LARP7_MOUSE
ID LARP7_MOUSE Reviewed; 570 AA.
AC Q05CL8; Q3TSC2; Q8K2Y6; Q8VDW3; Q9CSI2; Q9CSI9; Q9CUQ5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=La-related protein 7 {ECO:0000303|PubMed:23154982};
DE AltName: Full=La ribonucleoprotein domain family member 7 {ECO:0000303|PubMed:23154982};
GN Name=Larp7 {ECO:0000303|PubMed:23154982, ECO:0000312|MGI:MGI:107634};
GN Synonyms=D3Wsu161e {ECO:0000312|MGI:MGI:107634};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-355 AND 388-570 (ISOFORM 1).
RC STRAIN=Czech II, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-342 AND 511-570 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg, Embryo, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251; SER-253; SER-256;
RP THR-260; SER-334 AND THR-335, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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 [8]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23154982; DOI=10.1101/gad.202242.112;
RA Okamura D., Maeda I., Taniguchi H., Tokitake Y., Ikeda M., Ozato K.,
RA Mise N., Abe K., Noce T., Izpisua Belmonte J.C., Matsui Y.;
RT "Cell cycle gene-specific control of transcription has a critical role in
RT proliferation of primordial germ cells.";
RL Genes Dev. 26:2477-2482(2012).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=22865833; DOI=10.1002/humu.22175;
RA Alazami A.M., Al-Owain M., Alzahrani F., Shuaib T., Al-Shamrani H.,
RA Al-Falki Y.H., Al-Qahtani S.M., Alsheddi T., Colak D., Alkuraya F.S.;
RT "Loss of function mutation in LARP7, chaperone of 7SK ncRNA, causes a
RT syndrome of facial dysmorphism, intellectual disability, and primordial
RT dwarfism.";
RL Hum. Mutat. 33:1429-1434(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PHE-38.
RX PubMed=32017896; DOI=10.1016/j.molcel.2020.01.002;
RA Wang X., Li Z.T., Yan Y., Lin P., Tang W., Hasler D., Meduri R., Li Y.,
RA Hua M.M., Qi H.T., Lin D.H., Shi H.J., Hui J., Li J., Li D., Yang J.H.,
RA Lin J., Meister G., Fischer U., Liu M.F.;
RT "LARP7-mediated U6 snRNA modification ensures splicing fidelity and
RT spermatogenesis in mice.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: RNA-binding protein that specifically binds distinct small
CC nuclear RNA (snRNAs) and regulates their processing and function
CC (PubMed:32017896). Specifically binds the 7SK snRNA (7SK RNA) and acts
CC as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby
CC acting as a negative regulator of transcription elongation by RNA
CC polymerase II (By similarity). The 7SK RNP complex sequesters the
CC positive transcription elongation factor b (P-TEFb) in a large inactive
CC 7SK RNP complex preventing RNA polymerase II phosphorylation and
CC subsequent transcriptional elongation (By similarity). The 7SK RNP
CC complex also promotes snRNA gene transcription by RNA polymerase II via
CC interaction with the little elongation complex (LEC) (By similarity).
CC LARP7 specifically binds to the highly conserved 3'-terminal U-rich
CC stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA,
CC whereas P-TEFb is released from the complex (By similarity). LARP7 also
CC acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA
CC processing (PubMed:32017896). Specifically binds U6 snRNAs and
CC associates with a subset of box C/D RNP complexes: promotes U6 snRNA
CC 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP
CC complexes (PubMed:32017896). U6 snRNA 2'-O-methylation is required for
CC mRNA splicing fidelity (PubMed:32017896). Binds U6 snRNAs with a 5'-
CC CAGGG-3' sequence motif (By similarity). U6 snRNA processing is
CC required for spermatogenesis (PubMed:32017896).
CC {ECO:0000250|UniProtKB:Q4G0J3, ECO:0000269|PubMed:32017896}.
CC -!- SUBUNIT: Core component of the 7SK RNP complex, at least composed of
CC 7SK RNA, LARP7, MEPCE, HEXIM1 (or HEXIM2) and P-TEFb (composed of CDK9
CC and CCNT1/cyclin-T1) (By similarity). Interacts with METTL16 (By
CC similarity). Interacts with RBM7; upon genotoxic stress this
CC interaction is enhanced, triggering the release of inactive P-TEFb
CC complex from the core, yielding to P-TEFb complex activation (By
CC similarity). Associates with box C/D small nucleolar ribonucleoprotein
CC (snoRNP) complexes (PubMed:32017896). {ECO:0000250|UniProtKB:Q4G0J3,
CC ECO:0000269|PubMed:32017896}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:32017896}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q05CL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05CL8-2; Sequence=VSP_024022, VSP_024023;
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in primordial germ cells
CC (PubMed:23154982). Ubiquitously expressed in the embryo
CC (PubMed:22865833). {ECO:0000269|PubMed:22865833,
CC ECO:0000269|PubMed:23154982}.
CC -!- DOMAIN: The xRRM domain binds the 3' end of 7SK snRNA (7SK RNA) at the
CC top of stem-loop 4. {ECO:0000250|UniProtKB:Q4G0J3}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality between embryonic day 17.5
CC dpc and birth (PubMed:23154982). Conditional knockout mice lacking
CC Larp7 in germline cells show defects in spermatogenesis: males are
CC sterile, whereas all females display normal fertility
CC (PubMed:32017896). Cells show reduced 2'-O-methylation of U6 snRNAs and
CC defects in mRNA splicing (PubMed:32017896).
CC {ECO:0000269|PubMed:23154982, ECO:0000269|PubMed:32017896}.
CC -!- SIMILARITY: Belongs to the LARP7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23165.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC113952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020127; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC023165; AAH23165.1; ALT_SEQ; mRNA.
DR EMBL; BC029178; AAH29178.2; -; mRNA.
DR EMBL; AK012726; BAB28435.1; -; mRNA.
DR EMBL; AK012772; BAB28459.1; -; mRNA.
DR EMBL; AK015041; BAB29687.1; -; mRNA.
DR EMBL; AK162147; BAE36753.1; -; mRNA.
DR CCDS; CCDS38626.1; -. [Q05CL8-1]
DR RefSeq; NP_613059.2; NM_138593.2. [Q05CL8-1]
DR AlphaFoldDB; Q05CL8; -.
DR SMR; Q05CL8; -.
DR BioGRID; 205727; 12.
DR IntAct; Q05CL8; 6.
DR MINT; Q05CL8; -.
DR STRING; 10090.ENSMUSP00000029588; -.
DR iPTMnet; Q05CL8; -.
DR PhosphoSitePlus; Q05CL8; -.
DR SwissPalm; Q05CL8; -.
DR EPD; Q05CL8; -.
DR jPOST; Q05CL8; -.
DR MaxQB; Q05CL8; -.
DR PaxDb; Q05CL8; -.
DR PeptideAtlas; Q05CL8; -.
DR PRIDE; Q05CL8; -.
DR ProteomicsDB; 264838; -. [Q05CL8-1]
DR ProteomicsDB; 264839; -. [Q05CL8-2]
DR DNASU; 28036; -.
DR Ensembl; ENSMUST00000029588; ENSMUSP00000029588; ENSMUSG00000027968. [Q05CL8-1]
DR GeneID; 28036; -.
DR KEGG; mmu:28036; -.
DR UCSC; uc008rhd.1; mouse. [Q05CL8-1]
DR CTD; 51574; -.
DR MGI; MGI:107634; Larp7.
DR VEuPathDB; HostDB:ENSMUSG00000027968; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154949; -.
DR HOGENOM; CLU_020946_2_0_1; -.
DR InParanoid; Q05CL8; -.
DR OMA; RKAVHKM; -.
DR OrthoDB; 1499213at2759; -.
DR PhylomeDB; Q05CL8; -.
DR TreeFam; TF314476; -.
DR BioGRID-ORCS; 28036; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Larp7; mouse.
DR PRO; PR:Q05CL8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q05CL8; protein.
DR Bgee; ENSMUSG00000027968; Expressed in seminiferous tubule of testis and 249 other tissues.
DR ExpressionAtlas; Q05CL8; baseline and differential.
DR Genevisible; Q05CL8; MM.
DR GO; GO:0120259; C:7SK snRNP; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IMP:UniProtKB.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0036093; P:germ cell proliferation; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0035562; P:negative regulation of chromatin binding; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; ISS:UniProtKB.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:1990438; P:U6 2'-O-snRNA methylation; IMP:UniProtKB.
DR CDD; cd08032; LARP_7; 1.
DR CDD; cd12290; RRM1_LARP7; 1.
DR CDD; cd12542; RRM2_LARP7; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR014886; La_xRRM.
DR InterPro; IPR034946; LARP7_La.
DR InterPro; IPR034887; LARP7_RRM1.
DR InterPro; IPR034910; LARP7_RRM2.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF08777; RRM_3; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Differentiation; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spermatogenesis; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..570
FT /note="La-related protein 7"
FT /id="PRO_0000281144"
FT DOMAIN 22..116
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 119..197
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 438..551
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT VAR_SEQ 179..185
FT /note="FLNNPPE -> VRTSVGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024022"
FT VAR_SEQ 186..570
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024023"
FT MUTAGEN 38
FT /note="F->A: Reduced binding to U6 snRNA without affecting
FT binding to 7SK RNA. Reduced 2'-O-methylation of U6 snRNAs."
FT /evidence="ECO:0000269|PubMed:32017896"
FT CONFLICT 13
FT /note="T -> TE (in Ref. 2; BC020127)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="P -> L (in Ref. 2; AAH23165)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="K -> R (in Ref. 3; BAB28459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 64802 MW; 025EB8EC3CA58F22 CRC64;
METENQKTME ESTKRKEEKK KRSRVKQVLA DIAKQVDFWF GDANLHKDKF LREQIEKSRD
GYVDISLLVS FNKMKKLTTD GKLIARALKS SSVVELDLEG TRIRRKKPLG ERPKDEEERT
VYVELLPKNV THSWIERVFG KCGNVVYISI PHYKSTGDPK GFAFVEFETK EQAAKAIEFL
NNPPEEAPRK PGIFPKTVKN KPIPSLRVAE EKKKKKKKKG RIKKEESVQA KESAVDSSSS
GVCKATKRPR TASEGSEAET PEAPKQPAKK KKKRDKVEAS SLPEARAGKR ERCSAEDEDC
LPPRPKAKKR AQKDGVGQAA SEVSKESRDL EFCSTEEEKE TDRKGDSLSK VKRKHKKKHK
ERHKMGEEVI PLRVLSKTEW MDLKKEYLAL QKASMASLKK TISQIKLESE METDCKAPTA
GSGQECSTQE KVSAQGPQFV TGVIVKIVSG EPLPGRKQVK DILATISEVV YIDLLEGDTE
CHARFKTPED AQAVMNAQTE IRKKHSWNLE VLSGDHEQRY WQKILVDRQA KLNQPREKKR
GTEKLITKAE KIRLAKTQQA SQHIRFSEYD
