SYN1_HUMAN
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 03-AUG-2022, entry version 208.
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 EPILX.
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).
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. The complex formed with NOS1 and CAPON
CC proteins is necessary for specific nitric-oxid functions at a
CC presynaptic level.
CC -!- SUBUNIT: Homodimer. Interacts with CAPON. Forms a ternary complex with
CC NOS1. Isoform Ib interacts with PRNP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse. Golgi apparatus {ECO:0000250}.
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 at least four different protein kinases. It is
CC probable that phosphorylation plays a role in the regulation of
CC synapsin-1 in the nerve terminal.
CC -!- PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic
CC vesicles. {ECO:0000250}.
CC -!- DISEASE: Epilepsy, X-linked, with variable learning disabilities and
CC behavior disorders (EPILX) [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 -!- 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; 38.
DR CORUM; P17600; -.
DR IntAct; P17600; 23.
DR MINT; P17600; -.
DR STRING; 9606.ENSP00000295987; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
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; P17600; -.
DR PeptideAtlas; P17600; -.
DR PRIDE; P17600; -.
DR ProteomicsDB; 53494; -. [P17600-1]
DR ProteomicsDB; 53495; -. [P17600-2]
DR ABCD; P17600; 1 sequenced antibody.
DR Antibodypedia; 403; 1103 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 CTD; 6853; -.
DR DisGeNET; 6853; -.
DR GeneCards; SYN1; -.
DR HGNC; HGNC:11494; SYN1.
DR HPA; ENSG00000008056; Tissue enriched (brain).
DR MalaCards; SYN1; -.
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; APMTQGQ; -.
DR OrthoDB; 799740at2759; -.
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; 10 hits in 703 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 124 other tissues.
DR ExpressionAtlas; P17600; baseline and differential.
DR Genevisible; P17600; HS.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005829; C:cytosol; IEA:Ensembl.
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: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; NAS:ParkinsonsUK-UCL.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR028713; SYN1.
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:SF24; PTHR10841:SF24; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR Pfam; PF10581; Synapsin_N; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS00415; SYNAPSIN_1; 1.
DR PROSITE; PS00416; SYNAPSIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Epilepsy; Glycoprotein;
KW Golgi apparatus; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW 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 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
