RAVR2_HUMAN
ID RAVR2_HUMAN Reviewed; 691 AA.
AC Q9HCJ3; Q6P141; Q9NPV7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ribonucleoprotein PTB-binding 2;
DE AltName: Full=Protein raver-2;
GN Name=RAVER2; Synonyms=KIAA1579;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-691 (ISOFORM 1).
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-691.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP IDENTIFICATION BY 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP STRUCTURE BY NMR OF 71-145.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in BAB13405.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: May bind single-stranded nucleic acids. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with PTBP1 and RAVER1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=May shuttle between the nucleus and the cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HCJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCJ3-2; Sequence=VSP_013676;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB046799; BAB13405.1; ALT_INIT; mRNA.
DR EMBL; BC065303; AAH65303.1; -; mRNA.
DR EMBL; AL359613; CAB94883.1; -; mRNA.
DR CCDS; CCDS41345.1; -. [Q9HCJ3-2]
DR PIR; T50631; T50631.
DR RefSeq; NP_060681.2; NM_018211.3. [Q9HCJ3-2]
DR RefSeq; XP_006710801.2; XM_006710738.3.
DR PDB; 1WG1; NMR; -; A=71-145.
DR PDBsum; 1WG1; -.
DR AlphaFoldDB; Q9HCJ3; -.
DR SMR; Q9HCJ3; -.
DR BioGRID; 120520; 13.
DR IntAct; Q9HCJ3; 5.
DR STRING; 9606.ENSP00000360112; -.
DR iPTMnet; Q9HCJ3; -.
DR PhosphoSitePlus; Q9HCJ3; -.
DR BioMuta; RAVER2; -.
DR DMDM; 67466983; -.
DR EPD; Q9HCJ3; -.
DR jPOST; Q9HCJ3; -.
DR MassIVE; Q9HCJ3; -.
DR MaxQB; Q9HCJ3; -.
DR PaxDb; Q9HCJ3; -.
DR PeptideAtlas; Q9HCJ3; -.
DR PRIDE; Q9HCJ3; -.
DR ProteomicsDB; 81738; -. [Q9HCJ3-1]
DR ProteomicsDB; 81739; -. [Q9HCJ3-2]
DR Antibodypedia; 51338; 68 antibodies from 14 providers.
DR DNASU; 55225; -.
DR Ensembl; ENST00000294428.7; ENSP00000294428.3; ENSG00000162437.14. [Q9HCJ3-1]
DR Ensembl; ENST00000371072.8; ENSP00000360112.4; ENSG00000162437.14. [Q9HCJ3-2]
DR GeneID; 55225; -.
DR KEGG; hsa:55225; -.
DR MANE-Select; ENST00000294428.8; ENSP00000294428.3; NM_001366165.2; NP_001353094.1.
DR UCSC; uc001dbs.3; human. [Q9HCJ3-1]
DR CTD; 55225; -.
DR DisGeNET; 55225; -.
DR GeneCards; RAVER2; -.
DR HGNC; HGNC:25577; RAVER2.
DR HPA; ENSG00000162437; Low tissue specificity.
DR MIM; 609953; gene.
DR neXtProt; NX_Q9HCJ3; -.
DR OpenTargets; ENSG00000162437; -.
DR PharmGKB; PA144596391; -.
DR VEuPathDB; HostDB:ENSG00000162437; -.
DR eggNOG; ENOG502QUKC; Eukaryota.
DR GeneTree; ENSGT00940000158648; -.
DR HOGENOM; CLU_016492_2_0_1; -.
DR InParanoid; Q9HCJ3; -.
DR OMA; LTGHHKQ; -.
DR OrthoDB; 249777at2759; -.
DR PhylomeDB; Q9HCJ3; -.
DR TreeFam; TF331660; -.
DR PathwayCommons; Q9HCJ3; -.
DR SignaLink; Q9HCJ3; -.
DR BioGRID-ORCS; 55225; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; RAVER2; human.
DR EvolutionaryTrace; Q9HCJ3; -.
DR GenomeRNAi; 55225; -.
DR Pharos; Q9HCJ3; Tbio.
DR PRO; PR:Q9HCJ3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HCJ3; protein.
DR Bgee; ENSG00000162437; Expressed in jejunal mucosa and 170 other tissues.
DR ExpressionAtlas; Q9HCJ3; baseline and differential.
DR Genevisible; Q9HCJ3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034636; RAVER2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23189:SF6; PTHR23189:SF6; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..691
FT /note="Ribonucleoprotein PTB-binding 2"
FT /id="PRO_0000081490"
FT DOMAIN 69..140
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 142..220
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 231..309
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 397..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_013676"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1WG1"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1WG1"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1WG1"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1WG1"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1WG1"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:1WG1"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1WG1"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1WG1"
SQ SEQUENCE 691 AA; 74339 MW; 03E287BAF9EE10F8 CRC64;
MAAAAGDGGG EGGAGLGSAA GLGPGPGLRG QGPSAEAHEG APDPMPAALH PEEVAARLQR
MQRELSNRRK ILVKNLPQDS NCQEVHDLLK DYDLKYCYVD RNKRTAFVTL LNGEQAQNAI
QMFHQYSFRG KDLIVQLQPT DALLCITNVP ISFTSEEFEE LVRAYGNIER CFLVYSEVTG
HSKGYGFVEY MKKDFAAKAR LELLGRQLGA SALFAQWMDV NLLASELIHS KCLCIDKLPS
DYRDSEELLQ IFSSVHKPVF CQLAQDEGSY VGGFAVVEYS TAEQAEEVQQ AADGMTIKGS
KVQVSFCAPG APGRSTLAAL IAAQRVMHSN QKGLLPEPNP VQIMKSLNNP AMLQVLLQPQ
LCGRAVKPAV LGTPHSLPHL MNPSISPAFL HLNKAHQSSV MGNTSNLFLQ NLSHIPLAQQ
QLMKFENIHT NNKPGLLGEP PAVVLQTALG IGSVLPLKKE LGHHHGEAHK TSSLIPTQTT
ITAGMGMLPF FPNQHIAGQA GPGHSNTQEK QPATVGMAEG NFSGSQPYLQ SFPNLAAGSL
LVGHHKQQQS QPKGTEISSG AASKNQTSLL GEPPKEIRLS KNPYLNLASV LPSVCLSSPA
SKTTLHKTGI ASSILDAISQ GSESQHALEK CIAYSPPFGD YAQVSSLRNE KRGSSYLISA
PEGGSVECVD QHSQGTGAYY METYLKKKRV Y
