ID SNPC3_HUMAN Reviewed; 411 AA. AC Q92966; D3DRI8; Q2VPI6; Q5T285; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=snRNA-activating protein complex subunit 3; DE Short=SNAPc subunit 3; DE AltName: Full=Proximal sequence element-binding transcription factor subunit beta; DE Short=PSE-binding factor subunit beta; DE Short=PTF subunit beta; DE AltName: Full=Small nuclear RNA-activating complex polypeptide 3; DE AltName: Full=snRNA-activating protein complex 50 kDa subunit; DE Short=SNAPc 50 kDa subunit; GN Name=SNAPC3; Synonyms=SNAP50; 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=Teratocarcinoma; RX PubMed=9003788; DOI=10.1002/j.1460-2075.1996.tb01104.x; RA Henry R.W., Ma B., Sadowski C.L., Kobayashi R., Hernandez N.; RT "Cloning and characterization of SNAP50, a subunit of the snRNA-activating RT protein complex SNAPc."; RL EMBO J. 15:7129-7136(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8816454; DOI=10.1128/mcb.16.10.5419; RA Bai L., Wang Z., Yoon J.B., Roeder R.G.; RT "Cloning and characterization of the beta subunit of human proximal RT sequence element-binding transcription factor and its involvement in RT transcription of small nuclear RNA genes by RNA polymerases II and III."; RL Mol. Cell. Biol. 16:5419-5426(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). 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=Skin; 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 INTERACTION WITH SNAPC1. RX PubMed=11056176; DOI=10.1074/jbc.m009301200; RA Ma B., Hernandez N.; RT "A map of protein-protein contacts within the small nuclear RNA-activating RT protein complex SNAPc."; RL J. Biol. Chem. 276:5027-5035(2001). RN [7] RP FUNCTION, AND INTERACTION WITH SNAPC1. RX PubMed=12621023; DOI=10.1074/jbc.m204247200; RA Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.; RT "The small nuclear RNA-activating protein 190 Myb DNA binding domain RT stimulates TATA box-binding protein-TATA box recognition."; RL J. Biol. Chem. 278:18649-18657(2003). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). CC -!- FUNCTION: Part of the SNAPc complex required for the transcription of CC both RNA polymerase II and III small-nuclear RNA genes. Binds to the CC proximal sequence element (PSE), a non-TATA-box basal promoter element CC common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA CC TATA box. {ECO:0000269|PubMed:12621023}. CC -!- SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1, CC SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC3 interacts with SNAPC1. CC {ECO:0000269|PubMed:11056176, ECO:0000269|PubMed:12621023}. CC -!- INTERACTION: CC Q92966; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-1760638, EBI-1104570; CC Q92966; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-1760638, EBI-10181988; CC Q92966; Q9BPX1: HSD17B14; NbExp=4; IntAct=EBI-1760638, EBI-742664; CC Q92966; P04792: HSPB1; NbExp=3; IntAct=EBI-1760638, EBI-352682; CC Q92966; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-1760638, EBI-715394; CC Q92966; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1760638, EBI-10975473; CC Q92966; I6L9F6: NEFL; NbExp=3; IntAct=EBI-1760638, EBI-10178578; CC Q92966; Q8NI38: NFKBID; NbExp=6; IntAct=EBI-1760638, EBI-10271199; CC Q92966; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1760638, EBI-396669; CC Q92966; Q16533: SNAPC1; NbExp=4; IntAct=EBI-1760638, EBI-11915024; CC Q92966; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-1760638, EBI-12938570; CC Q92966; O95801: TTC4; NbExp=3; IntAct=EBI-1760638, EBI-1050890; CC Q92966; Q05086-3: UBE3A; NbExp=3; IntAct=EBI-1760638, EBI-11026619; CC Q92966; O76024: WFS1; NbExp=3; IntAct=EBI-1760638, EBI-720609; CC Q92966; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-1760638, EBI-4395669; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the SNAPC3/SRD2 family. {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; U71300; AAC50948.1; -; mRNA. DR EMBL; U66413; AAD09214.1; -; mRNA. DR EMBL; AL441925; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58681.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58682.1; -; Genomic_DNA. DR EMBL; BC014985; AAH14985.1; -; mRNA. DR EMBL; BC108743; AAI08744.1; -; mRNA. DR EMBL; BC121011; AAI21012.1; -; mRNA. DR EMBL; BC121012; AAI21013.1; -; mRNA. DR CCDS; CCDS6478.1; -. DR RefSeq; NP_001034786.1; NM_001039697.1. DR RefSeq; XP_016870545.1; XM_017015056.1. DR RefSeq; XP_016870546.1; XM_017015057.1. DR PDB; 7XUR; EM; 3.49 A; B=1-411. DR PDB; 7ZWC; EM; 3.20 A; b=1-411. DR PDB; 7ZWD; EM; 3.00 A; b=1-411. DR PDB; 7ZX7; EM; 3.40 A; b=1-411. DR PDB; 7ZX8; EM; 3.00 A; b=1-411. DR PDB; 7ZXE; EM; 3.50 A; b=1-411. DR PDB; 8ITY; EM; 3.90 A; 3=1-411. DR PDB; 8IUE; EM; 4.10 A; 3=1-411. DR PDB; 8IUH; EM; 3.40 A; 3=1-411. DR PDBsum; 7XUR; -. DR PDBsum; 7ZWC; -. DR PDBsum; 7ZWD; -. DR PDBsum; 7ZX7; -. DR PDBsum; 7ZX8; -. DR PDBsum; 7ZXE; -. DR PDBsum; 8ITY; -. DR PDBsum; 8IUE; -. DR PDBsum; 8IUH; -. DR AlphaFoldDB; Q92966; -. DR EMDB; EMD-14996; -. DR EMDB; EMD-14997; -. DR EMDB; EMD-15006; -. DR EMDB; EMD-15007; -. DR EMDB; EMD-15009; -. DR EMDB; EMD-33477; -. DR EMDB; EMD-35712; -. DR EMDB; EMD-35719; -. DR EMDB; EMD-35722; -. DR SMR; Q92966; -. DR BioGRID; 112503; 25. DR CORUM; Q92966; -. DR IntAct; Q92966; 20. DR MINT; Q92966; -. DR STRING; 9606.ENSP00000370200; -. DR iPTMnet; Q92966; -. DR PhosphoSitePlus; Q92966; -. DR BioMuta; SNAPC3; -. DR DMDM; 8134719; -. DR EPD; Q92966; -. DR jPOST; Q92966; -. DR MassIVE; Q92966; -. DR MaxQB; Q92966; -. DR PaxDb; 9606-ENSP00000370200; -. DR PeptideAtlas; Q92966; -. DR ProteomicsDB; 75633; -. DR Pumba; Q92966; -. DR Antibodypedia; 10045; 162 antibodies from 23 providers. DR DNASU; 6619; -. DR Ensembl; ENST00000380821.8; ENSP00000370200.3; ENSG00000164975.16. DR Ensembl; ENST00000467062.5; ENSP00000436699.1; ENSG00000164975.16. DR Ensembl; ENST00000490969.5; ENSP00000432393.1; ENSG00000164975.16. DR Ensembl; ENST00000610884.4; ENSP00000483273.1; ENSG00000164975.16. DR GeneID; 6619; -. DR KEGG; hsa:6619; -. DR MANE-Select; ENST00000380821.8; ENSP00000370200.3; NM_001039697.2; NP_001034786.1. DR UCSC; uc003zlt.4; human. DR AGR; HGNC:11136; -. DR CTD; 6619; -. DR DisGeNET; 6619; -. DR GeneCards; SNAPC3; -. DR HGNC; HGNC:11136; SNAPC3. DR HPA; ENSG00000164975; Low tissue specificity. DR MIM; 602348; gene. DR neXtProt; NX_Q92966; -. DR OpenTargets; ENSG00000164975; -. DR PharmGKB; PA35984; -. DR VEuPathDB; HostDB:ENSG00000164975; -. DR eggNOG; KOG2664; Eukaryota. DR GeneTree; ENSGT00390000005708; -. DR HOGENOM; CLU_041861_0_1_1; -. DR InParanoid; Q92966; -. DR OMA; VHRDDCL; -. DR OrthoDB; 978987at2759; -. DR PhylomeDB; Q92966; -. DR TreeFam; TF317705; -. DR PathwayCommons; Q92966; -. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter. DR SignaLink; Q92966; -. DR BioGRID-ORCS; 6619; 766 hits in 1170 CRISPR screens. DR ChiTaRS; SNAPC3; human. DR GeneWiki; SNAPC3; -. DR GenomeRNAi; 6619; -. DR Pharos; Q92966; Tbio. DR PRO; PR:Q92966; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q92966; Protein. DR Bgee; ENSG00000164975; Expressed in ganglionic eminence and 204 other cell types or tissues. DR ExpressionAtlas; Q92966; baseline and differential. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0019185; C:snRNA-activating protein complex; IBA:GO_Central. DR GO; GO:0003681; F:bent DNA binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; NAS:ARUK-UCL. DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0009301; P:snRNA transcription; TAS:ProtInc. DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc. DR InterPro; IPR022042; snRNA-activating_su3. DR PANTHER; PTHR13421; SNRNA-ACTIVATING PROTEIN COMPLEX SUBUNIT 3; 1. DR PANTHER; PTHR13421:SF16; SNRNA-ACTIVATING PROTEIN COMPLEX SUBUNIT 3; 1. DR Pfam; PF12251; SNAPC3; 1. DR Genevisible; Q92966; HS. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..411 FT /note="snRNA-activating protein complex subunit 3" FT /id="PRO_0000072024" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 63..82 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 398 FT /note="E -> A (in dbSNP:rs3087653)" FT /id="VAR_051366" FT STRAND 32..37 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 44..54 FT /evidence="ECO:0007829|PDB:7ZWC" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 77..90 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 94..103 FT /evidence="ECO:0007829|PDB:7ZWC" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:8IUH" FT HELIX 128..143 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 151..160 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 181..187 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:7ZWC" FT TURN 212..218 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 250..253 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 255..260 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:7XUR" FT HELIX 271..279 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:7ZWC" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 317..327 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:7ZWC" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:8IUH" FT STRAND 358..361 FT /evidence="ECO:0007829|PDB:8IUH" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:7ZWC" FT HELIX 381..388 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 389..393 FT /evidence="ECO:0007829|PDB:7ZWC" FT STRAND 395..398 FT /evidence="ECO:0007829|PDB:7XUR" FT STRAND 400..403 FT /evidence="ECO:0007829|PDB:7ZWC" FT TURN 407..409 FT /evidence="ECO:0007829|PDB:7ZWC" SQ SEQUENCE 411 AA; 46753 MW; 920584BE4CFA366A CRC64; MAEGSRGGPT CSGVGGRQDP VSGSGGCNFP EYELPELNTR AFHVGAFGEL WRGRLRGAGD LSLREPPASA LPGSQAADSD REDAAVARDL DCSLEAAAEL RAVCGLDKLK CLEDGEDPEV IPENTDLVTL GVRKRFLEHR EETITIDRAC RQETFVYEME SHAIGKKPEN SADMIEEGEL ILSVNILYPV IFHKHKEHKP YQTMLVLGSQ KLTQLRDSIR CVSDLQIGGE FSNTPDQAPE HISKDLYKSA FFYFEGTFYN DKRYPECRDL SRTIIEWSES HDRGYGKFQT ARMEDFTFND LCIKLGFPYL YCHQGDCEHV IVITDIRLVH HDDCLDRTLY PLLIKKHWLW TRKCFVCKMY TARWVTNNDS FAPEDPCFFC DVCFRMLHYD SEGNKLGEFL AYPYVDPGTF N //