HNRH1_MOUSE
ID HNRH1_MOUSE Reviewed; 449 AA.
AC O35737;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H;
DE Short=hnRNP H;
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H, N-terminally processed;
GN Name=Hnrnph1; Synonyms=Hnrph, Hnrph1;
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 [MRNA].
RC TISSUE=Neuroblastoma;
RA Wolff A., Landon F., Portier M.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 PROTEIN SEQUENCE OF 99-114 AND 300-326, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-233, AND IDENTIFICATION BY MASS
RP 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 -!- FUNCTION: This protein is a component of the heterogeneous nuclear
CC ribonucleoprotein (hnRNP) complexes which provide the substrate for the
CC processing events that pre-mRNAs undergo before becoming functional,
CC translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative
CC splicing regulation. Inhibits, together with CUGBP1, insulin receptor
CC (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds
CC poly(RG) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and
CC HNRNPH1. Identified in the spliceosome C complex. Interacts with
CC IGF2BP1. Interacts with CUGBP1; the interaction is RNA-dependent.
CC Interacts with MBNL1; the interaction in RNA-independent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-terminal
CC QRRM bound poly(RC) and poly(RU). None of the repeats bound detectable
CC amounts of poly(RA).
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DR EMBL; Y14196; CAA74583.1; -; mRNA.
DR EMBL; BC056224; AAH56224.1; -; mRNA.
DR CCDS; CCDS24634.1; -.
DR RefSeq; NP_067485.1; NM_021510.2.
DR RefSeq; XP_017170179.1; XM_017314690.1.
DR RefSeq; XP_017170180.1; XM_017314691.1.
DR AlphaFoldDB; O35737; -.
DR SMR; O35737; -.
DR BioGRID; 208484; 85.
DR CORUM; O35737; -.
DR IntAct; O35737; 19.
DR MINT; O35737; -.
DR STRING; 10090.ENSMUSP00000076989; -.
DR iPTMnet; O35737; -.
DR PhosphoSitePlus; O35737; -.
DR SwissPalm; O35737; -.
DR REPRODUCTION-2DPAGE; IPI00133916; -.
DR REPRODUCTION-2DPAGE; O35737; -.
DR EPD; O35737; -.
DR jPOST; O35737; -.
DR PaxDb; O35737; -.
DR PeptideAtlas; O35737; -.
DR PRIDE; O35737; -.
DR ProteomicsDB; 273303; -.
DR Antibodypedia; 17692; 330 antibodies from 29 providers.
DR DNASU; 59013; -.
DR Ensembl; ENSMUST00000069304; ENSMUSP00000070503; ENSMUSG00000007850.
DR Ensembl; ENSMUST00000109142; ENSMUSP00000104770; ENSMUSG00000007850.
DR GeneID; 59013; -.
DR KEGG; mmu:59013; -.
DR UCSC; uc007isj.1; mouse.
DR CTD; 3187; -.
DR MGI; MGI:1891925; Hnrnph1.
DR VEuPathDB; HostDB:ENSMUSG00000007850; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000153503; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; O35737; -.
DR OMA; SANEQHI; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 59013; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Hnrnph1; mouse.
DR PRO; PR:O35737; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35737; protein.
DR Bgee; ENSMUSG00000007850; Expressed in embryonic post-anal tail and 258 other tissues.
DR ExpressionAtlas; O35737; baseline and differential.
DR Genevisible; O35737; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR012996; Znf_CHHC.
DR Pfam; PF00076; RRM_1; 3.
DR Pfam; PF08080; zf-RNPHF; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..449
FT /note="Heterogeneous nuclear ribonucleoprotein H"
FT /id="PRO_0000081858"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT CHAIN 2..449
FT /note="Heterogeneous nuclear ribonucleoprotein H, N-
FT terminally processed"
FT /id="PRO_0000367120"
FT DOMAIN 11..90
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 111..188
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 234..249
FT /note="1-1"
FT DOMAIN 289..364
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 354..372
FT /note="2-1"
FT REPEAT 374..392
FT /note="2-2"
FT REPEAT 418..433
FT /note="1-2"
FT REGION 234..433
FT /note="2 X 16 AA Gly-rich approximate repeats"
FT REGION 354..392
FT /note="2 X 19 AA perfect repeats"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein H, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 233
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 233
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 246
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55795"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P31943"
SQ SEQUENCE 449 AA; 49199 MW; BF6138CA982D5484 CRC64;
MMLGAEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE GRPSGEAFVE
LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT GPNSPDTAND GFVRLRGLPF
GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY
IEIFKSSRAE VRTHYDPPRK LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY
GGYDDYNGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA NMQHRYVELF
LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY
GGGYGGQSSM SGYDQVLQEN SSDFQSNIA
