HNRL2_MOUSE
ID HNRL2_MOUSE Reviewed; 745 AA.
AC Q00PI9; F8VPM4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 2;
DE AltName: Full=MLF1-associated nuclear protein;
GN Name=Hnrnpul2; Synonyms=Hnrpul2, Manp {ECO:0000312|EMBL:AAY44301.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAY44301.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MLF1, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=129 {ECO:0000312|EMBL:AAY44301.1};
RX PubMed=17008314; DOI=10.1074/jbc.m605401200;
RA Winteringham L.N., Endersby R., Kobelke S., McCulloch R.K., Williams J.H.,
RA Stillitano J., Cornwall S.M., Ingley E., Klinken S.P.;
RT "Myeloid leukemia factor 1 associates with a novel heterogeneous nuclear
RT ribonucleoprotein U-like molecule.";
RL J. Biol. Chem. 281:38791-38800(2006).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; THR-163; SER-166;
RP SER-183; SER-186; SER-224 AND SER-226, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-654; ARG-682; ARG-736 AND
RP ARG-745, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- SUBUNIT: Binds to MLF1 and retains it in the nucleus.
CC {ECO:0000269|PubMed:17008314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17008314}.
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DR EMBL; DQ000354; AAY44301.1; -; mRNA.
DR EMBL; AC129217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37908.1; -.
DR RefSeq; NP_001074665.1; NM_001081196.1.
DR AlphaFoldDB; Q00PI9; -.
DR SMR; Q00PI9; -.
DR BioGRID; 212995; 24.
DR IntAct; Q00PI9; 10.
DR MINT; Q00PI9; -.
DR STRING; 10090.ENSMUSP00000094515; -.
DR iPTMnet; Q00PI9; -.
DR PhosphoSitePlus; Q00PI9; -.
DR SwissPalm; Q00PI9; -.
DR EPD; Q00PI9; -.
DR jPOST; Q00PI9; -.
DR MaxQB; Q00PI9; -.
DR PaxDb; Q00PI9; -.
DR PeptideAtlas; Q00PI9; -.
DR PRIDE; Q00PI9; -.
DR ProteomicsDB; 273372; -.
DR DNASU; 68693; -.
DR Ensembl; ENSMUST00000096753; ENSMUSP00000094515; ENSMUSG00000071659.
DR GeneID; 68693; -.
DR KEGG; mmu:68693; -.
DR UCSC; uc008gng.1; mouse.
DR CTD; 221092; -.
DR MGI; MGI:1915943; Hnrnpul2.
DR VEuPathDB; HostDB:ENSMUSG00000071659; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000160376; -.
DR HOGENOM; CLU_012140_1_0_1; -.
DR InParanoid; Q00PI9; -.
DR OMA; DSRGLKM; -.
DR OrthoDB; 778148at2759; -.
DR PhylomeDB; Q00PI9; -.
DR TreeFam; TF317301; -.
DR BioGRID-ORCS; 68693; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Hnrnpul2; mouse.
DR PRO; PR:Q00PI9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q00PI9; protein.
DR Bgee; ENSMUSG00000071659; Expressed in ureter smooth muscle and 260 other tissues.
DR Genevisible; Q00PI9; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR CDD; cd12884; SPRY_hnRNP; 1.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035778; SPRY_hnRNP_U.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..745
FT /note="Heterogeneous nuclear ribonucleoprotein U-like
FT protein 2"
FT /id="PRO_0000278143"
FT DOMAIN 3..37
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 224..417
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 44..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..98
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 654
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 682
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 736
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 745
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 277
FT /note="S -> F (in Ref. 1; AAY44301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 84940 MW; EE89D3F94E9D6488 CRC64;
MEVKRLKVTE LRSELQRRGL DSRGLKMDLA QRLQEALDAE MLEDEAGVGG AGPGGACKAE
PRPVAASGGG PGGDEEEEDD DEEEDEEALL EDEDEEPPPA QALGQAAQPP PEPPETSAME
AESEASDTPA EATAGSGGVN GGEEHDNGKG EEDGPEERSG DETPGSEAPG DKAVEEQGDD
QDSEKSKPAG SDGERRGVKR QRDEKDEHGR AYYEFREEAY HSRSKSPPPP EEEAKDEEED
QTLVNLDTYT SDLHFQISKD RYGGQPLFSE KFPTLWSGAR STYGVTKGKV CFEAKVTQNL
PMKEGCTEVS LLRVGWSVDF SCSQLGEDEF SYGFDGRGLK AENGQFEEFG QTFGENDVIG
CFANFETEEV ELSFSKNGED LGVAFRISKE SLADRALLPH VLCKNCVVEL NFGQKEEPFF
PPPEEFVFIH AVPVEERVRT AVPPKTIEEC EVILMVGLPG SGKTQWALKY AKDNPERRYN
VLGAETVLTQ MRMKGLEEPE MDPKSRDLLV QQASQCLSKL VQIASRSKRN FILDQCNVYN
SGQRRKLLLF KTFSRKVVVV VPNEEDWKRR LELRKEVEGD DVPESIMLEM KANFSLPEKC
DYMDEVTYGE LEKEEAQPIV TKYKEEARKL LPPSEKRTNR RNNRNKRNRQ NRSRGQGYVG
GQRRGYDNRA YGQQYWGQSG NRGGYRNFYD RYRGDYERFY SRDYEYNRYR DYYRQYNRDW
QNYYYHHQQD RDRYYRNYYG YQGYR
