ID RIMB2_HUMAN Reviewed; 1052 AA. AC O15034; Q96ID2; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 3. DT 24-JAN-2024, entry version 179. DE RecName: Full=RIMS-binding protein 2; DE Short=RIM-BP2; GN Name=RIMBP2; Synonyms=KIAA0318, RBP2; 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 1). RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Fetal kidney; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [5] RP STRUCTURE BY NMR OF 158-244; 477-593 AND 839-1017. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domains and FNIII domain of KIAA0318 RT protein."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Plays a role in the synaptic transmission as bifunctional CC linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CC CACNA1B. {ECO:0000250}. CC -!- SUBUNIT: Interacts with RIMS1, RIMS2, CACNA1D and CACNA1B, and CC potentially with other Ca(2+) channel alpha-1 isoforms. {ECO:0000250}. CC -!- INTERACTION: CC O15034-2; P41227: NAA10; NbExp=3; IntAct=EBI-12906594, EBI-747693; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Synapse CC {ECO:0000250}. Note=Synaptic plasma membrane. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O15034-1; Sequence=Displayed; CC Name=2; CC IsoId=O15034-2; Sequence=VSP_009212, VSP_009214, VSP_009215; CC Name=3; CC IsoId=O15034-3; Sequence=VSP_009213, VSP_009216; CC -!- DOMAIN: The SH3 domains mediate binding to a proline-rich motif in CC RIMS1, RIMS2, CACNA1D and CACNA1B. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20776.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB002316; BAA20776.1; ALT_INIT; mRNA. DR EMBL; BX641152; CAE46066.1; -; mRNA. DR EMBL; AC063926; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007632; AAH07632.1; -; mRNA. DR CCDS; CCDS31925.1; -. [O15034-1] DR RefSeq; NP_056162.4; NM_015347.4. [O15034-1] DR PDB; 1WIE; NMR; -; A=160-242. DR PDB; 2CSI; NMR; -; A=955-1017. DR PDB; 2CSP; NMR; -; A=477-593. DR PDB; 2CSQ; NMR; -; A=841-924. DR PDBsum; 1WIE; -. DR PDBsum; 2CSI; -. DR PDBsum; 2CSP; -. DR PDBsum; 2CSQ; -. DR AlphaFoldDB; O15034; -. DR BMRB; O15034; -. DR SMR; O15034; -. DR BioGRID; 117051; 7. DR IntAct; O15034; 6. DR STRING; 9606.ENSP00000261655; -. DR GlyCosmos; O15034; 3 sites, 1 glycan. DR GlyGen; O15034; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; O15034; -. DR PhosphoSitePlus; O15034; -. DR BioMuta; RIMBP2; -. DR EPD; O15034; -. DR jPOST; O15034; -. DR MassIVE; O15034; -. DR PaxDb; 9606-ENSP00000261655; -. DR PeptideAtlas; O15034; -. DR ProteomicsDB; 48391; -. [O15034-1] DR ProteomicsDB; 48392; -. [O15034-2] DR ProteomicsDB; 48393; -. [O15034-3] DR ABCD; O15034; 3 sequenced antibodies. DR Antibodypedia; 65349; 49 antibodies from 13 providers. DR DNASU; 23504; -. DR Ensembl; ENST00000261655.8; ENSP00000261655.4; ENSG00000060709.17. [O15034-1] DR GeneID; 23504; -. DR KEGG; hsa:23504; -. DR UCSC; uc001uil.3; human. [O15034-1] DR AGR; HGNC:30339; -. DR CTD; 23504; -. DR DisGeNET; 23504; -. DR GeneCards; RIMBP2; -. DR HGNC; HGNC:30339; RIMBP2. DR HPA; ENSG00000060709; Tissue enhanced (brain, parathyroid gland, pituitary gland). DR MIM; 611602; gene. DR neXtProt; NX_O15034; -. DR OpenTargets; ENSG00000060709; -. DR PharmGKB; PA143485594; -. DR VEuPathDB; HostDB:ENSG00000060709; -. DR eggNOG; KOG3632; Eukaryota. DR GeneTree; ENSGT00950000183203; -. DR HOGENOM; CLU_001979_0_0_1; -. DR InParanoid; O15034; -. DR OrthoDB; 5403222at2759; -. DR PhylomeDB; O15034; -. DR TreeFam; TF316230; -. DR PathwayCommons; O15034; -. DR SignaLink; O15034; -. DR SIGNOR; O15034; -. DR BioGRID-ORCS; 23504; 12 hits in 1148 CRISPR screens. DR ChiTaRS; RIMBP2; human. DR EvolutionaryTrace; O15034; -. DR GenomeRNAi; 23504; -. DR Pharos; O15034; Tdark. DR PRO; PR:O15034; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; O15034; Protein. DR Bgee; ENSG00000060709; Expressed in Brodmann (1909) area 10 and 146 other cell types or tissues. DR ExpressionAtlas; O15034; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central. DR CDD; cd00063; FN3; 3. DR CDD; cd12014; SH3_RIM-BP_1; 1. DR CDD; cd12012; SH3_RIM-BP_2; 1. DR CDD; cd12013; SH3_RIM-BP_3; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 2.30.30.40; SH3 Domains; 3. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR035753; RIM-BP_SH3_2. DR InterPro; IPR035755; RIM-BP_SH3_3. DR InterPro; IPR040325; RIMBP1/2/3. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR14234; RIM BINDING PROTEIN-RELATED; 1. DR PANTHER; PTHR14234:SF18; RIMS-BINDING PROTEIN 2; 1. DR Pfam; PF07653; SH3_2; 2. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00060; FN3; 3. DR SMART; SM00326; SH3; 3. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR SUPFAM; SSF50044; SH3-domain; 3. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS50002; SH3; 3. DR Genevisible; O15034; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Membrane; KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse. FT CHAIN 1..1052 FT /note="RIMS-binding protein 2" FT /id="PRO_0000221383" FT DOMAIN 167..234 FT /note="SH3 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 297..390 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 393..475 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 489..590 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 848..916 FT /note="SH3 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 952..1019 FT /note="SH3 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 115..164 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 584..615 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 629..666 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 697..716 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 767..787 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 805..829 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1029..1052 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 584..598 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 704 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JIR1" FT MOD_RES 712 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JIR1" FT MOD_RES 832 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80U40" FT MOD_RES 839 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80U40" FT MOD_RES 841 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q80U40" FT VAR_SEQ 1..863 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_009213" FT VAR_SEQ 1..92 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009212" FT VAR_SEQ 735..737 FT /note="PHC -> MVS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009214" FT VAR_SEQ 738..1052 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009215" FT VAR_SEQ 1045..1052 FT /note="KKSVHFTP -> VSKPI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_009216" FT VARIANT 593 FT /note="P -> R (in dbSNP:rs2292664)" FT /id="VAR_057714" FT VARIANT 888 FT /note="D -> N (in dbSNP:rs11060869)" FT /id="VAR_057715" FT CONFLICT 1051 FT /note="T -> I (in Ref. 1; BAA20776)" FT /evidence="ECO:0000305" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:1WIE" FT STRAND 169..176 FT /evidence="ECO:0007829|PDB:1WIE" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:1WIE" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:1WIE" FT STRAND 199..205 FT /evidence="ECO:0007829|PDB:1WIE" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:1WIE" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:1WIE" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:1WIE" FT STRAND 491..495 FT /evidence="ECO:0007829|PDB:2CSP" FT STRAND 503..509 FT /evidence="ECO:0007829|PDB:2CSP" FT STRAND 519..522 FT /evidence="ECO:0007829|PDB:2CSP" FT STRAND 524..539 FT /evidence="ECO:0007829|PDB:2CSP" FT STRAND 545..551 FT /evidence="ECO:0007829|PDB:2CSP" FT HELIX 552..557 FT /evidence="ECO:0007829|PDB:2CSP" FT STRAND 562..570 FT /evidence="ECO:0007829|PDB:2CSP" FT HELIX 583..586 FT /evidence="ECO:0007829|PDB:2CSP" FT STRAND 851..854 FT /evidence="ECO:0007829|PDB:2CSQ" FT TURN 861..863 FT /evidence="ECO:0007829|PDB:2CSQ" FT STRAND 864..866 FT /evidence="ECO:0007829|PDB:2CSQ" FT HELIX 868..871 FT /evidence="ECO:0007829|PDB:2CSQ" FT STRAND 882..889 FT /evidence="ECO:0007829|PDB:2CSQ" FT STRAND 894..899 FT /evidence="ECO:0007829|PDB:2CSQ" FT STRAND 902..907 FT /evidence="ECO:0007829|PDB:2CSQ" FT TURN 908..910 FT /evidence="ECO:0007829|PDB:2CSQ" FT STRAND 911..913 FT /evidence="ECO:0007829|PDB:2CSQ" FT STRAND 954..958 FT /evidence="ECO:0007829|PDB:2CSI" FT TURN 965..967 FT /evidence="ECO:0007829|PDB:2CSI" FT STRAND 971..973 FT /evidence="ECO:0007829|PDB:2CSI" FT TURN 974..976 FT /evidence="ECO:0007829|PDB:2CSI" FT STRAND 985..991 FT /evidence="ECO:0007829|PDB:2CSI" FT STRAND 994..1002 FT /evidence="ECO:0007829|PDB:2CSI" FT STRAND 1005..1010 FT /evidence="ECO:0007829|PDB:2CSI" FT HELIX 1011..1013 FT /evidence="ECO:0007829|PDB:2CSI" SQ SEQUENCE 1052 AA; 116026 MW; 065FADD690A7A8BC CRC64; MREAAERRQQ LQLEHDQALA VLSAKQQEID LLQKSKVREL EEKCRTQSEQ FNLLSRDLEK FRQHAGKIDL LGGSAVAPLD ISTAPSKPFP QFMNGLATSL GKGQESAIGG SSAIGEYIRP LPQPGDRPEP LSAKPTFLSR SGSARCRSES DMENERNSNT SKQRYSGKVH LCVARYSYNP FDGPNENPEA ELPLTAGKYL YVYGDMDEDG FYEGELLDGQ RGLVPSNFVD FVQDNESRLA STLGNEQDQN FINHSGIGLE GEHILDLHSP THIDAGITDN SAGTLDVNID DIGEDIVPYP RKITLIKQLA KSVIVGWEPP AVPPGWGTVS SYNVLVDKET RMNLTLGSRT KALIEKLNMA ACTYRISVQC VTSRGSSDEL QCTLLVGKDV VVAPSHLRVD NITQISAQLS WLPTNSNYSH VIFLNEEEFD IVKAARYKYQ FFNLRPNMAY KVKVLAKPHQ MPWQLPLEQR EKKEAFVEFS TLPAGPPAPP QDVTVQAGVT PATIRVSWRP PVLTPTGLSN GANVTGYGVY AKGQRVAEVI FPTADSTAVE LVRLRSLEAK GVTVRTLSAQ GESVDSAVAA VPPELLVPPT PHPRPAPQSK PLASSGVPET KDEHLGPHAR MDEAWEQSRA PGPVHGHMLE PPVGPGRRSP SPSRILPQPQ GTPVSTTVAK AMAREAAQRV AESSRLEKRS VFLERSSAGQ YAASDEEDAY DSPDFKRRGA SVDDFLKGSE LGKQPHCCHG DEYHTESSRG SDLSDIMEED EEELYSEMQL EDGGRRRPSG TSHNALKILG NPASAGRVDH MGRRFPRGSA GPQRSRPVTV PSIDDYGRDR LSPDFYEESE TDPGAEELPA RIFVALFDYD PLTMSPNPDA AEEELPFKEG QIIKVYGDKD ADGFYRGETC ARLGLIPCNM VSEIQADDEE MMDQLLRQGF LPLNTPVEKI ERSRRSGRRH SVSTRRMVAL YDYDPRESSP NVDVEAELTF CTGDIITVFG EIDEDGFYYG ELNGQKGLVP SNFLEEVPDD VEVYLSDAPS HYSQDTPMRS KAKRKKSVHF TP //