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Protein

Synaptotagmin-7

Gene

SYT7

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

Functioni

Ca2+ sensor involved in Ca2+-dependent exocytosis of secretory and synaptic vesicles through Ca2+ and phospholipid binding to the C2 domain (By similarity). Ca2+ induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). SYT7 binds Ca2+ with high affinity and slow kinetics compared to other synaptotagmins (By similarity). Involved in Ca2+-triggered lysosomal exocytosis, a major component of the plasma membrane repair (PubMed:11342594). Ca2+-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages (By similarity). Ca2+-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts (By similarity). In case of infection, involved in participates cell invasion by Trypanosoma cruzi via Ca2+-triggered lysosomal exocytosis (PubMed:11342594, PubMed:15811535). Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes (By similarity). Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca2+ into the axon terminal after spike generation, increasing the release probability of neurotransmitters (By similarity). Probably mediates synaptic facilitation by directly increasing the probability of release (By similarity). May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca2+ and by forming a complex with calmodulin (By similarity). Also acts as a regulator of Ca2+-dependent insulin and glucagon secretion in beta-cells (By similarity). Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (By similarity). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (By similarity).By similarity2 Publications

Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per C2 domain. The ions are bound to the C2 domains.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi166 – 1661Calcium 1By similarity
Metal bindingi166 – 1661Calcium 2By similarity
Metal bindingi172 – 1721Calcium 1By similarity
Metal bindingi225 – 2251Calcium 1By similarity
Metal bindingi225 – 2251Calcium 2By similarity
Metal bindingi227 – 2271Calcium 1By similarity
Metal bindingi227 – 2271Calcium 2By similarity
Metal bindingi227 – 2271Calcium 3By similarity
Metal bindingi230 – 2301Calcium 3By similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi233 – 2331Calcium 3By similarity
Metal bindingi297 – 2971Calcium 4By similarity
Metal bindingi297 – 2971Calcium 5By similarity
Metal bindingi303 – 3031Calcium 5By similarity
Metal bindingi357 – 3571Calcium 4By similarity
Metal bindingi357 – 3571Calcium 5By similarity
Metal bindingi359 – 3591Calcium 4By similarity
Metal bindingi359 – 3591Calcium 5By similarity
Metal bindingi359 – 3591Calcium 6By similarity
Metal bindingi362 – 3621Calcium 6By similarity
Metal bindingi365 – 3651Calcium 4By similarity
Metal bindingi365 – 3651Calcium 6By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

Calcium, Calmodulin-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-7Curated
Alternative name(s):
IPCA-7
Prostate cancer-associated protein 7
Synaptotagmin VII
Short name:
SytVII
Gene namesi
Name:SYT7Imported
Synonyms:PCANAP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:11514. SYT7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616VesicularSequence analysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence analysisAdd
BLAST
Topological domaini38 – 403366CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Peroxisome, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36295.

Polymorphism and mutation databases

BioMutaiSYT7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Synaptotagmin-7PRO_0000183957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei58 – 581PhosphothreonineBy similarity
Modified residuei61 – 611PhosphoserineBy similarity
Modified residuei122 – 1221PhosphoserineBy similarity

Post-translational modificationi

Palmitoylated at its vesicular N-terminus; palmitoylation is required for localization to lysosome and phagocytosis in macrophages.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiO43581.
PaxDbiO43581.
PRIDEiO43581.

PTM databases

iPTMnetiO43581.
PhosphoSiteiO43581.
SwissPalmiO43581.

Expressioni

Tissue specificityi

Expressed in a variety of adult and fetal tissues.

Gene expression databases

BgeeiO43581.
CleanExiHS_SYT7.
ExpressionAtlasiO43581. baseline and differential.
GenevisibleiO43581. HS.

Organism-specific databases

HPAiHPA012869.

Interactioni

Subunit structurei

Homodimer. Can also form heterodimers with SYT6, SYT9 and SYT10. Interacts with calmodulin (CALM1, CALM2 or CALM3). Interacts with CD63; required for localization to lysosomes.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SIAH1Q8IUQ43EBI-10184345,EBI-747107

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114525. 3 interactions.
IntActiO43581. 1 interaction.
STRINGi9606.ENSP00000263846.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi138 – 1458Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi152 – 16110Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi173 – 1819Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi202 – 2065Combined sources
Helixi211 – 2144Combined sources
Beta strandi217 – 2259Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi233 – 2419Combined sources
Turni242 – 2443Combined sources
Beta strandi251 – 2555Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8KNMR-A132-259[»]
ProteinModelPortaliO43581.
SMRiO43581. Positions 101-403.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43581.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini137 – 239103C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini268 – 371104C2 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The C2 domains bind Ca2+ and membranes. Binding to membranes involves Ca2+-dependent phospholipid binding. Compared to other members of the family, the C2 domains of SYT7 dock and insert into cellular membranes in response to intracellular Ca2+ concentrations that are lower than those required for other synaptotagmins (PubMed:22966849). The two C2 domains bind independently to planar membranes, without interdomain cooperativity (PubMed:25437758). Moreover, SYT7 C2 domains insert more deeply into membranes compared to other synaptotagmins (PubMed:26322740, PubMed:26333120).4 Publications

Sequence similaritiesi

Belongs to the synaptotagmin family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiO43581.
KOiK19907.
PhylomeDBiO43581.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015427. Synaptotagmin7.
[Graphical view]
PANTHERiPTHR10024:SF230. PTHR10024:SF230. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43581-1) [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
MYRDPEAASP GAPSRDVLLV SAIITVSLSV TVVLCGLCHW CQRKLGKRYK
60 70 80 90 100
NSLETVGTPD SGRGRSEKKA IKLPAGGKAV NTAPVPGQTP HDESDRRTEP
110 120 130 140 150
RSSVSDLVNS LTSEMLMLSP GSEEDEAHEG CSRENLGRIQ FSVGYNFQES
160 170 180 190 200
TLTVKIMKAQ ELPAKDFSGT SDPFVKIYLL PDKKHKLETK VKRKNLNPHW
210 220 230 240 250
NETFLFEGFP YEKVVQRILY LQVLDYDRFS RNDPIGEVSI PLNKVDLTQM
260 270 280 290 300
QTFWKDLKPC SDGSGSRGEL LLSLCYNPSA NSIIVNIIKA RNLKAMDIGG
310 320 330 340 350
TSDPYVKVWL MYKDKRVEKK KTVTMKRNLN PIFNESFAFD IPTEKLRETT
360 370 380 390 400
IIITVMDKDK LSRNDVIGKI YLSWKSGPGE VKHWKDMIAR PRQPVAQWHQ

LKA
Note: Major isoform.1 Publication
Length:403
Mass (Da):45,501
Last modified:September 23, 2008 - v3
Checksum:iC9BFB26D298EDBE4
GO
Isoform 2 (identifier: O43581-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: I → INGTLLSGAK...HLAAGKLNLS

Note: No experimental confirmation available.
Show »
Length:478
Mass (Da):52,821
Checksum:i6F6B1DD2C9AFF15F
GO
Isoform 3 (identifier: O43581-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NDLDRDFWNN...QNQNAQGDKR

Show »
Length:686
Mass (Da):75,797
Checksum:i96C75AAD8D9CCBFB
GO
Isoform 4 (identifier: O43581-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NDLDRDFWNN...QNQNAQGDKR

Show »
Length:611
Mass (Da):68,478
Checksum:i68702B2463439DB6
GO
Isoform 5 (identifier: O43581-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: I → INDLDRDFWN...HLAAGKLNLS

Show »
Length:522
Mass (Da):58,019
Checksum:iDFA24AF0D17AD221
GO
Isoform 6 (identifier: O43581-6) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIbeta1 Publication

, Syt7betaCurated

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: I → INDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYAPYGDPRLSL

Show »
Length:447
Mass (Da):50,700
Checksum:i70A51A39F51AFB7F
GO

Sequence cautioni

The sequence AAB92667.1 differs from that shown. Reason: Frameshift at positions 6, 10 and 15. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541V → L in AAB92667 (PubMed:9615227).Curated
Sequence conflicti188 – 1881E → K in AAB92667 (PubMed:9615227).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti332 – 3321I → N.1 Publication
Corresponds to variant rs407740 [ dbSNP | Ensembl ].
VAR_052241

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 711I → INGTLLSGAKVAAAAGLAVE REGRLGEKPAPVPPPGEDAL RSGGAAPSEPGSGGKAGRGR WRTVQSHLAAGKLNLS in isoform 2. 1 PublicationVSP_045991
Alternative sequencei71 – 711I → INDLDRDFWNNNESTVQQKW SSYPPKEFILNISPYAPYGD PRLSLNGTLLSGAKVAAAAG LAVEREGRLGEKPAPVPPPG EDALRSGGAAPSEPGSGGKA GRGRWRTVQSHLAAGKLNLS in isoform 5. VSP_058231
Alternative sequencei71 – 711I → INDLDRDFWNNNESTVQQKW SSYPPKEFILNISPYAPYGD PRLSL in isoform 6. VSP_058232
Alternative sequencei72 – 721K → NDLDRDFWNNNESTVQQKWS SYPPKEFILNISPYAPYGDP RLSLNGTLLSGAKVAAAAGL AVEREGRLGEKPAPVPPPGE DALRSGGAAPSEPGSGGKAG RGRWRTVQSHLAAGKLNLSN FEDSTLSTATTLESIPSSTG EPKCQRPRTLMRQQSLQQPL SQHQRGRQPSQPTTSQSLGQ LQAHMASAPGPNPRAYGRGQ ARQGTSAGSKYRAAGGRSRS NPGSWDHVVGQIRNRGLDMK SFLEGRMVVLSLVLGLSEQD DFANIPDLQNPGTQQNQNAQ GDKR in isoform 3. VSP_058233
Alternative sequencei72 – 721K → NDLDRDFWNNNESTVQQKWS SYPPKEFILNISPYAPYGDP RLSLNFEDSTLSTATTLESI PSSTGEPKCQRPRTLMRQQS LQQPLSQHQRGRQPSQPTTS QSLGQLQAHMASAPGPNPRA YGRGQARQGTSAGSKYRAAG GRSRSNPGSWDHVVGQIRNR GLDMKSFLEGRMVVLSLVLG LSEQDDFANIPDLQNPGTQQ NQNAQGDKR in isoform 4. VSP_058234

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038535 mRNA. Translation: AAB92667.1. Frameshift.
AP002754 Genomic DNA. No translation available.
AP003108 Genomic DNA. No translation available.
AP003559 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73956.1.
BC125170 mRNA. Translation: AAI25171.1.
BC125171 mRNA. No translation available.
CCDSiCCDS31577.1. [O43581-1]
CCDS58139.1. [O43581-2]
RefSeqiNP_001238994.1. NM_001252065.1. [O43581-2]
NP_001287702.1. NM_001300773.1.
NP_004191.2. NM_004200.3. [O43581-1]
XP_005274440.1. XM_005274383.3.
XP_005274442.1. XM_005274385.3.
UniGeneiHs.131188.
Hs.684589.

Genome annotation databases

EnsembliENST00000263846; ENSP00000263846; ENSG00000011347. [O43581-1]
ENST00000535826; ENSP00000437720; ENSG00000011347. [O43581-5]
ENST00000539008; ENSP00000439694; ENSG00000011347. [O43581-3]
ENST00000540677; ENSP00000444201; ENSG00000011347. [O43581-2]
ENST00000542670; ENSP00000444019; ENSG00000011347. [O43581-4]
ENST00000542836; ENSP00000444568; ENSG00000011347. [O43581-6]
GeneIDi9066.
KEGGihsa:9066.
UCSCiuc001nrv.4. human. [O43581-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038535 mRNA. Translation: AAB92667.1. Frameshift.
AP002754 Genomic DNA. No translation available.
AP003108 Genomic DNA. No translation available.
AP003559 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73956.1.
BC125170 mRNA. Translation: AAI25171.1.
BC125171 mRNA. No translation available.
CCDSiCCDS31577.1. [O43581-1]
CCDS58139.1. [O43581-2]
RefSeqiNP_001238994.1. NM_001252065.1. [O43581-2]
NP_001287702.1. NM_001300773.1.
NP_004191.2. NM_004200.3. [O43581-1]
XP_005274440.1. XM_005274383.3.
XP_005274442.1. XM_005274385.3.
UniGeneiHs.131188.
Hs.684589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8KNMR-A132-259[»]
ProteinModelPortaliO43581.
SMRiO43581. Positions 101-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114525. 3 interactions.
IntActiO43581. 1 interaction.
STRINGi9606.ENSP00000263846.

PTM databases

iPTMnetiO43581.
PhosphoSiteiO43581.
SwissPalmiO43581.

Polymorphism and mutation databases

BioMutaiSYT7.

Proteomic databases

MaxQBiO43581.
PaxDbiO43581.
PRIDEiO43581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263846; ENSP00000263846; ENSG00000011347. [O43581-1]
ENST00000535826; ENSP00000437720; ENSG00000011347. [O43581-5]
ENST00000539008; ENSP00000439694; ENSG00000011347. [O43581-3]
ENST00000540677; ENSP00000444201; ENSG00000011347. [O43581-2]
ENST00000542670; ENSP00000444019; ENSG00000011347. [O43581-4]
ENST00000542836; ENSP00000444568; ENSG00000011347. [O43581-6]
GeneIDi9066.
KEGGihsa:9066.
UCSCiuc001nrv.4. human. [O43581-1]

Organism-specific databases

CTDi9066.
GeneCardsiSYT7.
H-InvDBHIX0009693.
HGNCiHGNC:11514. SYT7.
HPAiHPA012869.
MIMi604146. gene.
neXtProtiNX_O43581.
PharmGKBiPA36295.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiO43581.
KOiK19907.
PhylomeDBiO43581.
TreeFamiTF315600.

Miscellaneous databases

ChiTaRSiSYT7. human.
EvolutionaryTraceiO43581.
GeneWikiiSYT7.
GenomeRNAii9066.
NextBioi33971.
PROiO43581.
SOURCEiSearch...

Gene expression databases

BgeeiO43581.
CleanExiHS_SYT7.
ExpressionAtlasiO43581. baseline and differential.
GenevisibleiO43581. HS.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015427. Synaptotagmin7.
[Graphical view]
PANTHERiPTHR10024:SF230. PTHR10024:SF230. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transcript mapping of the human chromosome 11q12-q13.1 gene-rich region identifies several newly described conserved genes."
    Cooper P.R., Nowak N.J., Higgins M.J., Church D.M., Shows T.B.
    Genomics 49:419-429(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-332.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
  5. "The Exocytosis-regulatory protein synaptotagmin VII mediates cell invasion by Trypanosoma cruzi."
    Caler E.V., Chakrabarti S., Fowler K.T., Rao S., Andrews N.W.
    J. Exp. Med. 193:1097-1104(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and human."
    Fukuda M., Ogata Y., Saegusa C., Kanno E., Mikoshiba K.
    Biochem. J. 365:173-180(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. "Trypanosoma cruzi invades synaptotagmin VII-deficient cells by a PI-3 kinase independent pathway."
    Chakrabarti S., Andrade L.O., Andrews N.W.
    Mol. Biochem. Parasitol. 141:125-128(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: mechanistic contrast between isoforms 1 and 7."
    Brandt D.S., Coffman M.D., Falke J.J., Knight J.D.
    Biochemistry 51:7654-7664(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  9. "Lateral diffusion of proteins on supported lipid bilayers: additive friction of synaptotagmin 7 C2A-C2B tandem domains."
    Vasquez J.K., Chantranuvatana K., Giardina D.T., Coffman M.D., Knight J.D.
    Biochemistry 53:7904-7913(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  10. "Membrane docking of the synaptotagmin 7 C2A domain: electron paramagnetic resonance measurements show contributions from two membrane binding loops."
    Osterberg J.R., Chon N.L., Boo A., Maynard F.A., Lin H., Knight J.D.
    Biochemistry 54:5684-5695(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  11. "Membrane docking of the synaptotagmin 7 C2A Domain: computation reveals interplay between electrostatic and hydrophobic contributions."
    Chon N.L., Osterberg J.R., Henderson J., Khan H.M., Reuter N., Knight J.D., Lin H.
    Biochemistry 54:5696-5711(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  12. "Solution structure of the first C2 domain of synaptotagmin VII."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 132-259.

Entry informationi

Entry nameiSYT7_HUMAN
AccessioniPrimary (citable) accession number: O43581
Secondary accession number(s): F5GZC2
, F5GZU9, F5H126, F5H1N2, F5H6C1, Q08AH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: September 23, 2008
Last modified: May 11, 2016
This is version 146 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.