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Protein

Synaptotagmin-11

Gene

Syt11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may serve as Ca2+ sensors in the process of vesicular trafficking and exocytosis.By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi187 – 1871Calcium 1By similarity
Metal bindingi187 – 1871Calcium 2By similarity
Metal bindingi194 – 1941Calcium 1By similarity
Metal bindingi248 – 2481Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi249 – 2491Calcium 1By similarity
Metal bindingi249 – 2491Calcium 2By similarity
Metal bindingi249 – 2491Calcium 3By similarity
Metal bindingi252 – 2521Calcium 3By similarity
Metal bindingi255 – 2551Calcium 2By similarity
Metal bindingi255 – 2551Calcium 3By similarity

GO - Molecular functioni

  • beta-tubulin binding Source: ParkinsonsUK-UCL
  • clathrin binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: GO_Central
  • translation initiation factor binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • calcium ion-regulated exocytosis of neurotransmitter Source: GO_Central
  • calcium ion regulated lysosome exocytosis Source: ParkinsonsUK-UCL
  • negative regulation of interleukin-6 secretion Source: ParkinsonsUK-UCL
  • negative regulation of phagocytosis Source: ParkinsonsUK-UCL
  • negative regulation of tumor necrosis factor secretion Source: ParkinsonsUK-UCL
  • plasma membrane repair Source: ParkinsonsUK-UCL
  • positive regulation of protein localization to phagocytic vesicle Source: ParkinsonsUK-UCL
  • protein homotetramerization Source: ParkinsonsUK-UCL
  • regulation of defense response to bacterium Source: ParkinsonsUK-UCL
  • regulation of phagosome maturation Source: ParkinsonsUK-UCL
  • response to wounding Source: ParkinsonsUK-UCL
  • vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-11
Alternative name(s):
Synaptotagmin XI
Short name:
SytXI
Gene namesi
Name:Syt11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1859547. Syt11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515VesicularSequence analysisAdd
BLAST
Transmembranei16 – 3621HelicalSequence analysisAdd
BLAST
Topological domaini37 – 430394CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: ParkinsonsUK-UCL
  • early phagosome Source: ParkinsonsUK-UCL
  • integral component of plasma membrane Source: MGI
  • lysosome Source: ParkinsonsUK-UCL
  • phagocytic cup Source: ParkinsonsUK-UCL
  • recycling endosome Source: ParkinsonsUK-UCL
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Synaptotagmin-11PRO_0000183970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei133 – 1331PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated and targeted to the proteasome complex for degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9R0N3.
PaxDbiQ9R0N3.
PRIDEiQ9R0N3.

PTM databases

iPTMnetiQ9R0N3.
PhosphoSiteiQ9R0N3.
SwissPalmiQ9R0N3.

Expressioni

Gene expression databases

BgeeiQ9R0N3.
CleanExiMM_SYT11.
ExpressionAtlasiQ9R0N3. baseline and differential.
GenevisibleiQ9R0N3. MM.

Interactioni

Subunit structurei

Homodimer. Can also form heterodimers. Interacts with PARK2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Vti1aQ9JI512EBI-647443,EBI-7573650From a different organism.

GO - Molecular functioni

  • beta-tubulin binding Source: ParkinsonsUK-UCL
  • clathrin binding Source: GO_Central
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: GO_Central
  • translation initiation factor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

IntActiQ9R0N3. 22 interactions.
MINTiMINT-4136545.
STRINGi10090.ENSMUSP00000088464.

Structurei

3D structure databases

ProteinModelPortaliQ9R0N3.
SMRiQ9R0N3. Positions 157-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini173 – 26189C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini303 – 39694C2 2PROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ9R0N3.
KOiK19911.
OMAiIKVDYGD.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028699. SYT11.
[Graphical view]
PANTHERiPTHR10024:SF115. PTHR10024:SF115. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R0N3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEITNIRPS FDVSPVAAGL IGASVLVVCV SVTVFVWTCC HQQAEKKHKT
60 70 80 90 100
PPYKFIHMLK GISIYPETLS NKKKIIKVRR DKDGPRRESG RGNLLINAES
110 120 130 140 150
GLLSHDKDPR GPSPASCMDQ LPIKRDYGEE LRSPMTSLTP GESKATSPSS
160 170 180 190 200
PEEDVMLGSL TFSVDYNFPK KALVVTIQEA HGLPVMDDQT QGSDPYIKMT
210 220 230 240 250
ILPDKRHRVK TRVLRKTLDP VFDETFTFYG IPYSQLQDLV LHFLVLSFDR
260 270 280 290 300
FSRDDVIGEV MVPLAGVDPS TGKVQLTRDI IKRNIQKCIS RGELQVSLSY
310 320 330 340 350
QPVAQRMTVV VLKARHLPKM DITGLSGNPY VKVNVYYGRK RIAKKKTHVK
360 370 380 390 400
KCTLNPVFNE SFIYDIPTDL LPDISIEFLV IDFDRTTKNE VVGRLILGAH
410 420 430
SVTTSGAEHW REVCESPRKP IAKWHSLSEY
Length:430
Mass (Da):48,333
Last modified:July 27, 2011 - v2
Checksum:i4E989259BE4FB423
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451A → P in BAA85780 (PubMed:10531343).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026808 mRNA. Translation: BAA85780.1.
AK144169 mRNA. Translation: BAE25745.1.
BC054526 mRNA. Translation: AAH54526.1.
CCDSiCCDS38484.1.
RefSeqiNP_061274.2. NM_018804.3.
XP_006501411.1. XM_006501348.1.
XP_006501412.1. XM_006501349.1.
UniGeneiMm.379376.

Genome annotation databases

EnsembliENSMUST00000090945; ENSMUSP00000088464; ENSMUSG00000068923.
ENSMUST00000107505; ENSMUSP00000103129; ENSMUSG00000068923.
GeneIDi229521.
KEGGimmu:229521.
UCSCiuc008pwk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026808 mRNA. Translation: BAA85780.1.
AK144169 mRNA. Translation: BAE25745.1.
BC054526 mRNA. Translation: AAH54526.1.
CCDSiCCDS38484.1.
RefSeqiNP_061274.2. NM_018804.3.
XP_006501411.1. XM_006501348.1.
XP_006501412.1. XM_006501349.1.
UniGeneiMm.379376.

3D structure databases

ProteinModelPortaliQ9R0N3.
SMRiQ9R0N3. Positions 157-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0N3. 22 interactions.
MINTiMINT-4136545.
STRINGi10090.ENSMUSP00000088464.

PTM databases

iPTMnetiQ9R0N3.
PhosphoSiteiQ9R0N3.
SwissPalmiQ9R0N3.

Proteomic databases

MaxQBiQ9R0N3.
PaxDbiQ9R0N3.
PRIDEiQ9R0N3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090945; ENSMUSP00000088464; ENSMUSG00000068923.
ENSMUST00000107505; ENSMUSP00000103129; ENSMUSG00000068923.
GeneIDi229521.
KEGGimmu:229521.
UCSCiuc008pwk.1. mouse.

Organism-specific databases

CTDi23208.
MGIiMGI:1859547. Syt11.

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiQ9R0N3.
KOiK19911.
OMAiIKVDYGD.
TreeFamiTF315600.

Miscellaneous databases

ChiTaRSiSyt11. mouse.
PROiQ9R0N3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0N3.
CleanExiMM_SYT11.
ExpressionAtlasiQ9R0N3. baseline and differential.
GenevisibleiQ9R0N3. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028699. SYT11.
[Graphical view]
PANTHERiPTHR10024:SF115. PTHR10024:SF115. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X."
    Fukuda M., Kanno E., Mikoshiba K.
    J. Biol. Chem. 274:31421-31427(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Cerebellum.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiSYT11_MOUSE
AccessioniPrimary (citable) accession number: Q9R0N3
Secondary accession number(s): Q7TQG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.