ID   SNPC1_HUMAN             Reviewed;         368 AA.
AC   Q16533;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=snRNA-activating protein complex subunit 1;
DE            Short=SNAPc subunit 1;
DE   AltName: Full=Proximal sequence element-binding transcription factor subunit gamma;
DE            Short=PSE-binding factor subunit gamma;
DE            Short=PTF subunit gamma;
DE   AltName: Full=Small nuclear RNA-activating complex polypeptide 1;
DE   AltName: Full=snRNA-activating protein complex 43 kDa subunit;
DE            Short=SNAPc 43 kDa subunit;
GN   Name=SNAPC1; Synonyms=SNAP43;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7715707; DOI=10.1038/374653a0;
RA   Henry R.W., Sadowski C.L., Kobayashi R., Hernandez N.;
RT   "A TBP-TAF complex required for transcription of human snRNA genes by RNA
RT   polymerase II and III.";
RL   Nature 374:653-656(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8524284; DOI=10.1128/mcb.16.1.1;
RA   Yoon J.B., Roeder R.G.;
RT   "Cloning of two proximal sequence element-binding transcription factor
RT   subunits (gamma and delta) that are required for transcription of small
RT   nuclear RNA genes by RNA polymerases II and III and interact with the TATA-
RT   binding protein.";
RL   Mol. Cell. Biol. 16:1-9(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and 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   [4]
RP   INTERACTION WITH SNAPC3 AND SNAPC4.
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   [5]
RP   FUNCTION, AND INTERACTION WITH SNAPC3 AND TBP.
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-290, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
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. SNAPC1 interacts with SNAPC3, SNAPC4
CC       and TBP. {ECO:0000269|PubMed:11056176, ECO:0000269|PubMed:12621023}.
CC   -!- INTERACTION:
CC       Q16533; Q16204: CCDC6; NbExp=3; IntAct=EBI-11915024, EBI-1045350;
CC       Q16533; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-11915024, EBI-742102;
CC       Q16533; O14929: HAT1; NbExp=3; IntAct=EBI-11915024, EBI-2339359;
CC       Q16533; O75031: HSF2BP; NbExp=3; IntAct=EBI-11915024, EBI-7116203;
CC       Q16533; Q92966: SNAPC3; NbExp=4; IntAct=EBI-11915024, EBI-1760638;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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; Z47542; CAA87590.1; -; mRNA.
DR   EMBL; U44754; AAC50358.1; -; mRNA.
DR   EMBL; BC014984; AAH14984.1; -; mRNA.
DR   EMBL; BC019038; AAH19038.1; -; mRNA.
DR   CCDS; CCDS9755.1; -.
DR   PIR; JC6081; JC6081.
DR   RefSeq; NP_003073.1; NM_003082.3.
DR   PDB; 7XUR; EM; 3.49 A; C=1-268.
DR   PDB; 7ZWC; EM; 3.20 A; a=1-368.
DR   PDB; 7ZWD; EM; 3.00 A; a=1-368.
DR   PDB; 7ZX7; EM; 3.40 A; a=1-368.
DR   PDB; 7ZX8; EM; 3.00 A; a=1-368.
DR   PDB; 7ZXE; EM; 3.50 A; a=1-368.
DR   PDB; 8ITY; EM; 3.90 A; 1=1-368.
DR   PDB; 8IUE; EM; 4.10 A; 1=1-368.
DR   PDB; 8IUH; EM; 3.40 A; 1=1-368.
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; Q16533; -.
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; Q16533; -.
DR   BioGRID; 112501; 113.
DR   CORUM; Q16533; -.
DR   DIP; DIP-504N; -.
DR   IntAct; Q16533; 17.
DR   STRING; 9606.ENSP00000216294; -.
DR   iPTMnet; Q16533; -.
DR   PhosphoSitePlus; Q16533; -.
DR   BioMuta; SNAPC1; -.
DR   DMDM; 8134716; -.
DR   EPD; Q16533; -.
DR   jPOST; Q16533; -.
DR   MassIVE; Q16533; -.
DR   MaxQB; Q16533; -.
DR   PaxDb; 9606-ENSP00000216294; -.
DR   PeptideAtlas; Q16533; -.
DR   ProteomicsDB; 60896; -.
DR   Pumba; Q16533; -.
DR   Antibodypedia; 11585; 196 antibodies from 23 providers.
DR   DNASU; 6617; -.
DR   Ensembl; ENST00000216294.5; ENSP00000216294.4; ENSG00000023608.5.
DR   GeneID; 6617; -.
DR   KEGG; hsa:6617; -.
DR   MANE-Select; ENST00000216294.5; ENSP00000216294.4; NM_003082.4; NP_003073.1.
DR   UCSC; uc001xft.3; human.
DR   AGR; HGNC:11134; -.
DR   CTD; 6617; -.
DR   DisGeNET; 6617; -.
DR   GeneCards; SNAPC1; -.
DR   HGNC; HGNC:11134; SNAPC1.
DR   HPA; ENSG00000023608; Low tissue specificity.
DR   MIM; 600591; gene.
DR   neXtProt; NX_Q16533; -.
DR   OpenTargets; ENSG00000023608; -.
DR   PharmGKB; PA35982; -.
DR   VEuPathDB; HostDB:ENSG00000023608; -.
DR   eggNOG; KOG4746; Eukaryota.
DR   GeneTree; ENSGT00390000018691; -.
DR   HOGENOM; CLU_067254_0_0_1; -.
DR   InParanoid; Q16533; -.
DR   OMA; LNVHEHY; -.
DR   OrthoDB; 3045295at2759; -.
DR   PhylomeDB; Q16533; -.
DR   TreeFam; TF324445; -.
DR   PathwayCommons; Q16533; -.
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; Q16533; -.
DR   BioGRID-ORCS; 6617; 730 hits in 1153 CRISPR screens.
DR   ChiTaRS; SNAPC1; human.
DR   GeneWiki; SNAPC1; -.
DR   GenomeRNAi; 6617; -.
DR   Pharos; Q16533; Tbio.
DR   PRO; PR:Q16533; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q16533; Protein.
DR   Bgee; ENSG00000023608; Expressed in cartilage tissue and 192 other cell types or tissues.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0019185; C:snRNA-activating protein complex; IBA:GO_Central.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; TAS:ARUK-UCL.
DR   GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; TAS:ARUK-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
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   InterPro; IPR019188; SNAPC1.
DR   PANTHER; PTHR15131; SMALL NUCLEAR RNA ACTIVATING COMPLEX, POLYPEPTIDE 1; 1.
DR   PANTHER; PTHR15131:SF3; SNRNA-ACTIVATING PROTEIN COMPLEX SUBUNIT 1; 1.
DR   Pfam; PF09808; SNAPC1; 1.
DR   Genevisible; Q16533; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..368
FT                   /note="snRNA-activating protein complex subunit 1"
FT                   /id="PRO_0000072017"
FT   REGION          1..168
FT                   /note="SNAPC3-binding"
FT   REGION          164..268
FT                   /note="SNAPC4-binding"
FT   REGION          224..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   HELIX           7..19
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           26..36
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           38..42
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           48..66
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           72..87
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:7XUR"
FT   HELIX           104..116
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           120..131
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           167..171
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           174..194
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          195..200
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           212..231
FT                   /evidence="ECO:0007829|PDB:7ZWC"
SQ   SEQUENCE   368 AA;  42994 MW;  324E89CF8B540C32 CRC64;
     MGTPPGLQTD CEALLSRFQE TDSVRFEDFT ELWRNMKFGT IFCGRMRNLE KNMFTKEALA
     LAWRYFLPPY TFQIRVGALY LLYGLYNTQL CQPKQKIRVA LKDWDEVLKF QQDLVNAQHF
     DAAYIFRKLR LDRAFHFTAM PKLLSYRMKK KIHRAEVTEE FKDPSDRVMK LITSDVLEEM
     LNVHDHYQNM KHVISVDKSK PDKALSLIKD DFFDNIKNIV LEHQQWHKDR KNPSLKSKTN
     DGEEKMEGNS QETERCERAE SLAKIKSKAF SVVIQASKSR RHRQVKLDSS DSDSASGQGQ
     VKATRKKEKK ERLKPAGRKM SLRNKGNVQN IHKEDKPLSL SMPVITEEEE NESLSGTEFT
     ASKKRRKH
//