CBARP_HUMAN
ID CBARP_HUMAN Reviewed; 705 AA.
AC Q8N350; K7EJP2; O43385;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Voltage-dependent calcium channel beta subunit-associated regulatory protein {ECO:0000305};
GN Name=CBARP {ECO:0000312|HGNC:HGNC:28617};
GN Synonyms=C19orf26 {ECO:0000312|HGNC:HGNC:28617};
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 GENOMIC DNA] (ISOFORM 1).
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-703, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-304 AND SER-703, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-698; SER-699 AND SER-703, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-507 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: Negatively regulates voltage-gated calcium channels by
CC preventing the interaction between their alpha and beta subunits.
CC Thereby, negatively regulates calcium channels activity at the plasma
CC membrane and indirectly inhibits calcium-regulated exocytosis.
CC {ECO:0000250|UniProtKB:Q66L44}.
CC -!- SUBUNIT: Interacts with voltage-dependent calcium channels CACNB1,
CC CACNB2, CACNB3 and CACNB4 beta subunits; prevents their interaction
CC with the CACNA1C alpha subunit thereby negatively regulating the
CC activity of the corresponding calcium channels.
CC {ECO:0000250|UniProtKB:Q66L44}.
CC -!- INTERACTION:
CC Q8N350-4; O95870: ABHD16A; NbExp=3; IntAct=EBI-19051169, EBI-348517;
CC Q8N350-4; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-19051169, EBI-12069500;
CC Q8N350-4; Q5R3K3: CALHM6; NbExp=3; IntAct=EBI-19051169, EBI-19051471;
CC Q8N350-4; Q6N075: MFSD5; NbExp=3; IntAct=EBI-19051169, EBI-3920969;
CC Q8N350-4; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-19051169, EBI-12070086;
CC Q8N350-4; O43639: NCK2; NbExp=3; IntAct=EBI-19051169, EBI-713635;
CC Q8N350-4; Q9H237-2: PORCN; NbExp=3; IntAct=EBI-19051169, EBI-18254170;
CC Q8N350-4; Q8N357: SLC35F6; NbExp=3; IntAct=EBI-19051169, EBI-713484;
CC Q8N350-4; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-19051169, EBI-2823239;
CC Q8N350-4; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-19051169, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q66L44}; Single-pass type III
CC membrane protein {ECO:0000250|UniProtKB:Q66L44}. Cell membrane
CC {ECO:0000250|UniProtKB:Q66L44}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:Q66L44}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q66L44}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N350-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N350-4; Sequence=VSP_058134, VSP_058135;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH28156.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AC004221; AAC04305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC028156; AAH28156.1; ALT_INIT; mRNA.
DR CCDS; CCDS12057.2; -. [Q8N350-4]
DR PIR; T00492; T00492.
DR RefSeq; NP_689982.3; NM_152769.2. [Q8N350-4]
DR AlphaFoldDB; Q8N350; -.
DR SMR; Q8N350; -.
DR BioGRID; 129072; 87.
DR IntAct; Q8N350; 25.
DR MINT; Q8N350; -.
DR STRING; 9606.ENSP00000465260; -.
DR GlyGen; Q8N350; 1 site.
DR iPTMnet; Q8N350; -.
DR PhosphoSitePlus; Q8N350; -.
DR BioMuta; CBARP; -.
DR DMDM; 73919246; -.
DR EPD; Q8N350; -.
DR jPOST; Q8N350; -.
DR MassIVE; Q8N350; -.
DR MaxQB; Q8N350; -.
DR PaxDb; Q8N350; -.
DR PeptideAtlas; Q8N350; -.
DR PRIDE; Q8N350; -.
DR Antibodypedia; 2282; 67 antibodies from 18 providers.
DR DNASU; 255057; -.
DR Ensembl; ENST00000590083.5; ENSP00000465260.1; ENSG00000099625.14. [Q8N350-4]
DR Ensembl; ENST00000650044.2; ENSP00000497208.1; ENSG00000099625.14. [Q8N350-3]
DR GeneID; 255057; -.
DR KEGG; hsa:255057; -.
DR MANE-Select; ENST00000650044.2; ENSP00000497208.1; NM_001393918.1; NP_001380847.1.
DR UCSC; uc002lrm.4; human.
DR UCSC; uc060qwp.1; human. [Q8N350-3]
DR CTD; 255057; -.
DR GeneCards; CBARP; -.
DR HGNC; HGNC:28617; CBARP.
DR HPA; ENSG00000099625; Tissue enhanced (brain, pituitary gland).
DR neXtProt; NX_Q8N350; -.
DR OpenTargets; ENSG00000099625; -.
DR PharmGKB; PA134919853; -.
DR VEuPathDB; HostDB:ENSG00000099625; -.
DR eggNOG; ENOG502QQ2E; Eukaryota.
DR GeneTree; ENSGT00390000009230; -.
DR HOGENOM; CLU_015082_2_0_1; -.
DR InParanoid; Q8N350; -.
DR OMA; HNQETER; -.
DR OrthoDB; 830111at2759; -.
DR TreeFam; TF331130; -.
DR PathwayCommons; Q8N350; -.
DR SignaLink; Q8N350; -.
DR BioGRID-ORCS; 255057; 17 hits in 1060 CRISPR screens.
DR GenomeRNAi; 255057; -.
DR Pharos; Q8N350; Tbio.
DR PRO; PR:Q8N350; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N350; protein.
DR Bgee; ENSG00000099625; Expressed in adenohypophysis and 129 other tissues.
DR ExpressionAtlas; Q8N350; baseline and differential.
DR Genevisible; Q8N350; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:1903170; P:negative regulation of calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
DR InterPro; IPR037658; CBARP.
DR PANTHER; PTHR28597; PTHR28597; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..705
FT /note="Voltage-dependent calcium channel beta subunit-
FT associated regulatory protein"
FT /id="PRO_0000079983"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q66L44"
FT TRANSMEM 46..66
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q66L44"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66L44"
FT MOD_RES 698
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q66L44"
FT VAR_SEQ 386..453
FT /note="LEAAEAAGGASPDSPPERGAGSAGPEQQQPPLEPDAERDAGPEQAQTSYRDL
FT WSLRASLELHAAASDH -> YFSVDGGARGGPVGPCPPSPPPRRPRERSPGPVDTRSPA
FT SSGKAPPRGGLTGATSPAWTRGGKQGETG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_058134"
FT VAR_SEQ 454..705
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_058135"
FT CONFLICT 256
FT /note="S -> L (in Ref. 2; AAH28156)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="H -> R (in Ref. 2; AAH28156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 73929 MW; C116E348E8B7AD2B CRC64;
MQPTATMATA ATTTTTTTAT VALTTSWDNA TGRPTAEPDP ILDNYVLLVV VMSLFVGGTL
VVLSGVLLLC KRCWDVHQRL NRAMEEAEKT TTTYLDNGTH PAQDPDFRGE DPECQDAETE
RFLSTSSTGR RVSFNEAALF EQSRKTQDKG RRYTLTEGDF HHLKNARLTH LHLPPLKIVT
IHECDSGEAS SATTPHPATS PKATLAIFQP PGKALTGRSV GPSSALPGDP YNSAAGATDF
AEISPSASSD SGEGTSLDAG TRSTKAGGPG AAAGPGEAGP GSGAGTVLQF LTRLRRHASL
DGASPYFKVK KWKLEPSQRA ASLDTRGSPK RHHFQRQRAA SESTEQEEGD APQEDFIQYI
ARAGDAVAFP HPRPFLASPP PALGRLEAAE AAGGASPDSP PERGAGSAGP EQQQPPLEPD
AERDAGPEQA QTSYRDLWSL RASLELHAAA SDHSSSGNDR DSVRSGDSSG SGSGGAAPAF
PPPSPPAPRP KDGEARRLLQ MDSGYASIEG RGAGDDTEPP AAPARPRSPR AWPRRPRRDY
SIDEKTDALF HEFLRHDPHF DDTPAAARHR ARAHPHARKQ WQRGRQHSDP GARAAPALAG
TPAPPAGAAR PARAPLRRGD SVDGPPDGRT LGGAGDDPAI PVIEEEPGGG GCPGSGLCVL
PSGSVLDKLA AGLDERLFPP RLAEPVVATP ALVAAAPTSP DHSPA
