDV PHIIMQGDAR RRRNENYFDD IPRSKLERQM
AQTGDWGEPS ITLRPPNEAT ASTPVQYWQH HPEKLIFQSC DYKAFYLGSM LIKELRGTES
TQDACAKMRA NCQKSTEQMK KVPTIILSVS YKGVKFIDAA NKNIIAEHEI RNISCAAQDP
EDLSTFAYIT KDLKSNHHYC HVFTAFDVNL AYEIILTLGQ AFEVAYQLAL QARKGGHSST
LPESFENKPS KPIPKPRVSI RKSVQIDPSE QKTLANLPWI VEPGQEAKRG INTKYETTIF


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