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TSSK3_HUMAN
ID   TSSK3_HUMAN             Reviewed;         268 AA.
AC   Q96PN8; Q5TEE5;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Testis-specific serine/threonine-protein kinase 3;
DE            Short=TSK-3;
DE            Short=TSSK-3;
DE            Short=Testis-specific kinase 3;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase 22C;
GN   Name=TSSK3; Synonyms=SPOGA3, STK22C;
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].
RC   TISSUE=Testis;
RX   PubMed=11597141; DOI=10.1006/geno.2001.6628;
RA   Visconti P.E., Hao Z., Purdon M.A., Stein P., Balsara B.R., Testa J.R.,
RA   Herr J.C., Moss S.B., Kopf G.S.;
RT   "Cloning and chromosomal localization of a gene encoding a novel
RT   serine/threonine kinase belonging to the subfamily of testis-specific
RT   kinases.";
RL   Genomics 77:163-170(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RA   Mao Y., Xie Y., Jiang M.;
RT   "Cloning and characterization of a novel human TSSK3 gene.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   VARIANTS [LARGE SCALE ANALYSIS] THR-140 AND LEU-235.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: May be involved in a signaling pathway during male germ cell
CC       development or mature sperm function.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-168,
CC       potentially by autophosphorylation. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96PN8; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-3918381, EBI-10173507;
CC       Q96PN8; Q03989: ARID5A; NbExp=3; IntAct=EBI-3918381, EBI-948603;
CC       Q96PN8; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-3918381, EBI-12811889;
CC       Q96PN8; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-3918381, EBI-739879;
CC       Q96PN8; Q96H22-3: CENPN; NbExp=3; IntAct=EBI-3918381, EBI-19948078;
CC       Q96PN8; Q96D03: DDIT4L; NbExp=4; IntAct=EBI-3918381, EBI-742054;
CC       Q96PN8; P55039: DRG2; NbExp=3; IntAct=EBI-3918381, EBI-750565;
CC       Q96PN8; Q9BQ95: ECSIT; NbExp=3; IntAct=EBI-3918381, EBI-712452;
CC       Q96PN8; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-3918381, EBI-2349927;
CC       Q96PN8; O00167-2: EYA2; NbExp=3; IntAct=EBI-3918381, EBI-12807776;
CC       Q96PN8; Q08379: GOLGA2; NbExp=6; IntAct=EBI-3918381, EBI-618309;
CC       Q96PN8; Q9UKT9: IKZF3; NbExp=8; IntAct=EBI-3918381, EBI-747204;
CC       Q96PN8; Q0VD86: INCA1; NbExp=3; IntAct=EBI-3918381, EBI-6509505;
CC       Q96PN8; O95678: KRT75; NbExp=3; IntAct=EBI-3918381, EBI-2949715;
CC       Q96PN8; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-3918381, EBI-11953846;
CC       Q96PN8; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-3918381, EBI-10241252;
CC       Q96PN8; P52954: LBX1; NbExp=3; IntAct=EBI-3918381, EBI-20141748;
CC       Q96PN8; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-3918381, EBI-12039345;
CC       Q96PN8; P25791-3: LMO2; NbExp=3; IntAct=EBI-3918381, EBI-11959475;
CC       Q96PN8; Q8TBB1: LNX1; NbExp=7; IntAct=EBI-3918381, EBI-739832;
CC       Q96PN8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-3918381, EBI-741037;
CC       Q96PN8; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-3918381, EBI-12516603;
CC       Q96PN8; A8MW99: MEI4; NbExp=3; IntAct=EBI-3918381, EBI-19944212;
CC       Q96PN8; Q13084: MRPL28; NbExp=3; IntAct=EBI-3918381, EBI-723426;
CC       Q96PN8; P35548: MSX2; NbExp=3; IntAct=EBI-3918381, EBI-6447480;
CC       Q96PN8; P15173: MYOG; NbExp=3; IntAct=EBI-3918381, EBI-3906629;
CC       Q96PN8; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-3918381, EBI-5662487;
CC       Q96PN8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-3918381, EBI-10271199;
CC       Q96PN8; O00746: NME4; NbExp=3; IntAct=EBI-3918381, EBI-744871;
CC       Q96PN8; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-3918381, EBI-10302990;
CC       Q96PN8; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-3918381, EBI-949255;
CC       Q96PN8; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-3918381, EBI-710402;
CC       Q96PN8; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-3918381, EBI-11320284;
CC       Q96PN8; Q9BYM8: RBCK1; NbExp=6; IntAct=EBI-3918381, EBI-2340624;
CC       Q96PN8; Q04864: REL; NbExp=3; IntAct=EBI-3918381, EBI-307352;
CC       Q96PN8; Q04864-2: REL; NbExp=3; IntAct=EBI-3918381, EBI-10829018;
CC       Q96PN8; Q9BVN2: RUSC1; NbExp=5; IntAct=EBI-3918381, EBI-6257312;
CC       Q96PN8; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-3918381, EBI-12037847;
CC       Q96PN8; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-3918381, EBI-10269374;
CC       Q96PN8; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-3918381, EBI-10269322;
CC       Q96PN8; P51692: STAT5B; NbExp=3; IntAct=EBI-3918381, EBI-1186119;
CC       Q96PN8; Q96PV0: SYNGAP1; NbExp=3; IntAct=EBI-3918381, EBI-2682386;
CC       Q96PN8; P15884: TCF4; NbExp=3; IntAct=EBI-3918381, EBI-533224;
CC       Q96PN8; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-3918381, EBI-3923210;
CC       Q96PN8; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-3918381, EBI-11139477;
CC       Q96PN8; Q96PF1: TGM7; NbExp=3; IntAct=EBI-3918381, EBI-12029034;
CC       Q96PN8; Q08117: TLE5; NbExp=3; IntAct=EBI-3918381, EBI-717810;
CC       Q96PN8; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-3918381, EBI-17716262;
CC       Q96PN8; Q86XT4: TRIM50; NbExp=6; IntAct=EBI-3918381, EBI-9867283;
CC       Q96PN8; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-3918381, EBI-2130429;
CC       Q96PN8; Q9C026: TRIM9; NbExp=3; IntAct=EBI-3918381, EBI-720828;
CC       Q96PN8; Q15654: TRIP6; NbExp=3; IntAct=EBI-3918381, EBI-742327;
CC       Q96PN8; P06132: UROD; NbExp=3; IntAct=EBI-3918381, EBI-2871776;
CC       Q96PN8; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-3918381, EBI-11975223;
CC       Q96PN8; Q99990: VGLL1; NbExp=3; IntAct=EBI-3918381, EBI-11983165;
CC       Q96PN8; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-3918381, EBI-2799833;
CC       Q96PN8; P13994: YJU2B; NbExp=3; IntAct=EBI-3918381, EBI-716093;
CC       Q96PN8; P24278: ZBTB25; NbExp=3; IntAct=EBI-3918381, EBI-739899;
CC       Q96PN8; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-3918381, EBI-12030590;
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The mouse homolog is Stk22d.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AF296450; AAK97141.1; -; mRNA.
DR   EMBL; AY048701; AAL02128.1; -; Transcribed_RNA.
DR   EMBL; AL109945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07532.1; -; Genomic_DNA.
DR   EMBL; BC035354; AAH35354.1; -; mRNA.
DR   CCDS; CCDS362.1; -.
DR   RefSeq; NP_443073.1; NM_052841.3.
DR   AlphaFoldDB; Q96PN8; -.
DR   SMR; Q96PN8; -.
DR   BioGRID; 123564; 67.
DR   IntAct; Q96PN8; 76.
DR   STRING; 9606.ENSP00000362634; -.
DR   BindingDB; Q96PN8; -.
DR   ChEMBL; CHEMBL3414416; -.
DR   iPTMnet; Q96PN8; -.
DR   PhosphoSitePlus; Q96PN8; -.
DR   BioMuta; TSSK3; -.
DR   DMDM; 30316270; -.
DR   MassIVE; Q96PN8; -.
DR   MaxQB; Q96PN8; -.
DR   PaxDb; Q96PN8; -.
DR   PeptideAtlas; Q96PN8; -.
DR   PRIDE; Q96PN8; -.
DR   Antibodypedia; 31305; 96 antibodies from 22 providers.
DR   DNASU; 81629; -.
DR   Ensembl; ENST00000373534.4; ENSP00000362634.3; ENSG00000162526.7.
DR   GeneID; 81629; -.
DR   KEGG; hsa:81629; -.
DR   MANE-Select; ENST00000373534.4; ENSP00000362634.3; NM_052841.4; NP_443073.1.
DR   UCSC; uc001bvf.4; human.
DR   CTD; 81629; -.
DR   DisGeNET; 81629; -.
DR   GeneCards; TSSK3; -.
DR   HGNC; HGNC:15473; TSSK3.
DR   HPA; ENSG00000162526; Group enriched (bone marrow, testis).
DR   MIM; 607660; gene.
DR   neXtProt; NX_Q96PN8; -.
DR   OpenTargets; ENSG00000162526; -.
DR   PharmGKB; PA37964; -.
DR   VEuPathDB; HostDB:ENSG00000162526; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00940000161490; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q96PN8; -.
DR   OMA; IRYCHGF; -.
DR   OrthoDB; 947464at2759; -.
DR   PhylomeDB; Q96PN8; -.
DR   TreeFam; TF352374; -.
DR   PathwayCommons; Q96PN8; -.
DR   SignaLink; Q96PN8; -.
DR   SIGNOR; Q96PN8; -.
DR   BioGRID-ORCS; 81629; 40 hits in 1112 CRISPR screens.
DR   ChiTaRS; TSSK3; human.
DR   GenomeRNAi; 81629; -.
DR   Pharos; Q96PN8; Tchem.
DR   PRO; PR:Q96PN8; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q96PN8; protein.
DR   Bgee; ENSG00000162526; Expressed in sperm and 102 other tissues.
DR   ExpressionAtlas; Q96PN8; baseline and differential.
DR   Genevisible; Q96PN8; HS.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   CDD; cd14163; STKc_TSSK3-like; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR042709; TSSK3_STKc.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Differentiation; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Spermatogenesis; Transferase.
FT   CHAIN           1..268
FT                   /note="Testis-specific serine/threonine-protein kinase 3"
FT                   /id="PRO_0000086770"
FT   DOMAIN          10..265
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VARIANT         71
FT                   /note="I -> V (in dbSNP:rs35508255)"
FT                   /id="VAR_051678"
FT   VARIANT         140
FT                   /note="A -> T (in dbSNP:rs55786268)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041245"
FT   VARIANT         235
FT                   /note="S -> L (in dbSNP:rs35457991)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041246"
SQ   SEQUENCE   268 AA;  30102 MW;  EF91F91DD216F671 CRC64;
     MEDFLLSNGY QLGKTIGEGT YSKVKEAFSK KHQRKVAIKV IDKMGGPEEF IQRFLPRELQ
     IVRTLDHKNI IQVYEMLESA DGKICLVMEL AEGGDVFDCV LNGGPLPESR AKALFRQMVE
     AIRYCHGCGV AHRDLKCENA LLQGFNLKLT DFGFAKVLPK SHRELSQTFC GSTAYAAPEV
     LQGIPHDSKK GDVWSMGVVL YVMLCASLPF DDTDIPKMLW QQQKGVSFPT HLSISADCQD
     LLKRLLEPDM ILRPSIEEVS WHPWLAST
 
 
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