SYPH_HUMAN
ID SYPH_HUMAN Reviewed; 313 AA.
AC P08247; B2R7L6; B7Z359; Q6P2F7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Synaptophysin;
DE AltName: Full=Major synaptic vesicle protein p38;
GN Name=SYP;
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 1).
RX PubMed=3120152; DOI=10.1093/nar/15.22.9607;
RA Suedhof T.C., Lottspeich F., Greengard P., Mehl E., Jahn R.;
RT "The cDNA and derived amino acid sequences for rat and human
RT synaptophysin.";
RL Nucleic Acids Res. 15:9607-9607(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1975480;
RA Oezcelik T., Lafreniere R.G., Archer B.T. III, Johnston P.A., Willard H.F.,
RA Francke U., Suedhof T.C.;
RT "Synaptophysin: structure of the human gene and assignment to the X
RT chromosome in man and mouse.";
RL Am. J. Hum. Genet. 47:551-561(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9344658; DOI=10.1006/geno.1997.4941;
RA Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S., D'Urso M.,
RA Craig I.W.;
RT "Sequence-based exon prediction around the synaptophysin locus reveals a
RT gene-rich area containing novel genes in human proximal Xp.";
RL Genomics 45:340-347(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
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 [6]
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 [7]
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).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=8838578; DOI=10.1002/jnr.490430111;
RA Harigaya Y., Shoji M., Shirao T., Hirai S.;
RT "Disappearance of actin-binding protein, drebrin, from hippocampal synapses
RT in Alzheimer's disease.";
RL J. Neurosci. Res. 43:87-92(1996).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [10]
RP INTERACTION WITH SRCIN1, AND SUBCELLULAR LOCATION.
RX PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x;
RA Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R.,
RA Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.;
RT "Characterization of a multidomain adaptor protein, p140Cap, as part of a
RT pre-synaptic complex.";
RL J. Neurochem. 107:61-72(2008).
RN [11]
RP VARIANTS XLID96 ARG-217; GLU-277 AND SER-293, AND VARIANTS [LARGE SCALE
RP ANALYSIS] GLN-2; LEU-158; ASN-166 AND ASN-248.
RX PubMed=19377476; DOI=10.1038/ng.367;
RA Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C.,
RA O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M.,
RA Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J.,
RA Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M.,
RA Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P.,
RA Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R.,
RA Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R.,
RA de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M.,
RA Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U.,
RA Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M.,
RA Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T.,
RA Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C.,
RA Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L.,
RA Futreal P.A., Stratton M.R.;
RT "A systematic, large-scale resequencing screen of X-chromosome coding exons
RT in mental retardation.";
RL Nat. Genet. 41:535-543(2009).
RN [12]
RP VARIANT GLN-72.
RX PubMed=28669405; DOI=10.1016/j.ajhg.2017.05.016;
RG CAUSES Study;
RG EPGEN Study;
RA Lehman A., Thouta S., Mancini G.M.S., Naidu S., van Slegtenhorst M.,
RA McWalter K., Person R., Mwenifumbo J., Salvarinova R., Guella I.,
RA McKenzie M.B., Datta A., Connolly M.B., Kalkhoran S.M., Poburko D.,
RA Friedman J.M., Farrer M.J., Demos M., Desai S., Claydon T.;
RT "Loss-of-function and gain-of-function mutations in KCNQ5 cause
RT intellectual disability or epileptic encephalopathy.";
RL Am. J. Hum. Genet. 101:65-74(2017).
CC -!- FUNCTION: Possibly involved in structural functions as organizing other
CC membrane components or in targeting the vesicles to the plasma
CC membrane. Involved in the regulation of short-term and long-term
CC synaptic plasticity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer or homotetramer. Interacts with SRCIN1
CC (PubMed:18662323). Interacts with VAMP2; the interaction is inhibit by
CC interaction of VAPM2 with SEPT8 (By similarity).
CC {ECO:0000250|UniProtKB:P07825, ECO:0000269|PubMed:18662323}.
CC -!- INTERACTION:
CC P08247; P05067: APP; NbExp=3; IntAct=EBI-9071725, EBI-77613;
CC P08247; P53365: ARFIP2; NbExp=3; IntAct=EBI-9071725, EBI-638194;
CC P08247; O75155: CAND2; NbExp=3; IntAct=EBI-9071725, EBI-5656182;
CC P08247; O95971: CD160; NbExp=3; IntAct=EBI-9071725, EBI-4314390;
CC P08247; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-9071725, EBI-517508;
CC P08247; O95363: FARS2; NbExp=3; IntAct=EBI-9071725, EBI-2513774;
CC P08247; P39905-3: GDNF; NbExp=3; IntAct=EBI-9071725, EBI-12702062;
CC P08247; Q9UBD0: HSFX2; NbExp=3; IntAct=EBI-9071725, EBI-947253;
CC P08247; P42858: HTT; NbExp=13; IntAct=EBI-9071725, EBI-466029;
CC P08247; Q8TAC2: JOSD2; NbExp=3; IntAct=EBI-9071725, EBI-12205593;
CC P08247; P13473-2: LAMP2; NbExp=3; IntAct=EBI-9071725, EBI-21591415;
CC P08247; Q9C0E8-2: LNPK; NbExp=3; IntAct=EBI-9071725, EBI-11024283;
CC P08247; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-9071725, EBI-740987;
CC P08247; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-9071725, EBI-11988931;
CC P08247; Q6IN84: MRM1; NbExp=3; IntAct=EBI-9071725, EBI-5454865;
CC P08247; Q96E11: MRRF; NbExp=3; IntAct=EBI-9071725, EBI-2855755;
CC P08247; Q96E29: MTERF3; NbExp=3; IntAct=EBI-9071725, EBI-7825321;
CC P08247; Q9HB07: MYG1; NbExp=3; IntAct=EBI-9071725, EBI-709754;
CC P08247; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-9071725, EBI-11978907;
CC P08247; Q96AL5: PBX3; NbExp=5; IntAct=EBI-9071725, EBI-741171;
CC P08247; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-9071725, EBI-14223623;
CC P08247; O60664: PLIN3; NbExp=3; IntAct=EBI-9071725, EBI-725795;
CC P08247; Q96T60: PNKP; NbExp=3; IntAct=EBI-9071725, EBI-1045072;
CC P08247; P30405: PPIF; NbExp=5; IntAct=EBI-9071725, EBI-5544229;
CC P08247; O75127: PTCD1; NbExp=3; IntAct=EBI-9071725, EBI-2560233;
CC P08247; P43378: PTPN9; NbExp=3; IntAct=EBI-9071725, EBI-742898;
CC P08247; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-9071725, EBI-3232108;
CC P08247; Q9Y371: SH3GLB1; NbExp=6; IntAct=EBI-9071725, EBI-2623095;
CC P08247; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-9071725, EBI-2872322;
CC P08247; Q13596: SNX1; NbExp=3; IntAct=EBI-9071725, EBI-2822329;
CC P08247; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9071725, EBI-742688;
CC P08247; O60225-2: SSX5; NbExp=3; IntAct=EBI-9071725, EBI-12033476;
CC P08247; Q96DR4: STARD4; NbExp=3; IntAct=EBI-9071725, EBI-17217258;
CC P08247; Q8WY91: THAP4; NbExp=3; IntAct=EBI-9071725, EBI-726691;
CC P08247; Q13885: TUBB2A; NbExp=3; IntAct=EBI-9071725, EBI-711595;
CC P08247; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-9071725, EBI-12261790;
CC P08247; Q96P53: WDFY2; NbExp=3; IntAct=EBI-9071725, EBI-9478589;
CC P08247; Q9Y4P8-4: WIPI2; NbExp=3; IntAct=EBI-9071725, EBI-12205107;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:18662323}; Multi-pass membrane
CC protein {ECO:0000255}. Synapse, synaptosome
CC {ECO:0000269|PubMed:18662323}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08247-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08247-2; Sequence=VSP_056897;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, with expression in the
CC hippocampus, the neuropil in the dentate gyrus, where expression is
CC higher in the outer half of the molecular layer than in the inner half,
CC and in the neuropil of CA4 and CA3 (PubMed:8838578). Expressed in the
CC putamen (at protein level) (PubMed:17296554).
CC {ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:8838578}.
CC -!- DOMAIN: The calcium-binding activity is thought to be localized in the
CC cytoplasmic tail of the protein.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:P07825}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 96 (XLID96)
CC [MIM:300802]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:19377476}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Synaptophysin entry;
CC URL="https://en.wikipedia.org/wiki/Synaptophysin";
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DR EMBL; X06389; CAA29686.1; -; mRNA.
DR EMBL; U93305; AAB92358.1; -; Genomic_DNA.
DR EMBL; AK295524; BAH12095.1; -; mRNA.
DR EMBL; AK313030; BAG35863.1; -; mRNA.
DR EMBL; AK315953; BAH14324.1; -; mRNA.
DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50685.1; -; Genomic_DNA.
DR EMBL; BC064550; AAH64550.1; -; mRNA.
DR CCDS; CCDS14321.1; -. [P08247-1]
DR PIR; A35699; A35699.
DR RefSeq; NP_003170.1; NM_003179.2. [P08247-1]
DR AlphaFoldDB; P08247; -.
DR BioGRID; 112721; 133.
DR IntAct; P08247; 65.
DR STRING; 9606.ENSP00000263233; -.
DR TCDB; 9.B.130.1.4; the tetraspan vesicle membrane protein (tvp) family.
DR GlyGen; P08247; 1 site.
DR iPTMnet; P08247; -.
DR PhosphoSitePlus; P08247; -.
DR BioMuta; SYP; -.
DR DMDM; 135162; -.
DR jPOST; P08247; -.
DR MassIVE; P08247; -.
DR MaxQB; P08247; -.
DR PaxDb; P08247; -.
DR PeptideAtlas; P08247; -.
DR PRIDE; P08247; -.
DR ProteomicsDB; 52100; -. [P08247-1]
DR ProteomicsDB; 6493; -.
DR ABCD; P08247; 1 sequenced antibody.
DR Antibodypedia; 501; 1336 antibodies from 53 providers.
DR DNASU; 6855; -.
DR Ensembl; ENST00000263233.9; ENSP00000263233.4; ENSG00000102003.12. [P08247-1]
DR Ensembl; ENST00000479808.5; ENSP00000418169.1; ENSG00000102003.12. [P08247-1]
DR GeneID; 6855; -.
DR KEGG; hsa:6855; -.
DR MANE-Select; ENST00000263233.9; ENSP00000263233.4; NM_003179.3; NP_003170.1.
DR UCSC; uc004dmz.2; human. [P08247-1]
DR CTD; 6855; -.
DR DisGeNET; 6855; -.
DR GeneCards; SYP; -.
DR HGNC; HGNC:11506; SYP.
DR HPA; ENSG00000102003; Group enriched (brain, pituitary gland, retina).
DR MalaCards; SYP; -.
DR MIM; 300802; phenotype.
DR MIM; 313475; gene.
DR neXtProt; NX_P08247; -.
DR OpenTargets; ENSG00000102003; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA36288; -.
DR VEuPathDB; HostDB:ENSG00000102003; -.
DR eggNOG; ENOG502QT4W; Eukaryota.
DR GeneTree; ENSGT01030000234637; -.
DR HOGENOM; CLU_064642_0_0_1; -.
DR InParanoid; P08247; -.
DR OMA; APTCRGD; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; P08247; -.
DR TreeFam; TF315804; -.
DR PathwayCommons; P08247; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; P08247; -.
DR SIGNOR; P08247; -.
DR BioGRID-ORCS; 6855; 15 hits in 700 CRISPR screens.
DR ChiTaRS; SYP; human.
DR GeneWiki; Synaptophysin; -.
DR GenomeRNAi; 6855; -.
DR Pharos; P08247; Tbio.
DR PRO; PR:P08247; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P08247; protein.
DR Bgee; ENSG00000102003; Expressed in right hemisphere of cerebellum and 148 other tissues.
DR ExpressionAtlas; P08247; baseline and differential.
DR Genevisible; P08247; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; NAS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:0016188; P:synaptic vesicle maturation; NAS:UniProtKB.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; NAS:UniProtKB.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR001285; Synaptophysin/porin.
DR InterPro; IPR028714; SYP.
DR PANTHER; PTHR10306; PTHR10306; 1.
DR PANTHER; PTHR10306:SF10; PTHR10306:SF10; 1.
DR Pfam; PF01284; MARVEL; 1.
DR PRINTS; PR00220; SYNAPTOPHYSN.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS00604; SYNAPTOP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasmic vesicle; Disease variant;
KW Glycoprotein; Intellectual disability; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..313
FT /note="Synaptophysin"
FT /id="PRO_0000179161"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..106
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..199
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..227
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 238..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..305
FT /note="Repeats, Gly-rich"
FT MOD_RES 81
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62277"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056897"
FT VARIANT 2
FT /note="L -> Q (in dbSNP:rs200470034)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062983"
FT VARIANT 72
FT /note="E -> Q"
FT /evidence="ECO:0000269|PubMed:28669405"
FT /id="VAR_079223"
FT VARIANT 158
FT /note="S -> L"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062984"
FT VARIANT 166
FT /note="D -> N"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062985"
FT VARIANT 217
FT /note="G -> R (in XLID96; dbSNP:rs137852561)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062986"
FT VARIANT 248
FT /note="D -> N (in dbSNP:rs782086106)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062987"
FT VARIANT 277
FT /note="D -> E (in XLID96; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062988"
FT VARIANT 293
FT /note="G -> S (in XLID96; unknown pathological
FT significance; dbSNP:rs139475570)"
FT /evidence="ECO:0000269|PubMed:19377476"
FT /id="VAR_062989"
FT CONFLICT 196
FT /note="P -> L (in Ref. 7; AAH64550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 33845 MW; 592289C43B12EFA7 CRC64;
MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYSGE LQLSVDCANK
TESDLSIEVE FEYPFRLHQV YFDAPTCRGG TTKVFLVGDY SSSAEFFVTV AVFAFLYSMG
ALATYIFLQN KYRENNKGPM LDFLATAVFA FMWLVSSSAW AKGLSDVKMA TDPENIIKEM
PVCRQTGNTC KELRDPVTSG LNTSVVFGFL NLVLWVGNLW FVFKETGWAA PFLRAPPGAP
EKQPAPGDAY GDAGYGQGPG GYGPQDSYGP QGGYQPDYGQ PAGSGGSGYG PQGDYGQQGY
GPQGAPTSFS NQM
