SNPC3_HUMAN
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 03-AUG-2022, entry version 169.
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}.
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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 AlphaFoldDB; Q92966; -.
DR BioGRID; 112503; 23.
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; Q92966; -.
DR PeptideAtlas; Q92966; -.
DR PRIDE; Q92966; -.
DR ProteomicsDB; 75633; -.
DR Antibodypedia; 10045; 141 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 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; WSEAHDR; -.
DR OrthoDB; 1595999at2759; -.
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; 745 hits in 1080 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 202 other tissues.
DR ExpressionAtlas; Q92966; baseline and differential.
DR Genevisible; Q92966; HS.
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; PTHR13421; 1.
DR Pfam; PF12251; SNAPC3; 1.
PE 1: Evidence at protein level;
KW 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"
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
