ANS1B_RAT
ID ANS1B_RAT Reviewed; 1260 AA.
AC P0C6S7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH
RP DLG4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP 935-HIS--ARG-938, AND PROTEOLYTIC CLEAVAGE.
RC TISSUE=Brain;
RX PubMed=17334360; DOI=10.1038/nn1867;
RA Jordan B.A., Fernholz B.D., Khatri L., Ziff E.B.;
RT "Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers
RT and protein synthesis in neurons.";
RL Nat. Neurosci. 10:427-435(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 3), AND SUBCELLULAR LOCATION.
RX PubMed=15169875; DOI=10.1074/mcp.m400045-mcp200;
RA Jordan B.A., Fernholz B.D., Boussac M., Xu C., Grigorean G., Ziff E.B.,
RA Neubert T.A.;
RT "Identification and verification of novel rodent postsynaptic density
RT proteins.";
RL Mol. Cell. Proteomics 3:857-871(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; THR-773 AND SER-775, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Isoform 2 may participate in the regulation of nucleoplasmic
CC coilin protein interactions in neuronal and transformed cells.
CC {ECO:0000269|PubMed:17334360}.
CC -!- FUNCTION: Isoform 3 can regulate global protein synthesis by altering
CC nucleolar numbers. {ECO:0000269|PubMed:17334360}.
CC -!- SUBUNIT: Interacts with EPHA8 (By similarity). Isoform 2 interacts with
CC COIL. Isoform 3 interacts with DLG4. {ECO:0000250,
CC ECO:0000269|PubMed:17334360}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P0C6S7-1; Sequence=Displayed;
CC Name=2; Synonyms=AIDA-1e;
CC IsoId=P0C6S7-2; Sequence=VSP_032720, VSP_032721, VSP_032723;
CC Name=3; Synonyms=AIDA-1d;
CC IsoId=P0C6S7-3; Sequence=VSP_032720, VSP_032721, VSP_032722;
CC -!- TISSUE SPECIFICITY: Isoform 3 is brain specific and highly enriched in
CC the postsynaptic densities (PSDs), especially in cortical, striatal and
CC hippocampal PSDs. {ECO:0000269|PubMed:17334360}.
CC -!- PTM: Nuclear translocation of isoform 3 requires an NMDAR-dependent
CC proteolytic cleavage. A 35 kDa N-terminal form shuttles to the nucleus.
CC {ECO:0000269|PubMed:17334360}.
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DR EMBL; AABR03061338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03059811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03060233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03057703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03055414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03055479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03055359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006241311.1; XM_006241249.3. [P0C6S7-2]
DR AlphaFoldDB; P0C6S7; -.
DR SMR; P0C6S7; -.
DR BioGRID; 260815; 2.
DR IntAct; P0C6S7; 1.
DR MINT; P0C6S7; -.
DR STRING; 10116.ENSRNOP00000056036; -.
DR iPTMnet; P0C6S7; -.
DR PhosphoSitePlus; P0C6S7; -.
DR SwissPalm; P0C6S7; -.
DR PaxDb; P0C6S7; -.
DR PRIDE; P0C6S7; -.
DR Ensembl; ENSRNOT00000119672; ENSRNOP00000083437; ENSRNOG00000024870. [P0C6S7-2]
DR GeneID; 314721; -.
DR CTD; 56899; -.
DR RGD; 1565556; Anks1b.
DR eggNOG; KOG0507; Eukaryota.
DR GeneTree; ENSGT00940000154572; -.
DR InParanoid; P0C6S7; -.
DR OrthoDB; 549581at2759; -.
DR PhylomeDB; P0C6S7; -.
DR PRO; PR:P0C6S7; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0097120; P:receptor localization to synapse; IMP:MGI.
DR GO; GO:1900383; P:regulation of synaptic plasticity by receptor localization to synapse; ISO:RGD.
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 Alternative splicing; ANK repeat; Cell projection; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1260
FT /note="Ankyrin repeat and sterile alpha motif domain-
FT containing protein 1B"
FT /id="PRO_0000327261"
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 298..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 935..938
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 305..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIZ1"
FT MOD_RES 773
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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..771
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17334360"
FT /id="VSP_032720"
FT VAR_SEQ 772..807
FT /note="RTPSFTSEWEEIDKIMNSIDVGINSELEGMNGEATR -> MMWQCHLSAQDY
FT RYYPVDGYSLLKRFPLHPLTG (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17334360"
FT /id="VSP_032721"
FT VAR_SEQ 963..1022
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17334360"
FT /id="VSP_032723"
FT VAR_SEQ 1022
FT /note="Q -> QSSVCEIWTNQNAGFPFSAIHQVHN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17334360"
FT /id="VSP_032722"
FT MUTAGEN 935..938
FT /note="HRKR->AAAA: Does not shuttle to the nucleus in
FT response to NMDA stimulation."
FT /evidence="ECO:0000269|PubMed:17334360"
FT MUTAGEN 1000..1003
FT /note="RRRR->AAAA: Shuttles to the nucleus is irrespective
FT of NMDA stimulation."
SQ 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
