CT2NL_MOUSE
ID CT2NL_MOUSE Reviewed; 638 AA.
AC Q99LJ0; Q6ZPR0; Q8BSV1; Q922L8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=CTTNBP2 N-terminal-like protein;
GN Name=Cttnbp2nl; Synonyms=Kiaa1433;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH CTTN, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Regulates lamellipodial actin dynamics in a CTTN-dependent
CC manner. {ECO:0000250|UniProtKB:Q8SX68}.
CC -!- SUBUNIT: May form homomers (By similarity). May interact with MOB4,
CC PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4, STRIP1 and STRIP2 (By
CC similarity). Interacts with CTTN/cortactin; this interaction may
CC redistribute CTTN to stress fibers. {ECO:0000250,
CC ECO:0000269|PubMed:23015759}.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q8SX68}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:23015759}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skin, also detectable in
CC spleen and lung (at protein level). Very low levels, if any, in brain
CC (at protein level).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98169.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129359; BAC98169.1; ALT_INIT; mRNA.
DR EMBL; AK029901; BAC26666.1; -; mRNA.
DR EMBL; AK030438; BAC26964.1; -; mRNA.
DR EMBL; BC003236; AAH03236.1; -; mRNA.
DR EMBL; BC006952; AAH06952.1; -; mRNA.
DR CCDS; CCDS17707.1; -.
DR RefSeq; NP_001156804.1; NM_001163332.1.
DR RefSeq; NP_001156805.1; NM_001163333.1.
DR RefSeq; NP_084525.1; NM_030249.4.
DR RefSeq; XP_011238590.1; XM_011240288.2.
DR AlphaFoldDB; Q99LJ0; -.
DR SMR; Q99LJ0; -.
DR BioGRID; 219770; 1.
DR STRING; 10090.ENSMUSP00000076751; -.
DR iPTMnet; Q99LJ0; -.
DR PhosphoSitePlus; Q99LJ0; -.
DR jPOST; Q99LJ0; -.
DR MaxQB; Q99LJ0; -.
DR PaxDb; Q99LJ0; -.
DR PeptideAtlas; Q99LJ0; -.
DR PRIDE; Q99LJ0; -.
DR ProteomicsDB; 285385; -.
DR Antibodypedia; 2021; 109 antibodies from 23 providers.
DR DNASU; 80281; -.
DR Ensembl; ENSMUST00000077548; ENSMUSP00000076751; ENSMUSG00000062127.
DR Ensembl; ENSMUST00000098763; ENSMUSP00000096359; ENSMUSG00000062127.
DR GeneID; 80281; -.
DR KEGG; mmu:80281; -.
DR UCSC; uc008quv.2; mouse.
DR CTD; 55917; -.
DR MGI; MGI:1933137; Cttnbp2nl.
DR VEuPathDB; HostDB:ENSMUSG00000062127; -.
DR eggNOG; KOG1103; Eukaryota.
DR GeneTree; ENSGT00950000182852; -.
DR HOGENOM; CLU_028813_1_0_1; -.
DR InParanoid; Q99LJ0; -.
DR OMA; MLVMECK; -.
DR OrthoDB; 660559at2759; -.
DR PhylomeDB; Q99LJ0; -.
DR TreeFam; TF325130; -.
DR BioGRID-ORCS; 80281; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cttnbp2nl; mouse.
DR PRO; PR:Q99LJ0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99LJ0; protein.
DR Bgee; ENSMUSG00000062127; Expressed in endothelial cell of lymphatic vessel and 248 other tissues.
DR ExpressionAtlas; Q99LJ0; baseline and differential.
DR Genevisible; Q99LJ0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0034763; P:negative regulation of transmembrane transport; ISO:MGI.
DR GO; GO:0032410; P:negative regulation of transporter activity; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF09727; CortBP2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..638
FT /note="CTTNBP2 N-terminal-like protein"
FT /id="PRO_0000226998"
FT REGION 280..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..284
FT /evidence="ECO:0000255"
FT COMPBIAS 360..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT CONFLICT 92
FT /note="N -> D (in Ref. 2; BAC26964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 69841 MW; 9E3CC4364E73972C CRC64;
MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI SDPLMALQRD
FETLKEKNDS EKQPVCTNPL SVLKAVMKQC KNMQERMLSQ LAAAESRHRK VILDLEEERQ
RHAQDTAEGD DVTYMLEKER ERLTQQLEFE KSQVKKFEKE QKKLSSQLEE ERTRHKQLSS
MLVLECRKAT SKAAEEGQKA GELSLKLDKE KSRASKLEEE LAAERKRGLQ TEAQVEKQLS
EFDIEREQLR AKLNREENRT RALKEEVESL KKLVKDLEAA QQHRSTSEQG REPVTMSRGT
ATEPPMRVSA FCQTESVQTE RSHGSVITKL TDTGLPGPTT AAYSYAKANG HCDPEIQTTR
ELTSDSSTEN QGPPREKSAV AAQEKPVENG GCPVGTETPV TMPSHLPSSG SSLSPSSTAS
SSLTSSPCSS PVLTKRLLGS AASSPGYQSS YQVGINQRFH AARHKFQSQA DQDQQASGLQ
SPPSRDLSPT LLDNSAAKQL ARNTVTQVLS RFTNQGPIKP VSPNSSPFGT DYRNLASTAS
PRGDTSHSPT PGKVSSPLSP LSPGIKSPTI PRAERGNPPP IPPKKPGLTP SQSATTPVTK
THSQASSLAA TEDLASSCSP SAVVANGKDV EILLPTSS
