CD2B2_MOUSE
ID CD2B2_MOUSE Reviewed; 342 AA.
AC Q9CWK3; Q3TJX5;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=CD2 antigen cytoplasmic tail-binding protein 2;
DE Short=CD2 cytoplasmic domain-binding protein 2;
DE Short=CD2 tail-binding protein 2;
GN Name=Cd2bp2;
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 STRAIN=C57BL/6J; TISSUE=Embryo, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP
CC complex that is involved in spliceosome assembly. {ECO:0000250}.
CC -!- SUBUNIT: Component of the U5 snRNP complex composed of the U5 snRNA and
CC at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23, TXNL4A and
CC CD2BP2. Interacts directly with TXNL4A and PRPF6. Interacts (via GYF
CC domain) with CD2 (via Pro-rich sequence in the cytoplasmic domain).
CC Interacts with PQBP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly nuclear. {ECO:0000250}.
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DR EMBL; BC006920; AAH06920.1; -; mRNA.
DR EMBL; AK010582; BAB27044.1; -; mRNA.
DR EMBL; AK030393; BAC26940.1; -; mRNA.
DR EMBL; AK031694; BAC27518.1; -; mRNA.
DR EMBL; AK034689; BAC28798.1; -; mRNA.
DR EMBL; AK167249; BAE39370.1; -; mRNA.
DR CCDS; CCDS21859.1; -.
DR RefSeq; NP_001272834.1; NM_001285905.1.
DR RefSeq; NP_001272835.1; NM_001285906.1.
DR RefSeq; NP_001272836.1; NM_001285907.1.
DR RefSeq; NP_081629.1; NM_027353.4.
DR RefSeq; XP_006508260.1; XM_006508197.2.
DR RefSeq; XP_006508261.1; XM_006508198.3.
DR AlphaFoldDB; Q9CWK3; -.
DR SMR; Q9CWK3; -.
DR BioGRID; 213930; 1.
DR STRING; 10090.ENSMUSP00000132963; -.
DR iPTMnet; Q9CWK3; -.
DR PhosphoSitePlus; Q9CWK3; -.
DR EPD; Q9CWK3; -.
DR jPOST; Q9CWK3; -.
DR MaxQB; Q9CWK3; -.
DR PaxDb; Q9CWK3; -.
DR PRIDE; Q9CWK3; -.
DR ProteomicsDB; 283747; -.
DR Antibodypedia; 27184; 195 antibodies from 30 providers.
DR DNASU; 70233; -.
DR Ensembl; ENSMUST00000035771; ENSMUSP00000044790; ENSMUSG00000042502.
DR Ensembl; ENSMUST00000166791; ENSMUSP00000132963; ENSMUSG00000042502.
DR Ensembl; ENSMUST00000205316; ENSMUSP00000145888; ENSMUSG00000042502.
DR Ensembl; ENSMUST00000206026; ENSMUSP00000146167; ENSMUSG00000042502.
DR GeneID; 70233; -.
DR KEGG; mmu:70233; -.
DR UCSC; uc009juj.2; mouse.
DR CTD; 10421; -.
DR MGI; MGI:1917483; Cd2bp2.
DR VEuPathDB; HostDB:ENSMUSG00000042502; -.
DR eggNOG; KOG2950; Eukaryota.
DR GeneTree; ENSGT00390000012483; -.
DR HOGENOM; CLU_062973_0_0_1; -.
DR InParanoid; Q9CWK3; -.
DR OMA; VRKCGEN; -.
DR OrthoDB; 773475at2759; -.
DR PhylomeDB; Q9CWK3; -.
DR TreeFam; TF313042; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 70233; 17 hits in 75 CRISPR screens.
DR ChiTaRS; Cd2bp2; mouse.
DR PRO; PR:Q9CWK3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CWK3; protein.
DR Bgee; ENSMUSG00000042502; Expressed in saccule of membranous labyrinth and 248 other tissues.
DR ExpressionAtlas; Q9CWK3; baseline and differential.
DR Genevisible; Q9CWK3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005682; C:U5 snRNP; ISO:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR039905; CD2BP2/Lin1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR PANTHER; PTHR13138; PTHR13138; 1.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..342
FT /note="CD2 antigen cytoplasmic tail-binding protein 2"
FT /id="PRO_0000089438"
FT DOMAIN 281..339
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95400"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95400"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95400"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95400"
SQ SEQUENCE 342 AA; 37694 MW; 6B00FBE777A19206 CRC64;
MPKRKVTFQG VGDEDGEDEI SVPKKKLVDP VAAAGGPGSR FKGKHSLDSD EEDDDEEGSS
KYDILASEDV EGQEAATLPS EGGVRITPFN LQEEMEEGHF DADGNYFLNQ DAQIRDSWLD
NIDWVRIKER PPDKHQVSDS EEEDSLGQTP MSAQALLEGL LELLLPRETV AGALRRLGAR
GGGKGSNSKG TGRPNSPQRL DRLSGLADQM VARGNLGVYQ ETRERLAMRL KGLGCRAQGS
HDPTPPPSLD MFAEEVAEGE LETPTPTQRE EAESAGDGLM DVMWEYKWEN TGDAELYGPF
TSAQMQTWVS EGYFPDGVYC RKLDPPGGQF YNSKRIDFEL YT
