SNPC5_HUMAN
ID SNPC5_HUMAN Reviewed; 98 AA.
AC O75971; A8K7N6; Q96CF3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=snRNA-activating protein complex subunit 5;
DE Short=SNAPc subunit 5;
DE AltName: Full=Small nuclear RNA-activating complex polypeptide 5;
DE AltName: Full=snRNA-activating protein complex 19 kDa subunit;
DE Short=SNAPc 19 kDa subunit;
GN Name=SNAPC5; Synonyms=SNAP19;
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).
RX PubMed=9732265; DOI=10.1101/gad.12.17.2664;
RA Henry R.W., Mittal V., Ma B., Kobayashi R., Hernandez N.;
RT "SNAP19 mediates the assembly of a functional core promoter complex (SNAPc)
RT shared by RNA polymerases II and III.";
RL Genes Dev. 12:2664-2672(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Urinary bladder;
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 [5]
RP INTERACTION WITH SNAPC4, AND MUTAGENESIS OF LEU-8 AND LEU-18.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, 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 [8]
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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.
CC -!- SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1,
CC SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC5 interacts with SNAPC4.
CC {ECO:0000269|PubMed:11056176}.
CC -!- INTERACTION:
CC O75971; Q4VCS5-2: AMOT; NbExp=3; IntAct=EBI-749483, EBI-3891843;
CC O75971; Q8WWE8: CYTH4; NbExp=3; IntAct=EBI-749483, EBI-10277443;
CC O75971; P35638-2: DDIT3; NbExp=3; IntAct=EBI-749483, EBI-10173632;
CC O75971; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-749483, EBI-928842;
CC O75971; Q13287: NMI; NbExp=8; IntAct=EBI-749483, EBI-372942;
CC O75971; O94818-2: NOL4; NbExp=3; IntAct=EBI-749483, EBI-10190763;
CC O75971; Q8NFP7: NUDT10; NbExp=3; IntAct=EBI-749483, EBI-726826;
CC O75971; P37198: NUP62; NbExp=3; IntAct=EBI-749483, EBI-347978;
CC O75971; O60232: ZNRD2; NbExp=3; IntAct=EBI-749483, EBI-741415;
CC O75971-2; A2BDD9: AMOT; NbExp=3; IntAct=EBI-12004298, EBI-17286414;
CC O75971-2; Q9NXL2-1: ARHGEF38; NbExp=3; IntAct=EBI-12004298, EBI-18172597;
CC O75971-2; Q13515: BFSP2; NbExp=3; IntAct=EBI-12004298, EBI-10229433;
CC O75971-2; P78537: BLOC1S1; NbExp=3; IntAct=EBI-12004298, EBI-348630;
CC O75971-2; Q8NA61-2: CBY2; NbExp=5; IntAct=EBI-12004298, EBI-11524851;
CC O75971-2; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-12004298, EBI-10181422;
CC O75971-2; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-12004298, EBI-979174;
CC O75971-2; Q02930-3: CREB5; NbExp=3; IntAct=EBI-12004298, EBI-10192698;
CC O75971-2; Q15438: CYTH1; NbExp=3; IntAct=EBI-12004298, EBI-997830;
CC O75971-2; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-12004298, EBI-11748557;
CC O75971-2; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-12004298, EBI-2870039;
CC O75971-2; P47211: GALR1; NbExp=3; IntAct=EBI-12004298, EBI-6624741;
CC O75971-2; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-12004298, EBI-3917143;
CC O75971-2; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-12004298, EBI-717919;
CC O75971-2; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-12004298, EBI-713401;
CC O75971-2; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-12004298, EBI-712105;
CC O75971-2; P25791-3: LMO2; NbExp=3; IntAct=EBI-12004298, EBI-11959475;
CC O75971-2; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-12004298, EBI-12516603;
CC O75971-2; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-12004298, EBI-348259;
CC O75971-2; P13349: MYF5; NbExp=3; IntAct=EBI-12004298, EBI-17491620;
CC O75971-2; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-12004298, EBI-928842;
CC O75971-2; Q13287: NMI; NbExp=3; IntAct=EBI-12004298, EBI-372942;
CC O75971-2; O94818-2: NOL4; NbExp=3; IntAct=EBI-12004298, EBI-10190763;
CC O75971-2; P52435: POLR2J; NbExp=3; IntAct=EBI-12004298, EBI-394753;
CC O75971-2; P78317: RNF4; NbExp=3; IntAct=EBI-12004298, EBI-2340927;
CC O75971-2; Q8WXG8: S100Z; NbExp=3; IntAct=EBI-12004298, EBI-12198403;
CC O75971-2; Q9H169-2: STMN4; NbExp=3; IntAct=EBI-12004298, EBI-20117546;
CC O75971-2; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-12004298, EBI-11961968;
CC O75971-2; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-12004298, EBI-6116822;
CC O75971-2; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-12004298, EBI-12272076;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75971-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75971-2; Sequence=VSP_012785;
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DR EMBL; AF093593; AAC61873.1; -; mRNA.
DR EMBL; AK292051; BAF84740.1; -; mRNA.
DR EMBL; CH471082; EAW77771.1; -; Genomic_DNA.
DR EMBL; BC014315; AAH14315.1; -; mRNA.
DR CCDS; CCDS10217.1; -. [O75971-1]
DR CCDS; CCDS86469.1; -. [O75971-2]
DR RefSeq; NP_001316542.1; NM_001329613.1. [O75971-2]
DR RefSeq; NP_001316544.1; NM_001329615.1. [O75971-1]
DR RefSeq; NP_006040.1; NM_006049.3. [O75971-1]
DR AlphaFoldDB; O75971; -.
DR SMR; O75971; -.
DR BioGRID; 115590; 47.
DR CORUM; O75971; -.
DR IntAct; O75971; 39.
DR MINT; O75971; -.
DR STRING; 9606.ENSP00000319597; -.
DR iPTMnet; O75971; -.
DR PhosphoSitePlus; O75971; -.
DR BioMuta; SNAPC5; -.
DR EPD; O75971; -.
DR jPOST; O75971; -.
DR MassIVE; O75971; -.
DR MaxQB; O75971; -.
DR PaxDb; O75971; -.
DR PeptideAtlas; O75971; -.
DR PRIDE; O75971; -.
DR ProteomicsDB; 50333; -. [O75971-1]
DR ProteomicsDB; 50334; -. [O75971-2]
DR Antibodypedia; 26135; 135 antibodies from 25 providers.
DR DNASU; 10302; -.
DR Ensembl; ENST00000307979.7; ENSP00000308439.7; ENSG00000174446.13. [O75971-2]
DR Ensembl; ENST00000316634.6; ENSP00000319597.5; ENSG00000174446.13. [O75971-1]
DR Ensembl; ENST00000395589.6; ENSP00000378954.2; ENSG00000174446.13. [O75971-1]
DR Ensembl; ENST00000562411.5; ENSP00000454421.1; ENSG00000174446.13. [O75971-1]
DR Ensembl; ENST00000563480.6; ENSP00000457892.1; ENSG00000174446.13. [O75971-1]
DR GeneID; 10302; -.
DR KEGG; hsa:10302; -.
DR MANE-Select; ENST00000316634.6; ENSP00000319597.5; NM_001329615.2; NP_001316544.1.
DR UCSC; uc002apu.2; human. [O75971-1]
DR CTD; 10302; -.
DR DisGeNET; 10302; -.
DR GeneCards; SNAPC5; -.
DR HGNC; HGNC:15484; SNAPC5.
DR HPA; ENSG00000174446; Low tissue specificity.
DR MalaCards; SNAPC5; -.
DR MIM; 605979; gene.
DR neXtProt; NX_O75971; -.
DR OpenTargets; ENSG00000174446; -.
DR PharmGKB; PA37967; -.
DR VEuPathDB; HostDB:ENSG00000174446; -.
DR eggNOG; ENOG502S8MI; Eukaryota.
DR GeneTree; ENSGT00390000010331; -.
DR HOGENOM; CLU_167684_0_0_1; -.
DR InParanoid; O75971; -.
DR OMA; ETEVHIN; -.
DR PhylomeDB; O75971; -.
DR TreeFam; TF328823; -.
DR PathwayCommons; O75971; -.
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; O75971; -.
DR BioGRID-ORCS; 10302; 620 hits in 1086 CRISPR screens.
DR ChiTaRS; SNAPC5; human.
DR GeneWiki; SNAPC5; -.
DR GenomeRNAi; 10302; -.
DR Pharos; O75971; Tdark.
DR PRO; PR:O75971; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O75971; protein.
DR Bgee; ENSG00000174446; Expressed in endothelial cell and 212 other tissues.
DR ExpressionAtlas; O75971; baseline and differential.
DR Genevisible; O75971; 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:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:GO_Central.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:GO_Central.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IDA:GO_Central.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IEA:InterPro.
DR InterPro; IPR029138; SNAPC5.
DR PANTHER; PTHR15333; PTHR15333; 1.
DR Pfam; PF15497; SNAPC5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..98
FT /note="snRNA-activating protein complex subunit 5"
FT /id="PRO_0000072028"
FT REGION 73..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 31..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012785"
FT MUTAGEN 8
FT /note="L->A: Reduced SNAPC4 binding in both the presence or
FT absence of SNAPC1."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 18
FT /note="L->A: Minimal effect on SNAPC4 binding in the
FT absence of SNAPC1. Reduced SNAPC4 binding in the presence
FT of SNAPC1."
FT /evidence="ECO:0000269|PubMed:11056176"
SQ SEQUENCE 98 AA; 11328 MW; 4D797E35AF2D1485 CRC64;
MLSRLQELRK EEETLLRLKA ALHDQLNRLK VEELALQSMI SSRRGDEMLS SHTVPEQSHD
MLVHVDNEAS INQTTLELST KSHVTEEEEE EEEEESDS