C19L2_HUMAN
ID C19L2_HUMAN Reviewed; 894 AA.
AC Q2TBE0; A4FU66; A4FU67; A4FU68; A8KAD6; Q6PHW1; Q96MI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=CWF19-like protein 2;
GN Name=CWF19L2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-894 (ISOFORM 1).
RC TISSUE=Prostate, and Trachea;
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 MRNA] OF 119-894 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 120-894 (ISOFORMS 2 AND 3), AND VARIANTS
RP TYR-443 AND CYS-894.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-360; SER-372 AND
RP SER-479, AND 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-604, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-171 AND LYS-604, AND
RP IDENTIFICATION BY MASS 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).
CC -!- INTERACTION:
CC Q2TBE0; O94929-2: ABLIM3; NbExp=3; IntAct=EBI-5453285, EBI-11961672;
CC Q2TBE0; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-5453285, EBI-702390;
CC Q2TBE0; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-5453285, EBI-4400025;
CC Q2TBE0; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-5453285, EBI-1642333;
CC Q2TBE0; Q9P1Z2: CALCOCO1; NbExp=6; IntAct=EBI-5453285, EBI-749920;
CC Q2TBE0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-5453285, EBI-739580;
CC Q2TBE0; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-5453285, EBI-3866279;
CC Q2TBE0; Q9H257: CARD9; NbExp=3; IntAct=EBI-5453285, EBI-751319;
CC Q2TBE0; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-5453285, EBI-11530605;
CC Q2TBE0; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-5453285, EBI-10171570;
CC Q2TBE0; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-5453285, EBI-10171416;
CC Q2TBE0; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-5453285, EBI-2808286;
CC Q2TBE0; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-5453285, EBI-347573;
CC Q2TBE0; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-5453285, EBI-11522539;
CC Q2TBE0; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-5453285, EBI-739624;
CC Q2TBE0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-5453285, EBI-742887;
CC Q2TBE0; Q96M91: CFAP53; NbExp=3; IntAct=EBI-5453285, EBI-742422;
CC Q2TBE0; Q8N137: CNTROB; NbExp=3; IntAct=EBI-5453285, EBI-947360;
CC Q2TBE0; Q69YN2: CWF19L1; NbExp=3; IntAct=EBI-5453285, EBI-719164;
CC Q2TBE0; P17661: DES; NbExp=3; IntAct=EBI-5453285, EBI-1055572;
CC Q2TBE0; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-5453285, EBI-11988027;
CC Q2TBE0; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-5453285, EBI-742102;
CC Q2TBE0; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-5453285, EBI-10175124;
CC Q2TBE0; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-5453285, EBI-11977403;
CC Q2TBE0; A1L4K1: FSD2; NbExp=3; IntAct=EBI-5453285, EBI-5661036;
CC Q2TBE0; P51114-2: FXR1; NbExp=3; IntAct=EBI-5453285, EBI-11022345;
CC Q2TBE0; P51116: FXR2; NbExp=3; IntAct=EBI-5453285, EBI-740459;
CC Q2TBE0; O95995: GAS8; NbExp=3; IntAct=EBI-5453285, EBI-1052570;
CC Q2TBE0; P14136: GFAP; NbExp=6; IntAct=EBI-5453285, EBI-744302;
CC Q2TBE0; Q08379: GOLGA2; NbExp=3; IntAct=EBI-5453285, EBI-618309;
CC Q2TBE0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-5453285, EBI-5916454;
CC Q2TBE0; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-5453285, EBI-717919;
CC Q2TBE0; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-5453285, EBI-748420;
CC Q2TBE0; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-5453285, EBI-746704;
CC Q2TBE0; Q96ED9: HOOK2; NbExp=3; IntAct=EBI-5453285, EBI-743290;
CC Q2TBE0; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-5453285, EBI-10961706;
CC Q2TBE0; O75031: HSF2BP; NbExp=3; IntAct=EBI-5453285, EBI-7116203;
CC Q2TBE0; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-5453285, EBI-81279;
CC Q2TBE0; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-5453285, EBI-11522367;
CC Q2TBE0; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-5453285, EBI-1055254;
CC Q2TBE0; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-5453285, EBI-2556193;
CC Q2TBE0; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-5453285, EBI-749265;
CC Q2TBE0; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-5453285, EBI-10213781;
CC Q2TBE0; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-5453285, EBI-14069005;
CC Q2TBE0; Q6A162: KRT40; NbExp=3; IntAct=EBI-5453285, EBI-10171697;
CC Q2TBE0; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-5453285, EBI-12039345;
CC Q2TBE0; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-5453285, EBI-10175218;
CC Q2TBE0; P48059-3: LIMS1; NbExp=3; IntAct=EBI-5453285, EBI-12864460;
CC Q2TBE0; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-5453285, EBI-1216080;
CC Q2TBE0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-5453285, EBI-741037;
CC Q2TBE0; Q8TC57: M1AP; NbExp=3; IntAct=EBI-5453285, EBI-748182;
CC Q2TBE0; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-5453285, EBI-742610;
CC Q2TBE0; P50221: MEOX1; NbExp=6; IntAct=EBI-5453285, EBI-2864512;
CC Q2TBE0; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-5453285, EBI-742948;
CC Q2TBE0; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-5453285, EBI-11522433;
CC Q2TBE0; Q15742: NAB2; NbExp=6; IntAct=EBI-5453285, EBI-8641936;
CC Q2TBE0; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-5453285, EBI-928842;
CC Q2TBE0; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-5453285, EBI-9640281;
CC Q2TBE0; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-5453285, EBI-14066006;
CC Q2TBE0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5453285, EBI-79165;
CC Q2TBE0; O43586: PSTPIP1; NbExp=3; IntAct=EBI-5453285, EBI-1050964;
CC Q2TBE0; Q6NUQ1: RINT1; NbExp=6; IntAct=EBI-5453285, EBI-726876;
CC Q2TBE0; Q15427: SF3B4; NbExp=6; IntAct=EBI-5453285, EBI-348469;
CC Q2TBE0; Q13573: SNW1; NbExp=3; IntAct=EBI-5453285, EBI-632715;
CC Q2TBE0; O75558: STX11; NbExp=3; IntAct=EBI-5453285, EBI-714135;
CC Q2TBE0; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-5453285, EBI-529518;
CC Q2TBE0; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-5453285, EBI-1644036;
CC Q2TBE0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-5453285, EBI-1105213;
CC Q2TBE0; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-5453285, EBI-10175039;
CC Q2TBE0; Q12933: TRAF2; NbExp=3; IntAct=EBI-5453285, EBI-355744;
CC Q2TBE0; P36406: TRIM23; NbExp=3; IntAct=EBI-5453285, EBI-740098;
CC Q2TBE0; P14373: TRIM27; NbExp=6; IntAct=EBI-5453285, EBI-719493;
CC Q2TBE0; O94972: TRIM37; NbExp=6; IntAct=EBI-5453285, EBI-741602;
CC Q2TBE0; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-5453285, EBI-2130429;
CC Q2TBE0; Q9C026: TRIM9; NbExp=6; IntAct=EBI-5453285, EBI-720828;
CC Q2TBE0; P08670: VIM; NbExp=3; IntAct=EBI-5453285, EBI-353844;
CC Q2TBE0; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-5453285, EBI-2799833;
CC Q2TBE0; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-5453285, EBI-742740;
CC Q2TBE0; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-5453285, EBI-12030590;
CC Q2TBE0; P13682: ZNF35; NbExp=3; IntAct=EBI-5453285, EBI-11041653;
CC Q2TBE0; Q8N720: ZNF655; NbExp=3; IntAct=EBI-5453285, EBI-625509;
CC Q2TBE0; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-5453285, EBI-527853;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2TBE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TBE0-2; Sequence=VSP_030592, VSP_030593;
CC Name=3;
CC IsoId=Q2TBE0-3; Sequence=VSP_030590, VSP_030591;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CWF19 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10440.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI10441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI10441.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI10442.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI10443.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI18670.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71307.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF85690.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AP000766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK056905; BAB71307.1; ALT_INIT; mRNA.
DR EMBL; AK293001; BAF85690.1; ALT_SEQ; mRNA.
DR EMBL; BC056241; AAH56241.1; -; mRNA.
DR EMBL; BC110439; AAI10440.1; ALT_INIT; mRNA.
DR EMBL; BC110440; AAI10441.1; ALT_SEQ; mRNA.
DR EMBL; BC110441; AAI10442.1; ALT_INIT; mRNA.
DR EMBL; BC110442; AAI10443.2; ALT_INIT; mRNA.
DR EMBL; BC118669; AAI18670.1; ALT_INIT; mRNA.
DR CCDS; CCDS8336.2; -. [Q2TBE0-1]
DR RefSeq; NP_689647.2; NM_152434.2. [Q2TBE0-1]
DR PDB; 6ID0; EM; 2.90 A; U=1-894.
DR PDB; 6ID1; EM; 2.86 A; U=1-894.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR AlphaFoldDB; Q2TBE0; -.
DR SMR; Q2TBE0; -.
DR BioGRID; 126821; 147.
DR IntAct; Q2TBE0; 104.
DR STRING; 9606.ENSP00000282251; -.
DR iPTMnet; Q2TBE0; -.
DR PhosphoSitePlus; Q2TBE0; -.
DR BioMuta; CWF19L2; -.
DR DMDM; 300669615; -.
DR EPD; Q2TBE0; -.
DR jPOST; Q2TBE0; -.
DR MassIVE; Q2TBE0; -.
DR MaxQB; Q2TBE0; -.
DR PaxDb; Q2TBE0; -.
DR PeptideAtlas; Q2TBE0; -.
DR PRIDE; Q2TBE0; -.
DR ProteomicsDB; 61491; -. [Q2TBE0-1]
DR ProteomicsDB; 61492; -. [Q2TBE0-2]
DR ProteomicsDB; 61493; -. [Q2TBE0-3]
DR Antibodypedia; 50383; 40 antibodies from 15 providers.
DR DNASU; 143884; -.
DR Ensembl; ENST00000282251.10; ENSP00000282251.5; ENSG00000152404.16. [Q2TBE0-1]
DR GeneID; 143884; -.
DR KEGG; hsa:143884; -.
DR MANE-Select; ENST00000282251.10; ENSP00000282251.5; NM_152434.3; NP_689647.2.
DR UCSC; uc010rvp.3; human. [Q2TBE0-1]
DR CTD; 143884; -.
DR DisGeNET; 143884; -.
DR GeneCards; CWF19L2; -.
DR HGNC; HGNC:26508; CWF19L2.
DR HPA; ENSG00000152404; Low tissue specificity.
DR neXtProt; NX_Q2TBE0; -.
DR OpenTargets; ENSG00000152404; -.
DR PharmGKB; PA134914164; -.
DR VEuPathDB; HostDB:ENSG00000152404; -.
DR eggNOG; KOG2477; Eukaryota.
DR GeneTree; ENSGT00940000155627; -.
DR HOGENOM; CLU_015540_0_0_1; -.
DR InParanoid; Q2TBE0; -.
DR OMA; FMKCLTR; -.
DR OrthoDB; 1407830at2759; -.
DR PhylomeDB; Q2TBE0; -.
DR TreeFam; TF351271; -.
DR PathwayCommons; Q2TBE0; -.
DR SignaLink; Q2TBE0; -.
DR BioGRID-ORCS; 143884; 439 hits in 1076 CRISPR screens.
DR ChiTaRS; CWF19L2; human.
DR GenomeRNAi; 143884; -.
DR Pharos; Q2TBE0; Tdark.
DR PRO; PR:Q2TBE0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q2TBE0; protein.
DR Bgee; ENSG00000152404; Expressed in tendon of biceps brachii and 176 other tissues.
DR ExpressionAtlas; Q2TBE0; baseline and differential.
DR Genevisible; Q2TBE0; HS.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR040194; Cwf19-like.
DR InterPro; IPR006768; Cwf19-like_C_dom-1.
DR InterPro; IPR006767; Cwf19-like_C_dom-2.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR12072; PTHR12072; 1.
DR Pfam; PF04677; CwfJ_C_1; 1.
DR Pfam; PF04676; CwfJ_C_2; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..894
FT /note="CWF19-like protein 2"
FT /id="PRO_0000315648"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..107
FT /evidence="ECO:0000255"
FT COILED 166..281
FT /evidence="ECO:0000255"
FT COILED 502..530
FT /evidence="ECO:0000255"
FT COILED 644..675
FT /evidence="ECO:0000255"
FT COMPBIAS 14..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..100
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 604
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 625..672
FT /note="FMGKTDGDYYTLDDMFVSKAAERERLGEEEENQRKKAIAEHRSLAAQM ->
FT QLRENVLVKRKRTKGKKLLLSIGVLLHKWKNVCIVLTALNFPSILLLQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030590"
FT VAR_SEQ 673..894
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030591"
FT VAR_SEQ 735..742
FT /note="MFRKSLVK -> IKSRTVIQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030592"
FT VAR_SEQ 743..894
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030593"
FT VARIANT 210
FT /note="P -> T (in dbSNP:rs608634)"
FT /id="VAR_038268"
FT VARIANT 443
FT /note="H -> Y (in dbSNP:rs659040)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038269"
FT VARIANT 445
FT /note="H -> Q (in dbSNP:rs35968518)"
FT /id="VAR_038270"
FT VARIANT 537
FT /note="G -> R (in dbSNP:rs17106909)"
FT /id="VAR_038271"
FT VARIANT 894
FT /note="Y -> C (in dbSNP:rs3758911)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038272"
FT CONFLICT 584
FT /note="E -> K (in Ref. 3; AAI10443)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="M -> G (in Ref. 3; AAH56241)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="P -> L (in Ref. 2; BAF85690)"
FT /evidence="ECO:0000305"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 592..596
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 599..608
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 615..621
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:6ID0"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 637..642
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 651..660
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 662..673
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 676..683
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:6ID0"
FT STRAND 694..699
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 711..717
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 727..746
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 753..756
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 775..778
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 781..790
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 821..825
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 828..833
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 846..853
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 858..861
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 869..875
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 876..882
FT /evidence="ECO:0007829|PDB:6ID1"
SQ SEQUENCE 894 AA; 103787 MW; E40E8289255C57CF CRC64;
MATSMAAASG RFESAKSIEE RKEQTRNARA EVLRQAKANF EKEERRKELK RLRGEDTWML
PDVNERIEQF SQEHSVKKKK KKDKHSKKAK KEKKKKSKKQ KYEKNNESSD SSSSSEDEWV
EAVPSQTPDK EKAWKVKDEK SGKDDTQIIK RDEWMTVDFM SVKTVSSSSL KAEKETMRKI
EQEKNQALEQ SKLMERELNP YWKDGGTGLP PEDCSVSSIT KVSVVEDGGL SWLRKSYLRM
KEQAEKQSRN FEDIVAERYG SMEIFQSKLE DAEKAASTKE DYRRERWRKP TYSDKAQNCQ
ESRESDLVKY GNSSRDRYAT TDTAKNSNNE KFIGDEKDKR PGSLETCRRE SNPRQNQEFS
FGNLRAKFLR PSDDEELSFH SKGRKFEPLS SSSALVAQGS LCSGFRKPTK NSEERLTSWS
RSDGRGDKKH SNQKPSETST DEHQHVPEDP REKSQDEVLR DDPPKKEHLR DTKSTFAGSP
ERESIHILSV DEKNKLGAKI IKAEMMGNME LAEQLKVQLE KANKFKETIT QIPKKSGVEN
EDQQEVILVR TDQSGRVWPV NTPGKSLESQ GGRRKRQMVS THEERERVRY FHDDDNLSLN
DLVKNEKMGT AENQNKLFMR MASKFMGKTD GDYYTLDDMF VSKAAERERL GEEEENQRKK
AIAEHRSLAA QMEKCLYCFD SSQFPKHLIV AIGVKVYLCL PNVRSLTEGH CLIVPLQHHR
AATLLDEDIW EEIQMFRKSL VKMFEDKGLD CIFLETNMSM KKQYHMVYEC IPLPKEVGDM
APIYFKKAIM ESDEEWSMNK KLIDLSSKDI RKSVPRGLPY FSVDFGLHGG FAHVIEDQHK
FPHYFGKEII GGMLDIEPRL WRKGIRESFE DQRKKALQFA QWWKPYDFTK SKNY
