ID SYN1_HUMAN Reviewed; 705 AA. AC P17600; B1AJQ1; O75825; Q5H9A9; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 3. DT 27-MAR-2024, entry version 217. DE RecName: Full=Synapsin-1; DE AltName: Full=Brain protein 4.1; DE AltName: Full=Synapsin I; GN Name=SYN1; 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 [GENOMIC DNA], AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX PubMed=2110562; DOI=10.1016/s0021-9258(19)39008-8; RA Suedhof T.C.; RT "The structure of the human synapsin I gene and protein."; RL J. Biol. Chem. 265:7849-7852(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). 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 [GENOMIC DNA] OF 1-125. RX PubMed=2118519; DOI=10.1016/s0021-9258(18)77206-2; RA Sauerwald A., Hoesche C., Oschwald R., Kilimann M.W.; RT "The 5'-flanking region of the synapsin I gene. A G+C-rich, TATA- and CAAT- RT less, phylogenetically conserved sequence with cell type-specific promoter RT function."; RL J. Biol. Chem. 265:14932-14937(1990). RN [5] RP INVOLVEMENT IN EPILX1. RX PubMed=14985377; DOI=10.1136/jmg.2003.013680; RA Garcia C.C., Blair H.J., Seager M., Coulthard A., Tennant S., Buddles M., RA Curtis A., Goodship J.A.; RT "Identification of a mutation in synapsin I, a synaptic vesicle protein, in RT a family with epilepsy."; RL J. Med. Genet. 41:183-187(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551 AND SER-553, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=15822905; DOI=10.1021/pr0498436; RA DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., RA Pant H.C., Dosemeci A.; RT "Phosphoproteomic analysis of synaptosomes from human cerebral cortex."; RL J. Proteome Res. 4:306-315(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551 AND SER-553, 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). RN [8] RP VARIANTS XLID50 THR-550 AND 555-GLN--ASP-705 DEL, CHARACTERIZATION OF RP VARIANTS XLID50 THR-550 AND 555-GLN--ASP-705 DEL, VARIANT ALA-567, RP CHARACTERIZATION OF VARIANT ALA-567, INVOLVEMENT IN XLID50, SUBCELLULAR RP LOCATION, FUNCTION, AND PHOSPHORYLATION. RX PubMed=21441247; DOI=10.1093/hmg/ddr122; RA Fassio A., Patry L., Congia S., Onofri F., Piton A., Gauthier J., Pozzi D., RA Messa M., Defranchi E., Fadda M., Corradi A., Baldelli P., Lapointe L., RA St-Onge J., Meloche C., Mottron L., Valtorta F., Khoa Nguyen D., RA Rouleau G.A., Benfenati F., Cossette P.; RT "SYN1 loss-of-function mutations in autism and partial epilepsy cause RT impaired synaptic function."; RL Hum. Mol. Genet. 20:2297-2307(2011). RN [9] RP INTERACTION WITH SYN2, FUNCTION, AND CHARACTERIZATION OF VARIANT XLID50 RP 555-GLN--ASP-705 DEL. RX PubMed=23406870; DOI=10.1093/hmg/ddt071; RA Lignani G., Raimondi A., Ferrea E., Rocchi A., Paonessa F., Cesca F., RA Orlando M., Tkatch T., Valtorta F., Cossette P., Baldelli P., Benfenati F.; RT "Epileptogenic Q555X SYN1 mutant triggers imbalances in release dynamics RT and short-term plasticity."; RL Hum. Mol. Genet. 22:2186-2199(2013). RN [10] RP VARIANT XLID50 TRP-79, AND CHARACTERIZATION OF VARIANT XLID50 TRP-79. RX PubMed=28973667; DOI=10.1093/hmg/ddx352; RA Guarnieri F.C., Pozzi D., Raimondi A., Fesce R., Valente M.M., RA Delvecchio V.S., Van Esch H., Matteoli M., Benfenati F., D'Adamo P., RA Valtorta F.; RT "A novel SYN1 missense mutation in non-syndromic X-linked intellectual RT disability affects synaptic vesicle life cycle, clustering and mobility."; RL Hum. Mol. Genet. 26:4699-4714(2017). CC -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and CC binds to the cytoskeleton. Acts as a regulator of synaptic vesicles CC trafficking, involved in the control of neurotransmitter release at the CC pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved CC in the regulation of axon outgrowth and synaptogenesis (By similarity). CC The complex formed with NOS1 and CAPON proteins is necessary for CC specific nitric-oxid functions at a presynaptic level (By similarity). CC {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951, CC ECO:0000269|PubMed:21441247, ECO:0000269|PubMed:23406870}. CC -!- SUBUNIT: Homodimer (By similarity). Can form oligomers with SYN2 CC (PubMed:23406870). Interacts with CAPON. Forms a ternary complex with CC NOS1 (By similarity). Isoform Ib interacts with PRNP (By similarity). CC {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951, CC ECO:0000269|PubMed:23406870}. CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:O88935}. Golgi CC apparatus {ECO:0000250|UniProtKB:O88935}. Presynapse CC {ECO:0000269|PubMed:21441247}. Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle {ECO:0000250|UniProtKB:P09951}. Note=Dissociates from CC synaptic vesicles and redistributes into the axon during action CC potential firing, in a step that precedes fusion of vesicles with the CC plasma membrane. Reclusters to presynapses after the cessation of CC synaptic activity. {ECO:0000250|UniProtKB:P09951}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=IA; CC IsoId=P17600-1; Sequence=Displayed; CC Name=IB; CC IsoId=P17600-2; Sequence=VSP_006316, VSP_006317; CC -!- DOMAIN: The A region binds phospholipids with a preference for CC negatively charged species. {ECO:0000250}. CC -!- PTM: Substrate of different protein kinases. Phosphorylated by CaMK2 CC and MAPK1 (PubMed:21441247). Phosphorylation, including phosphorylation CC at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, CC regulates its rate of dispersion, and controls the kinetics of vesicle CC pool turnover and neurotransmitter release (By similarity) CC (PubMed:21441247). {ECO:0000250|UniProtKB:P09951, CC ECO:0000269|PubMed:21441247}. CC -!- DISEASE: Epilepsy, X-linked 1, with variable learning disabilities and CC behavior disorders (EPILX1) [MIM:300491]: A neurologic disorder CC characterized by variable combinations of epilepsy, learning CC difficulties, macrocephaly, and aggressive behavior. CC {ECO:0000269|PubMed:14985377}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Intellectual developmental disorder, X-linked 50 (XLID50) CC [MIM:300115]: A form of intellectual disability, a disorder CC characterized by significantly below average general intellectual CC functioning associated with impairments in adaptive behavior and CC manifested during the developmental period. Intellectual deficiency is CC the only primary symptom of non-syndromic X-linked forms, while CC syndromic forms present with associated physical, neurological and/or CC psychiatric manifestations. {ECO:0000269|PubMed:21441247, CC ECO:0000269|PubMed:23406870, ECO:0000269|PubMed:28973667}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}. 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; M58378; AAC41930.1; -; Genomic_DNA. DR EMBL; M58321; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58341; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58351; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58353; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58359; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58371; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58372; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58373; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58374; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58375; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58376; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58377; AAC41930.1; JOINED; Genomic_DNA. DR EMBL; M58378; AAC41931.1; ALT_SEQ; Genomic_DNA. DR EMBL; M58321; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58341; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58351; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58353; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58359; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58371; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58372; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58373; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58374; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58375; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58376; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; M58377; AAC41931.1; JOINED; Genomic_DNA. DR EMBL; AL009172; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z84466; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471164; EAW59313.1; -; Genomic_DNA. DR EMBL; M55301; AAA60608.1; -; Genomic_DNA. DR CCDS; CCDS14280.1; -. [P17600-1] DR CCDS; CCDS35233.1; -. [P17600-2] DR PIR; A35363; A35363. DR RefSeq; NP_008881.2; NM_006950.3. [P17600-1] DR RefSeq; NP_598006.1; NM_133499.2. [P17600-2] DR AlphaFoldDB; P17600; -. DR SMR; P17600; -. DR BioGRID; 112719; 40. DR CORUM; P17600; -. DR IntAct; P17600; 23. DR MINT; P17600; -. DR STRING; 9606.ENSP00000295987; -. DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate. DR GlyCosmos; P17600; 13 sites, 1 glycan. DR GlyGen; P17600; 13 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P17600; -. DR PhosphoSitePlus; P17600; -. DR BioMuta; SYN1; -. DR DMDM; 73920800; -. DR EPD; P17600; -. DR jPOST; P17600; -. DR MassIVE; P17600; -. DR MaxQB; P17600; -. DR PaxDb; 9606-ENSP00000295987; -. DR PeptideAtlas; P17600; -. DR ProteomicsDB; 53494; -. [P17600-1] DR ProteomicsDB; 53495; -. [P17600-2] DR ABCD; P17600; 1 sequenced antibody. DR Antibodypedia; 403; 1194 antibodies from 45 providers. DR DNASU; 6853; -. DR Ensembl; ENST00000295987.13; ENSP00000295987.7; ENSG00000008056.14. [P17600-1] DR Ensembl; ENST00000340666.5; ENSP00000343206.4; ENSG00000008056.14. [P17600-2] DR GeneID; 6853; -. DR KEGG; hsa:6853; -. DR MANE-Select; ENST00000295987.13; ENSP00000295987.7; NM_006950.3; NP_008881.2. DR UCSC; uc004did.4; human. [P17600-1] DR AGR; HGNC:11494; -. DR CTD; 6853; -. DR DisGeNET; 6853; -. DR GeneCards; SYN1; -. DR HGNC; HGNC:11494; SYN1. DR HPA; ENSG00000008056; Tissue enriched (brain). DR MalaCards; SYN1; -. DR MIM; 300115; phenotype. DR MIM; 300491; phenotype. DR MIM; 313440; gene. DR neXtProt; NX_P17600; -. DR OpenTargets; ENSG00000008056; -. DR Orphanet; 85294; X-linked epilepsy-learning disabilities-behavior disorders syndrome. DR PharmGKB; PA36276; -. DR VEuPathDB; HostDB:ENSG00000008056; -. DR eggNOG; KOG3895; Eukaryota. DR GeneTree; ENSGT00940000161978; -. DR HOGENOM; CLU_010582_3_0_1; -. DR InParanoid; P17600; -. DR OMA; QWITEVS; -. DR OrthoDB; 5487039at2759; -. DR PhylomeDB; P17600; -. DR TreeFam; TF319919; -. DR PathwayCommons; P17600; -. DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle. DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR SignaLink; P17600; -. DR SIGNOR; P17600; -. DR BioGRID-ORCS; 6853; 11 hits in 775 CRISPR screens. DR ChiTaRS; SYN1; human. DR GeneWiki; Synapsin_I; -. DR GenomeRNAi; 6853; -. DR Pharos; P17600; Tbio. DR PRO; PR:P17600; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P17600; Protein. DR Bgee; ENSG00000008056; Expressed in right frontal lobe and 126 other cell types or tissues. DR ExpressionAtlas; P17600; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0098793; C:presynapse; IDA:UniProtKB. DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; TAS:ParkinsonsUK-UCL. DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central. DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; TAS:ParkinsonsUK-UCL. DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl. DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; TAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0048666; P:neuron development; IEA:Ensembl. DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central. DR GO; GO:0046928; P:regulation of neurotransmitter secretion; TAS:ParkinsonsUK-UCL. DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:UniProtKB. DR GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR001359; Synapsin. DR InterPro; IPR020898; Synapsin_ATP-bd_dom. DR InterPro; IPR019735; Synapsin_CS. DR InterPro; IPR019736; Synapsin_P_site. DR InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom. DR PANTHER; PTHR10841; SYNAPSIN; 1. DR PANTHER; PTHR10841:SF24; SYNAPSIN-1; 1. DR Pfam; PF02078; Synapsin; 1. DR Pfam; PF02750; Synapsin_C; 1. DR Pfam; PF10581; Synapsin_N; 1. DR PRINTS; PR01368; SYNAPSIN. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR PROSITE; PS00415; SYNAPSIN_1; 1. DR PROSITE; PS00416; SYNAPSIN_2; 1. DR Genevisible; P17600; HS. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Cell projection; Cytoplasmic vesicle; KW Disease variant; Epilepsy; Glycoprotein; Golgi apparatus; KW Intellectual disability; Methylation; Phosphoprotein; Reference proteome; KW Repeat; Synapse. FT CHAIN 1..705 FT /note="Synapsin-1" FT /id="PRO_0000183018" FT REGION 1..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..28 FT /note="A" FT REGION 29..112 FT /note="B; linker" FT REGION 113..420 FT /note="C; actin-binding and synaptic-vesicle binding" FT REGION 418..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 421..655 FT /note="D; Pro-rich linker" FT REGION 656..705 FT /note="E" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..41 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 455..486 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..533 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 541..556 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 557..573 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 614..630 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 9 FT /note="Phosphoserine; by CaMK1 and PKA" FT /evidence="ECO:0000250|UniProtKB:P09951" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 62 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09951" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09951" FT MOD_RES 312 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 430 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 432 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 436 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P09951" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 476 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 534 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 547 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 551 FT /note="Phosphoserine; by PDPK1" FT /evidence="ECO:0007744|PubMed:15822905, FT ECO:0007744|PubMed:21406692" FT MOD_RES 553 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15822905, FT ECO:0007744|PubMed:21406692" FT MOD_RES 556 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 568 FT /note="Phosphoserine; by CaMK2" FT /evidence="ECO:0000250|UniProtKB:P17599" FT MOD_RES 605 FT /note="Phosphoserine; by CaMK2" FT /evidence="ECO:0000250|UniProtKB:P17599" FT MOD_RES 622 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 663 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 665 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 679 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT MOD_RES 683 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88935" FT CARBOHYD 55 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 87 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 96 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 103 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 261 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 432 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 526 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 564 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 578 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT VAR_SEQ 661..669 FT /note="NKSQSLTNA -> KASPAQAQP (in isoform IB)" FT /evidence="ECO:0000305" FT /id="VSP_006316" FT VAR_SEQ 670..705 FT /note="Missing (in isoform IB)" FT /evidence="ECO:0000305" FT /id="VSP_006317" FT VARIANT 79 FT /note="S -> W (in XLID50; results in reduced synaptic FT vesicle mobility, increased clustering of synaptic vesicles FT at presynatptic terminals and increased frequency of FT miniature excitatory postsynaptic currents; FT dbSNP:rs2057941303)" FT /evidence="ECO:0000269|PubMed:28973667" FT /id="VAR_086821" FT VARIANT 550 FT /note="A -> T (in XLID50; uncertain significance; no effect FT on phosphorylation by CaMK2 and MAPK1; has no effect on FT axon elongation when tested in SYN1-knockout mouse neurons; FT slightly reduced protein targeting to presynapse; FT dbSNP:rs397514680)" FT /evidence="ECO:0000269|PubMed:21441247" FT /id="VAR_086822" FT VARIANT 555..705 FT /note="Missing (in XLID50; affects excitatory and FT inhibitory synaptic transmission leading to neuronal FT hyperexcitability; fails to rescue defective synaptic FT vesicle exocytosis in SYN1-knockout mouse neurons; results FT in severely decreased phosphorylation by CaMK2 and MAPK1; FT results in delayed axon elongation when tested in FT SYN1-knockout mouse neurons; severely reduced interaction FT with SYN2; has no effect on protein targeting to FT presynapse)" FT /evidence="ECO:0000269|PubMed:21441247, FT ECO:0000269|PubMed:23406870" FT /id="VAR_086823" FT VARIANT 567 FT /note="T -> A (no effect on phosphorylation by CaMK2 and FT MAPK1; has no effect on axon elongation when tested in FT SYN1-knockout mouse neurons; slightly reduced protein FT targeting to presynapse; dbSNP:rs200533370)" FT /evidence="ECO:0000269|PubMed:21441247" FT /id="VAR_086824" FT CONFLICT 138 FT /note="E -> G (in Ref. 1; AAC41930/AAC41931)" FT /evidence="ECO:0000305" FT CONFLICT 631 FT /note="R -> A (in Ref. 1; AAC41930/AAC41931)" FT /evidence="ECO:0000305" SQ SEQUENCE 705 AA; 74111 MW; BE4CE46C942300B0 CRC64; MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPGAHSP GATPGPGTAT AERSSGVAPA ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG GGSGGAGRGG AASRVLLVID EPHTDWAKYF KGKKIHGEID IKVEQAEFSD LNLVAHANGG FSVDMEVLRN GVKVVRSLKP DFVLIRQHAF SMARNGDYRS LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG TEEFPLIDQT FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS DRYKLWVDTC SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD EDKQLIVELV VNKMAQALPR QRQRDASPGR GSHGQTPSPG ALPLGRQTSQ QPAGPPAQQR PPPQGGPPQP GPGPQRQGPP LQQRPPPQGQ QHLSGLGPPA GSPLPQRLPS PTSAPQQPAS QAAPPTQGQG RQSRPVAGGP GAPPAARPPA SPSPQRQAGP PQATRQTSVS GPAPPKASGA PPGGQQRQGP PQKPPGPAGP TRQASQAGPV PRTGPPTTQQ PRPSGPGPAG RPKPQLAQKP SQDVPPPATA AAGGPPHPQL NKSQSLTNAF NLPEPAPPRP SLSQDEVKAE TIRSLRKSFA SLFSD //