Full text data of HNRNPH3
HNRNPH3
(HNRPH3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Heterogeneous nuclear ribonucleoprotein H3; hnRNP H3 (Heterogeneous nuclear ribonucleoprotein 2H9; hnRNP 2H9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heterogeneous nuclear ribonucleoprotein H3; hnRNP H3 (Heterogeneous nuclear ribonucleoprotein 2H9; hnRNP 2H9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P31942
ID HNRH3_HUMAN Reviewed; 346 AA.
AC P31942; A8K682; B3KRE1; Q9BSX1; Q9NP53; Q9NP96; Q9NPA7; Q9NPI4;
read moreAC Q9UFU4; Q9Y4J5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 140.
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 MASS
RP 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 MASS
RP 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;
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.
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.
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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 PIR; T17207; T17207.
DR RefSeq; NP_036339.1; NM_012207.2.
DR RefSeq; NP_067676.2; NM_021644.3.
DR RefSeq; XP_005269805.1; XM_005269748.1.
DR RefSeq; XP_005269806.1; XM_005269749.1.
DR RefSeq; XP_005269808.1; XM_005269751.1.
DR RefSeq; XP_005269809.1; XM_005269752.1.
DR UniGene; Hs.643472; -.
DR ProteinModelPortal; P31942; -.
DR SMR; P31942; 10-97, 194-270.
DR IntAct; P31942; 44.
DR MINT; MINT-5004191; -.
DR PhosphoSite; P31942; -.
DR DMDM; 23503095; -.
DR PaxDb; P31942; -.
DR PRIDE; P31942; -.
DR Ensembl; ENST00000265866; ENSP00000265866; ENSG00000096746.
DR Ensembl; ENST00000354695; ENSP00000346726; ENSG00000096746.
DR GeneID; 3189; -.
DR KEGG; hsa:3189; -.
DR UCSC; uc001jnw.4; human.
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 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:HPA.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:UniProtKB.
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.
FT DOMAIN 195 270 RRM 2.
FT COMPBIAS 108 344 Gly-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 121 121 Asymmetric dimethylarginine.
FT MOD_RES 216 216 Phosphoserine.
FT MOD_RES 287 287 Omega-N-methylarginine.
FT MOD_RES 298 298 Phosphoserine.
FT MOD_RES 314 314 Phosphothreonine.
FT VAR_SEQ 1 137 Missing (in isoform 6).
FT /FTId=VSP_005841.
FT VAR_SEQ 1 131 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_005839.
FT VAR_SEQ 1 49 Missing (in isoform 3).
FT /FTId=VSP_005838.
FT VAR_SEQ 132 146 Missing (in isoform 2).
FT /FTId=VSP_005840.
FT VAR_SEQ 138 145 RGGDGYDG -> MCFSLNYT (in isoform 6).
FT /FTId=VSP_005842.
FT VAR_SEQ 259 276 QHRYIELFLNSTPGGGSG -> RKWCLWHTILFPKREFIK
FT (in isoform 5 and isoform 6).
FT /FTId=VSP_005843.
FT VAR_SEQ 277 346 Missing (in isoform 5 and isoform 6).
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
//
ID HNRH3_HUMAN Reviewed; 346 AA.
AC P31942; A8K682; B3KRE1; Q9BSX1; Q9NP53; Q9NP96; Q9NPA7; Q9NPI4;
read moreAC Q9UFU4; Q9Y4J5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 140.
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 MASS
RP 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 MASS
RP 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;
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.
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.
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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 PIR; T17207; T17207.
DR RefSeq; NP_036339.1; NM_012207.2.
DR RefSeq; NP_067676.2; NM_021644.3.
DR RefSeq; XP_005269805.1; XM_005269748.1.
DR RefSeq; XP_005269806.1; XM_005269749.1.
DR RefSeq; XP_005269808.1; XM_005269751.1.
DR RefSeq; XP_005269809.1; XM_005269752.1.
DR UniGene; Hs.643472; -.
DR ProteinModelPortal; P31942; -.
DR SMR; P31942; 10-97, 194-270.
DR IntAct; P31942; 44.
DR MINT; MINT-5004191; -.
DR PhosphoSite; P31942; -.
DR DMDM; 23503095; -.
DR PaxDb; P31942; -.
DR PRIDE; P31942; -.
DR Ensembl; ENST00000265866; ENSP00000265866; ENSG00000096746.
DR Ensembl; ENST00000354695; ENSP00000346726; ENSG00000096746.
DR GeneID; 3189; -.
DR KEGG; hsa:3189; -.
DR UCSC; uc001jnw.4; human.
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 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:HPA.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:UniProtKB.
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.
FT DOMAIN 195 270 RRM 2.
FT COMPBIAS 108 344 Gly-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 121 121 Asymmetric dimethylarginine.
FT MOD_RES 216 216 Phosphoserine.
FT MOD_RES 287 287 Omega-N-methylarginine.
FT MOD_RES 298 298 Phosphoserine.
FT MOD_RES 314 314 Phosphothreonine.
FT VAR_SEQ 1 137 Missing (in isoform 6).
FT /FTId=VSP_005841.
FT VAR_SEQ 1 131 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_005839.
FT VAR_SEQ 1 49 Missing (in isoform 3).
FT /FTId=VSP_005838.
FT VAR_SEQ 132 146 Missing (in isoform 2).
FT /FTId=VSP_005840.
FT VAR_SEQ 138 145 RGGDGYDG -> MCFSLNYT (in isoform 6).
FT /FTId=VSP_005842.
FT VAR_SEQ 259 276 QHRYIELFLNSTPGGGSG -> RKWCLWHTILFPKREFIK
FT (in isoform 5 and isoform 6).
FT /FTId=VSP_005843.
FT VAR_SEQ 277 346 Missing (in isoform 5 and isoform 6).
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
//
MIM
602324
*RECORD*
*FIELD* NO
602324
*FIELD* TI
*602324 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3; HNRNPH3
;;HNRPH3;;
2H9
*FIELD* TX
read moreThe RNAs found in the nucleus include pre-mRNAs, mature mRNAs, and
intermediate reaction products. Collectively these RNAs are termed
heterogeneous nuclear RNAs (hnRNAs). Ribonucleoprotein (RNP) complexes
consisting of hnRNAs and associated proteins are responsible for RNA
splicing and processing. Mahe et al. (1997) used antibodies against
ribonucleoprotein complexes to clone the gene of 1 such protein, which
the authors termed 2H9, from a human HeLa cell cDNA library. The
sequence of 2H9 predicts a 346-amino acid polypeptide containing 2
putative RNA binding domains. The 2H9 gene shares significant homology
with other RNPs, including HNRPH1 (601035), HNRPH2 (300610), and HNRPF
(601037). Specific antibodies against 2H9 can inhibit in vitro splicing,
suggesting that 2H9 is involved in this process. Immunofluorescence
staining revealed that 2H9 is localized to the nucleus, particularly in
nuclear bodies.
Mahe et al. (1997) used isotopic in situ hybridization to map the 2H9
gene to human chromosome 10q22.
*FIELD* RF
1. Mahe, D.; Mahl, P.; Gattoni, R.; Fischer, N.; Mattei, M.-G.; Stevenin,
J.; Fuchs, J.-P.: Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. J.
Biol. Chem. 272: 1827-1836, 1997.
*FIELD* CD
Jennifer P. Macke: 2/9/1998
*FIELD* ED
terry: 05/27/2010
wwang: 8/27/2008
dholmes: 2/11/1998
dholmes: 2/10/1998
*RECORD*
*FIELD* NO
602324
*FIELD* TI
*602324 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H3; HNRNPH3
;;HNRPH3;;
2H9
*FIELD* TX
read moreThe RNAs found in the nucleus include pre-mRNAs, mature mRNAs, and
intermediate reaction products. Collectively these RNAs are termed
heterogeneous nuclear RNAs (hnRNAs). Ribonucleoprotein (RNP) complexes
consisting of hnRNAs and associated proteins are responsible for RNA
splicing and processing. Mahe et al. (1997) used antibodies against
ribonucleoprotein complexes to clone the gene of 1 such protein, which
the authors termed 2H9, from a human HeLa cell cDNA library. The
sequence of 2H9 predicts a 346-amino acid polypeptide containing 2
putative RNA binding domains. The 2H9 gene shares significant homology
with other RNPs, including HNRPH1 (601035), HNRPH2 (300610), and HNRPF
(601037). Specific antibodies against 2H9 can inhibit in vitro splicing,
suggesting that 2H9 is involved in this process. Immunofluorescence
staining revealed that 2H9 is localized to the nucleus, particularly in
nuclear bodies.
Mahe et al. (1997) used isotopic in situ hybridization to map the 2H9
gene to human chromosome 10q22.
*FIELD* RF
1. Mahe, D.; Mahl, P.; Gattoni, R.; Fischer, N.; Mattei, M.-G.; Stevenin,
J.; Fuchs, J.-P.: Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. J.
Biol. Chem. 272: 1827-1836, 1997.
*FIELD* CD
Jennifer P. Macke: 2/9/1998
*FIELD* ED
terry: 05/27/2010
wwang: 8/27/2008
dholmes: 2/11/1998
dholmes: 2/10/1998