CTTB2_HUMAN
ID CTTB2_HUMAN Reviewed; 1663 AA.
AC Q8WZ74; O43389; Q7LG11; Q9C0A5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=C7orf8, CORTBP2, KIAA1758;
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], VARIANT VAL-1213, AND TISSUE SPECIFICITY.
RX PubMed=11707066; DOI=10.1006/geno.2001.6651;
RA Cheung J., Petek E., Nakabayashi K., Tsui L.-C., Vincent J.B.,
RA Scherer S.W.;
RT "Identification of the human cortactin-binding protein-2 gene from the
RT autism candidate region at 7q31.";
RL Genomics 78:7-11(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stacy R., Subramanian S., Deodato C., Burkhardt P., Song Y., Paddock M.,
RA Chang J., Zhou Y., Haugen E., Waring D., Chapman P., Hayden H., Levy R.,
RA Wu Z., Rouse G., James R., Phelps K., Olson M.V., Kaul R.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1663.
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin
CC in hippocampal neurons, thus controls dendritic spinogenesis and
CC dendritic spine maintenance. {ECO:0000250}.
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:0000250}.
CC -!- INTERACTION:
CC Q8WZ74; Q8WYA1-3: ARNTL2; NbExp=3; IntAct=EBI-1774260, EBI-12268276;
CC Q8WZ74; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-1774260, EBI-12845222;
CC Q8WZ74; O75031: HSF2BP; NbExp=3; IntAct=EBI-1774260, EBI-7116203;
CC Q8WZ74; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1774260, EBI-6509505;
CC Q8WZ74; P02533: KRT14; NbExp=3; IntAct=EBI-1774260, EBI-702178;
CC Q8WZ74; P43364: MAGEA11; NbExp=3; IntAct=EBI-1774260, EBI-739552;
CC Q8WZ74; A8MW99: MEI4; NbExp=3; IntAct=EBI-1774260, EBI-19944212;
CC Q8WZ74; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-1774260, EBI-2692890;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Note=Remains associated with
CC dendritic spines even after glutamate stimulation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest expression in brain. Also expressed in
CC kidney, pancreas, lung, heart, liver, skeletal muscle and placenta.
CC {ECO:0000269|PubMed:11707066}.
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DR EMBL; AF377960; AAL32176.1; -; mRNA.
DR EMBL; DQ354388; ABC79049.1; -; Genomic_DNA.
DR EMBL; DQ354389; ABC79051.1; -; Genomic_DNA.
DR EMBL; DQ354390; ABC79053.1; -; Genomic_DNA.
DR EMBL; DQ354391; ABC79055.1; -; Genomic_DNA.
DR EMBL; DQ356257; ABC87052.1; -; Genomic_DNA.
DR EMBL; DQ356259; ABC87056.1; -; Genomic_DNA.
DR EMBL; DQ356260; ABC87058.1; -; Genomic_DNA.
DR EMBL; DQ356261; ABC87060.1; -; Genomic_DNA.
DR EMBL; DQ356262; ABC87062.1; -; Genomic_DNA.
DR EMBL; DQ356264; ABC87066.1; -; Genomic_DNA.
DR EMBL; AC004240; AAC04501.2; -; Genomic_DNA.
DR EMBL; BC106000; AAI06001.1; -; mRNA.
DR EMBL; AB051545; BAB21849.1; -; mRNA.
DR CCDS; CCDS5774.1; -.
DR RefSeq; NP_219499.1; NM_033427.2.
DR AlphaFoldDB; Q8WZ74; -.
DR SMR; Q8WZ74; -.
DR BioGRID; 123842; 47.
DR IntAct; Q8WZ74; 38.
DR STRING; 9606.ENSP00000160373; -.
DR GlyGen; Q8WZ74; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8WZ74; -.
DR PhosphoSitePlus; Q8WZ74; -.
DR BioMuta; CTTNBP2; -.
DR DMDM; 74751641; -.
DR EPD; Q8WZ74; -.
DR jPOST; Q8WZ74; -.
DR MassIVE; Q8WZ74; -.
DR MaxQB; Q8WZ74; -.
DR PaxDb; Q8WZ74; -.
DR PeptideAtlas; Q8WZ74; -.
DR PRIDE; Q8WZ74; -.
DR ProteomicsDB; 75231; -.
DR Antibodypedia; 3970; 95 antibodies from 19 providers.
DR DNASU; 83992; -.
DR Ensembl; ENST00000160373.8; ENSP00000160373.3; ENSG00000077063.11.
DR GeneID; 83992; -.
DR KEGG; hsa:83992; -.
DR MANE-Select; ENST00000160373.8; ENSP00000160373.3; NM_033427.3; NP_219499.1.
DR UCSC; uc003vjf.4; human.
DR CTD; 83992; -.
DR DisGeNET; 83992; -.
DR GeneCards; CTTNBP2; -.
DR HGNC; HGNC:15679; CTTNBP2.
DR HPA; ENSG00000077063; Tissue enhanced (brain).
DR MIM; 609772; gene.
DR neXtProt; NX_Q8WZ74; -.
DR OpenTargets; ENSG00000077063; -.
DR PharmGKB; PA26774; -.
DR VEuPathDB; HostDB:ENSG00000077063; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR GeneTree; ENSGT00940000158293; -.
DR HOGENOM; CLU_004926_0_0_1; -.
DR InParanoid; Q8WZ74; -.
DR OMA; MCPVEAL; -.
DR OrthoDB; 264951at2759; -.
DR PhylomeDB; Q8WZ74; -.
DR TreeFam; TF325130; -.
DR PathwayCommons; Q8WZ74; -.
DR SignaLink; Q8WZ74; -.
DR BioGRID-ORCS; 83992; 6 hits in 1067 CRISPR screens.
DR ChiTaRS; CTTNBP2; human.
DR GeneWiki; CTTNBP2; -.
DR GenomeRNAi; 83992; -.
DR Pharos; Q8WZ74; Tbio.
DR PRO; PR:Q8WZ74; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WZ74; protein.
DR Bgee; ENSG00000077063; Expressed in cortical plate and 165 other tissues.
DR ExpressionAtlas; Q8WZ74; baseline and differential.
DR Genevisible; Q8WZ74; HS.
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; IBA:GO_Central.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0050807; P:regulation of synapse organization; IBA:GO_Central.
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; PF12796; Ank_2; 2.
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 ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1663
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000227002"
FT REPEAT 709..739
FT /note="ANK 1"
FT REPEAT 743..772
FT /note="ANK 2"
FT REPEAT 776..805
FT /note="ANK 3"
FT REPEAT 809..838
FT /note="ANK 4"
FT REPEAT 842..871
FT /note="ANK 5"
FT REPEAT 912..942
FT /note="ANK 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 393..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 498
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 1148
FT /note="Q -> K (in dbSNP:rs10274022)"
FT /id="VAR_048294"
FT VARIANT 1213
FT /note="L -> V (in dbSNP:rs62617115)"
FT /evidence="ECO:0000269|PubMed:11707066"
FT /id="VAR_025535"
SQ SEQUENCE 1663 AA; 181051 MW; 367B933A177D6E3B CRC64;
MATDGASCEP DLSRAPEDAA GAAAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGDKEK KPVCTNPLSI LEAVMAHCKK
MQERMSAQLA AAESRQKKLE MEKLQLQALE QEHKKLAARL EEERGKNKQV VLMLVKECKQ
LSGKVIEEAQ KLEDVMAKLE EEKKKTNELE EELSAEKRRS TEMEAQMEKQ LSEFDTEREQ
LRAKLNREEA HTTDLKEEID KMRKMIEQLK RGSDSKPSLS LPRKTKDRRL VSISVGTEGT
VTRSVACQTD LVTENADHMK KLPLTMPVKP STGSPLVSAN AKGSVCTSAT MARPGIDRQA
SYGDLIGASV PAFPPPSANK IEENGPSTGS TPDPTSSTPP LPSNAAPPTA QTPGIAPQNS
QAPPMHSLHS PCANTSLHPG LNPRIQAARF RFQGNANDPD QNGNTTQSPP SRDVSPTSRD
NLVAKQLARN TVTQALSRFT SPQAGAPSRP GVPPTGDVGT HPPVGRTSLK THGVARVDRG
NPPPIPPKKP GLSQTPSPPH PQLKVIIDSS RASNTGAKVD NKTVASTPSS LPQGNRVINE
ENLPKSSSPQ LPPKPSIDLT VAPAGCAVSA LATSQVGAWP AATPGLNQPA CSDSSLVIPT
TIAFCSSINP VSASSCRPGA SDSLLVTASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ
GNVTLLSMLL NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLSAEAQV NAADKNGFTP
LCAAAAQGHF ECVELLISYD ANINHAADGG QTPLYLACKN GNKECIKLLL EAGTNRSVKT
TDGWTPVHAA VDTGNVDSLK LLMYHRIPAH GNSFNEEESE SSVFDLDGGE ESPEGISKPV
VPADLINHAN REGWTAAHIA ASKGFKNCLE ILCRHGGLEP ERRDKCNRTV HDVATDDCKH
LLENLNALKI PLRISVGEIE PSNYGSDDLE CENTICALNI RKQTSWDDFS KAVSQALTNH
FQAISSDGWW SLEDVTCNNT TDSNIGLSAR SIRSITLGNV PWSVGQSFAQ SPWDFMRKNK
AEHITVLLSG PQEGCLSSVT YASMIPLQMM QNYLRLVEQY HNVIFHGPEG SLQDYIVHQL
ALCLKHRQMA AGFSCEIVRA EVDAGFSKEQ LLDLFISSAC LIPVKQSPSK KKIIIILENL
EKSSLSELLR DFLAPLENRS TESPCTFQKG NGLSECYYFH ENCFLMGTIA KACLQGSDLL
VQQHFRWVQL RWDGEPMQGL LQRFLRRKVV NKFKGQAPSP CDPVCKIVDW ALSVWRQLNS
CLARLGTPEA LLGPKYFLSC PVVPGHAQVT VKWMSKLWNG VIAPRVQEAI LSRASVKRQP
GFGQTTAKRH PSQGQQAVVK AALSILLNKA VLHGCPLPRA ELDQHTADFK GGSFPLSIVS
SYNTCNKKKG ESGAWRKVNT SPRRKSGRFS LPTWNKPDLS TEGMKNKTIS QLNCNRNASL
SKQKSLENDL SLTLNLDQRL SLGSDDEADL VKELQSMCSS KSESDISKIA DSRDDLRMFD
SSGNNPVLSA TINNLRMPVS QKEVSPLSSH QTTECSNSKS KTELGVSRVK SFLPVPRSKV
TQCSQNTKRS SSSSNTRQIE INNNSKEVNW NLHKNEHLEK PNK
