STRN_HUMAN
ID STRN_HUMAN Reviewed; 780 AA.
AC O43815; Q3KP65; Q53TQ8; Q9NP38;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Striatin;
GN Name=STRN;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9693043; DOI=10.1006/geno.1998.5342;
RA Moqrich A., Mattei M.-G., Bartoli M., Rakitina T., Baillat G., Monneron A.,
RA Castets F.;
RT "Cloning of human striatin cDNA (STRN), gene mapping to 2p22-p21, and
RT preferential expression in brain.";
RL Genomics 51:136-139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-229; SER-245 AND
RP SER-259, AND 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Calmodulin-binding protein which may function as scaffolding
CC or signaling protein and may play a role in dendritic Ca(2+) signaling.
CC -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A) (Potential).
CC Interacts with CTTNBP2; this interaction may regulate dendritic spine
CC distribution of STRN. Activation of glutamate receptors weakens the
CC interaction with CTTNBP2 (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- INTERACTION:
CC O43815; Q9P2B4: CTTNBP2NL; NbExp=6; IntAct=EBI-1046642, EBI-1774273;
CC O43815; Q9Y3A3: MOB4; NbExp=5; IntAct=EBI-1046642, EBI-713935;
CC O43815; Q9BUL8: PDCD10; NbExp=5; IntAct=EBI-1046642, EBI-740195;
CC O43815; P67775: PPP2CA; NbExp=5; IntAct=EBI-1046642, EBI-712311;
CC O43815; P30153: PPP2R1A; NbExp=8; IntAct=EBI-1046642, EBI-302388;
CC O43815; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-1046642, EBI-726876;
CC O43815; Q9Y6E0: STK24; NbExp=4; IntAct=EBI-1046642, EBI-740175;
CC O43815; O00506: STK25; NbExp=5; IntAct=EBI-1046642, EBI-618295;
CC O43815; Q13033: STRN3; NbExp=9; IntAct=EBI-1046642, EBI-1053857;
CC O43815; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-1046642, EBI-1105213;
CC O43815; Q9H2K2: TNKS2; NbExp=2; IntAct=EBI-1046642, EBI-4398527;
CC O43815; Q9Y228: TRAF3IP3; NbExp=2; IntAct=EBI-1046642, EBI-765817;
CC O43815-2; Q9BUL8: PDCD10; NbExp=3; IntAct=EBI-1266294, EBI-740195;
CC O43815-2; P30153: PPP2R1A; NbExp=3; IntAct=EBI-1266294, EBI-302388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, dendritic
CC spine {ECO:0000250}. Note=CTTNBP2-binding may regulate dendritic spine
CC distribution. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43815-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43815-2; Sequence=VSP_023495, VSP_023496;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in brain.
CC {ECO:0000269|PubMed:9693043}.
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/STRNID44243ch2p22.html";
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DR EMBL; AJ223814; CAA11560.1; -; mRNA.
DR EMBL; AC007404; AAY24273.1; -; Genomic_DNA.
DR EMBL; AC007382; AAF66162.1; -; Genomic_DNA.
DR EMBL; BC106879; AAI06880.1; -; mRNA.
DR CCDS; CCDS1784.1; -. [O43815-1]
DR RefSeq; NP_003153.2; NM_003162.3. [O43815-1]
DR AlphaFoldDB; O43815; -.
DR SMR; O43815; -.
DR BioGRID; 112674; 124.
DR CORUM; O43815; -.
DR ELM; O43815; -.
DR IntAct; O43815; 78.
DR MINT; O43815; -.
DR STRING; 9606.ENSP00000263918; -.
DR iPTMnet; O43815; -.
DR PhosphoSitePlus; O43815; -.
DR BioMuta; STRN; -.
DR CPTAC; CPTAC-1640; -.
DR CPTAC; CPTAC-1724; -.
DR CPTAC; CPTAC-1725; -.
DR CPTAC; CPTAC-1737; -.
DR EPD; O43815; -.
DR jPOST; O43815; -.
DR MassIVE; O43815; -.
DR MaxQB; O43815; -.
DR PaxDb; O43815; -.
DR PeptideAtlas; O43815; -.
DR PRIDE; O43815; -.
DR ProteomicsDB; 49179; -. [O43815-1]
DR ProteomicsDB; 49180; -. [O43815-2]
DR Antibodypedia; 2791; 190 antibodies from 28 providers.
DR DNASU; 6801; -.
DR Ensembl; ENST00000263918.9; ENSP00000263918.4; ENSG00000115808.12. [O43815-1]
DR Ensembl; ENST00000379213.3; ENSP00000368513.2; ENSG00000115808.12. [O43815-2]
DR GeneID; 6801; -.
DR KEGG; hsa:6801; -.
DR MANE-Select; ENST00000263918.9; ENSP00000263918.4; NM_003162.4; NP_003153.2.
DR UCSC; uc002rpn.4; human. [O43815-1]
DR CTD; 6801; -.
DR DisGeNET; 6801; -.
DR GeneCards; STRN; -.
DR HGNC; HGNC:11424; STRN.
DR HPA; ENSG00000115808; Low tissue specificity.
DR MIM; 614765; gene.
DR neXtProt; NX_O43815; -.
DR OpenTargets; ENSG00000115808; -.
DR PharmGKB; PA36224; -.
DR VEuPathDB; HostDB:ENSG00000115808; -.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR HOGENOM; CLU_009108_2_0_1; -.
DR InParanoid; O43815; -.
DR OMA; IASHPTM; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; O43815; -.
DR TreeFam; TF313387; -.
DR PathwayCommons; O43815; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9673766; Signaling by cytosolic PDGFRA and PDGFRB fusion proteins.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; O43815; -.
DR SIGNOR; O43815; -.
DR BioGRID-ORCS; 6801; 252 hits in 1073 CRISPR screens.
DR ChiTaRS; STRN; human.
DR GeneWiki; STRN; -.
DR GenomeRNAi; 6801; -.
DR Pharos; O43815; Tbio.
DR PRO; PR:O43815; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43815; protein.
DR Bgee; ENSG00000115808; Expressed in endothelial cell and 186 other tissues.
DR Genevisible; O43815; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; NAS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013258; Striatin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08232; Striatin; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell projection; Coiled coil;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW WD repeat.
FT CHAIN 1..780
FT /note="Striatin"
FT /id="PRO_0000051232"
FT REPEAT 461..500
FT /note="WD 1"
FT REPEAT 514..553
FT /note="WD 2"
FT REPEAT 567..606
FT /note="WD 3"
FT REPEAT 662..701
FT /note="WD 4"
FT REPEAT 704..743
FT /note="WD 5"
FT REPEAT 750..779
FT /note="WD 6"
FT REGION 55..63
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 124..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..166
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 289..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..120
FT /evidence="ECO:0000255"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55106"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O55106"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 29..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023495"
FT VAR_SEQ 311..348
FT /note="EKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKR -> G (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023496"
FT CONFLICT 191
FT /note="S -> I (in Ref. 1; CAA11560)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="L -> P (in Ref. 1; CAA11560)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="T -> I (in Ref. 1; CAA11560)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="P -> S (in Ref. 1; CAA11560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 86132 MW; DDB18A11102BEA35 CRC64;
MDEQAGPGVF FSNNHPGAGG AKGLGPLAEA AAAGDGAAAA GAARAQYSLP GILHFLQHEW
ARFEVERAQW EVERAELQAQ IAFLQGERKG QENLKKDLVR RIKMLEYALK QERAKYHKLK
YGTELNQGDM KPPSYDSDEG NETEVQPQQN SQLMWKQGRQ LLRQYLQEVG YTDTILDVKS
KRVRALLGFS SDVTDREDDK NQDSVVNGTE AEVKETAMIA KSELTDSASV LDNFKFLESA
AADFSDEDED DDVDGREKSV IDTSTIVRKK ALPDSGEDRD TKEALKEFDF LVTSEEGDNE
SRSAGDGTDW EKEDQCLMPE AWNVDQGVIT KLKEQYKKER KGKKGVKRPN RSKLQDMLAN
LRDVDELPSL QPSVGSPSRP SSSRLPEHEI NRADEVEALT FPPSSGKSFI MGADEALESE
LGLGELAGLT VANEADSLTY DIANNKDALR KTWNPKFTLR SHFDGIRALA FHPIEPVLIT
ASEDHTLKMW NLQKTAPAKK STSLDVEPIY TFRAHKGPVL CVVMSSNGEQ CYSGGTDGLI
QGWNTTNPNI DPYDSYDPSV LRGPLLGHTD AVWGLAYSAA HQRLLSCSAD GTLRLWNTTE
VAPALSVFND TKELGIPASV DLVSSDPSHM VASFSKGYTS IFNMETQQRI LTLESNVDTT
ANSSCQINRV ISHPTLPISI TAHEDRHIKF YDNNTGKLIH SMVAHLEAVT SLAVDPNGLY
LMSGSHDCSI RLWNLESKTC IQEFTAHRKK FEESIHDVAF HPSKCYIASA GADALAKVFV
