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CTTB2_RAT
ID   CTTB2_RAT               Reviewed;        1649 AA.
AC   Q2IBD4; O88864;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Cortactin-binding protein 2;
DE            Short=CortBP2;
GN   Name=Cttnbp2;
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] (ISOFORM 2).
RX   PubMed=9813110; DOI=10.1046/j.1365-2443.1998.00216.x;
RA   Ohoka Y., Takai Y.;
RT   "Isolation and characterization of cortactin isoforms and a novel
RT   cortactin-binding protein, CBP90.";
RL   Genes Cells 3:603-612(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=12917688; DOI=10.1038/nature01858;
RA   Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA   Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA   Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA   Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA   Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA   Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA   Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA   Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA   Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA   Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA   Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA   Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA   Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA   Haussler D., Green P., Miller W., Green E.D.;
RT   "Comparative analyses of multi-species sequences from targeted genomic
RT   regions.";
RL   Nature 424:788-793(2003).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH CTTN, AND SUBCELLULAR LOCATION.
RX   PubMed=22262902; DOI=10.1523/jneurosci.4405-11.2012;
RA   Chen Y.K., Hsueh Y.P.;
RT   "Cortactin-binding protein 2 modulates the mobility of cortactin and
RT   regulates dendritic spine formation and maintenance.";
RL   J. Neurosci. 32:1043-1055(2012).
RN   [6]
RP   INTERACTION WITH STRN; STRN4 AND MOB4.
RX   PubMed=23015759; DOI=10.1091/mbc.e12-05-0365;
RA   Chen Y.K., Chen C.Y., Hu H.T., Hsueh Y.P.;
RT   "CTTNBP2, but not CTTNBP2NL, regulates dendritic spinogenesis and synaptic
RT   distribution of the striatin-PP2A complex.";
RL   Mol. Biol. Cell 23:4383-4392(2012).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, AND IDENTIFICATION BY
RP   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: Regulates the dendritic spine distribution of CTTN/cortactin
CC       in hippocampal neurons, and thus controls dendritic spinogenesis and
CC       dendritic spine maintenance. {ECO:0000269|PubMed:22262902}.
CC   -!- SUBUNIT: Interacts with CTTN/cortactin SH3 domain. Interacts with STRN,
CC       STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic
CC       spine distribution of STRN and STRN4 in hippocampal neurons. Activation
CC       of glutamate receptors weakens the interaction with STRN and STRN4.
CC       {ECO:0000269|PubMed:22262902, ECO:0000269|PubMed:23015759}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC       projection, dendritic spine {ECO:0000269|PubMed:22262902}. Note=Remains
CC       associated with dendritic spines even after glutamate stimulation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=CTTNBP2-L;
CC         IsoId=Q2IBD4-1; Sequence=Displayed;
CC       Name=2; Synonyms=CTTNBP2-S;
CC         IsoId=Q2IBD4-2; Sequence=VSP_046479, VSP_046480;
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DR   EMBL; AF053768; AAC35911.1; -; mRNA.
DR   EMBL; DP000027; AAR16316.1; -; Genomic_DNA.
DR   EMBL; AC087251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473959; EDM15128.1; -; Genomic_DNA.
DR   RefSeq; NP_001107873.1; NM_001114401.1. [Q2IBD4-1]
DR   AlphaFoldDB; Q2IBD4; -.
DR   SMR; Q2IBD4; -.
DR   BioGRID; 251850; 1.
DR   IntAct; Q2IBD4; 1.
DR   MINT; Q2IBD4; -.
DR   STRING; 10116.ENSRNOP00000011135; -.
DR   CarbonylDB; Q2IBD4; -.
DR   iPTMnet; Q2IBD4; -.
DR   PhosphoSitePlus; Q2IBD4; -.
DR   jPOST; Q2IBD4; -.
DR   PaxDb; Q2IBD4; -.
DR   PRIDE; Q2IBD4; -.
DR   Ensembl; ENSRNOT00000087167; ENSRNOP00000072761; ENSRNOG00000061845. [Q2IBD4-1]
DR   GeneID; 282587; -.
DR   KEGG; rno:282587; -.
DR   UCSC; RGD:628691; rat. [Q2IBD4-1]
DR   CTD; 83992; -.
DR   RGD; 628691; Cttnbp2.
DR   eggNOG; ENOG502QWG2; Eukaryota.
DR   GeneTree; ENSGT00940000158293; -.
DR   HOGENOM; CLU_004926_0_0_1; -.
DR   InParanoid; Q2IBD4; -.
DR   OMA; MCPVEAL; -.
DR   OrthoDB; 264951at2759; -.
DR   PhylomeDB; Q2IBD4; -.
DR   TreeFam; TF325130; -.
DR   PRO; PR:Q2IBD4; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Proteomes; UP000234681; Chromosome 4.
DR   Bgee; ENSRNOG00000061845; Expressed in frontal cortex and 18 other tissues.
DR   Genevisible; Q2IBD4; RN.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR   GO; GO:0007420; P:brain development; IEP:RGD.
DR   GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR   GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR019131; Cortactin-binding_p2_N.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF09727; CortBP2; 2.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cell projection; Coiled coil; Cytoplasm;
KW   Methylation; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT   CHAIN           1..1649
FT                   /note="Cortactin-binding protein 2"
FT                   /id="PRO_0000422173"
FT   REPEAT          699..729
FT                   /note="ANK 1"
FT   REPEAT          733..762
FT                   /note="ANK 2"
FT   REPEAT          766..795
FT                   /note="ANK 3"
FT   REPEAT          799..828
FT                   /note="ANK 4"
FT   REPEAT          832..861
FT                   /note="ANK 5"
FT   REPEAT          901..931
FT                   /note="ANK 6"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1527..1649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          118..275
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        330..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1532..1546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1569..1590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1603..1632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1633..1649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         495
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT   MOD_RES         1510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   VAR_SEQ         626..630
FT                   /note="VGAWP -> AGHPP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9813110"
FT                   /id="VSP_046479"
FT   VAR_SEQ         631..1649
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9813110"
FT                   /id="VSP_046480"
FT   CONFLICT        163
FT                   /note="R -> K (in Ref. 1; AAC35911)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="K -> Q (in Ref. 1; AAC35911)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="L -> F (in Ref. 1; AAC35911)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1649 AA;  178768 MW;  12C85BF86EB2634B CRC64;
     MATDSASCEP DLSRAPGDAE GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK PVCTNPLSIL EAVMAHCRKM
     QERMSAQLAA AESRQKKLEM EKLQLQALEQ EHKKLAAHLE EERGKNKHVV LMLVKECKQL
     SGKVVEEAQK LEEVMVKLEE EKKKTSELED QLSAEKQRSA GMEAQLEKQL FEFDTEREQL
     RAKLTREEAH TTDLKEEIDK MKKMMEQMKK GNDGKPGLSL PRKTKDKRLA SISVATEGPV
     TRSVACQTDV VTESTDPVKK LPLSVPIKPS TGSPLVSTNT KGNVGPSALL IRPGIDRQAS
     HSDLGPSPPT ALPSSASRIE ENGPSAGNAP DLSNSTPSTP SGTAPAAAQT LGAAPQNHSQ
     APPVHSLHSP CANTHPGLNP RIQAARFRFQ GNANDPDQNG NNTQSPPSRD VSPTSRDNLV
     AKQLARNTVT QALSRFTSPQ AGASSRLGAS PGGDAGTCPP VGRTGLKTPG AARVDRGNPP
     PIPPKKPGLS QTPSPPHPQL RASNAGAKVD NKIVASPPST LPQGTKVVNE ENVPKSSSPQ
     LPPKPSIDLT VASAGCPVSA LATSQVGAWP AETPGLNQPA CTDSSLVIPT TVAFRSSINP
     VSASSRSPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ GNVTLLSMLL
     NEEGLDINYC CEDSHSALYS AAKNGHTDCV RLLLNAEARV DAADKNGFTP LCVAAAQGHF
     ECIELLTAYN ANINHSAAGG QTPLYLACKT GNKECIKLLL EAGTDRSIKT RDGWTPIHAA
     VDTGNVDSLK LLMYHRVPAP GNSLSAEEPK SGLFSLNGGE SPPGSSKPVV PADLINHADK
     EGWTAAHIAA SKGFKNCLEI LCRHGGLEPE RRDKCNRTVH DVATDDCKHL LENLNALKIP
     LRISVGEIQP SNDGSDDFEC EHTICTLNIR KQTSWEDFSK AVSQALTNHF QAISSDGCWG
     LEDGTLNNTT DSCIGLGTSS IQSIMLGSIP WSTGQSFSQS PWDFMKKKKV EQVTVLLSGP
     QEGCLSSVTY TSMIPLQMLQ NYLRLVEQYH NVIFHGPEGS LQDYIANQLA LCMKHRQMAA
     GFPCEIVRAE VDSGFSKEQL VDVFISNACL IPVKQFPVKK KIIVILENLE KSSLSELLGD
     FLAPLENRST ESPCTFQKGN GTSECYYFHE NCFLLGTLAK ACLQGSDLLV QQHFRWVQLR
     WDCEPSQGLL QRFLRRKAVS KFRGQLPAPC DPVCKIVDWV ISVWRQLNSC LARLGTPEAL
     LGPKYFLSCP VVPGHAQATV KWMSKLWNAI IAPRVQEAIL SRAAMNKQPG ARQTASKKHP
     SQGQQAVVRA ALSILLNKAI LHGCPLPRTE LDQQIADFKG GSFPLSIVSS YSKKKGESAA
     WRKVNTSPRK KPGHFSSPMW NKPDLKHEGM RNKSVPHLNI NRSSSLSKQQ SLENDLSMTL
     TLDHRLSLGS DDEADLVKEL QSMCSSKSES DISKIADSRE DLRTFDSSRT NPVTSAPVNL
     RMPVPQKEAS PLSSHQTTEC SNSKSKTELG VSRVKSFLPV PRSKVAQCSQ NTKRSSSSSS
     NTRQLEINNN SKEENWNVDK HEHVEKRNK
 
 
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