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Q7L0J3

- SV2A_HUMAN

UniProt

Q7L0J3 - SV2A_HUMAN

Protein

Synaptic vesicle glycoprotein 2A

Gene

SV2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles By similarity.By similarity

    GO - Molecular functioni

    1. protein kinase binding Source: ParkinsonsUK-UCL
    2. receptor activity Source: Ensembl
    3. transmembrane transporter activity Source: InterPro

    GO - Biological processi

    1. cellular calcium ion homeostasis Source: Ensembl
    2. neurotransmitter transport Source: UniProtKB-KW

    Keywords - Biological processi

    Neurotransmitter transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_200616. Toxicity of botulinum toxin type E (BoNT/E).
    REACT_200617. Toxicity of botulinum toxin type D (BoNT/D).
    REACT_200659. Toxicity of botulinum toxin type F (BoNT/F).
    REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synaptic vesicle glycoprotein 2A
    Gene namesi
    Name:SV2A
    Synonyms:KIAA0736
    ORF Names:PSEC0174
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:20566. SV2A.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity; Multi-pass membrane protein By similarity
    Note: Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas By similarity.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. cytoplasm Source: HPA
    3. endoplasmic reticulum Source: LIFEdb
    4. integral component of membrane Source: UniProtKB-KW
    5. neuromuscular junction Source: Ensembl
    6. neuron projection Source: Ensembl
    7. presynaptic active zone Source: Ensembl
    8. synaptic vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasmic vesicle, Membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394564.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 742742Synaptic vesicle glycoprotein 2APRO_0000239764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei81 – 811Phosphoserine1 Publication
    Modified residuei84 – 841Phosphothreonine1 Publication
    Modified residuei480 – 4801PhosphotyrosineBy similarity
    Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1.By similarity
    N-glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ7L0J3.
    PaxDbiQ7L0J3.
    PeptideAtlasiQ7L0J3.
    PRIDEiQ7L0J3.

    PTM databases

    PhosphoSiteiQ7L0J3.

    Expressioni

    Gene expression databases

    BgeeiQ7L0J3.
    CleanExiHS_SV2A.
    GenevestigatoriQ7L0J3.

    Organism-specific databases

    HPAiCAB002226.
    HPA007863.

    Interactioni

    Subunit structurei

    Interacts with SYT1/synaptotagmin-1 in a calcium-dependent manner. Binds the adapter protein complex AP-2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi115229. 3 interactions.
    IntActiQ7L0J3. 3 interactions.
    MINTiMINT-4722799.
    STRINGi9606.ENSP00000358142.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7L0J3.
    SMRiQ7L0J3. Positions 168-396, 497-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 169169CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini191 – 20515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini227 – 2337CytoplasmicSequence Analysis
    Topological domaini255 – 2628ExtracellularSequence Analysis
    Topological domaini284 – 29411CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini316 – 33419ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini356 – 44792CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini469 – 598130ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini620 – 6267CytoplasmicSequence Analysis
    Topological domaini648 – 6514ExtracellularSequence Analysis
    Topological domaini673 – 68513CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini709 – 7124ExtracellularSequence Analysis
    Topological domaini732 – 74211CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei170 – 19021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei206 – 22621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei234 – 25421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei263 – 28321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei295 – 31521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei335 – 35521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei448 – 46821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei599 – 61921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei627 – 64721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei652 – 67221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei686 – 70823HelicalSequence AnalysisAdd
    BLAST
    Transmembranei713 – 73119HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 5757Interaction with SYT1By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the major facilitator superfamily.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0477.
    HOVERGENiHBG053967.
    InParanoidiQ7L0J3.
    KOiK06258.
    OMAiLTTMPES.
    OrthoDBiEOG74TWZ1.
    PhylomeDBiQ7L0J3.
    TreeFamiTF324824.

    Family and domain databases

    InterProiIPR001646. 5peptide_repeat.
    IPR011701. MFS.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005828. Sub_transporter.
    IPR005829. Sugar_transporter_CS.
    IPR022308. SV2.
    [Graphical view]
    PANTHERiPTHR24065. PTHR24065. 1 hit.
    PfamiPF07690. MFS_1. 1 hit.
    PF13599. Pentapeptide_4. 1 hit.
    PF00083. Sugar_tr. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 3 hits.
    TIGRFAMsiTIGR01299. synapt_SV2. 1 hit.
    PROSITEiPS50850. MFS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7L0J3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE    50
    EEDDDDDFPA PSDGYYRGEG TQDEEEGGAS SDATEGHDED DEIYEGEYQG 100
    IPRAESGGKG ERMADGAPLA GVRGGLSDGE GPPGGRGEAQ RRKEREELAQ 150
    QYEAILRECG HGRFQWTLYF VLGLALMADG VEVFVVGFVL PSAEKDMCLS 200
    DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS VNSVFAFFSS 250
    FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW 300
    MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA 350
    LTTQPESPRF FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI 400
    HQEDELIEIQ SDTGTWYQRW GVRALSLGGQ VWGNFLSCFG PEYRRITLMM 450
    MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY ASRTKVFPGE RVEHVTFNFT 500
    LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT SSNTFFRNCT 550
    FINTVFYNTD LFEYKFVNSR LINSTFLHNK EGCPLDVTGT GEGAYMVYFV 600
    SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVMSCVSCF FLSFGNSESA 650
    MIALLCLFGG VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG 700
    ISIFTSFVGI TKAAPILFAS AALALGSSLA LKLPETRGQV LQ 742
    Length:742
    Mass (Da):82,695
    Last modified:July 5, 2004 - v1
    Checksum:i913E216D5CFC2FB2
    GO
    Isoform 2 (identifier: Q7L0J3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         683-742: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:682
    Mass (Da):76,619
    Checksum:i926FD8E2F5EAF88F
    GO

    Sequence cautioni

    The sequence BAA34456.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI12573.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001G → D in CAD97824. (PubMed:17974005)Curated
    Sequence conflicti404 – 4041D → G in BAC11645. (PubMed:16303743)Curated
    Sequence conflicti493 – 4931E → G in CAD97824. (PubMed:17974005)Curated
    Sequence conflicti524 – 5241V → A in BAC11645. (PubMed:16303743)Curated
    Sequence conflicti544 – 5441T → A in BAC11645. (PubMed:16303743)Curated
    Sequence conflicti582 – 5821G → D in BAC11645. (PubMed:16303743)Curated
    Sequence conflicti611 – 6111G → R in BAC11645. (PubMed:16303743)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei683 – 74260Missing in isoform 2. 1 PublicationVSP_019265Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018279 mRNA. Translation: BAA34456.2. Different initiation.
    AK075480 mRNA. Translation: BAC11645.1.
    BX537754 mRNA. Translation: CAD97824.1.
    AL591493 Genomic DNA. Translation: CAI12572.1.
    AL591493 Genomic DNA. Translation: CAI12573.1. Sequence problems.
    CH471121 Genomic DNA. Translation: EAW53596.1.
    CH471121 Genomic DNA. Translation: EAW53598.1.
    BC000776 mRNA. Translation: AAH00776.2.
    BC045111 mRNA. Translation: AAH45111.1.
    CCDSiCCDS940.1. [Q7L0J3-1]
    RefSeqiNP_001265648.1. NM_001278719.1.
    NP_055664.3. NM_014849.4. [Q7L0J3-1]
    UniGeneiHs.516153.

    Genome annotation databases

    EnsembliENST00000369145; ENSP00000358141; ENSG00000159164. [Q7L0J3-2]
    ENST00000369146; ENSP00000358142; ENSG00000159164. [Q7L0J3-1]
    GeneIDi9900.
    KEGGihsa:9900.
    UCSCiuc001etg.3. human. [Q7L0J3-1]

    Polymorphism databases

    DMDMi74749878.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018279 mRNA. Translation: BAA34456.2 . Different initiation.
    AK075480 mRNA. Translation: BAC11645.1 .
    BX537754 mRNA. Translation: CAD97824.1 .
    AL591493 Genomic DNA. Translation: CAI12572.1 .
    AL591493 Genomic DNA. Translation: CAI12573.1 . Sequence problems.
    CH471121 Genomic DNA. Translation: EAW53596.1 .
    CH471121 Genomic DNA. Translation: EAW53598.1 .
    BC000776 mRNA. Translation: AAH00776.2 .
    BC045111 mRNA. Translation: AAH45111.1 .
    CCDSi CCDS940.1. [Q7L0J3-1 ]
    RefSeqi NP_001265648.1. NM_001278719.1.
    NP_055664.3. NM_014849.4. [Q7L0J3-1 ]
    UniGenei Hs.516153.

    3D structure databases

    ProteinModelPortali Q7L0J3.
    SMRi Q7L0J3. Positions 168-396, 497-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115229. 3 interactions.
    IntActi Q7L0J3. 3 interactions.
    MINTi MINT-4722799.
    STRINGi 9606.ENSP00000358142.

    Chemistry

    ChEMBLi CHEMBL1998.
    DrugBanki DB01202. Levetiracetam.

    PTM databases

    PhosphoSitei Q7L0J3.

    Polymorphism databases

    DMDMi 74749878.

    Proteomic databases

    MaxQBi Q7L0J3.
    PaxDbi Q7L0J3.
    PeptideAtlasi Q7L0J3.
    PRIDEi Q7L0J3.

    Protocols and materials databases

    DNASUi 9900.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369145 ; ENSP00000358141 ; ENSG00000159164 . [Q7L0J3-2 ]
    ENST00000369146 ; ENSP00000358142 ; ENSG00000159164 . [Q7L0J3-1 ]
    GeneIDi 9900.
    KEGGi hsa:9900.
    UCSCi uc001etg.3. human. [Q7L0J3-1 ]

    Organism-specific databases

    CTDi 9900.
    GeneCardsi GC01M149874.
    HGNCi HGNC:20566. SV2A.
    HPAi CAB002226.
    HPA007863.
    MIMi 185860. gene.
    neXtProti NX_Q7L0J3.
    PharmGKBi PA128394564.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0477.
    HOVERGENi HBG053967.
    InParanoidi Q7L0J3.
    KOi K06258.
    OMAi LTTMPES.
    OrthoDBi EOG74TWZ1.
    PhylomeDBi Q7L0J3.
    TreeFami TF324824.

    Enzyme and pathway databases

    Reactomei REACT_200616. Toxicity of botulinum toxin type E (BoNT/E).
    REACT_200617. Toxicity of botulinum toxin type D (BoNT/D).
    REACT_200659. Toxicity of botulinum toxin type F (BoNT/F).
    REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).

    Miscellaneous databases

    ChiTaRSi SV2A. human.
    GeneWikii SV2A.
    GenomeRNAii 9900.
    NextBioi 37327.
    PROi Q7L0J3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7L0J3.
    CleanExi HS_SV2A.
    Genevestigatori Q7L0J3.

    Family and domain databases

    InterProi IPR001646. 5peptide_repeat.
    IPR011701. MFS.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005828. Sub_transporter.
    IPR005829. Sugar_transporter_CS.
    IPR022308. SV2.
    [Graphical view ]
    PANTHERi PTHR24065. PTHR24065. 1 hit.
    Pfami PF07690. MFS_1. 1 hit.
    PF13599. Pentapeptide_4. 1 hit.
    PF00083. Sugar_tr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103473. SSF103473. 3 hits.
    TIGRFAMsi TIGR01299. synapt_SV2. 1 hit.
    PROSITEi PS50850. MFS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Teratocarcinoma.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Retina.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain and Ovary.
    8. "The synaptic vesicle protein SV2A is the binding site for the antiepileptic drug levetiracetam."
      Lynch B.A., Lambeng N., Nocka K., Kensel-Hammes P., Bajjalieh S.M., Matagne A., Fuks B.
      Proc. Natl. Acad. Sci. U.S.A. 101:9861-9866(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION AS BINDING-SITE FOR ANTIEPILEPTIC DRUG LEVETIRACETAM.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-81 AND THR-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiSV2A_HUMAN
    AccessioniPrimary (citable) accession number: Q7L0J3
    Secondary accession number(s): D3DUZ7
    , O94841, Q5QNX8, Q7Z3L6, Q8NBJ6, Q9BVZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Identified as the brain binding-site for the antiepileptic drug levetiracetam/lev.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3