ID CHERP_HUMAN Reviewed; 916 AA. AC Q8IWX8; O00302; Q4G0Y5; Q8WU30; Q99492; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 31-MAY-2011, entry version 67. DE RecName: Full=Calcium homeostasis endoplasmic reticulum protein; DE AltName: Full=ERPROT 213-21; DE AltName: Full=SR-related CTD-associated factor 6; GN Name=CHERP; Synonyms=DAN26, SCAF6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-199. RA Sampson N.D., Hewitt J.E.; RT "Functional characterization of the novel SR-related CTD associated RT factor, SCAF6."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-607. RC TISSUE=Lymphoblast; RX MEDLINE=97051922; PubMed=8896557; DOI=10.1038/ng1196-285; RA Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M., RA Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O., RA Stevanin G., Agid Y., Brice A.; RT "Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with RT high sensitivity to expanded CAG/glutamine repeats."; RL Nat. Genet. 14:285-291(1996). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-916, FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND VARIANT HIS-199. RX MEDLINE=20256781; PubMed=10794731; DOI=10.1042/0264-6021:3480189; RA LaPlante J.M., O'Rourke F., Lu X., Fein A., Olsen A., Feinstein M.B.; RT "Cloning of human Ca2+ homoeostasis endoplasmic reticulum protein RT (CHERP): regulated expression of antisense cDNA depletes CHERP, RT inhibits intracellular Ca2+ mobilization and decreases cell RT proliferation."; RL Biochem. J. 348:189-199(2000). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=8010949; RA O'Rourke F., Soons K., Flaumenhauft R., Watras J., Baio-Larue C., RA Matthews E., Feinstein M.B.; RT "Ca2+ release by inositol 1,4,5-trisphosphate is blocked by the K(+)- RT channel blockers apamin and tetrapentylammonium ion, and a monoclonal RT antibody to a 63 kDa membrane protein: reversal of blockade by K+ RT ionophores nigericin and valinomycin and purification of the 63 kDa RT antibody-binding protein."; RL Biochem. J. 300:673-683(1994). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12656674; DOI=10.1042/BJ20030013; RA O'Rourke F.A., LaPlante J.M., Feinstein M.B.; RT "Antisense-mediated loss of calcium homoeostasis endoplasmic reticulum RT protein (CHERP; ERPROT213-21) impairs Ca2+ mobilization, nuclear RT factor of activated T-cells (NFAT) activation and cell proliferation RT in Jurkat T-lymphocytes."; RL Biochem. J. 373:133-143(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817; RP THR-819; SER-822; SER-823; SER-828; SER-830 AND SER-904, AND MASS RP SPECTROMETRY. 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-815; SER-817; THR-819 AND SER-822, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815 AND SER-817, AND RP MASS SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-879 AND LYS-901, AND RP MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in calcium homeostasis, growth and CC proliferation. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. CC Endoplasmic reticulum. Note=Distributed throughout the cytoplasm CC and also localizes to the perinuclear region of both human CC erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with CC ITPR1. CC -!- TISSUE SPECIFICITY: Expressed in brain, placenta, lung, liver, CC kidney, pancreas, cardiac and skeletal muscle, and in cultured HEL CC and Dami cells. CC -!- SIMILARITY: Contains 1 CID domain. CC -!- SIMILARITY: Contains 1 G-patch domain. CC -!- SIMILARITY: Contains 1 SURP motif repeat. CC -!- SEQUENCE CAUTION: CC Sequence=AAB53327.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAH21294.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=CAA69591.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=CAA69591.1; Type=Frameshift; Positions=450; 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; AF536542; AAN77183.1; -; mRNA. DR EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021294; AAH21294.1; ALT_INIT; mRNA. DR EMBL; Y08265; CAA69591.1; ALT_SEQ; mRNA. DR EMBL; U94836; AAB53327.1; ALT_INIT; mRNA. DR IPI; IPI00333010; -. DR RefSeq; NP_006378.3; NM_006387.5. DR UniGene; Hs.728764; -. DR HSSP; Q8CH02; 1UG0. DR ProteinModelPortal; Q8IWX8; -. DR SMR; Q8IWX8; 5-67. DR STRING; Q8IWX8; -. DR PhosphoSite; Q8IWX8; -. DR PRIDE; Q8IWX8; -. DR Ensembl; ENST00000198939; ENSP00000198939; ENSG00000085872. DR GeneID; 10523; -. DR KEGG; hsa:10523; -. DR UCSC; uc002nei.1; human. DR UCSC; uc002nej.2; human. DR CTD; 10523; -. DR GeneCards; GC19M016197; -. DR HGNC; HGNC:16930; CHERP. DR neXtProt; NX_Q8IWX8; -. DR PharmGKB; PA26459; -. DR GeneTree; ENSGT00600000084415; -. DR HOGENOM; HBG445457; -. DR HOVERGEN; HBG052716; -. DR InParanoid; Q8IWX8; -. DR OrthoDB; EOG4BCDMG; -. DR NextBio; 39918; -. DR ArrayExpress; Q8IWX8; -. DR Bgee; Q8IWX8; -. DR CleanEx; HS_CHERP; -. DR Genevestigator; Q8IWX8; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI. DR GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR InterPro; IPR006903; DUF618. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR000467; G_patch. DR InterPro; IPR006569; RNA_polymerase_II_lsu_CTD. DR InterPro; IPR000061; Surp. DR Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1. DR Pfam; PF04818; DUF618; 1. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF01805; Surp; 1. DR SMART; SM00443; G_patch; 1. DR SMART; SM00582; RPR; 1. DR SMART; SM00648; SWAP; 1. DR SUPFAM; SSF48464; ENTH_VHS; 1. DR PROSITE; PS51391; CID; 1. DR PROSITE; PS50174; G_PATCH; 1. DR PROSITE; PS50128; SURP; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Endoplasmic reticulum; KW Phosphoprotein; Polymorphism. FT CHAIN 1 916 Calcium homeostasis endoplasmic reticulum FT protein. FT /FTId=PRO_0000299492. FT REPEAT 15 57 SURP motif. FT DOMAIN 149 289 CID. FT DOMAIN 841 891 G-patch. FT COMPBIAS 279 346 Gln-rich. FT COMPBIAS 355 682 Pro-rich. FT COMPBIAS 718 816 Arg-rich. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 18 18 N6-acetyllysine. FT MOD_RES 714 714 Phosphotyrosine (By similarity). FT MOD_RES 813 813 Phosphoserine. FT MOD_RES 815 815 Phosphoserine. FT MOD_RES 817 817 Phosphoserine. FT MOD_RES 819 819 Phosphothreonine. FT MOD_RES 822 822 Phosphoserine. FT MOD_RES 823 823 Phosphoserine. FT MOD_RES 828 828 Phosphoserine. FT MOD_RES 830 830 Phosphoserine. FT MOD_RES 879 879 N6-acetyllysine. FT MOD_RES 901 901 N6-acetyllysine. FT MOD_RES 904 904 Phosphoserine. FT VARIANT 199 199 N -> H (in dbSNP:rs1043448). FT /FTId=VAR_034833. FT CONFLICT 99 99 A -> D (in Ref. 4; CAA69591). FT CONFLICT 175 175 A -> G (in Ref. 4; CAA69591). FT CONFLICT 185 185 K -> T (in Ref. 4; CAA69591). FT CONFLICT 189 189 H -> Y (in Ref. 4; CAA69591). FT CONFLICT 203 203 A -> V (in Ref. 4; CAA69591). FT CONFLICT 418 418 K -> N (in Ref. 4; CAA69591). FT CONFLICT 490 490 S -> N (in Ref. 4; CAA69591). FT CONFLICT 776 776 Y -> S (in Ref. 1; AAN77183). FT CONFLICT 778 778 R -> C (in Ref. 1; AAN77183). SQ SEQUENCE 916 AA; 103702 MW; 0C5D56F4DE4C5B9B CRC64; MEMPLPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL ALEQQQLICK QQTPELEPAA TMPPLPQPPL APAAPIPPAQ GAPSMDELIQ QSQWNLQQQE QHLLALRQEQ VTAAVAHAVE QQMQKLLEET QLDMNEFDNL LQPIIDTCTK DAISAGKNWM FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS SVVQPVQLAF QQQIQTLKTQ HEEFVTSLAQ QQQQQQQQQQ QLQMPQMEAE VKATPPPPAP PPAPAPAPAI PPTTQPDDSK PPIQMPGSSE YEAPGGVQDP AAAGPRGPGP HDQIPPNKPP WFDQPHPVAP WGQQQPPEQP PYPHHQGGPP HCPPWNNSHE GMWGEQRGDP GWNGQRDAPW NNQPDAAWNS QFEGPWNSQH EQPPWGGGQR EPPFRMQRPP HFRGPFPPHQ QHPQFNQPPH PHNFNRFPPR FMQDDFPPRH PFERPPYPHR FDYPQGDFPA EMGPPHHHPG HRMPHPGINE HPPWAGPQHP DFGPPPHGFN GQPPHMRRQG PPHINHDDPS LVPNVPYFDL PAGLMAPLVK LEDHEYKPLD PKDIRLPPPM PPSERLLAAV EAFYSPPSHD RPRNSEGWEQ NGLYEFFRAK MRARRRKGQE KRNSGPSRSR SRSKSRGRSS SRSNSRSSKS SGSYSRSRSR SCSRSYSRSR SRSRSRSRSS RSRSRSQSRS RSKSYSPGRR RRSRSRSPTP PSSAGLGSNS APPIPDSRLG EENKGHQMLV KMGWSGSGGL GAKEQGIQDP IKGGDVRDKW DQYKGVGVAL DDPYENYRRN KSYSFIARMK ARDECK //