ID   SYN2_HUMAN              Reviewed;         582 AA.
AC   Q92777; A0A087WW96; A0A087X2E3; A8MY98;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 4.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Synapsin-2;
DE   AltName: Full=Synapsin II;
GN   Name=SYN2;
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 IIB).
RC   TISSUE=Brain;
RX   PubMed=8964517; DOI=10.1016/0378-1119(96)00234-x;
RA   Xie Y.;
RT   "Cloning and sequencing analysis of a human synapsin IIb-encoding brain
RT   cDNA.";
RL   Gene 173:289-290(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIA AND IIB).
RC   TISSUE=Brain;
RX   PubMed=10565545; DOI=10.3109/10425179909033936;
RA   Porton B., Kao H.-T., Greengard P.;
RT   "Cloning of cDNAs encoding human synapsins IIa and IIb.";
RL   DNA Seq. 10:49-54(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   INVOLVEMENT IN SCZD.
RX   PubMed=15449241; DOI=10.1086/425588;
RA   Chen Q., He G., Qin W., Chen Q.Y., Zhao X.Z., Duan S.W., Liu X.M.,
RA   Feng G.Y., Xu Y.F., St Clair D., Li M., Wang J.H., Xing Y.L., Shi J.G.,
RA   He L.;
RT   "Family-based association study of synapsin II and schizophrenia.";
RL   Am. J. Hum. Genet. 75:873-877(2004).
RN   [5]
RP   INTERACTION WITH SYN1.
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).
CC   -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, binds
CC       to the cytoskeleton, and is believed to function in the regulation of
CC       neurotransmitter release. May play a role in noradrenaline secretion by
CC       sympathetic neurons (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Can form oligomers with SYN1 (PubMed:23406870). Interacts with
CC       CAPON. {ECO:0000250|UniProtKB:Q63537, ECO:0000269|PubMed:23406870}.
CC   -!- SUBCELLULAR LOCATION: Synapse.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=IIa;
CC         IsoId=Q92777-1; Sequence=Displayed;
CC       Name=IIb;
CC         IsoId=Q92777-2; Sequence=VSP_006320, VSP_006321;
CC   -!- TISSUE SPECIFICITY: Central and peripheral nervous systems.
CC   -!- DOMAIN: The A region binds phospholipids with a preference for
CC       negatively charged species. {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-10 dissociates synapsins from synaptic
CC       vesicles. Phosphorylation at Ser-425 by MAPK1/ERK2 and/or MAPK3/ERK1
CC       may play a role in noradrenaline secretion by sympathetic neurons (By
CC       similarity). {ECO:0000250}.
CC   -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial
CC       psychotic disorder or group of disorders characterized by disturbances
CC       in the form and content of thought (e.g. delusions, hallucinations), in
CC       mood (e.g. inappropriate affect), in sense of self and relationship to
CC       the external world (e.g. loss of ego boundaries, withdrawal), and in
CC       behavior (e.g bizarre or apparently purposeless behavior). Although it
CC       affects emotions, it is distinguished from mood disorders in which such
CC       disturbances are primary. Similarly, there may be mild impairment of
CC       cognitive function, and it is distinguished from the dementias in which
CC       disturbed cognitive function is considered primary. Some patients
CC       manifest schizophrenic as well as bipolar disorder symptoms and are
CC       often given the diagnosis of schizoaffective disorder.
CC       {ECO:0000269|PubMed:15449241}. Note=Disease susceptibility may be
CC       associated with variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
CC   -!- CAUTION: There are several mRNAs and ESTs supporting this gene model.
CC       However, the genome sequence encoding the N-terminal part contains
CC       several sequence discrepancies. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AC022234; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AC022234; Type=Miscellaneous discrepancy; Note=Several in-frame stop codons.; Evidence={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; U40215; AAC50718.1; -; mRNA.
DR   EMBL; AF077671; AAC28368.1; -; mRNA.
DR   EMBL; AF077737; AAC33789.1; -; mRNA.
DR   EMBL; ABBA01025208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS74900.1; -. [Q92777-1]
DR   CCDS; CCDS74901.1; -. [Q92777-2]
DR   RefSeq; NP_003169.2; NM_003178.5. [Q92777-2]
DR   RefSeq; NP_598328.1; NM_133625.4. [Q92777-1]
DR   AlphaFoldDB; Q92777; -.
DR   SMR; Q92777; -.
DR   BioGRID; 112720; 24.
DR   CORUM; Q92777; -.
DR   IntAct; Q92777; 9.
DR   MINT; Q92777; -.
DR   STRING; 9606.ENSP00000480050; -.
DR   GlyGen; Q92777; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q92777; -.
DR   PhosphoSitePlus; Q92777; -.
DR   BioMuta; SYN2; -.
DR   DMDM; 223634710; -.
DR   EPD; Q92777; -.
DR   jPOST; Q92777; -.
DR   MassIVE; Q92777; -.
DR   PaxDb; 9606-ENSP00000480050; -.
DR   PeptideAtlas; Q92777; -.
DR   ProteomicsDB; 75457; -. [Q92777-1]
DR   ProteomicsDB; 75458; -. [Q92777-2]
DR   ABCD; Q92777; 1 sequenced antibody.
DR   Antibodypedia; 4054; 164 antibodies from 29 providers.
DR   DNASU; 6854; -.
DR   Ensembl; ENST00000620175.4; ENSP00000484916.1; ENSG00000157152.17. [Q92777-2]
DR   Ensembl; ENST00000621198.5; ENSP00000480050.1; ENSG00000157152.17. [Q92777-1]
DR   GeneID; 6854; -.
DR   KEGG; hsa:6854; -.
DR   MANE-Select; ENST00000621198.5; ENSP00000480050.1; NM_133625.6; NP_598328.1.
DR   AGR; HGNC:11495; -.
DR   CTD; 6854; -.
DR   DisGeNET; 6854; -.
DR   GeneCards; SYN2; -.
DR   HGNC; HGNC:11495; SYN2.
DR   HPA; ENSG00000157152; Tissue enriched (brain).
DR   MalaCards; SYN2; -.
DR   MIM; 181500; phenotype.
DR   MIM; 600755; gene.
DR   neXtProt; NX_Q92777; -.
DR   OpenTargets; ENSG00000157152; -.
DR   VEuPathDB; HostDB:ENSG00000157152; -.
DR   eggNOG; KOG3895; Eukaryota.
DR   GeneTree; ENSGT00940000156062; -.
DR   InParanoid; Q92777; -.
DR   OMA; GTCSVNM; -.
DR   OrthoDB; 5487039at2759; -.
DR   PhylomeDB; Q92777; -.
DR   PathwayCommons; Q92777; -.
DR   Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR   SignaLink; Q92777; -.
DR   SIGNOR; Q92777; -.
DR   BioGRID-ORCS; 6854; 11 hits in 284 CRISPR screens.
DR   ChiTaRS; SYN2; human.
DR   GenomeRNAi; 6854; -.
DR   Pharos; Q92777; Tbio.
DR   PRO; PR:Q92777; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q92777; Protein.
DR   Bgee; ENSG00000157152; Expressed in middle temporal gyrus and 143 other cell types or tissues.
DR   ExpressionAtlas; Q92777; baseline and differential.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005524; F:ATP binding; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0007269; P:neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
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:SF20; SYNAPSIN-2; 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   UCD-2DPAGE; Q92777; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Reference proteome; Schizophrenia;
KW   Synapse.
FT   CHAIN           1..582
FT                   /note="Synapsin-2"
FT                   /id="PRO_0000183021"
FT   REGION          1..29
FT                   /note="A"
FT   REGION          16..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..112
FT                   /note="B; linker"
FT   REGION          113..420
FT                   /note="C; actin-binding and synaptic-vesicle binding"
FT   REGION          420..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..457
FT                   /note="G; Pro-rich linker"
FT   REGION          458..533
FT                   /note="H; Pro/Ser-rich linker"
FT   REGION          534..582
FT                   /note="E"
FT   COMPBIAS        29..46
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..75
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..485
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine; by PKA and CaMK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q63537"
FT   MOD_RES         421
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64332"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64332"
FT   VAR_SEQ         458..478
FT                   /note="GPGQPQGMQPPGKVLPPRRLP -> CLQYILDCNGIAVGPKQVQAS (in
FT                   isoform IIb)"
FT                   /evidence="ECO:0000303|PubMed:10565545,
FT                   ECO:0000303|PubMed:8964517"
FT                   /id="VSP_006320"
FT   VAR_SEQ         479..582
FT                   /note="Missing (in isoform IIb)"
FT                   /evidence="ECO:0000303|PubMed:10565545,
FT                   ECO:0000303|PubMed:8964517"
FT                   /id="VSP_006321"
FT   VARIANT         506
FT                   /note="T -> A (in dbSNP:rs794999)"
FT                   /id="VAR_059825"
FT   CONFLICT        61
FT                   /note="R -> K (in Ref. 2; AAC28368/AAC33789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="P -> A (in Ref. 1; AAC50718)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   582 AA;  62996 MW;  1EB4EC12FF090329 CRC64;
     MMNFLRRRLS DSSFIANLPN GYMTDLQRPE PQQPPPPPPP GPGAASASAA PPTASPGPER
     RPPPASAPAP QPAPTPSVGS SFFSSLSQAV KQTAASAGLV DAPAPAPAAA RKAKVLLVVD
     EPHADWAKCF RGKKVLGDYD IKVEQAEFSE LNLVAHADGT YAVDMQVLRN GTKVVRSFRP
     DFVLIRQHAF GMAENEDFRH LIIGMQYAGL PSINSLESIY NFCDKPWVFA QLVAIYKTLG
     GEKFPLIEQT YYPNHKEMLT LPTFPVVVKI GHAHSGMGKV KVENHYDFQD IASVVALTQT
     YATAEPFIDS KYDIRVQKIG NNYKAYMRTS ISGNWKTNTG SAMLEQIAMS DRYKLWVDTC
     SEMFGGLDIC AVKAVHGKDG KDYIFEVMDC SMPLIGEHQV EDRQLITELV ISKMNQLLSR
     TPALSPQRPL TTQQPQSGTL KDPDSSKTPP QRPPPQGGPG QPQGMQPPGK VLPPRRLPPG
     PSLPPSSSSS SSSSSSAPQR PGGPTTHGDA PSSSSSLAEA QPPLAAPPQK PQPHPQLNKS
     QSLTNAFSFS ESSFFRSSAN EDEAKAETIR SLRKSFASLF SD
//