ID CD2B2_HUMAN Reviewed; 341 AA.
AC O95400; B2RDX2; Q9ULP2;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 01-MAY-2013, entry version 111.
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;
DE AltName: Full=U5 snRNP 52K protein;
DE Short=U5-52K;
GN Name=CD2BP2; Synonyms=KIAA1178;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CD2.
RX PubMed=9843987; DOI=10.1073/pnas.95.25.14897;
RA Nishizawa K., Freund C., Li J., Wagner G., Reinherz E.L.;
RT "Identification of a proline-binding motif regulating CD2-triggered T
RT lymphocyte activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14897-14902(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-341.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH PRPF6 AND TXNL4A, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15840814; DOI=10.1261/rna.2300805;
RA Laggerbauer B., Liu S., Makarov E., Vornlocher H.P., Makarova O.,
RA Ingelfinger D., Achsel T., Luhrmann R.;
RT "The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K
RT (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon
RT tri-snRNP formation.";
RL RNA 11:598-608(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP SUBUNIT.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5
RT tri-snRNP.";
RL RNA 12:1418-1430(2006).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17906334; DOI=10.1093/intimm/dxm100;
RA Heinze M., Kofler M., Freund C.;
RT "Investigating the functional role of CD2BP2 in T cells.";
RL Int. Immunol. 19:1313-1318(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-118; SER-194 AND
RP SER-195, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP STRUCTURE BY NMR OF 280-341.
RX PubMed=10404223; DOI=10.1038/10712;
RA Freund C., Dotsch V., Nishizawa K., Reinherz E.L., Wagner G.;
RT "The GYF domain is a novel structural fold that is involved in
RT lymphoid signaling through proline-rich sequences.";
RL Nat. Struct. Biol. 6:656-660(1999).
RN [18]
RP STRUCTURE BY NMR OF 280-341, INTERACTION WITH CD2 PEPTIDE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12426371;
RA Freund C., Kuhne R., Yang H., Park S., Reinherz E.L., Wagner G.;
RT "Dynamic interaction of CD2 with the GYF and the SH3 domain of
RT compartmentalized effector molecules.";
RL EMBO J. 21:5985-5995(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 256-341 IN COMPLEX WITH
RP TXNL4A, AND INTERACTION WITH TXNL4A.
RX PubMed=17467737; DOI=10.1016/j.jmb.2007.03.077;
RA Nielsen T.K., Liu S., Luhrmann R., Ficner R.;
RT "Structural basis for the bifunctionality of the U5 snRNP 52K protein
RT (CD2BP2).";
RL J. Mol. Biol. 369:902-908(2007).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the U5
CC snRNP complex that is involved in spliceosome assembly.
CC -!- SUBUNIT: Component of the U5 snRNP complex composed of the U5
CC snRNA and at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23,
CC TXNL4A and CD2BP2. Interacts directly with TXNL4A and PRPF6.
CC Interacts (via GYF domain) with CD2 (via Pro-rich sequence in the
CC cytoplasmic domain).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC nuclear.
CC -!- SIMILARITY: Contains 1 GYF domain.
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DR EMBL; AF104222; AAC84141.1; -; mRNA.
DR EMBL; AK315708; BAG38069.1; -; mRNA.
DR EMBL; CH471192; EAW52260.1; -; Genomic_DNA.
DR EMBL; BC000495; AAH00495.1; -; mRNA.
DR EMBL; BC001947; AAH01947.1; -; mRNA.
DR EMBL; AB033004; BAA86492.1; -; mRNA.
DR IPI; IPI00006103; -.
DR RefSeq; NP_001230575.1; NM_001243646.1.
DR RefSeq; NP_006101.1; NM_006110.2.
DR UniGene; Hs.202677; -.
DR PDB; 1GYF; NMR; -; A=280-341.
DR PDB; 1L2Z; NMR; -; A=280-341.
DR PDB; 1SYX; X-ray; 2.35 A; B/D/F=256-341.
DR PDBsum; 1GYF; -.
DR PDBsum; 1L2Z; -.
DR PDBsum; 1SYX; -.
DR ProteinModelPortal; O95400; -.
DR IntAct; O95400; 4.
DR MINT; MINT-99472; -.
DR STRING; 9606.ENSP00000304903; -.
DR PhosphoSite; O95400; -.
DR PaxDb; O95400; -.
DR PRIDE; O95400; -.
DR DNASU; 10421; -.
DR Ensembl; ENST00000305596; ENSP00000304903; ENSG00000169217.
DR Ensembl; ENST00000569466; ENSP00000456935; ENSG00000169217.
DR GeneID; 10421; -.
DR KEGG; hsa:10421; -.
DR UCSC; uc002dxr.3; human.
DR CTD; 10421; -.
DR GeneCards; GC16M030363; -.
DR HGNC; HGNC:1656; CD2BP2.
DR HPA; HPA041508; -.
DR MIM; 604470; gene.
DR neXtProt; NX_O95400; -.
DR PharmGKB; PA26209; -.
DR eggNOG; NOG301637; -.
DR HOGENOM; HOG000007061; -.
DR HOVERGEN; HBG056920; -.
DR InParanoid; O95400; -.
DR KO; K13099; -.
DR OMA; QTWVNEG; -.
DR OrthoDB; EOG4R503D; -.
DR PhylomeDB; O95400; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; CD2BP2; human.
DR EvolutionaryTrace; O95400; -.
DR GenomeRNAi; 10421; -.
DR NextBio; 39496; -.
DR ArrayExpress; O95400; -.
DR Bgee; O95400; -.
DR CleanEx; HS_CD2BP2; -.
DR Genevestigator; O95400; -.
DR GermOnline; ENSG00000169217; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005682; C:U5 snRNP; IDA:BHF-UCL.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
DR GO; GO:0000244; P:assembly of spliceosomal tri-snRNP; NAS:BHF-UCL.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; GYF; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 341 CD2 antigen cytoplasmic tail-binding
FT protein 2.
FT /FTId=PRO_0000089437.
FT DOMAIN 280 338 GYF.
FT MOD_RES 49 49 Phosphoserine.
FT MOD_RES 118 118 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 195 195 Phosphoserine.
FT VARIANT 231 231 G -> D (in dbSNP:rs13330462).
FT /FTId=VAR_050772.
FT VARIANT 262 262 T -> I (in dbSNP:rs34391305).
FT /FTId=VAR_050773.
FT STRAND 282 293
FT STRAND 296 300
FT HELIX 301 309
FT STRAND 318 324
FT HELIX 332 334
FT HELIX 337 340
SQ SEQUENCE 341 AA; 37646 MW; 8E9A7EE0C40474D5 CRC64;
MPKRKVTFQG VGDEEDEDEI IVPKKKLVDP VAGSGGPGSR FKGKHSLDSD EEEDDDDGGS
SKYDILASED VEGQEAATLP SEGGVRITPF NLQEEMEEGH FDADGNYFLN RDAQIRDSWL
DNIDWVKIRE RPPGQRQASD SEEEDSLGQT SMSAQALLEG LLELLLPRET VAGALRRLGA
RGGGKGRKGP GQPSSPQRLD RLSGLADQMV ARGNLGVYQE TRERLAMRLK GLGCQTLGPH
NPTPPPSLDM FAEELAEEEL ETPTPTQRGE AESRGDGLVD VMWEYKWENT GDAELYGPFT
SAQMQTWVSE GYFPDGVYCR KLDPPGGQFY NSKRIDFDLY T
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