Full text data of HNRNPH1
HNRNPH1
(HNRPH, HNRPH1)
[Confidence: low (only semi-automatic identification from reviews)]
Heterogeneous nuclear ribonucleoprotein H; hnRNP H; Heterogeneous nuclear ribonucleoprotein H, N-terminally processed
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heterogeneous nuclear ribonucleoprotein H; hnRNP H; Heterogeneous nuclear ribonucleoprotein H, N-terminally processed
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P31943
ID HNRH1_HUMAN Reviewed; 449 AA.
AC P31943; B3KW86; D3DWQ2; Q6IBM4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 156.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 180-184; 193-197
RP AND 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
RT a ubiquitously expressed subfamily of related but distinct proteins
RT encoded 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.,
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 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 (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
RT project: 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;
RP 233-259; 276-294; 300-347 AND 356-375, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT MET-1 AND MET-2, METHYLATION AT ARG-233,
RP AND MASS 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.,
RA Cooper W.N., Calvo F., Kolch W., Vousden K.H., Lukashchuk N.,
RA 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 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 [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
RT protein 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
RP SPLICEOSOMAL 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 MASS
RP SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [14]
RP FUNCTION, INTERACTION WITH CUGBP1 AND MBNL1, RNA-BINDING, AND
RP INDUCTION.
RX PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
RA Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L.,
RA Reddy S.;
RT "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-
RT associated 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 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, AND MASS
RP SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP 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 [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.,
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP 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).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, AND MASS
RP SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: This protein is a component of the heterogeneous nuclear
CC ribonucleoprotein (hnRNP) complexes which provide the substrate
CC for the processing events that pre-mRNAs undergo before becoming
CC functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA
CC alternative splicing regulation. Inhibits, together with CUGBP1,
CC insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast.
CC Binds to the IR RNA. Binds poly(RG).
CC -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
CC and HNRNPH1. Identified in the spliceosome C complex. Interacts
CC with IGF2BP1. Interacts with CUGBP1; the interaction is RNA-
CC dependent. Interacts with MBNL1; the interaction in RNA-
CC independent.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- INDUCTION: Up-regulated in myotonic dystrophy pathophysiology
CC (DM).
CC -!- DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-
CC terminal QRRM bound poly(RC) and poly(RU). None of the repeats
CC bound detectable amounts of poly(RA).
CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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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 PIR; I39358; I39358.
DR RefSeq; NP_001244222.1; NM_001257293.1.
DR RefSeq; NP_005511.1; NM_005520.2.
DR UniGene; Hs.604001; -.
DR PDB; 2LXU; NMR; -; A=7-111.
DR PDBsum; 2LXU; -.
DR ProteinModelPortal; P31943; -.
DR SMR; P31943; 7-193, 283-393.
DR IntAct; P31943; 55.
DR MINT; MINT-1160934; -.
DR STRING; 9606.ENSP00000349168; -.
DR PhosphoSite; P31943; -.
DR DMDM; 1710632; -.
DR REPRODUCTION-2DPAGE; IPI00013881; -.
DR REPRODUCTION-2DPAGE; P31943; -.
DR PaxDb; P31943; -.
DR PRIDE; P31943; -.
DR Ensembl; ENST00000356731; ENSP00000349168; ENSG00000169045.
DR Ensembl; ENST00000393432; ENSP00000377082; ENSG00000169045.
DR Ensembl; ENST00000442819; ENSP00000397797; ENSG00000169045.
DR GeneID; 3187; -.
DR KEGG; hsa:3187; -.
DR UCSC; uc003mke.4; human.
DR CTD; 3187; -.
DR GeneCards; GC05M179043; -.
DR HGNC; HGNC:5041; HNRNPH1.
DR HPA; HPA001359; -.
DR HPA; HPA016884; -.
DR MIM; 601035; gene.
DR neXtProt; NX_P31943; -.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA162391284; -.
DR eggNOG; NOG262593; -.
DR HOGENOM; HOG000220896; -.
DR HOVERGEN; HBG055557; -.
DR KO; K12898; -.
DR OrthoDB; EOG7BS4BZ; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; HNRNPH1; human.
DR GeneWiki; HNRPH1; -.
DR GenomeRNAi; 3187; -.
DR NextBio; 12670; -.
DR PRO; PR:P31943; -.
DR ArrayExpress; P31943; -.
DR Bgee; P31943; -.
DR CleanEx; HS_HNRNPH1; -.
DR Genevestigator; P31943; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008266; F:poly(U) RNA binding; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR012996; Znf_CHHC.
DR Pfam; PF08080; zf-RNPHF; 1.
DR SMART; SM00360; RRM; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1 449 Heterogeneous nuclear ribonucleoprotein
FT H.
FT /FTId=PRO_0000367119.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 449 Heterogeneous nuclear ribonucleoprotein
FT H, N-terminally processed.
FT /FTId=PRO_0000081857.
FT DOMAIN 11 90 RRM 1.
FT DOMAIN 111 188 RRM 2.
FT REPEAT 234 249 1-1.
FT DOMAIN 289 364 RRM 3.
FT REPEAT 354 372 2-1.
FT REPEAT 374 392 2-2.
FT REPEAT 418 433 1-2.
FT REGION 234 433 2 X 16 AA Gly-rich approximate repeats.
FT REGION 354 392 2 X 19 AA perfect repeats.
FT MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
FT nuclear ribonucleoprotein H; alternate.
FT MOD_RES 2 2 N-acetylmethionine; in Heterogeneous
FT nuclear ribonucleoprotein H, N-terminally
FT processed.
FT MOD_RES 23 23 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT MOD_RES 233 233 Dimethylated arginine; alternate.
FT MOD_RES 233 233 Omega-N-methylarginine; alternate.
FT MOD_RES 246 246 Phosphotyrosine.
FT MOD_RES 310 310 Phosphoserine (By similarity).
FT CONFLICT 188 188 R -> G (in Ref. 2; CAG33059).
FT STRAND 9 17
FT HELIX 24 30
FT TURN 31 33
FT HELIX 39 41
FT STRAND 42 47
FT STRAND 51 62
FT HELIX 64 71
FT TURN 72 75
FT STRAND 84 88
FT HELIX 90 98
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
//
ID HNRH1_HUMAN Reviewed; 449 AA.
AC P31943; B3KW86; D3DWQ2; Q6IBM4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 156.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 180-184; 193-197
RP AND 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
RT a ubiquitously expressed subfamily of related but distinct proteins
RT encoded 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.,
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 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 (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
RT project: 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;
RP 233-259; 276-294; 300-347 AND 356-375, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT MET-1 AND MET-2, METHYLATION AT ARG-233,
RP AND MASS 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.,
RA Cooper W.N., Calvo F., Kolch W., Vousden K.H., Lukashchuk N.,
RA 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 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 [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
RT protein 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
RP SPLICEOSOMAL 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 MASS
RP SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [14]
RP FUNCTION, INTERACTION WITH CUGBP1 AND MBNL1, RNA-BINDING, AND
RP INDUCTION.
RX PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
RA Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L.,
RA Reddy S.;
RT "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-
RT associated 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 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, AND MASS
RP SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP 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 [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.,
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP 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).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, AND MASS
RP SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: This protein is a component of the heterogeneous nuclear
CC ribonucleoprotein (hnRNP) complexes which provide the substrate
CC for the processing events that pre-mRNAs undergo before becoming
CC functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA
CC alternative splicing regulation. Inhibits, together with CUGBP1,
CC insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast.
CC Binds to the IR RNA. Binds poly(RG).
CC -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
CC and HNRNPH1. Identified in the spliceosome C complex. Interacts
CC with IGF2BP1. Interacts with CUGBP1; the interaction is RNA-
CC dependent. Interacts with MBNL1; the interaction in RNA-
CC independent.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- INDUCTION: Up-regulated in myotonic dystrophy pathophysiology
CC (DM).
CC -!- DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-
CC terminal QRRM bound poly(RC) and poly(RU). None of the repeats
CC bound detectable amounts of poly(RA).
CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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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 PIR; I39358; I39358.
DR RefSeq; NP_001244222.1; NM_001257293.1.
DR RefSeq; NP_005511.1; NM_005520.2.
DR UniGene; Hs.604001; -.
DR PDB; 2LXU; NMR; -; A=7-111.
DR PDBsum; 2LXU; -.
DR ProteinModelPortal; P31943; -.
DR SMR; P31943; 7-193, 283-393.
DR IntAct; P31943; 55.
DR MINT; MINT-1160934; -.
DR STRING; 9606.ENSP00000349168; -.
DR PhosphoSite; P31943; -.
DR DMDM; 1710632; -.
DR REPRODUCTION-2DPAGE; IPI00013881; -.
DR REPRODUCTION-2DPAGE; P31943; -.
DR PaxDb; P31943; -.
DR PRIDE; P31943; -.
DR Ensembl; ENST00000356731; ENSP00000349168; ENSG00000169045.
DR Ensembl; ENST00000393432; ENSP00000377082; ENSG00000169045.
DR Ensembl; ENST00000442819; ENSP00000397797; ENSG00000169045.
DR GeneID; 3187; -.
DR KEGG; hsa:3187; -.
DR UCSC; uc003mke.4; human.
DR CTD; 3187; -.
DR GeneCards; GC05M179043; -.
DR HGNC; HGNC:5041; HNRNPH1.
DR HPA; HPA001359; -.
DR HPA; HPA016884; -.
DR MIM; 601035; gene.
DR neXtProt; NX_P31943; -.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA162391284; -.
DR eggNOG; NOG262593; -.
DR HOGENOM; HOG000220896; -.
DR HOVERGEN; HBG055557; -.
DR KO; K12898; -.
DR OrthoDB; EOG7BS4BZ; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; HNRNPH1; human.
DR GeneWiki; HNRPH1; -.
DR GenomeRNAi; 3187; -.
DR NextBio; 12670; -.
DR PRO; PR:P31943; -.
DR ArrayExpress; P31943; -.
DR Bgee; P31943; -.
DR CleanEx; HS_HNRNPH1; -.
DR Genevestigator; P31943; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008266; F:poly(U) RNA binding; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR012996; Znf_CHHC.
DR Pfam; PF08080; zf-RNPHF; 1.
DR SMART; SM00360; RRM; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1 449 Heterogeneous nuclear ribonucleoprotein
FT H.
FT /FTId=PRO_0000367119.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 449 Heterogeneous nuclear ribonucleoprotein
FT H, N-terminally processed.
FT /FTId=PRO_0000081857.
FT DOMAIN 11 90 RRM 1.
FT DOMAIN 111 188 RRM 2.
FT REPEAT 234 249 1-1.
FT DOMAIN 289 364 RRM 3.
FT REPEAT 354 372 2-1.
FT REPEAT 374 392 2-2.
FT REPEAT 418 433 1-2.
FT REGION 234 433 2 X 16 AA Gly-rich approximate repeats.
FT REGION 354 392 2 X 19 AA perfect repeats.
FT MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
FT nuclear ribonucleoprotein H; alternate.
FT MOD_RES 2 2 N-acetylmethionine; in Heterogeneous
FT nuclear ribonucleoprotein H, N-terminally
FT processed.
FT MOD_RES 23 23 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT MOD_RES 233 233 Dimethylated arginine; alternate.
FT MOD_RES 233 233 Omega-N-methylarginine; alternate.
FT MOD_RES 246 246 Phosphotyrosine.
FT MOD_RES 310 310 Phosphoserine (By similarity).
FT CONFLICT 188 188 R -> G (in Ref. 2; CAG33059).
FT STRAND 9 17
FT HELIX 24 30
FT TURN 31 33
FT HELIX 39 41
FT STRAND 42 47
FT STRAND 51 62
FT HELIX 64 71
FT TURN 72 75
FT STRAND 84 88
FT HELIX 90 98
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
//
MIM
601035
*RECORD*
*FIELD* NO
601035
*FIELD* TI
*601035 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H1; HNRNPH1
;;HNRPH1;;
HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H
read more*FIELD* TX
CLONING
Heterogeneous nuclear ribonucleoproteins (hnRNPs) constitute a set of
polypeptides that bind heterogeneous nuclear RNA (hnRNA), the
transcripts produced by RNA polymerase II (see 180660). More than 20
such proteins have been described and designated with letters from A to
U. By molecular cDNA cloning, 2-dimensional gel immunoblotting, and
amino acid microsequencing, Honore et al. (1995) identified 3
sequence-unique and distinct proteins that constitute a subfamily of
ubiquitously expressed hnRNPs. The identity between hnRNPs H and H-prime
(300610) was 96%, between H and F (601037), 78%, and between H-prime and
F, 75%.
MAPPING
By fluorescence in situ hybridization, Honore et al. (1995) mapped the
HNRNPH1 gene to chromosome 5q35.3.
GENE FUNCTION
Masuda et al. (2008) identified a key nucleotide in an intron of the
CHRNA1 gene (100690) that is part of an intronic splicing silencer (ISS)
sequence targeted by hnRNP H and suppresses inclusion of an alternative
exon in the CHRNA1 gene. Analysis of the human genome suggested that the
hnRNP H-binding motif 'UGGG' is overrepresented close to the 3-prime
ends of introns. Masuda et al. (2008) found that alternative exons of
several other genes, including GRIP1 (604597), FAS (TNFRSF6; 134637),
VPS13C (608879), and NRCAM (601581) are downregulated by hnRNP H. These
findings suggest that presence of the hnRNP H-binding motif close to the
3-prime end of an intron is an essential, and perhaps underestimated,
splicing regulator of the downstream exon.
*FIELD* RF
1. Honore, B.; Rasmussen, H. H.; Vorum, H.; Dejgaard, K.; Liu, X.;
Gromov, P.; Madsen, P.; Gesser, B.; Tommerup, N.; Celis, J. E.: Heterogeneous
nuclear ribonucleoproteins H, H-prime, and F are members of a ubiquitously
expressed subfamily of related but distinct proteins encoded by genes
mapping to different chromosomes. J. Biol. Chem. 270: 28780-28789,
1995.
2. Masuda, A.; Shen, X.-M.; Ito, M.; Matsuura, T.; Engel, A. G.; Ohno,
K.: hnRNP H enhances skipping of a nonfunctional exon P3A in CHRNA1
and a mutation disrupting its binding causes congenital myasthenic
syndrome. Hum. Molec. Genet. 17: 4022-4035, 2008.
*FIELD* CN
Cassandra L. Kniffin - updated: 4/4/2011
*FIELD* CD
Victor A. McKusick: 2/2/1996
*FIELD* ED
wwang: 04/11/2011
ckniffin: 4/4/2011
terry: 5/27/2010
alopez: 3/30/2010
wwang: 8/27/2008
alopez: 1/19/1999
dholmes: 2/9/1998
mark: 2/2/1996
*RECORD*
*FIELD* NO
601035
*FIELD* TI
*601035 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H1; HNRNPH1
;;HNRPH1;;
HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H
read more*FIELD* TX
CLONING
Heterogeneous nuclear ribonucleoproteins (hnRNPs) constitute a set of
polypeptides that bind heterogeneous nuclear RNA (hnRNA), the
transcripts produced by RNA polymerase II (see 180660). More than 20
such proteins have been described and designated with letters from A to
U. By molecular cDNA cloning, 2-dimensional gel immunoblotting, and
amino acid microsequencing, Honore et al. (1995) identified 3
sequence-unique and distinct proteins that constitute a subfamily of
ubiquitously expressed hnRNPs. The identity between hnRNPs H and H-prime
(300610) was 96%, between H and F (601037), 78%, and between H-prime and
F, 75%.
MAPPING
By fluorescence in situ hybridization, Honore et al. (1995) mapped the
HNRNPH1 gene to chromosome 5q35.3.
GENE FUNCTION
Masuda et al. (2008) identified a key nucleotide in an intron of the
CHRNA1 gene (100690) that is part of an intronic splicing silencer (ISS)
sequence targeted by hnRNP H and suppresses inclusion of an alternative
exon in the CHRNA1 gene. Analysis of the human genome suggested that the
hnRNP H-binding motif 'UGGG' is overrepresented close to the 3-prime
ends of introns. Masuda et al. (2008) found that alternative exons of
several other genes, including GRIP1 (604597), FAS (TNFRSF6; 134637),
VPS13C (608879), and NRCAM (601581) are downregulated by hnRNP H. These
findings suggest that presence of the hnRNP H-binding motif close to the
3-prime end of an intron is an essential, and perhaps underestimated,
splicing regulator of the downstream exon.
*FIELD* RF
1. Honore, B.; Rasmussen, H. H.; Vorum, H.; Dejgaard, K.; Liu, X.;
Gromov, P.; Madsen, P.; Gesser, B.; Tommerup, N.; Celis, J. E.: Heterogeneous
nuclear ribonucleoproteins H, H-prime, and F are members of a ubiquitously
expressed subfamily of related but distinct proteins encoded by genes
mapping to different chromosomes. J. Biol. Chem. 270: 28780-28789,
1995.
2. Masuda, A.; Shen, X.-M.; Ito, M.; Matsuura, T.; Engel, A. G.; Ohno,
K.: hnRNP H enhances skipping of a nonfunctional exon P3A in CHRNA1
and a mutation disrupting its binding causes congenital myasthenic
syndrome. Hum. Molec. Genet. 17: 4022-4035, 2008.
*FIELD* CN
Cassandra L. Kniffin - updated: 4/4/2011
*FIELD* CD
Victor A. McKusick: 2/2/1996
*FIELD* ED
wwang: 04/11/2011
ckniffin: 4/4/2011
terry: 5/27/2010
alopez: 3/30/2010
wwang: 8/27/2008
alopez: 1/19/1999
dholmes: 2/9/1998
mark: 2/2/1996