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   27-MAR-2024, entry version 182.
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}.
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; 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; 38.
DR   IntAct; P70333; 9.
DR   MINT; P70333; -.
DR   STRING; 10090.ENSMUSP00000108828; -.
DR   GlyGen; P70333; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P70333; -.
DR   PhosphoSitePlus; P70333; -.
DR   SwissPalm; P70333; -.
DR   EPD; P70333; -.
DR   jPOST; P70333; -.
DR   MaxQB; P70333; -.
DR   PaxDb; 10090-ENSMUSP00000108828; -.
DR   PeptideAtlas; P70333; -.
DR   ProteomicsDB; 273160; -.
DR   Pumba; P70333; -.
DR   Antibodypedia; 343; 170 antibodies from 24 providers.
DR   DNASU; 56258; -.
DR   Ensembl; ENSMUST00000050331.13; ENSMUSP00000108827.2; ENSMUSG00000045427.14.
DR   Ensembl; ENSMUST00000059297.6; ENSMUSP00000050838.6; ENSMUSG00000045427.14.
DR   Ensembl; ENSMUST00000074950.11; ENSMUSP00000074483.5; ENSMUSG00000045427.14.
DR   Ensembl; ENSMUST00000113202.8; ENSMUSP00000108828.2; ENSMUSG00000045427.14.
DR   Ensembl; ENSMUST00000113203.2; ENSMUSP00000108829.2; ENSMUSG00000045427.14.
DR   GeneID; 56258; -.
DR   KEGG; mmu:56258; -.
DR   UCSC; uc009ugh.1; mouse.
DR   AGR; MGI:1201779; -.
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; ATEMDWA; -.
DR   OrthoDB; 314723at2759; -.
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; 3 hits in 79 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 72 other cell types or tissues.
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   CDD; cd12729; RRM1_hnRNPH_hnRNPH2_hnRNPF; 1.
DR   CDD; cd12731; RRM2_hnRNPH_hnRNPH2_hnRNPF; 1.
DR   CDD; cd12734; RRM3_hnRNPH_hnRNPH2_hnRNPF; 1.
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   PANTHER; PTHR13976:SF33; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H2; 1.
DR   PANTHER; PTHR13976; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN-RELATED; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   Pfam; PF08080; zf-RNPHF; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR   PROSITE; PS50102; RRM; 3.
DR   Genevisible; P70333; MM.
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
//