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Heterogeneous nuclear ribonucleoprotein H (hnRNP H) [Cleaved into: Heterogeneous nuclear ribonucleoprotein H, N-terminally processed]

 HNRH1_HUMAN             Reviewed;         449 AA.
P31943; B3KW86; D3DWQ2; Q6IBM4;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
18-JUL-2018, entry version 200.
RecName: Full=Heterogeneous nuclear ribonucleoprotein H;
Short=hnRNP H;
Contains:
RecName: Full=Heterogeneous nuclear ribonucleoprotein H, N-terminally processed;
Name=HNRNPH1; Synonyms=HNRPH, HNRPH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 180-184; 193-197
AND 200-230.
PubMed=7499401; DOI=10.1074/jbc.270.48.28780;
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', 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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-14; 17-44; 50-68; 82-114; 151-167; 180-185;
233-259; 276-294; 300-347 AND 356-375, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT MET-1 AND MET-2, METHYLATION AT ARG-233,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, Cervix carcinoma, Hepatoma, Lung carcinoma,
Mammary carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Boldt K., von Kriegsheim A., Matallanas D.,
Cooper W.N., Calvo F., Kolch W., Vousden K.H., Lukashchuk N.,
Lilla S., Lempens A.;
Submitted (DEC-2008) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 2-14; 17-29; 88-114; 151-167; 263-275; 300-347;
344-375; 377-386; 418-432; 473-483 AND 542-553, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 127-135 AND 153-163.
PubMed=7512260; DOI=10.1093/nar/22.6.1059;
Matunis M.J., Xing J., Dreyfuss G.;
"The hnRNP F protein: unique primary structure, nucleic acid-binding
properties, and subcellular localization.";
Nucleic Acids Res. 22:1059-1067(1994).
[9]
PROTEIN SEQUENCE OF 200-230.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[10]
FUNCTION, AND INTERACTION WITH PTBP1; PTBP2 AND FUBP2.
PubMed=11003644; DOI=10.1128/MCB.20.20.7463-7479.2000;
Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y.,
Black D.L.;
"Cooperative assembly of an hnRNP complex induced by a tissue-specific
homolog of polypyrimidine tract binding protein.";
Mol. Cell. Biol. 20:7463-7479(2000).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
FUNCTION, INTERACTION WITH CUGBP1 AND MBNL1, RNA-BINDING, AND
INDUCTION.
PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L.,
Reddy S.;
"Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-
associated aberrant IR splicing.";
EMBO J. 25:4271-4283(2006).
[15]
INTERACTION WITH IGF2BP1.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-63, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-54 AND SER-63,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-233, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35; LYS-87 AND LYS-98, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: This protein is a component of the heterogeneous nuclear
ribonucleoprotein (hnRNP) complexes which provide the substrate
for the processing events that pre-mRNAs undergo before becoming
functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA
alternative splicing regulation. Inhibits, together with CUGBP1,
insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast.
Binds to the IR RNA. Binds poly(RG). {ECO:0000269|PubMed:11003644,
ECO:0000269|PubMed:16946708}.
-!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
and HNRNPH1. Identified in the spliceosome C complex. Interacts
with IGF2BP1. Interacts with CUGBP1; the interaction is RNA-
dependent. Interacts with MBNL1; the interaction in RNA-
independent. {ECO:0000269|PubMed:11003644,
ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16946708,
ECO:0000269|PubMed:17289661}.
-!- INTERACTION:
Q9HBE1-4:PATZ1; NbExp=4; IntAct=EBI-351590, EBI-11022007;
Q8WW24:TEKT4; NbExp=4; IntAct=EBI-351590, EBI-750487;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
-!- INDUCTION: Up-regulated in myotonic dystrophy pathophysiology
(DM). {ECO:0000269|PubMed:16946708}.
-!- DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-
terminal QRRM bound poly(RC) and poly(RU). None of the repeats
bound detectable amounts of poly(RA).
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EMBL; L22009; AAA91346.1; -; mRNA.
EMBL; CR456778; CAG33059.1; -; mRNA.
EMBL; AK124530; BAG54048.1; -; mRNA.
EMBL; CH471165; EAW53807.1; -; Genomic_DNA.
EMBL; CH471165; EAW53808.1; -; Genomic_DNA.
EMBL; BC001348; AAH01348.1; -; mRNA.
CCDS; CCDS4446.1; -.
PIR; I39358; I39358.
RefSeq; NP_001244222.1; NM_001257293.1.
RefSeq; NP_005511.1; NM_005520.2.
RefSeq; XP_016864904.1; XM_017009415.1.
RefSeq; XP_016864905.1; XM_017009416.1.
RefSeq; XP_016864906.1; XM_017009417.1.
UniGene; Hs.604001; -.
PDB; 2LXU; NMR; -; A=7-111.
PDBsum; 2LXU; -.
ProteinModelPortal; P31943; -.
SMR; P31943; -.
BioGrid; 109428; 270.
CORUM; P31943; -.
IntAct; P31943; 116.
MINT; P31943; -.
STRING; 9606.ENSP00000349168; -.
ChEMBL; CHEMBL3797013; -.
iPTMnet; P31943; -.
PhosphoSitePlus; P31943; -.
SwissPalm; P31943; -.
BioMuta; HNRNPH1; -.
DMDM; 1710632; -.
REPRODUCTION-2DPAGE; IPI00013881; -.
REPRODUCTION-2DPAGE; P31943; -.
EPD; P31943; -.
MaxQB; P31943; -.
PaxDb; P31943; -.
PeptideAtlas; P31943; -.
PRIDE; P31943; -.
ProteomicsDB; 54814; -.
Ensembl; ENST00000356731; ENSP00000349168; ENSG00000169045.
Ensembl; ENST00000393432; ENSP00000377082; ENSG00000169045.
Ensembl; ENST00000442819; ENSP00000397797; ENSG00000169045.
GeneID; 3187; -.
KEGG; hsa:3187; -.
UCSC; uc003mke.5; human.
CTD; 3187; -.
DisGeNET; 3187; -.
EuPathDB; HostDB:ENSG00000169045.17; -.
GeneCards; HNRNPH1; -.
HGNC; HGNC:5041; HNRNPH1.
HPA; CAB032820; -.
HPA; HPA000914; -.
HPA; HPA001359; -.
HPA; HPA016884; -.
MalaCards; HNRNPH1; -.
MIM; 601035; gene.
neXtProt; NX_P31943; -.
OpenTargets; ENSG00000169045; -.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA162391284; -.
eggNOG; KOG4211; Eukaryota.
eggNOG; ENOG410Z6M0; LUCA.
GeneTree; ENSGT00760000119102; -.
HOGENOM; HOG000220896; -.
HOVERGEN; HBG055557; -.
InParanoid; P31943; -.
KO; K12898; -.
PhylomeDB; P31943; -.
TreeFam; TF316157; -.
Reactome; R-HSA-6803529; FGFR2 alternative splicing.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
ChiTaRS; HNRNPH1; human.
GeneWiki; HNRPH1; -.
GenomeRNAi; 3187; -.
PRO; PR:P31943; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000169045; -.
CleanEx; HS_HNRNPH1; -.
ExpressionAtlas; P31943; baseline and differential.
Genevisible; P31943; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
Gene3D; 3.30.70.330; -; 3.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR012996; Znf_CHHC.
Pfam; PF00076; RRM_1; 3.
Pfam; PF08080; zf-RNPHF; 1.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Isopeptide bond; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
Spliceosome; Ubl conjugation.
CHAIN 1 449 Heterogeneous nuclear ribonucleoprotein
H.
/FTId=PRO_0000367119.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
CHAIN 2 449 Heterogeneous nuclear ribonucleoprotein
H, N-terminally processed.
/FTId=PRO_0000081857.
DOMAIN 11 90 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 111 188 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REPEAT 234 249 1-1.
DOMAIN 289 364 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REPEAT 354 372 2-1.
REPEAT 374 392 2-2.
REPEAT 418 433 1-2.
REGION 234 433 2 X 16 AA Gly-rich approximate repeats.
REGION 354 392 2 X 19 AA perfect repeats.
MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
nuclear ribonucleoprotein H; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 2 2 N-acetylmethionine; in Heterogeneous
nuclear ribonucleoprotein H, N-terminally
processed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 233 233 Dimethylated arginine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 233 233 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315,
ECO:0000269|Ref.6}.
MOD_RES 246 246 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:P55795}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 87 87 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 98 98 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CONFLICT 188 188 R -> G (in Ref. 2; CAG33059).
{ECO:0000305}.
STRAND 9 17 {ECO:0000244|PDB:2LXU}.
HELIX 24 30 {ECO:0000244|PDB:2LXU}.
TURN 31 33 {ECO:0000244|PDB:2LXU}.
HELIX 39 41 {ECO:0000244|PDB:2LXU}.
STRAND 42 47 {ECO:0000244|PDB:2LXU}.
STRAND 51 62 {ECO:0000244|PDB:2LXU}.
HELIX 64 71 {ECO:0000244|PDB:2LXU}.
TURN 72 75 {ECO:0000244|PDB:2LXU}.
STRAND 84 88 {ECO:0000244|PDB:2LXU}.
HELIX 90 98 {ECO:0000244|PDB:2LXU}.
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


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