HNRH2_MOUSE
ID HNRH2_MOUSE Reviewed; 449 AA.
AC P70333; Q3THV9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H2;
DE Short=hnRNP H2;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein H';
DE Short=hnRNP H';
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed;
GN Name=Hnrnph2; Synonyms=Hnrph2;
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 [GENOMIC DNA].
RC STRAIN=C129;
RX PubMed=7626884; DOI=10.1007/bf00364796;
RA Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W.,
RA Gibbs R.A.;
RT "Sixty-nine kilobases of contiguous human genomic sequence containing the
RT alpha-galactosidase A and Bruton's tyrosine kinase loci.";
RL Mamm. Genome 6:334-338(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Kidney, and Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-310, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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. Binds poly(RG) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a ribonucleoprotein complex containing mRNAs and
CC RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as
CC splicing regulator ARVCF. Interacts with TXNL4/DIM1.
CC {ECO:0000250|UniProtKB:P55795}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P55795}.
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DR EMBL; U58105; AAB47243.1; -; Genomic_DNA.
DR EMBL; AK077716; BAC36976.1; -; mRNA.
DR EMBL; AK164115; BAE37634.1; -; mRNA.
DR EMBL; AK168116; BAE40087.1; -; mRNA.
DR EMBL; AK169104; BAE40886.1; -; mRNA.
DR EMBL; BC005461; AAH05461.1; -; mRNA.
DR CCDS; CCDS30397.1; -.
DR RefSeq; NP_001300645.1; NM_001313716.1.
DR RefSeq; NP_001300646.1; NM_001313717.1.
DR RefSeq; NP_063921.1; NM_019868.4.
DR AlphaFoldDB; P70333; -.
DR SMR; P70333; -.
DR BioGRID; 207865; 34.
DR IntAct; P70333; 8.
DR MINT; P70333; -.
DR STRING; 10090.ENSMUSP00000108828; -.
DR iPTMnet; P70333; -.
DR PhosphoSitePlus; P70333; -.
DR SwissPalm; P70333; -.
DR EPD; P70333; -.
DR jPOST; P70333; -.
DR MaxQB; P70333; -.
DR PaxDb; P70333; -.
DR PeptideAtlas; P70333; -.
DR PRIDE; P70333; -.
DR ProteomicsDB; 273160; -.
DR Antibodypedia; 343; 140 antibodies from 23 providers.
DR DNASU; 56258; -.
DR Ensembl; ENSMUST00000050331; ENSMUSP00000108827; ENSMUSG00000045427.
DR Ensembl; ENSMUST00000059297; ENSMUSP00000050838; ENSMUSG00000045427.
DR Ensembl; ENSMUST00000074950; ENSMUSP00000074483; ENSMUSG00000045427.
DR Ensembl; ENSMUST00000113202; ENSMUSP00000108828; ENSMUSG00000045427.
DR Ensembl; ENSMUST00000113203; ENSMUSP00000108829; ENSMUSG00000045427.
DR GeneID; 56258; -.
DR KEGG; mmu:56258; -.
DR UCSC; uc009ugh.1; mouse.
DR CTD; 3188; -.
DR MGI; MGI:1201779; Hnrnph2.
DR VEuPathDB; HostDB:ENSMUSG00000045427; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000153503; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; P70333; -.
DR OMA; GSRNRDF; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; P70333; -.
DR TreeFam; TF316157; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 56258; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Hnrnph2; mouse.
DR PRO; PR:P70333; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70333; protein.
DR Bgee; ENSMUSG00000045427; Expressed in ventricular zone and 69 other tissues.
DR Genevisible; P70333; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
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; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..449
FT /note="Heterogeneous nuclear ribonucleoprotein H2"
FT /id="PRO_0000434386"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT CHAIN 2..449
FT /note="Heterogeneous nuclear ribonucleoprotein H2, N-
FT terminally processed"
FT /id="PRO_0000081860"
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 H2, 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 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:21183079"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55795"
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; 49280 MW; 2ED0A7A87A7EDF5E CRC64;
MMLSTEGREG FVVKVRGLPW SCSAEEVMRF FSDCKIQNGT SGVRFIYTRE GRPSGEAFVE
LESEDEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT GPNSPDTAND GFVRLRGLPF
GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY
IEIFKSSRAE VRTHYDPPRK LMTMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY
GGYDDYGGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA
TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA NMQHRYVELF
LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY
GGGYGGQSSM SGYDQVLQEN SSDYQSNLA
