ID HNRH3_HUMAN Reviewed; 346 AA. AC P31942; A8K682; B3KRE1; Q9BSX1; Q9NP53; Q9NP96; Q9NPA7; Q9NPI4; AC Q9UFU4; Q9Y4J5; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 01-OCT-2014, entry version 148. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H3; DE Short=hnRNP H3; DE AltName: Full=Heterogeneous nuclear ribonucleoprotein 2H9; DE Short=hnRNP 2H9; GN Name=HNRNPH3; Synonyms=HNRPH3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=8999868; DOI=10.1074/jbc.272.3.1827; RA Mahe D., Mahl P., Gattoni R., Fischer N., Mattei M.-G., Stevenin J., RA Fuchs J.-P.; RT "Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. RT Relation with splicing and early heat shock-induced splicing arrest."; RL J. Biol. Chem. 272:1827-1836(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND RP 6). RX PubMed=10858537; RA Honore B.; RT "The hnRNP 2H9 gene, which is involved in the splicing reaction, is a RT multiply spliced gene."; RL Biochim. Biophys. Acta 1492:108-119(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Brain, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary, and Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 1-6; 56-76; 85-90; 98-104; 175-200; 223-253 AND RP 262-323, ACETYLATION AT MET-1, METHYLATION AT ARG-287, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 56-67; 206-222; 233-253 AND 262-287, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 94-104 AND 288-298. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [10] RP PROTEIN SEQUENCE OF 116-127, AND METHYLATION AT ARG-121. RX PubMed=11152131; DOI=10.1110/ps.9.11.2210; RA Yague J., Vazquez J., Lopez de Castro J.A.; RT "A post-translational modification of nuclear proteins, N(G),N(G)- RT dimethyl-Arg, found in a natural HLA class I peptide ligand."; RL Protein Sci. 9:2210-2217(2000). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-298 AND RP THR-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-298, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-298, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). CC -!- FUNCTION: Involved in the splicing process and participates in CC early heat shock-induced splicing arrest. Due to their great CC structural variations the different isoforms may possess different CC functions in the splicing reaction. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8999868}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=P31942-1; Sequence=Displayed; CC Name=2; Synonyms=2H9A; CC IsoId=P31942-2; Sequence=VSP_005840; CC Name=3; Synonyms=2H9B; CC IsoId=P31942-3; Sequence=VSP_005838; CC Name=4; Synonyms=2H9C; CC IsoId=P31942-4; Sequence=VSP_005839; CC Name=5; Synonyms=2H9D; CC IsoId=P31942-5; Sequence=VSP_005839, VSP_005843, VSP_005844; CC Name=6; Synonyms=2H9E; CC IsoId=P31942-6; Sequence=VSP_005841, VSP_005842, VSP_005843, CC VSP_005844; CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00176}. 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; L32610; AAD45179.1; -; mRNA. DR EMBL; AF132360; AAF68843.1; -; Genomic_DNA. DR EMBL; AF132360; AAF68844.1; -; Genomic_DNA. DR EMBL; AF132360; AAF68845.1; -; Genomic_DNA. DR EMBL; AF132360; AAF68846.1; -; Genomic_DNA. DR EMBL; AF132360; AAF68847.1; -; Genomic_DNA. DR EMBL; AF132360; AAF68848.1; -; Genomic_DNA. DR EMBL; AF132361; AAF68849.1; -; mRNA. DR EMBL; AF132362; AAF68850.1; -; mRNA. DR EMBL; AF132363; AAF68851.1; -; mRNA. DR EMBL; AF132364; AAF68852.1; -; mRNA. DR EMBL; AK091411; BAG52353.1; -; mRNA. DR EMBL; AK291547; BAF84236.1; -; mRNA. DR EMBL; AL117395; CAB55897.1; -; mRNA. DR EMBL; CH471083; EAW54281.1; -; Genomic_DNA. DR EMBL; CH471083; EAW54282.1; -; Genomic_DNA. DR EMBL; BC004511; AAH04511.2; -; mRNA. DR EMBL; BC039824; AAH39824.1; -; mRNA. DR CCDS; CCDS7278.1; -. [P31942-1] DR CCDS; CCDS7279.1; -. [P31942-2] DR PIR; T17207; T17207. DR RefSeq; NP_036339.1; NM_012207.2. [P31942-1] DR RefSeq; NP_067676.2; NM_021644.3. [P31942-2] DR RefSeq; XP_005269805.1; XM_005269748.2. [P31942-1] DR RefSeq; XP_005269806.1; XM_005269749.2. [P31942-2] DR RefSeq; XP_005269808.1; XM_005269751.2. [P31942-4] DR RefSeq; XP_005269809.1; XM_005269752.2. [P31942-4] DR RefSeq; XP_006717879.1; XM_006717816.1. [P31942-1] DR RefSeq; XP_006717880.1; XM_006717817.1. [P31942-2] DR UniGene; Hs.643472; -. DR ProteinModelPortal; P31942; -. DR SMR; P31942; 10-97, 194-270. DR BioGrid; 109430; 65. DR IntAct; P31942; 46. DR MINT; MINT-5004191; -. DR PhosphoSite; P31942; -. DR DMDM; 23503095; -. DR MaxQB; P31942; -. DR PaxDb; P31942; -. DR PRIDE; P31942; -. DR Ensembl; ENST00000265866; ENSP00000265866; ENSG00000096746. [P31942-1] DR Ensembl; ENST00000354695; ENSP00000346726; ENSG00000096746. [P31942-2] DR GeneID; 3189; -. DR KEGG; hsa:3189; -. DR UCSC; uc001jnw.4; human. [P31942-1] DR UCSC; uc001jnx.4; human. [P31942-2] DR CTD; 3189; -. DR GeneCards; GC10P070090; -. DR HGNC; HGNC:5043; HNRNPH3. DR HPA; HPA038264; -. DR MIM; 602324; gene. DR neXtProt; NX_P31942; -. DR PharmGKB; PA162391325; -. DR eggNOG; NOG262593; -. DR HOVERGEN; HBG055557; -. DR InParanoid; P31942; -. DR KO; K12898; -. DR OMA; PYDRPLG; -. DR OrthoDB; EOG7BS4BZ; -. DR PhylomeDB; P31942; -. DR TreeFam; TF316157; -. DR ChiTaRS; HNRNPH3; human. DR GeneWiki; HNRPH3; -. DR GenomeRNAi; 3189; -. DR NextBio; 12680; -. DR PRO; PR:P31942; -. DR ArrayExpress; P31942; -. DR Bgee; P31942; -. DR CleanEx; HS_HNRNPH3; -. DR Genevestigator; P31942; -. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProt. DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProt. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:UniProtKB. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Methylation; mRNA processing; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Ribonucleoprotein; RNA-binding. FT CHAIN 1 346 Heterogeneous nuclear ribonucleoprotein FT H3. FT /FTId=PRO_0000081861. FT DOMAIN 16 93 RRM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 195 270 RRM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT COMPBIAS 108 344 Gly-rich. FT MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.7}. FT MOD_RES 121 121 Asymmetric dimethylarginine. FT {ECO:0000269|PubMed:11152131}. FT MOD_RES 216 216 Phosphoserine. FT {ECO:0000269|PubMed:17081983, FT ECO:0000269|PubMed:18669648, FT ECO:0000269|PubMed:18691976, FT ECO:0000269|PubMed:19369195, FT ECO:0000269|PubMed:19690332, FT ECO:0000269|PubMed:20068231, FT ECO:0000269|PubMed:21406692}. FT MOD_RES 287 287 Omega-N-methylarginine. FT {ECO:0000269|Ref.7}. FT MOD_RES 298 298 Phosphoserine. FT {ECO:0000269|PubMed:19690332, FT ECO:0000269|PubMed:20068231, FT ECO:0000269|PubMed:21406692}. FT MOD_RES 314 314 Phosphothreonine. FT {ECO:0000269|PubMed:19690332}. FT VAR_SEQ 1 137 Missing (in isoform 6). FT {ECO:0000303|PubMed:10858537}. FT /FTId=VSP_005841. FT VAR_SEQ 1 131 Missing (in isoform 4 and isoform 5). FT {ECO:0000303|PubMed:10858537, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005}. FT /FTId=VSP_005839. FT VAR_SEQ 1 49 Missing (in isoform 3). FT {ECO:0000303|PubMed:10858537}. FT /FTId=VSP_005838. FT VAR_SEQ 132 146 Missing (in isoform 2). FT {ECO:0000303|PubMed:10858537, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_005840. FT VAR_SEQ 138 145 RGGDGYDG -> MCFSLNYT (in isoform 6). FT {ECO:0000303|PubMed:10858537}. FT /FTId=VSP_005842. FT VAR_SEQ 259 276 QHRYIELFLNSTPGGGSG -> RKWCLWHTILFPKREFIK FT (in isoform 5 and isoform 6). FT {ECO:0000303|PubMed:10858537}. FT /FTId=VSP_005843. FT VAR_SEQ 277 346 Missing (in isoform 5 and isoform 6). FT {ECO:0000303|PubMed:10858537}. FT /FTId=VSP_005844. FT VARIANT 163 163 N -> S (in dbSNP:rs2273903). FT /FTId=VAR_020333. FT VARIANT 284 284 G -> A (in dbSNP:rs16925347). FT /FTId=VAR_052226. SQ SEQUENCE 346 AA; 36926 MW; F7D14C2947930E9E CRC64; MDWVMKHNGP NDASDGTVRL RGLPFGCSKE EIVQFFQGLE IVPNGITLTM DYQGRSTGEA FVQFASKEIA ENALGKHKER IGHRYIEIFR SSRSEIKGFY DPPRRLLGQR PGPYDRPIGG RGGYYGAGRG SMYDRMRRGG DGYDGGYGGF DDYGGYNNYG YGNDGFDDRM RDGRGMGGHG YGGAGDASSG FHGGHFVHMR GLPFRATEND IANFFSPLNP IRVHIDIGAD GRATGEADVE FVTHEDAVAA MSKDKNNMQH RYIELFLNST PGGGSGMGGS GMGGYGRDGM DNQGGYGSVG RMGMGNNYSG GYGTPDGLGG YGRGGGGSGG YYGQGGMSGG GWRGMY //