HNRLL_MOUSE
ID HNRLL_MOUSE Reviewed; 591 AA.
AC Q921F4; Q3UIK6; Q6IR44; Q8BIP6; Q91W02; Q99J40;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein L-like;
GN Name=Hnrnpll; Synonyms=Hnrpll;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and Czech II;
RC TISSUE=Embryonic germ cell, and Mammary gland;
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 FUNCTION, MUTAGENESIS OF VAL-136, INDUCTION, AND STRUCTURE BY NMR OF RRM 1.
RX PubMed=19100700; DOI=10.1016/j.immuni.2008.11.004;
RA Wu Z., Jia X., de la Cruz L., Su X.-C., Marzolf B., Troisch P., Zak D.,
RA Hamilton A., Whittle B., Yu D., Sheahan D., Bertram E., Aderem A.,
RA Otting G., Goodnow C.C., Hoyne G.F.;
RT "Memory T cell RNA rearrangement programmed by heterogeneous nuclear
RT ribonucleoprotein hnRNPLL.";
RL Immunity 29:863-875(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS 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 [5]
RP STRUCTURE BY NMR OF 119-316.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domains in heterogeneous nuclear
RT ribonucleoprotein L-like.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein that functions as regulator of
CC alternative splicing for multiple target mRNAs, including PTPRC/CD45
CC and STAT5A. Required for alternative splicing of PTPRC.
CC {ECO:0000269|PubMed:19100700}.
CC -!- SUBUNIT: Interacts with HNRNPL. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q921F4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921F4-4; Sequence=VSP_013290, VSP_013291;
CC Name=3;
CC IsoId=Q921F4-5; Sequence=VSP_026132, VSP_026133;
CC -!- INDUCTION: Up-regulated in stimulated T-cells.
CC {ECO:0000269|PubMed:19100700}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK034860; BAC28858.1; -; mRNA.
DR EMBL; AK146879; BAE27500.1; ALT_INIT; mRNA.
DR EMBL; BC004763; AAH04763.1; -; mRNA.
DR EMBL; BC012849; AAH12849.2; -; mRNA.
DR EMBL; BC071184; AAH71184.1; -; mRNA.
DR CCDS; CCDS70845.1; -. [Q921F4-1]
DR RefSeq; NP_659051.3; NM_144802.4. [Q921F4-1]
DR PDB; 1WEX; NMR; -; A=117-207.
DR PDB; 2E5I; NMR; -; A=200-316.
DR PDBsum; 1WEX; -.
DR PDBsum; 2E5I; -.
DR AlphaFoldDB; Q921F4; -.
DR BMRB; Q921F4; -.
DR SMR; Q921F4; -.
DR BioGRID; 215518; 11.
DR IntAct; Q921F4; 2.
DR MINT; Q921F4; -.
DR STRING; 10090.ENSMUSP00000058308; -.
DR iPTMnet; Q921F4; -.
DR PhosphoSitePlus; Q921F4; -.
DR SwissPalm; Q921F4; -.
DR EPD; Q921F4; -.
DR jPOST; Q921F4; -.
DR MaxQB; Q921F4; -.
DR PaxDb; Q921F4; -.
DR PeptideAtlas; Q921F4; -.
DR PRIDE; Q921F4; -.
DR ProteomicsDB; 269611; -. [Q921F4-1]
DR ProteomicsDB; 269612; -. [Q921F4-4]
DR ProteomicsDB; 269613; -. [Q921F4-5]
DR Antibodypedia; 14627; 209 antibodies from 25 providers.
DR DNASU; 72692; -.
DR Ensembl; ENSMUST00000061331; ENSMUSP00000058308; ENSMUSG00000024095. [Q921F4-1]
DR Ensembl; ENSMUST00000184635; ENSMUSP00000139372; ENSMUSG00000024095. [Q921F4-1]
DR GeneID; 72692; -.
DR KEGG; mmu:72692; -.
DR UCSC; uc008dqk.2; mouse. [Q921F4-1]
DR CTD; 92906; -.
DR MGI; MGI:1919942; Hnrnpll.
DR VEuPathDB; HostDB:ENSMUSG00000024095; -.
DR eggNOG; KOG1456; Eukaryota.
DR GeneTree; ENSGT01030000234642; -.
DR HOGENOM; CLU_015171_0_0_1; -.
DR InParanoid; Q921F4; -.
DR OMA; AMFMFES; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q921F4; -.
DR TreeFam; TF354318; -.
DR BioGRID-ORCS; 72692; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Hnrnpll; mouse.
DR EvolutionaryTrace; Q921F4; -.
DR PRO; PR:Q921F4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q921F4; protein.
DR Bgee; ENSMUSG00000024095; Expressed in medial ganglionic eminence and 260 other tissues.
DR ExpressionAtlas; Q921F4; baseline and differential.
DR Genevisible; Q921F4; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR CDD; cd12781; RRM1_hnRPLL; 1.
DR CDD; cd12786; RRM2_hnRPLL; 1.
DR CDD; cd12700; RRM3_hnRPLL; 1.
DR CDD; cd12705; RRM4_hnRPLL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR034985; hnRPLL_RRM1.
DR InterPro; IPR034986; hnRPLL_RRM2.
DR InterPro; IPR034983; hnRPLL_RRM3.
DR InterPro; IPR034987; hnRPLL_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..591
FT /note="Heterogeneous nuclear ribonucleoprotein L-like"
FT /id="PRO_0000081610"
FT DOMAIN 125..199
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 215..293
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 384..458
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVV9"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVV9"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVV9"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVV9"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WVV9"
FT CROSSLNK 540
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WVV9"
FT VAR_SEQ 1..480
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026132"
FT VAR_SEQ 317..326
FT /note="DRGKGRQRQA -> GRYFTNFRMY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013290"
FT VAR_SEQ 327..591
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013291"
FT VAR_SEQ 522..591
FT /note="LCNDHEVLPFIKYKVFDAKASAKTLSGLLEWKCKTDAVEALTALNHYQIRVP
FT NGSNPYTLKLCFSTSSHL -> VGTEESSVRMLRFVFYVYVVFHSSASFENFSKILLFV
FT VSLVWVCVRRAYRLVVLDGFLC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026133"
FT MUTAGEN 136
FT /note="V->D: Alters RRM 1 stability. Abolishes regulation
FT of alternative splicing."
FT /evidence="ECO:0000269|PubMed:19100700"
FT CONFLICT 4
FT /note="S -> T (in Ref. 2; AAH12849)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> SGGG (in Ref. 2; AAH12849)"
FT /evidence="ECO:0000305"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1WEX"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:1WEX"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1WEX"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1WEX"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:1WEX"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1WEX"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:1WEX"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1WEX"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1WEX"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1WEX"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:2E5I"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:2E5I"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:2E5I"
FT STRAND 244..263
FT /evidence="ECO:0007829|PDB:2E5I"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:2E5I"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:2E5I"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2E5I"
SQ SEQUENCE 591 AA; 64125 MW; 431C0167DF619FB7 CRC64;
MSSSSSSSPK EETYEEDREF ESQAKRLKTE EGEIVYSAEE SENRQEATPQ AGSDSDSGGG
DGGDGDGGSG GGGDGEEGEG GEEGDEGDGD EGGSGGDEGG SGGGPRSMPL STEGGGSHHK
VSVSPVVHVR GLCESVVEAD LVEALEKFGT ICYVMMMPFK RQALVEFENI DSAKECVTFA
ADVPVYIAGQ QAFFNYSTSK RITRPGNTDD PSGGNKVLLL SIQNPLYPIT VDVLYTVCNP
VGKVQRIVIF KRNGIQAMVE FESVLCAQKA KAALNGADIY AGCCTLKIEY ARPTRLNVIR
NDNDSWDYTK PYLGRRDRGK GRQRQAILGD HPSSFRHDGY GSHGPLLPLP SRYRMGSRDT
PELVAYPLPQ ASSSYMHGGS PSGSVVMVSG LHQLKMNCSR VFNLFCLYGN IEKVKFMKTI
PGTALVEMGD EYAVERAVTH LNNVKLFGKR LNVCVSKQHS VVPSQIFELE DGTSSYKDFA
MSKNNRFTSA GQASKNIIQP PSCVLHYYNV PLCVTEETFT KLCNDHEVLP FIKYKVFDAK
ASAKTLSGLL EWKCKTDAVE ALTALNHYQI RVPNGSNPYT LKLCFSTSSH L
