ID   SNPC4_HUMAN             Reviewed;        1469 AA.
AC   Q5SXM2; Q9Y6P7;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   02-OCT-2024, entry version 173.
DE   RecName: Full=snRNA-activating protein complex subunit 4;
DE            Short=SNAPc subunit 4;
DE   AltName: Full=Proximal sequence element-binding transcription factor subunit alpha;
DE            Short=PSE-binding factor subunit alpha;
DE            Short=PTF subunit alpha;
DE   AltName: Full=snRNA-activating protein complex 190 kDa subunit;
DE            Short=SNAPc 190 kDa subunit;
GN   Name=SNAPC4 {ECO:0000312|EMBL:CAI13935.1, ECO:0000312|HGNC:HGNC:11137};
GN   Synonyms=SNAP190 {ECO:0000312|EMBL:AAC02972.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC02972.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH SNAPC2.
RC   TISSUE=Teratocarcinoma {ECO:0000312|EMBL:AAC02972.1};
RX   PubMed=9418884; DOI=10.1128/mcb.18.1.368;
RA   Wong M.W., Henry R.W., Ma B., Kobayashi R., Klages N., Matthias P.,
RA   Strubin M., Hernandez N.;
RT   "The large subunit of basal transcription factor SNAPc is a Myb domain
RT   protein that interacts with Oct-1.";
RL   Mol. Cell. Biol. 18:368-377(1998).
RN   [2] {ECO:0000312|EMBL:CAI13935.1}
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   [3] {ECO:0000305}
RP   INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC5, AND MUTAGENESIS OF GLN-94;
RP   GLN-115; LEU-1314; LEU-1355; LEU-1362; LEU-1364 AND LEU-1369.
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   [4] {ECO:0000305}
RP   FUNCTION, AND INTERACTION WITH TBP AND BRF2.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1157, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [6]
RP   IDENTIFICATION BY 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-1398 AND SER-1400, AND
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP   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).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-599; SER-626 AND
RP   SER-1224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   VARIANTS NEDRSO GLU-185; ASN-199; ARG-386; ASN-441; THR-479;
RP   810-ARG--VAL-1469 DEL AND VAL-967, AND INVOLVEMENT IN NEDRSO.
RX   PubMed=36965478; DOI=10.1016/j.ajhg.2023.03.001;
RG   Undiagnosed Diseases Network;
RA   Frost F.G., Morimoto M., Sharma P., Ruaud L., Belnap N., Calame D.G.,
RA   Uchiyama Y., Matsumoto N., Oud M.M., Ferreira E.A., Narayanan V.,
RA   Rangasamy S., Huentelman M., Emrick L.T., Sato-Shirai I., Kumada S.,
RA   Wolf N.I., Steinbach P.J., Huang Y., Pusey B.N., Passemard S., Levy J.,
RA   Drunat S., Vincent M., Guet A., Agolini E., Novelli A., Digilio M.C.,
RA   Rosenfeld J.A., Murphy J.L., Lupski J.R., Vezina G., Macnamara E.F.,
RA   Adams D.R., Acosta M.T., Tifft C.J., Gahl W.A., Malicdan M.C.V.;
RT   "Bi-allelic SNAPC4 variants dysregulate global alternative splicing and
RT   lead to neuroregression and progressive spastic paraparesis.";
RL   Am. J. Hum. Genet. 110:663-680(2023).
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, ECO:0000269|PubMed:9418884}.
CC   -!- SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1,
CC       SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1,
CC       SNAPC2, SNAPC5, BRF2 and TBP. {ECO:0000269|PubMed:11056176,
CC       ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:9418884}.
CC   -!- INTERACTION:
CC       Q5SXM2; Q16533: SNAPC1; NbExp=12; IntAct=EBI-2801093, EBI-11915024;
CC       Q5SXM2; O75971: SNAPC5; NbExp=3; IntAct=EBI-2801093, EBI-749483;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- DISEASE: Neurodevelopmental disorder with motor regression, progressive
CC       spastic paraplegia, and oromotor dysfunction (NEDRSO) [MIM:620515]: An
CC       autosomal recessive disorder characterized by delayed motor development
CC       and developmental regression after the first year of life, followed by
CC       progressive spasticity with gait alterations, paraparesis, and oromotor
CC       dysfunction. Most individuals have cerebral, cerebellar, or basal
CC       ganglia volume loss. {ECO:0000269|PubMed:36965478}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
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DR   EMBL; AF032387; AAC02972.1; -; mRNA.
DR   EMBL; AL592301; CAI13935.1; -; Genomic_DNA.
DR   CCDS; CCDS6998.1; -.
DR   PIR; T09219; T09219.
DR   RefSeq; NP_003077.2; NM_003086.3.
DR   RefSeq; XP_005266153.1; XM_005266096.2.
DR   RefSeq; XP_006717304.1; XM_006717241.2.
DR   RefSeq; XP_006717305.1; XM_006717242.3.
DR   PDB; 7XUR; EM; 3.49 A; A=1-505.
DR   PDB; 7ZWC; EM; 3.20 A; c=1-1469.
DR   PDB; 7ZWD; EM; 3.00 A; c=1-1469.
DR   PDB; 7ZX7; EM; 3.40 A; c=1-1469.
DR   PDB; 7ZX8; EM; 3.00 A; c=1-1469.
DR   PDB; 7ZXE; EM; 3.50 A; c=1-1469.
DR   PDB; 8ITY; EM; 3.90 A; 4=1-1469.
DR   PDB; 8IUE; EM; 4.10 A; 4=1-1469.
DR   PDB; 8IUH; EM; 3.40 A; 4=1-1469.
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; Q5SXM2; -.
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; Q5SXM2; -.
DR   BioGRID; 112505; 78.
DR   ComplexPortal; CPX-8637; SNAPc snRNA activating protein complex.
DR   CORUM; Q5SXM2; -.
DR   IntAct; Q5SXM2; 77.
DR   MINT; Q5SXM2; -.
DR   STRING; 9606.ENSP00000298532; -.
DR   GlyGen; Q5SXM2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5SXM2; -.
DR   PhosphoSitePlus; Q5SXM2; -.
DR   BioMuta; SNAPC4; -.
DR   DMDM; 74762223; -.
DR   jPOST; Q5SXM2; -.
DR   MassIVE; Q5SXM2; -.
DR   PaxDb; 9606-ENSP00000298532; -.
DR   PeptideAtlas; Q5SXM2; -.
DR   ProteomicsDB; 63996; -.
DR   Pumba; Q5SXM2; -.
DR   Antibodypedia; 18701; 199 antibodies from 21 providers.
DR   DNASU; 6621; -.
DR   Ensembl; ENST00000298532.2; ENSP00000298532.2; ENSG00000165684.6.
DR   Ensembl; ENST00000637388.2; ENSP00000490037.2; ENSG00000165684.6.
DR   Ensembl; ENST00000684778.1; ENSP00000510559.1; ENSG00000165684.6.
DR   GeneID; 6621; -.
DR   KEGG; hsa:6621; -.
DR   MANE-Select; ENST00000684778.1; ENSP00000510559.1; NM_003086.4; NP_003077.2.
DR   UCSC; uc004chh.4; human.
DR   AGR; HGNC:11137; -.
DR   CTD; 6621; -.
DR   DisGeNET; 6621; -.
DR   GeneCards; SNAPC4; -.
DR   HGNC; HGNC:11137; SNAPC4.
DR   HPA; ENSG00000165684; Low tissue specificity.
DR   MalaCards; SNAPC4; -.
DR   MIM; 602777; gene.
DR   MIM; 620515; phenotype.
DR   neXtProt; NX_Q5SXM2; -.
DR   OpenTargets; ENSG00000165684; -.
DR   PharmGKB; PA35985; -.
DR   VEuPathDB; HostDB:ENSG00000165684; -.
DR   eggNOG; KOG0049; Eukaryota.
DR   GeneTree; ENSGT00940000160404; -.
DR   HOGENOM; CLU_004641_0_0_1; -.
DR   InParanoid; Q5SXM2; -.
DR   OMA; MAFHQTK; -.
DR   OrthoDB; 1709448at2759; -.
DR   PhylomeDB; Q5SXM2; -.
DR   TreeFam; TF313064; -.
DR   PathwayCommons; Q5SXM2; -.
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; Q5SXM2; -.
DR   BioGRID-ORCS; 6621; 736 hits in 1178 CRISPR screens.
DR   ChiTaRS; SNAPC4; human.
DR   GeneWiki; SNAPC4; -.
DR   GenomeRNAi; 6621; -.
DR   Pharos; Q5SXM2; Tbio.
DR   PRO; PR:Q5SXM2; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q5SXM2; protein.
DR   Bgee; ENSG00000165684; Expressed in sural nerve and 163 other cell types or tissues.
DR   ExpressionAtlas; Q5SXM2; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0019185; C:snRNA-activating protein complex; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR   GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:ARUK-UCL.
DR   GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IDA:UniProtKB.
DR   CDD; cd00167; SANT; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 4.
DR   InterPro; IPR009057; Homeodomain-like_sf.
DR   InterPro; IPR051575; Myb-like_DNA-bd.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   PANTHER; PTHR46621; SNRNA-ACTIVATING PROTEIN COMPLEX SUBUNIT 4; 1.
DR   PANTHER; PTHR46621:SF1; SNRNA-ACTIVATING PROTEIN COMPLEX SUBUNIT 4; 1.
DR   Pfam; PF13921; Myb_DNA-bind_6; 2.
DR   SMART; SM00717; SANT; 5.
DR   SUPFAM; SSF46689; Homeodomain-like; 3.
DR   PROSITE; PS51294; HTH_MYB; 3.
DR   PROSITE; PS50090; MYB_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Disease variant; DNA-binding; Intellectual disability;
KW   Nucleus; Phosphoprotein; Proteomics identification; Reference proteome;
KW   Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1469
FT                   /note="snRNA-activating protein complex subunit 4"
FT                   /id="PRO_0000197120"
FT   DOMAIN          250..288
FT                   /note="Myb-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          289..343
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          344..395
FT                   /note="Myb-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          396..451
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          452..503
FT                   /note="HTH myb-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        317..341
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        424..447
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        476..499
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          16..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..133
FT                   /note="SNAPC5-binding"
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   REGION          501..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1121..1167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1184..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1281..1393
FT                   /note="SNAPC2-binding"
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   REGION          1430..1449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..516
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1032
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1430..1446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         599
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1157
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18220336"
FT   MOD_RES         1224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BP86"
FT   VARIANT         44
FT                   /note="D -> N (in dbSNP:rs7031489)"
FT                   /id="VAR_059455"
FT   VARIANT         185
FT                   /note="K -> E (in NEDRSO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089014"
FT   VARIANT         199
FT                   /note="D -> N (in NEDRSO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089015"
FT   VARIANT         386
FT                   /note="Q -> R (in NEDRSO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089016"
FT   VARIANT         441
FT                   /note="D -> N (in NEDRSO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089017"
FT   VARIANT         479
FT                   /note="I -> T (in NEDRSO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089018"
FT   VARIANT         799
FT                   /note="H -> Q (in dbSNP:rs3812571)"
FT                   /id="VAR_050193"
FT   VARIANT         810..1469
FT                   /note="Missing (in NEDRSO; likely pathogenic)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089019"
FT   VARIANT         967
FT                   /note="G -> V (in NEDRSO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36965478"
FT                   /id="VAR_089020"
FT   VARIANT         1448
FT                   /note="P -> S (in dbSNP:rs3812561)"
FT                   /id="VAR_050194"
FT   MUTAGEN         94
FT                   /note="Q->A: Abolishes SNAPC5 binding in the absence of
FT                   SNAPC1. Minimal effect on SNAPC5 binding in the presence of
FT                   SNAPC1."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         94
FT                   /note="Q->L: Abolishes SNAPC5 binding in the absence of
FT                   SNAPC1. Minimal effect on SNAPC5 binding in the presence of
FT                   SNAPC1."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         115
FT                   /note="Q->L: Abolishes SNAPC5 binding in the absence of
FT                   SNAPC1. Minimal effect on SNAPC5 binding in the presence of
FT                   SNAPC1."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         1314
FT                   /note="L->A: Abolishes SNAPC2-binding."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         1355
FT                   /note="L->A: Abolishes SNAPC2-binding."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         1362
FT                   /note="L->A: Abolishes SNAPC2-binding."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         1364
FT                   /note="L->A: Abolishes SNAPC2-binding."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   MUTAGEN         1369
FT                   /note="L->A: Decreased binding to SNAPC2."
FT                   /evidence="ECO:0000269|PubMed:11056176"
FT   CONFLICT        1046
FT                   /note="A -> G (in Ref. 1; AAC02972)"
FT                   /evidence="ECO:0000305"
FT   HELIX           83..122
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:7XUR"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           163..170
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           186..220
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           226..246
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           250..254
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:7ZXE"
FT   HELIX           263..266
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   TURN            267..270
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           277..286
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   TURN            289..291
FT                   /evidence="ECO:0007829|PDB:7XUR"
FT   HELIX           299..312
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           317..323
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           330..339
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          342..345
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           351..364
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           372..376
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   HELIX           384..393
FT                   /evidence="ECO:0007829|PDB:7ZWC"
FT   STRAND          394..396
FT                   /evidence="ECO:0007829|PDB:7ZXE"
FT   STRAND          397..399
FT                   /evidence="ECO:0007829|PDB:7XUR"
FT   HELIX           408..411
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           414..418
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           425..428
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           436..447
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           460..467
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   STRAND          470..472
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           478..481
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           488..501
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   TURN            502..504
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           506..509
FT                   /evidence="ECO:0007829|PDB:8IUH"
FT   HELIX           510..512
FT                   /evidence="ECO:0007829|PDB:8IUH"
SQ   SEQUENCE   1469 AA;  159433 MW;  78CBCFB1887E106C CRC64;
     MDVDAEREKI TQEIKELERI LDPGSSGSHV EISESSLESD SEADSLPSED LDPADPPISE
     EERWGEASND EDDPKDKTLP EDPETCLQLN MVYQEVIQEK LAEANLLLAQ NREQQEELMR
     DLAGSKGTKV KDGKSLPPST YMGHFMKPYF KDKVTGVGPP ANEDTREKAA QGIKAFEELL
     VTKWKNWEKA LLRKSVVSDR LQRLLQPKLL KLEYLHQKQS KVSSELERQA LEKQGREAEK
     EIQDINQLPE EALLGNRLDS HDWEKISNIN FEGSRSAEEI RKFWQNSEHP SINKQEWSRE
     EEERLQAIAA AHGHLEWQKI AEELGTSRSA FQCLQKFQQH NKALKRKEWT EEEDRMLTQL
     VQEMRVGSHI PYRRIVYYME GRDSMQLIYR WTKSLDPGLK KGYWAPEEDA KLLQAVAKYG
     EQDWFKIREE VPGRSDAQCR DRYLRRLHFS LKKGRWNLKE EEQLIELIEK YGVGHWAKIA
     SELPHRSGSQ CLSKWKIMMG KKQGLRRRRR RARHSVRWSS TSSSGSSSGS SGGSSSSSSS
     SSEEDEPEQA QAGEGDRALL SPQYMVPDMD LWVPARQSTS QPWRGGAGAW LGGPAASLSP
     PKGSSASQGG SKEASTTAAA PGEETSPVQV PARAHGPVPR SAQASHSADT RPAGAEKQAL
     EGGRRLLTVP VETVLRVLRA NTAARSCTQK EQLRQPPLPT SSPGVSSGDS VARSHVQWLR
     HRATQSGQRR WRHALHRRLL NRRLLLAVTP WVGDVVVPCT QASQRPAVVQ TQADGLREQL
     QQARLASTPV FTLFTQLFHI DTAGCLEVVR ERKALPPRLP QAGARDPPVH LLQASSSAQS
     TPGHLFPNVP AQEASKSASH KGSRRLASSR VERTLPQASL LASTGPRPKP KTVSELLQEK
     RLQEARAREA TRGPVVLPSQ LLVSSSVILQ PPLPHTPHGR PAPGPTVLNV PLSGPGAPAA
     AKPGTSGSWQ EAGTSAKDKR LSTMQALPLA PVFSEAEGTA PAASQAPALG PGQISVSCPE
     SGLGQSQAPA ASRKQGLPEA PPFLPAAPSP TPLPVQPLSL THIGGPHVAT SVPLPVTWVL
     TAQGLLPVPV PAVVSLPRPA GTPGPAGLLA TLLPPLTETR AAQGPRAPAL SSSWQPPANM
     NREPEPSCRT DTPAPPTHAL SQSPAEADGS VAFVPGEAQV AREIPEPRTS SHADPPEAEP
     PWSGRLPAFG GVIPATEPRG TPGSPSGTQE PRGPLGLEKL PLRQPGPEKG ALDLEKPPLP
     QPGPEKGALD LGLLSQEGEA ATQQWLGGQR GVRVPLLGSR LPYQPPALCS LRALSGLLLH
     KKALEHKATS LVVGGEAERP AGALQASLGL VRGQLQDNPA YLLLRARFLA AFTLPALLAT
     LAPQGVRTTL SVPSRVGSES EDEDLLSELE LADRDGQPGC TTATCPIQGA PDSGKCSASS
     CLDTSNDPDD LDVLRTRHAR HTRKRRRLV
//