HNRH2_HUMAN
ID HNRH2_HUMAN Reviewed; 449 AA.
AC P55795; A1L400; Q9HHA7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H2;
DE Short=hnRNP H2;
DE AltName: Full=FTP-3;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein H';
DE Short=hnRNP H';
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed;
GN Name=HNRNPH2; Synonyms=FTP3, HNRPH2;
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].
RX PubMed=7959728; DOI=10.1006/geno.1994.1310;
RA Vorechovsky I., Vetrie D., Holland J., Bentley D.R., Thomas K., Zhou J.N.,
RA Notarangelo L.D., Plebani A., Fontan G., Ochs H.D.;
RT "Isolation of cosmid and cDNA clones in the region surrounding the BTK gene
RT at Xq21.3-q22.";
RL Genomics 21:517-524(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9110171; DOI=10.1101/gr.7.4.315;
RA Oeltjen J.C., Malley T.M., Muzny D.M., Miller W., Gibbs R.A., Belmont J.W.;
RT "Large-scale comparative sequence analysis of the human and murine Bruton's
RT tyrosine kinase loci reveals conserved regulatory domains.";
RL Genome Res. 7:315-329(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP PROTEIN SEQUENCE OF 1-8; 88-114; 151-167; 276-294 AND 300-326, ACETYLATION
RP AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 17-29; 36-44; 88-98; 151-167; 263-275; 300-316 AND
RP 327-347, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH TXNL4.
RX PubMed=11054566; DOI=10.1016/s0378-1119(00)00372-3;
RA Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A.;
RT "Evidence that Dim1 associates with proteins involved in pre-mRNA splicing,
RT and delineation of residues essential for Dim1 interactions with hnRNP F
RT and Npw38/PQBP-1.";
RL Gene 257:33-43(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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 [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [19]
RP IDENTIFICATION IN RIBONUCLEOPROTEIN COMPLEX, INTERACTION WITH ARVCF, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24644279; DOI=10.1074/jbc.m113.530717;
RA Rappe U., Schlechter T., Aschoff M., Hotz-Wagenblatt A., Hofmann I.;
RT "Nuclear ARVCF protein binds splicing factors and contributes to the
RT regulation of alternative splicing.";
RL J. Biol. Chem. 289:12421-12434(2014).
RN [20]
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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP 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).
RN [22]
RP STRUCTURE BY NMR OF 103-193 AND 280-369.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domains in heterogeneous nuclear
RT ribonucleoprotein H.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [23]
RP VARIANTS MRXSB GLN-206; TRP-206 AND LEU-209, CHARACTERIZATION OF VARIANTS
RP MRXSB GLN-206; TRP-206 AND LEU-209, AND INVOLVEMENT IN MRXSB.
RX PubMed=27545675; DOI=10.1016/j.ajhg.2016.06.028;
RA Bain J.M., Cho M.T., Telegrafi A., Wilson A., Brooks S., Botti C.,
RA Gowans G., Autullo L.A., Krishnamurthy V., Willing M.C., Toler T.L.,
RA Ben-Zev B., Elpeleg O., Shen Y., Retterer K., Monaghan K.G., Chung W.K.;
RT "Variants in HNRNPH2 on the X chromosome are associated with a
RT neurodevelopmental disorder in females.";
RL Am. J. Hum. Genet. 99:728-734(2016).
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. Binds poly(RG).
CC -!- SUBUNIT: Component of a ribonucleoprotein complex containing mRNAs and
CC RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as
CC splicing regulator ARVCF (PubMed:24644279). Interacts with TXNL4/DIM1
CC (PubMed:11054566). {ECO:0000269|PubMed:11054566,
CC ECO:0000269|PubMed:24644279}.
CC -!- INTERACTION:
CC P55795; O75909-2: CCNK; NbExp=3; IntAct=EBI-352823, EBI-12010594;
CC P55795; O75031: HSF2BP; NbExp=3; IntAct=EBI-352823, EBI-7116203;
CC P55795; O43347: MSI1; NbExp=5; IntAct=EBI-352823, EBI-726515;
CC P55795; Q96DH6: MSI2; NbExp=6; IntAct=EBI-352823, EBI-2462339;
CC P55795; Q02809: PLOD1; NbExp=2; IntAct=EBI-352823, EBI-357174;
CC P55795; Q969V4: TEKT1; NbExp=8; IntAct=EBI-352823, EBI-10180409;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24644279}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic, Bain
CC type (MRXSB) [MIM:300986]: A form of intellectual disability, a
CC disorder characterized by significantly below average general
CC intellectual functioning associated with impairments in adaptive
CC behavior and manifested during the developmental period. MRXSB patients
CC manifest developmental delay, intellectual disability, autism,
CC hypotonia, seizures, and dysmorphic facial features. Only females are
CC affected. {ECO:0000269|PubMed:27545675}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
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DR EMBL; U01923; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U78027; AAB64202.1; -; Genomic_DNA.
DR EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471115; EAX02864.1; -; Genomic_DNA.
DR EMBL; BC130343; AAI30344.1; -; mRNA.
DR EMBL; BC130345; AAI30346.1; -; mRNA.
DR CCDS; CCDS14485.1; -.
DR RefSeq; NP_001027565.1; NM_001032393.2.
DR RefSeq; NP_062543.1; NM_019597.4.
DR PDB; 1WEZ; NMR; -; A=281-369.
DR PDB; 1WG5; NMR; -; A=103-193.
DR PDB; 6DG1; NMR; -; A=94-194.
DR PDBsum; 1WEZ; -.
DR PDBsum; 1WG5; -.
DR PDBsum; 6DG1; -.
DR AlphaFoldDB; P55795; -.
DR SMR; P55795; -.
DR BioGRID; 109429; 263.
DR IntAct; P55795; 107.
DR MINT; P55795; -.
DR STRING; 9606.ENSP00000361927; -.
DR ChEMBL; CHEMBL4296005; -.
DR GlyGen; P55795; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55795; -.
DR MetOSite; P55795; -.
DR PhosphoSitePlus; P55795; -.
DR SwissPalm; P55795; -.
DR BioMuta; HNRNPH2; -.
DR DMDM; 2500576; -.
DR REPRODUCTION-2DPAGE; IPI00026230; -.
DR EPD; P55795; -.
DR jPOST; P55795; -.
DR MassIVE; P55795; -.
DR MaxQB; P55795; -.
DR PaxDb; P55795; -.
DR PeptideAtlas; P55795; -.
DR PRIDE; P55795; -.
DR ProteomicsDB; 56867; -.
DR Antibodypedia; 343; 140 antibodies from 23 providers.
DR DNASU; 3188; -.
DR Ensembl; ENST00000316594.6; ENSP00000361927.2; ENSG00000126945.9.
DR GeneID; 3188; -.
DR KEGG; hsa:3188; -.
DR MANE-Select; ENST00000316594.6; ENSP00000361927.2; NM_019597.5; NP_062543.1.
DR UCSC; uc004ehm.4; human.
DR CTD; 3188; -.
DR DisGeNET; 3188; -.
DR GeneCards; HNRNPH2; -.
DR HGNC; HGNC:5042; HNRNPH2.
DR HPA; ENSG00000126945; Low tissue specificity.
DR MalaCards; HNRNPH2; -.
DR MIM; 300610; gene.
DR MIM; 300986; phenotype.
DR neXtProt; NX_P55795; -.
DR OpenTargets; ENSG00000126945; -.
DR PharmGKB; PA162391316; -.
DR VEuPathDB; HostDB:ENSG00000126945; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000153503; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; P55795; -.
DR OMA; GSRNRDF; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; P55795; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; P55795; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; P55795; -.
DR SIGNOR; P55795; -.
DR BioGRID-ORCS; 3188; 15 hits in 706 CRISPR screens.
DR EvolutionaryTrace; P55795; -.
DR GeneWiki; HNRPH2; -.
DR GenomeRNAi; 3188; -.
DR Pharos; P55795; Tbio.
DR PRO; PR:P55795; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P55795; protein.
DR Bgee; ENSG00000126945; Expressed in choroid plexus epithelium and 209 other tissues.
DR ExpressionAtlas; P55795; baseline and differential.
DR Genevisible; P55795; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
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; Disease variant;
KW Intellectual disability; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..449
FT /note="Heterogeneous nuclear ribonucleoprotein H2"
FT /id="PRO_0000081859"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT CHAIN 2..449
FT /note="Heterogeneous nuclear ribonucleoprotein H2, N-
FT terminally processed"
FT /id="PRO_0000434385"
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"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein H2, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70333"
FT MOD_RES 233
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 233
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 246
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
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:0000250|UniProtKB:P31943"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P31943"
FT VARIANT 206
FT /note="R -> Q (in MRXSB; dbSNP:rs886039764)"
FT /evidence="ECO:0000269|PubMed:27545675"
FT /id="VAR_077233"
FT VARIANT 206
FT /note="R -> W (in MRXSB; dbSNP:rs886039763)"
FT /evidence="ECO:0000269|PubMed:27545675"
FT /id="VAR_077234"
FT VARIANT 209
FT /note="P -> L (in MRXSB; dbSNP:rs1555988417)"
FT /evidence="ECO:0000269|PubMed:27545675"
FT /id="VAR_077235"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:6DG1"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1WG5"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:1WG5"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1WG5"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1WG5"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1WG5"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:1WG5"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:1WG5"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:1WG5"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1WG5"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1WG5"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1WG5"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1WEZ"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1WEZ"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:1WEZ"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:1WEZ"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:1WEZ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1WEZ"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:1WEZ"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:1WEZ"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1WEZ"
SQ SEQUENCE 449 AA; 49264 MW; C892523A638F07C7 CRC64;
MMLSTEGREG FVVKVRGLPW SCSADEVMRF FSDCKIQNGT SGIRFIYTRE GRPSGEAFVE
LESEEEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT GPNSPDTAND GFVRLRGLPF
GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY
IEIFKSSRAE VRTHYDPPRK LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY
GGYDDYGGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA
TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA NMQHRYVELF
LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY
GGGYGGQSSM SGYDQVLQEN SSDYQSNLA
