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Protein

Synaptic vesicle glycoprotein 2A

Gene

SV2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Neurotransmitter transport, Transport

Enzyme and pathway databases

ReactomeiREACT_263857. Toxicity of botulinum toxin type F (BoNT/F).
REACT_263924. Toxicity of botulinum toxin type D (BoNT/D).
REACT_264227. Toxicity of botulinum toxin type E (BoNT/E).
REACT_264537. 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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20566. SV2A.

Subcellular locationi

  • Cell junctionsynapse By similarity
  • 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). Colocalizes with ATP2B1 at photoreceptor synaptic terminals.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 169169CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence AnalysisAdd
BLAST
Topological domaini191 – 20515ExtracellularSequence AnalysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence AnalysisAdd
BLAST
Topological domaini227 – 2337CytoplasmicSequence Analysis
Transmembranei234 – 25421HelicalSequence AnalysisAdd
BLAST
Topological domaini255 – 2628ExtracellularSequence Analysis
Transmembranei263 – 28321HelicalSequence AnalysisAdd
BLAST
Topological domaini284 – 29411CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei295 – 31521HelicalSequence AnalysisAdd
BLAST
Topological domaini316 – 33419ExtracellularSequence AnalysisAdd
BLAST
Transmembranei335 – 35521HelicalSequence AnalysisAdd
BLAST
Topological domaini356 – 44792CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei448 – 46821HelicalSequence AnalysisAdd
BLAST
Topological domaini469 – 598130ExtracellularSequence AnalysisAdd
BLAST
Transmembranei599 – 61921HelicalSequence AnalysisAdd
BLAST
Topological domaini620 – 6267CytoplasmicSequence Analysis
Transmembranei627 – 64721HelicalSequence AnalysisAdd
BLAST
Topological domaini648 – 6514ExtracellularSequence Analysis
Transmembranei652 – 67221HelicalSequence AnalysisAdd
BLAST
Topological domaini673 – 68513CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei686 – 70823HelicalSequence AnalysisAdd
BLAST
Topological domaini709 – 7124ExtracellularSequence Analysis
Transmembranei713 – 73119HelicalSequence AnalysisAdd
BLAST
Topological domaini732 – 74211CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394564.

Chemistry

DrugBankiDB01202. Levetiracetam.

Polymorphism and mutation databases

DMDMi74749878.

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V11X-ray1.95B81-90[»]
ProteinModelPortaliQ7L0J3.
SMRiQ7L0J3. Positions 168-396, 497-577.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00550000074384.
HOVERGENiHBG053967.
InParanoidiQ7L0J3.
KOiK06258.
OMAiLTTMPES.
OrthoDBiEOG74TWZ1.
PhylomeDBiQ7L0J3.
TreeFamiTF324824.

Family and domain databases

InterProiIPR001646. 5peptide_repeat.
IPR011701. MFS.
IPR020846. MFS_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE
60 70 80 90 100
EEDDDDDFPA PSDGYYRGEG TQDEEEGGAS SDATEGHDED DEIYEGEYQG
110 120 130 140 150
IPRAESGGKG ERMADGAPLA GVRGGLSDGE GPPGGRGEAQ RRKEREELAQ
160 170 180 190 200
QYEAILRECG HGRFQWTLYF VLGLALMADG VEVFVVGFVL PSAEKDMCLS
210 220 230 240 250
DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS VNSVFAFFSS
260 270 280 290 300
FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
310 320 330 340 350
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA
360 370 380 390 400
LTTQPESPRF FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI
410 420 430 440 450
HQEDELIEIQ SDTGTWYQRW GVRALSLGGQ VWGNFLSCFG PEYRRITLMM
460 470 480 490 500
MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY ASRTKVFPGE RVEHVTFNFT
510 520 530 540 550
LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT SSNTFFRNCT
560 570 580 590 600
FINTVFYNTD LFEYKFVNSR LINSTFLHNK EGCPLDVTGT GEGAYMVYFV
610 620 630 640 650
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVMSCVSCF FLSFGNSESA
660 670 680 690 700
MIALLCLFGG VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG
710 720 730 740
ISIFTSFVGI TKAAPILFAS AALALGSSLA LKLPETRGQV LQ
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. Curated
The sequence CAI12573.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V11X-ray1.95B81-90[»]
ProteinModelPortaliQ7L0J3.
SMRiQ7L0J3. Positions 168-396, 497-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115229. 5 interactions.
IntActiQ7L0J3. 3 interactions.
MINTiMINT-4722799.
STRINGi9606.ENSP00000358142.

Chemistry

ChEMBLiCHEMBL1998.
DrugBankiDB01202. Levetiracetam.

PTM databases

PhosphoSiteiQ7L0J3.

Polymorphism and mutation databases

DMDMi74749878.

Proteomic databases

MaxQBiQ7L0J3.
PaxDbiQ7L0J3.
PeptideAtlasiQ7L0J3.
PRIDEiQ7L0J3.

Protocols and materials databases

DNASUi9900.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9900.
GeneCardsiGC01M149874.
HGNCiHGNC:20566. SV2A.
HPAiCAB002226.
HPA007863.
MIMi185860. gene.
neXtProtiNX_Q7L0J3.
PharmGKBiPA128394564.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00550000074384.
HOVERGENiHBG053967.
InParanoidiQ7L0J3.
KOiK06258.
OMAiLTTMPES.
OrthoDBiEOG74TWZ1.
PhylomeDBiQ7L0J3.
TreeFamiTF324824.

Enzyme and pathway databases

ReactomeiREACT_263857. Toxicity of botulinum toxin type F (BoNT/F).
REACT_263924. Toxicity of botulinum toxin type D (BoNT/D).
REACT_264227. Toxicity of botulinum toxin type E (BoNT/E).
REACT_264537. Toxicity of botulinum toxin type A (BoNT/A).

Miscellaneous databases

ChiTaRSiSV2A. human.
GeneWikiiSV2A.
GenomeRNAii9900.
NextBioi37327.
PROiQ7L0J3.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L0J3.
CleanExiHS_SV2A.
GenevestigatoriQ7L0J3.

Family and domain databases

InterProiIPR001646. 5peptide_repeat.
IPR011701. MFS.
IPR020846. MFS_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 119 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.