SNPH_HUMAN
ID SNPH_HUMAN Reviewed; 494 AA.
AC O15079; Q8IYI3;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Syntaphilin;
GN Name=SNPH; Synonyms=KIAA0374;
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 2), FUNCTION, INTERACTION WITH
RP SYNTAXIN-1, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10707983; DOI=10.1016/s0896-6273(00)80882-x;
RA Lao G., Scheuss V., Gerwin C.M., Su Q., Mochida S., Rettig J., Sheng Z.-H.;
RT "Syntaphilin: a syntaxin-1 clamp that controls SNARE assembly.";
RL Neuron 25:191-201(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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] (ISOFORM 1).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Inhibits SNARE complex formation by absorbing free syntaxin-
CC 1. {ECO:0000269|PubMed:10707983}.
CC -!- SUBUNIT: Binds to syntaxin-1.
CC -!- INTERACTION:
CC O15079; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-4401902, EBI-724719;
CC O15079; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-4401902, EBI-17589229;
CC O15079; P23025: XPA; NbExp=3; IntAct=EBI-4401902, EBI-295222;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Synapse, synaptosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15079-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15079-2; Sequence=VSP_037438;
CC -!- TISSUE SPECIFICITY: Brain specific. Found in synapses.
CC {ECO:0000269|PubMed:10707983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20829.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF187733; AAF29901.1; -; mRNA.
DR EMBL; AB002372; BAA20829.2; ALT_INIT; mRNA.
DR EMBL; AL136531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10643.1; -; Genomic_DNA.
DR EMBL; BC035788; AAH35788.1; -; mRNA.
DR CCDS; CCDS13012.1; -. [O15079-1]
DR CCDS; CCDS82590.1; -. [O15079-2]
DR RefSeq; NP_001305163.1; NM_001318234.1. [O15079-2]
DR RefSeq; NP_055538.2; NM_014723.3. [O15079-1]
DR AlphaFoldDB; O15079; -.
DR SMR; O15079; -.
DR BioGRID; 115099; 23.
DR IntAct; O15079; 4.
DR STRING; 9606.ENSP00000371297; -.
DR iPTMnet; O15079; -.
DR PhosphoSitePlus; O15079; -.
DR BioMuta; SNPH; -.
DR EPD; O15079; -.
DR MassIVE; O15079; -.
DR MaxQB; O15079; -.
DR PaxDb; O15079; -.
DR PeptideAtlas; O15079; -.
DR PRIDE; O15079; -.
DR ProteomicsDB; 48434; -. [O15079-1]
DR ProteomicsDB; 48435; -. [O15079-2]
DR Antibodypedia; 34949; 178 antibodies from 31 providers.
DR DNASU; 9751; -.
DR Ensembl; ENST00000381867.6; ENSP00000371291.1; ENSG00000101298.15. [O15079-2]
DR Ensembl; ENST00000381873.7; ENSP00000371297.3; ENSG00000101298.15. [O15079-1]
DR Ensembl; ENST00000614659.1; ENSP00000479696.1; ENSG00000101298.15. [O15079-2]
DR GeneID; 9751; -.
DR KEGG; hsa:9751; -.
DR MANE-Select; ENST00000381867.6; ENSP00000371291.1; NM_001318234.2; NP_001305163.1. [O15079-2]
DR UCSC; uc002wes.4; human. [O15079-1]
DR CTD; 9751; -.
DR DisGeNET; 9751; -.
DR GeneCards; SNPH; -.
DR HGNC; HGNC:15931; SNPH.
DR HPA; ENSG00000101298; Tissue enriched (brain).
DR MIM; 604942; gene.
DR neXtProt; NX_O15079; -.
DR OpenTargets; ENSG00000101298; -.
DR PharmGKB; PA38053; -.
DR VEuPathDB; HostDB:ENSG00000101298; -.
DR eggNOG; ENOG502QUYH; Eukaryota.
DR GeneTree; ENSGT00520000055634; -.
DR HOGENOM; CLU_019458_1_0_1; -.
DR InParanoid; O15079; -.
DR OMA; NSLCPIP; -.
DR OrthoDB; 391092at2759; -.
DR PhylomeDB; O15079; -.
DR TreeFam; TF332407; -.
DR PathwayCommons; O15079; -.
DR SignaLink; O15079; -.
DR BioGRID-ORCS; 9751; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; SNPH; human.
DR GenomeRNAi; 9751; -.
DR Pharos; O15079; Tbio.
DR PRO; PR:O15079; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O15079; protein.
DR Bgee; ENSG00000101298; Expressed in CA1 field of hippocampus and 168 other tissues.
DR ExpressionAtlas; O15079; baseline and differential.
DR Genevisible; O15079; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0017075; F:syntaxin-1 binding; NAS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:UniProtKB.
DR GO; GO:0016081; P:synaptic vesicle docking; NAS:UniProtKB.
DR InterPro; IPR026196; Syntaphilin.
DR InterPro; IPR028197; Syntaphilin/Syntabulin.
DR PANTHER; PTHR16208:SF1; PTHR16208:SF1; 1.
DR Pfam; PF15290; Syntaphilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..494
FT /note="Syntaphilin"
FT /id="PRO_0000072030"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 79..161
FT /evidence="ECO:0000255"
FT COMPBIAS 8..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U23"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U23"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80U23"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U23"
FT VAR_SEQ 1
FT /note="M -> MPGSGPSERMTWPGPALSAGPPTRPLSSAPGIPPIPPLTRTHSLM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10707983,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_037438"
SQ SEQUENCE 494 AA; 53537 MW; CD6269CB66792D2C CRC64;
MAMSLPGSRR TSAGSRRRTS PPVSVRDAYG TSSLSSSSNS GSYKGSDSSP TPRRSMKYTL
CSDNHGIKPP TPEQYLTPLQ QKEVCIRHLK ARLKDTQDRL QDRDTEIDDL KTQLSRMQED
WIEEECHRVE AQLALKEARK EIKQLKQVID TVKNNLIDKD KGLQKYFVDI NIQNKKLETL
LHSMEVAQNG MAKEDGTGES AGGSPARSLT RSSTYTKLSD PAVCGDRQPG DPSSGSAEDG
ADSGFAAADD TLSRTDALEA SSLLSSGVDC GTEETSLHSS FGLGPRFPAS NTYEKLLCGM
EAGVQASCMQ ERAIQTDFVQ YQPDLDTILE KVTQAQVCGT DPESGDRCPE LDAHPSGPRD
PNSAVVVTVG DELEAPEPIT RGPTPQRPGA NPNPGQSVSV VCPMEEEEEA AVAEKEPKSY
WSRHYIVDLL AVVVPAVPTV AWLCRSQRRQ GQPIYNISSL LRGCCTVALH SIRRISCRSL
SQPSPSPAGG GSQL
