GenomeNet

Database: UniProt
Entry: P23327
LinkDB: P23327
Original site: P23327 
ID   SRCH_HUMAN              Reviewed;         699 AA.
AC   P23327; Q504Y6;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   13-FEB-2019, entry version 146.
DE   RecName: Full=Sarcoplasmic reticulum histidine-rich calcium-binding protein;
DE   Flags: Precursor;
GN   Name=HRC; Synonyms=HCP;
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 VARIANTS.
RC   TISSUE=Skeletal muscle;
RX   PubMed=2037293; DOI=10.1016/0888-7543(91)90359-M;
RA   Hofmann S.L., Topham M., Hsieh C.-L., Francke U.;
RT   "cDNA and genomic cloning of HRC, a human sarcoplasmic reticulum
RT   protein, and localization of the gene to human chromosome 19 and mouse
RT   chromosome 7.";
RL   Genomics 9:656-669(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [5]
RP   PHOSPHORYLATION AT THR-76; SER-119; SER-145; SER-358; SER-431; SER-494
RP   AND SER-567.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted
RT   phosphoproteome.";
RL   Cell 161:1619-1632(2015).
CC   -!- FUNCTION: May play a role in the regulation of calcium
CC       sequestration or release in the SR of skeletal and cardiac muscle.
CC   -!- INTERACTION:
CC       E9Q401:Ryr2 (xeno); NbExp=3; IntAct=EBI-9639760, EBI-643628;
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen.
CC   -!- SIMILARITY: Belongs to the HRC family. {ECO:0000305}.
DR   EMBL; M60052; AAA88071.1; -; mRNA.
DR   EMBL; BC069795; AAH69795.1; -; mRNA.
DR   EMBL; BC069802; AAH69802.1; -; mRNA.
DR   EMBL; BC094691; AAH94691.1; -; mRNA.
DR   CCDS; CCDS12759.1; -.
DR   PIR; A54660; A54660.
DR   RefSeq; NP_002143.1; NM_002152.2.
DR   UniGene; Hs.436885; -.
DR   ProteinModelPortal; P23327; -.
DR   BioGrid; 109506; 6.
DR   IntAct; P23327; 5.
DR   STRING; 9606.ENSP00000252825; -.
DR   iPTMnet; P23327; -.
DR   PhosphoSitePlus; P23327; -.
DR   BioMuta; HRC; -.
DR   DMDM; 134873; -.
DR   MaxQB; P23327; -.
DR   PaxDb; P23327; -.
DR   PeptideAtlas; P23327; -.
DR   PRIDE; P23327; -.
DR   ProteomicsDB; 54080; -.
DR   Ensembl; ENST00000252825; ENSP00000252825; ENSG00000130528.
DR   GeneID; 3270; -.
DR   KEGG; hsa:3270; -.
DR   UCSC; uc002pmv.4; human.
DR   CTD; 3270; -.
DR   DisGeNET; 3270; -.
DR   EuPathDB; HostDB:ENSG00000130528.11; -.
DR   GeneCards; HRC; -.
DR   HGNC; HGNC:5178; HRC.
DR   HPA; HPA004833; -.
DR   MIM; 142705; gene.
DR   neXtProt; NX_P23327; -.
DR   OpenTargets; ENSG00000130528; -.
DR   PharmGKB; PA29452; -.
DR   eggNOG; ENOG410J2C1; Eukaryota.
DR   eggNOG; ENOG41122Z9; LUCA.
DR   GeneTree; ENSGT00730000111459; -.
DR   HOVERGEN; HBG016630; -.
DR   InParanoid; P23327; -.
DR   OMA; STEHRHQ; -.
DR   OrthoDB; 618515at2759; -.
DR   PhylomeDB; P23327; -.
DR   TreeFam; TF344276; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   ChiTaRS; HRC; human.
DR   GeneWiki; HRC_(gene); -.
DR   GenomeRNAi; 3270; -.
DR   PRO; PR:P23327; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000130528; Expressed in 108 organ(s), highest expression level in apex of heart.
DR   ExpressionAtlas; P23327; baseline and differential.
DR   Genevisible; P23327; HS.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; TAS:BHF-UCL.
DR   GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR   GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR   GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR   GO; GO:0045823; P:positive regulation of heart contraction; IGI:BHF-UCL.
DR   GO; GO:0010460; P:positive regulation of heart rate; IGI:BHF-UCL.
DR   GO; GO:1901899; P:positive regulation of relaxation of cardiac muscle; IGI:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:1903169; P:regulation of calcium ion transmembrane transport; IGI:BHF-UCL.
DR   GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; TAS:BHF-UCL.
DR   GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IGI:BHF-UCL.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IGI:BHF-UCL.
DR   GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR   GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IGI:BHF-UCL.
DR   GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IGI:BHF-UCL.
DR   GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IGI:BHF-UCL.
DR   InterPro; IPR019552; Hist_rich_Ca-bd.
DR   InterPro; IPR015666; HRC.
DR   PANTHER; PTHR15054; PTHR15054; 3.
DR   Pfam; PF10529; Hist_rich_Ca-bd; 4.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum; Signal.
FT   SIGNAL        1     28
FT   CHAIN        29    699       Sarcoplasmic reticulum histidine-rich
FT                                calcium-binding protein.
FT                                /FTId=PRO_0000022414.
FT   REPEAT      106    121       2-1.
FT   REPEAT      134    154       2-2.
FT   REPEAT      155    177       2-3.
FT   REPEAT      180    213       1-1.
FT   REPEAT      214    237       2-4.
FT   REPEAT      238    270       1-2.
FT   REPEAT      271    294       2-5.
FT   REPEAT      295    318       1-3.
FT   REPEAT      319    342       2-6.
FT   REPEAT      343    365       1-4.
FT   REGION      106    365       4 X tandem repeats, acidic.
FT   REGION      106    342       6 X approximate tandem repeats.
FT   REGION      627    673       Metal-binding. {ECO:0000255}.
FT   COMPBIAS    193    204       Glu-rich (acidic).
FT   COMPBIAS    246    261       Asp-rich (acidic).
FT   MOD_RES      76     76       Phosphothreonine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     119    119       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     145    145       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     333    333       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     358    358       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     431    431       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     494    494       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     567    567       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   VARIANT      43     43       S -> N (in dbSNP:rs3745298).
FT                                /FTId=VAR_021931.
FT   VARIANT      96     96       S -> A (in dbSNP:rs3745297).
FT                                /FTId=VAR_005623.
FT   VARIANT     204    204       Missing.
FT                                /FTId=VAR_011622.
SQ   SEQUENCE   699 AA;  80244 MW;  9922EEDF012C61DD CRC64;
     MGHHRPWLHA SVLWAGVASL LLPPAMTQQL RGDGLGFRNR NNSTGVAGLS EEASAELRHH
     LHSPRDHPDE NKDVSTENGH HFWSHPDREK EDEDVSKEYG HLLPGHRSQD HKVGDEGVSG
     EEVFAEHGGQ ARGHRGHGSE DTEDSAEHRH HLPSHRSHSH QDEDEDEVVS SEHHHHILRH
     GHRGHDGEDD EGEEEEEEEE EEEEASTEYG HQAHRHRGHG SEEDEDVSDG HHHHGPSHRH
     QGHEEDDDDD DDDDDDDDDD DVSIEYRHQA HRHQGHGIEE DEDVSDGHHH RDPSHRHRSH
     EEDDNDDDDV STEYGHQAHR HQDHRKEEVE AVSGEHHHHV PDHRHQGHRD EEEDEDVSTE
     RWHQGPQHVH HGLVDEEEEE EEITVQFGHY VASHQPRGHK SDEEDFQDEY KTEVPHHHHH
     RVPREEDEEV SAELGHQAPS HRQSHQDEET GHGQRGSIKE MSHHPPGHTV VKDRSHLRKD
     DSEEEKEKEE DPGSHEEDDE SSEQGEKGTH HGSRDQEDEE DEEEGHGLSL NQEEEEEEDK
     EEEEEEEDEE RREERAEVGA PLSPDHSEEE EEEEEGLEED EPRFTIIPNP LDRREEAGGA
     SSEEESGEDT GPQDAQEYGN YQPGSLCGYC SFCNRCTECE SCHCDEENMG EHCDQCQHCQ
     FCYLCPLVCE TVCAPGSYVD YFSSSLYQAL ADMLETPEP
//
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