CD2B2_HUMAN
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 03-AUG-2022, entry version 181.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 from
RT 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 (hPrp6), a
RT U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP
RT formation.";
RL RNA 11:598-608(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 tri-
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Li S.-J.,
RA 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 reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 sequential
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
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 lymphoid
RT signaling through proline-rich sequences.";
RL Nat. Struct. Biol. 6:656-660(1999).
RN [21]
RP STRUCTURE BY NMR OF 280-341, INTERACTION WITH CD2 PEPTIDE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12426371; DOI=10.1093/emboj/cdf602;
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 [22]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 256-341 IN COMPLEX WITH TXNL4A,
RP 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).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 280-341 IN COMPLEX WITH PQBP1 AND
RP TXNL4A, AND SUBUNIT.
RX PubMed=24781215; DOI=10.1038/ncomms4822;
RA Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.;
RT "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal
RT protein U5-15 kD.";
RL Nat. Commun. 5:3822-3822(2014).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP
CC complex that is involved in spliceosome assembly.
CC {ECO:0000269|PubMed:15840814}.
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. {ECO:0000269|PubMed:12426371,
CC ECO:0000269|PubMed:15840814, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:17467737, ECO:0000269|PubMed:24781215,
CC ECO:0000269|PubMed:9843987}.
CC -!- INTERACTION:
CC O95400; Q709F0: ACAD11; NbExp=4; IntAct=EBI-768015, EBI-2880718;
CC O95400; Q7Z591: AKNA; NbExp=2; IntAct=EBI-768015, EBI-2799297;
CC O95400; P06729: CD2; NbExp=9; IntAct=EBI-768015, EBI-3912464;
CC O95400; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-768015, EBI-716006;
CC O95400; P62136: PPP1CA; NbExp=2; IntAct=EBI-768015, EBI-357253;
CC O95400; P36873: PPP1CC; NbExp=3; IntAct=EBI-768015, EBI-356283;
CC O95400; O94906: PRPF6; NbExp=6; IntAct=EBI-768015, EBI-536755;
CC O95400; Q92530: PSMF1; NbExp=2; IntAct=EBI-768015, EBI-945916;
CC O95400; P14678: SNRPB; NbExp=8; IntAct=EBI-768015, EBI-372458;
CC O95400; P14678-2: SNRPB; NbExp=10; IntAct=EBI-768015, EBI-372475;
CC O95400; P63162: SNRPN; NbExp=4; IntAct=EBI-768015, EBI-712493;
CC O95400; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-768015, EBI-8451480;
CC O95400; P83876: TXNL4A; NbExp=3; IntAct=EBI-768015, EBI-746539;
CC O95400; Q9Y2W2: WBP11; NbExp=2; IntAct=EBI-768015, EBI-714455;
CC O95400; Q9UHR6: ZNHIT2; NbExp=4; IntAct=EBI-768015, EBI-2557592;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly nuclear.
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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 CCDS; CCDS10675.1; -.
DR RefSeq; NP_001230575.1; NM_001243646.1.
DR RefSeq; NP_006101.1; NM_006110.2.
DR PDB; 1GYF; NMR; -; A=280-341.
DR PDB; 1L2Z; NMR; -; A=280-341.
DR PDB; 1SYX; X-ray; 2.34 A; B/D/F=262-341.
DR PDB; 4BWS; X-ray; 2.50 A; C/F=280-341.
DR PDBsum; 1GYF; -.
DR PDBsum; 1L2Z; -.
DR PDBsum; 1SYX; -.
DR PDBsum; 4BWS; -.
DR AlphaFoldDB; O95400; -.
DR SMR; O95400; -.
DR BioGRID; 115690; 180.
DR CORUM; O95400; -.
DR ELM; O95400; -.
DR IntAct; O95400; 72.
DR MINT; O95400; -.
DR STRING; 9606.ENSP00000304903; -.
DR GlyGen; O95400; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95400; -.
DR MetOSite; O95400; -.
DR PhosphoSitePlus; O95400; -.
DR BioMuta; CD2BP2; -.
DR EPD; O95400; -.
DR jPOST; O95400; -.
DR MassIVE; O95400; -.
DR MaxQB; O95400; -.
DR PaxDb; O95400; -.
DR PeptideAtlas; O95400; -.
DR PRIDE; O95400; -.
DR ProteomicsDB; 50853; -.
DR Antibodypedia; 27184; 195 antibodies from 30 providers.
DR DNASU; 10421; -.
DR Ensembl; ENST00000305596.8; ENSP00000304903.3; ENSG00000169217.9.
DR Ensembl; ENST00000569466.1; ENSP00000456935.1; ENSG00000169217.9.
DR GeneID; 10421; -.
DR KEGG; hsa:10421; -.
DR MANE-Select; ENST00000305596.8; ENSP00000304903.3; NM_006110.3; NP_006101.1.
DR UCSC; uc002dxr.4; human.
DR CTD; 10421; -.
DR DisGeNET; 10421; -.
DR GeneCards; CD2BP2; -.
DR HGNC; HGNC:1656; CD2BP2.
DR HPA; ENSG00000169217; Low tissue specificity.
DR MIM; 604470; gene.
DR neXtProt; NX_O95400; -.
DR OpenTargets; ENSG00000169217; -.
DR PharmGKB; PA26209; -.
DR VEuPathDB; HostDB:ENSG00000169217; -.
DR eggNOG; KOG2950; Eukaryota.
DR GeneTree; ENSGT00390000012483; -.
DR HOGENOM; CLU_062973_0_0_1; -.
DR InParanoid; O95400; -.
DR OMA; VRKCGEN; -.
DR OrthoDB; 773475at2759; -.
DR PhylomeDB; O95400; -.
DR TreeFam; TF313042; -.
DR PathwayCommons; O95400; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O95400; -.
DR BioGRID-ORCS; 10421; 158 hits in 1078 CRISPR screens.
DR ChiTaRS; CD2BP2; human.
DR EvolutionaryTrace; O95400; -.
DR GeneWiki; CD2BP2; -.
DR GenomeRNAi; 10421; -.
DR Pharos; O95400; Tbio.
DR PRO; PR:O95400; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O95400; protein.
DR Bgee; ENSG00000169217; Expressed in tendon of biceps brachii and 212 other tissues.
DR ExpressionAtlas; O95400; baseline and differential.
DR Genevisible; O95400; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; 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:spliceosomal tri-snRNP complex assembly; NAS:BHF-UCL.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR IDEAL; IID00533; -.
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 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..341
FT /note="CD2 antigen cytoplasmic tail-binding protein 2"
FT /id="PRO_0000089437"
FT DOMAIN 280..338
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWK3"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 231
FT /note="G -> D (in dbSNP:rs13330462)"
FT /id="VAR_050772"
FT VARIANT 262
FT /note="T -> I (in dbSNP:rs34391305)"
FT /id="VAR_050773"
FT STRAND 282..293
FT /evidence="ECO:0007829|PDB:1SYX"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1SYX"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:1SYX"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:1SYX"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1SYX"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:1SYX"
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
