HNRH2_BOVIN
ID HNRH2_BOVIN Reviewed; 449 AA.
AC Q3SZF3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein H2;
DE Short=hnRNP H2;
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=HNRPH2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity).
CC {ECO:0000250}.
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. Interacts with TXNL4/DIM1.
CC {ECO:0000250|UniProtKB:P55795}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P55795}.
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DR EMBL; BC102894; AAI02895.1; -; mRNA.
DR RefSeq; NP_001069476.1; NM_001076008.1.
DR AlphaFoldDB; Q3SZF3; -.
DR SMR; Q3SZF3; -.
DR STRING; 9913.ENSBTAP00000009864; -.
DR PaxDb; Q3SZF3; -.
DR PeptideAtlas; Q3SZF3; -.
DR PRIDE; Q3SZF3; -.
DR GeneID; 534001; -.
DR KEGG; bta:534001; -.
DR CTD; 3188; -.
DR eggNOG; KOG4211; Eukaryota.
DR InParanoid; Q3SZF3; -.
DR OrthoDB; 603679at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..449
FT /note="Heterogeneous nuclear ribonucleoprotein H2"
FT /id="PRO_0000434384"
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_0000244428"
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:0000250|UniProtKB:P31943"
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:0000250|UniProtKB:P55795"
FT MOD_RES 246
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31943"
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:0000250|UniProtKB:P55795"
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"
SQ SEQUENCE 449 AA; 49265 MW; 85E6037382189A5D CRC64;
MMLSTEGREG FVVKVRGLPW SCSADEVMRF FSDCKIQNGT SGIRFIYTRE GRPSGEAFVE
LESEDEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT GPNSPDTAND GFVRLRGLPF
GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY
IEIFKSSRAE VRTHYDPPRK LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY
GGYDDYGGYN DGYGFGSDRF GRDQNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA
TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA NMQHRYVELF
LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM GISNQSSYGG PASQQLSGGY
GGGYGGQSSM SGYDQVLQEN SSDYQSNLA
