HNRH1_HUMAN
ID HNRH1_HUMAN Reviewed; 449 AA.
AC P31943; B3KW86; D3DWQ2; Q6IBM4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 225.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 180-184; 193-197 AND
RP 200-230.
RX PubMed=7499401; DOI=10.1074/jbc.270.48.28780;
RA Honore B., Rasmussen H.H., Vorum H., Dejgaard K., Liu X., Gromov P.,
RA Madsen P., Gesser B., Tommerup N., Celis J.E.;
RT "Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a
RT ubiquitously expressed subfamily of related but distinct proteins encoded
RT by genes mapping to different chromosomes.";
RL J. Biol. Chem. 270:28780-28789(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [6]
RP PROTEIN SEQUENCE OF 1-14; 17-44; 50-68; 82-114; 151-167; 180-185; 233-259;
RP 276-294; 300-347 AND 356-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT MET-1 AND MET-2, METHYLATION AT ARG-233, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma, Cervix carcinoma, Hepatoma, Lung carcinoma,
RC Mammary carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A., Matallanas D., Cooper W.N.,
RA Calvo F., Kolch W., Vousden K.H., Lukashchuk N., Lilla S., Lempens A.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 2-14; 17-29; 88-114; 151-167; 263-275; 300-347;
RP 344-375; 377-386; 418-432; 473-483 AND 542-553, AND IDENTIFICATION BY 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 [8]
RP PROTEIN SEQUENCE OF 127-135 AND 153-163.
RX PubMed=7512260; DOI=10.1093/nar/22.6.1059;
RA Matunis M.J., Xing J., Dreyfuss G.;
RT "The hnRNP F protein: unique primary structure, nucleic acid-binding
RT properties, and subcellular localization.";
RL Nucleic Acids Res. 22:1059-1067(1994).
RN [9]
RP PROTEIN SEQUENCE OF 200-230.
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 protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [10]
RP FUNCTION, AND INTERACTION WITH PTBP1; PTBP2 AND FUBP2.
RX PubMed=11003644; DOI=10.1128/mcb.20.20.7463-7479.2000;
RA Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y.,
RA Black D.L.;
RT "Cooperative assembly of an hnRNP complex induced by a tissue-specific
RT homolog of polypyrimidine tract binding protein.";
RL Mol. Cell. Biol. 20:7463-7479(2000).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, AND IDENTIFICATION BY
RP 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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP FUNCTION, INTERACTION WITH CUGBP1 AND MBNL1, RNA-BINDING, AND INDUCTION.
RX PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
RA Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S.;
RT "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated
RT aberrant IR splicing.";
RL EMBO J. 25:4271-4283(2006).
RN [15]
RP INTERACTION WITH IGF2BP1.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP 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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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., Buerckstuemmer T.,
RA 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-54 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-233, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35; LYS-87 AND LYS-98, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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). {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:16946708}.
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.
CC {ECO:0000269|PubMed:11003644, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC P31943; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-351590, EBI-1057448;
CC P31943; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-351590, EBI-744545;
CC P31943; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-351590, EBI-744556;
CC P31943; O75909-2: CCNK; NbExp=3; IntAct=EBI-351590, EBI-12010594;
CC P31943; Q92841: DDX17; NbExp=3; IntAct=EBI-351590, EBI-746012;
CC P31943; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-351590, EBI-948630;
CC P31943; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-351590, EBI-744099;
CC P31943; O95872: GPANK1; NbExp=3; IntAct=EBI-351590, EBI-751540;
CC P31943; Q13227: GPS2; NbExp=3; IntAct=EBI-351590, EBI-713355;
CC P31943; P52597: HNRNPF; NbExp=3; IntAct=EBI-351590, EBI-352986;
CC P31943; P31943: HNRNPH1; NbExp=3; IntAct=EBI-351590, EBI-351590;
CC P31943; P52272: HNRNPM; NbExp=3; IntAct=EBI-351590, EBI-486809;
CC P31943; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-351590, EBI-11953846;
CC P31943; P25800: LMO1; NbExp=3; IntAct=EBI-351590, EBI-8639312;
CC P31943; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-351590, EBI-11742507;
CC P31943; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-351590, EBI-739832;
CC P31943; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-351590, EBI-716006;
CC P31943; Q9NR56: MBNL1; NbExp=2; IntAct=EBI-351590, EBI-2805004;
CC P31943; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-351590, EBI-2513715;
CC P31943; Q96DH6: MSI2; NbExp=3; IntAct=EBI-351590, EBI-2462339;
CC P31943; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-351590, EBI-2858213;
CC P31943; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-351590, EBI-10271199;
CC P31943; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-351590, EBI-2949792;
CC P31943; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-351590, EBI-12813389;
CC P31943; Q9HBE1-4: PATZ1; NbExp=6; IntAct=EBI-351590, EBI-11022007;
CC P31943; P50542-3: PEX5; NbExp=3; IntAct=EBI-351590, EBI-12181987;
CC P31943; O15160: POLR1C; NbExp=4; IntAct=EBI-351590, EBI-1055079;
CC P31943; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-351590, EBI-12000762;
CC P31943; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-351590, EBI-744023;
CC P31943; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-351590, EBI-11963050;
CC P31943; Q9H0Z9: RBM38; NbExp=3; IntAct=EBI-351590, EBI-2840723;
CC P31943; P78317: RNF4; NbExp=3; IntAct=EBI-351590, EBI-2340927;
CC P31943; P14678-2: SNRPB; NbExp=3; IntAct=EBI-351590, EBI-372475;
CC P31943; P09234: SNRPC; NbExp=3; IntAct=EBI-351590, EBI-766589;
CC P31943; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-351590, EBI-742688;
CC P31943; Q13148: TARDBP; NbExp=7; IntAct=EBI-351590, EBI-372899;
CC P31943; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-351590, EBI-8644516;
CC P31943; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-351590, EBI-750487;
CC P31943; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-351590, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- INDUCTION: Up-regulated in myotonic dystrophy pathophysiology (DM).
CC {ECO:0000269|PubMed:16946708}.
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).
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; L22009; AAA91346.1; -; mRNA.
DR EMBL; CR456778; CAG33059.1; -; mRNA.
DR EMBL; AK124530; BAG54048.1; -; mRNA.
DR EMBL; CH471165; EAW53807.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53808.1; -; Genomic_DNA.
DR EMBL; BC001348; AAH01348.1; -; mRNA.
DR CCDS; CCDS4446.1; -.
DR PIR; I39358; I39358.
DR RefSeq; NP_001244222.1; NM_001257293.1.
DR RefSeq; NP_005511.1; NM_005520.2.
DR RefSeq; XP_016864904.1; XM_017009415.1.
DR RefSeq; XP_016864905.1; XM_017009416.1.
DR RefSeq; XP_016864906.1; XM_017009417.1.
DR PDB; 2LXU; NMR; -; A=7-111.
DR PDB; 6DHS; X-ray; 3.50 A; A/B/C/D=10-194.
DR PDBsum; 2LXU; -.
DR PDBsum; 6DHS; -.
DR AlphaFoldDB; P31943; -.
DR SMR; P31943; -.
DR BioGRID; 109428; 1493.
DR CORUM; P31943; -.
DR IntAct; P31943; 146.
DR MINT; P31943; -.
DR STRING; 9606.ENSP00000349168; -.
DR ChEMBL; CHEMBL3797013; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; P31943; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P31943; -.
DR MetOSite; P31943; -.
DR PhosphoSitePlus; P31943; -.
DR SwissPalm; P31943; -.
DR BioMuta; HNRNPH1; -.
DR DMDM; 1710632; -.
DR REPRODUCTION-2DPAGE; IPI00013881; -.
DR REPRODUCTION-2DPAGE; P31943; -.
DR EPD; P31943; -.
DR jPOST; P31943; -.
DR MassIVE; P31943; -.
DR MaxQB; P31943; -.
DR PaxDb; P31943; -.
DR PeptideAtlas; P31943; -.
DR PRIDE; P31943; -.
DR ProteomicsDB; 54814; -.
DR Antibodypedia; 17692; 330 antibodies from 29 providers.
DR DNASU; 3187; -.
DR Ensembl; ENST00000356731.9; ENSP00000349168.5; ENSG00000169045.17.
DR Ensembl; ENST00000393432.8; ENSP00000377082.4; ENSG00000169045.17.
DR Ensembl; ENST00000442819.6; ENSP00000397797.2; ENSG00000169045.17.
DR Ensembl; ENST00000638505.2; ENSP00000492076.2; ENSG00000284254.3.
DR Ensembl; ENST00000643310.2; ENSP00000495786.2; ENSG00000284254.3.
DR GeneID; 3187; -.
DR KEGG; hsa:3187; -.
DR MANE-Select; ENST00000393432.9; ENSP00000377082.4; NM_001257293.2; NP_001244222.1.
DR UCSC; uc003mke.5; human.
DR CTD; 3187; -.
DR DisGeNET; 3187; -.
DR GeneCards; HNRNPH1; -.
DR HGNC; HGNC:5041; HNRNPH1.
DR HPA; ENSG00000169045; Low tissue specificity.
DR MalaCards; HNRNPH1; -.
DR MIM; 601035; gene.
DR neXtProt; NX_P31943; -.
DR OpenTargets; ENSG00000169045; -.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA162391284; -.
DR VEuPathDB; HostDB:ENSG00000169045; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000153503; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; P31943; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; P31943; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; P31943; -.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; P31943; -.
DR SIGNOR; P31943; -.
DR BioGRID-ORCS; 3187; 674 hits in 1094 CRISPR screens.
DR ChiTaRS; HNRNPH1; human.
DR GeneWiki; HNRPH1; -.
DR GenomeRNAi; 3187; -.
DR Pharos; P31943; Tbio.
DR PRO; PR:P31943; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P31943; protein.
DR Bgee; ENSG00000169045; Expressed in right lobe of thyroid gland and 118 other tissues.
DR ExpressionAtlas; P31943; baseline and differential.
DR Genevisible; P31943; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008266; F:poly(U) RNA binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
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 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Methylation; 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_0000367119"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..449
FT /note="Heterogeneous nuclear ribonucleoprotein H, N-
FT terminally processed"
FT /id="PRO_0000081857"
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; in Heterogeneous nuclear
FT ribonucleoprotein H; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein H, N-terminally processed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 233
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 233
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315"
FT MOD_RES 246
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
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:0007744|PubMed:28112733"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 188
FT /note="R -> G (in Ref. 2; CAG33059)"
FT /evidence="ECO:0000305"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:6DHS"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:6DHS"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2LXU"
FT TURN 37..41
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6DHS"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 75..87
FT /evidence="ECO:0007829|PDB:6DHS"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6DHS"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6DHS"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:6DHS"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6DHS"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6DHS"
SQ SEQUENCE 449 AA; 49229 MW; 4ECF7A075C2526FF CRC64;
MMLGTEGGEG 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
