RIMB2_HUMAN
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 03-AUG-2022, entry version 173.
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};
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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; 6.
DR IntAct; O15034; 7.
DR STRING; 9606.ENSP00000261655; -.
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; O15034; -.
DR PeptideAtlas; O15034; -.
DR PRIDE; 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; 47 antibodies from 13 providers.
DR DNASU; 23504; -.
DR Ensembl; ENST00000261655.8; ENSP00000261655.4; ENSG00000060709.16. [O15034-1]
DR GeneID; 23504; -.
DR KEGG; hsa:23504; -.
DR UCSC; uc001uil.3; human. [O15034-1]
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; 102427at2759; -.
DR PhylomeDB; O15034; -.
DR TreeFam; TF316230; -.
DR PathwayCommons; O15034; -.
DR SignaLink; O15034; -.
DR SIGNOR; O15034; -.
DR BioGRID-ORCS; 23504; 12 hits in 1070 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 144 other tissues.
DR ExpressionAtlas; O15034; baseline and differential.
DR Genevisible; O15034; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; cd12012; SH3_RIM-BP_2; 1.
DR CDD; cd12013; SH3_RIM-BP_3; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035519; RIM-BP2.
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; PTHR14234; 2.
DR PANTHER; PTHR14234:SF18; PTHR14234:SF18; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50002; SH3; 3.
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
