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Q9R0N3

- SYT11_MOUSE

UniProt

Q9R0N3 - SYT11_MOUSE

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Protein

Synaptotagmin-11

Gene
Syt11
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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

Binds 3 calcium ions per subunit. The ions are bound to the C2 domains By similarity.

Sites

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. transporter activity Source: InterPro
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
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1859547. Syt11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515Vesicular Reviewed predictionAdd
BLAST
Transmembranei16 – 3621Helical; Reviewed predictionAdd
BLAST
Topological domaini37 – 430394Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. integral component of plasma membrane Source: MGI
  3. 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

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9R0N3.
PRIDEiQ9R0N3.

PTM databases

PhosphoSiteiQ9R0N3.

Expressioni

Gene expression databases

ArrayExpressiQ9R0N3.
BgeeiQ9R0N3.
CleanExiMM_SYT11.
GenevestigatoriQ9R0N3.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

IntActiQ9R0N3. 22 interactions.
MINTiMINT-4136545.

Structurei

3D structure databases

ProteinModelPortaliQ9R0N3.
SMRiQ9R0N3. Positions 157-429.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini173 – 26189C2 1Add
BLAST
Domaini303 – 39694C2 2Add
BLAST

Sequence similaritiesi

Belongs to the synaptotagmin family.
Contains 2 C2 domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292488.
GeneTreeiENSGT00750000117274.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiQ7TQG8.
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

MAEITNIRPS FDVSPVAAGL IGASVLVVCV SVTVFVWTCC HQQAEKKHKT    50
PPYKFIHMLK GISIYPETLS NKKKIIKVRR DKDGPRRESG RGNLLINAES 100
GLLSHDKDPR GPSPASCMDQ LPIKRDYGEE LRSPMTSLTP GESKATSPSS 150
PEEDVMLGSL TFSVDYNFPK KALVVTIQEA HGLPVMDDQT QGSDPYIKMT 200
ILPDKRHRVK TRVLRKTLDP VFDETFTFYG IPYSQLQDLV LHFLVLSFDR 250
FSRDDVIGEV MVPLAGVDPS TGKVQLTRDI IKRNIQKCIS RGELQVSLSY 300
QPVAQRMTVV VLKARHLPKM DITGLSGNPY VKVNVYYGRK RIAKKKTHVK 350
KCTLNPVFNE SFIYDIPTDL LPDISIEFLV IDFDRTTKNE VVGRLILGAH 400
SVTTSGAEHW REVCESPRKP IAKWHSLSEY 430
Length:430
Mass (Da):48,333
Last modified:July 27, 2011 - v2
Checksum:i4E989259BE4FB423
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451A → P in BAA85780. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB026808 mRNA. Translation: BAA85780.1 .
AK144169 mRNA. Translation: BAE25745.1 .
BC054526 mRNA. Translation: AAH54526.1 .
CCDSi CCDS38484.1.
RefSeqi NP_061274.2. NM_018804.3.
XP_006501411.1. XM_006501348.1.
XP_006501412.1. XM_006501349.1.
UniGenei Mm.379376.

3D structure databases

ProteinModelPortali Q9R0N3.
SMRi Q9R0N3. Positions 157-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9R0N3. 22 interactions.
MINTi MINT-4136545.

PTM databases

PhosphoSitei Q9R0N3.

Proteomic databases

PaxDbi Q9R0N3.
PRIDEi Q9R0N3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000090945 ; ENSMUSP00000088464 ; ENSMUSG00000068923 .
ENSMUST00000107505 ; ENSMUSP00000103129 ; ENSMUSG00000068923 .
GeneIDi 229521.
KEGGi mmu:229521.
UCSCi uc008pwk.1. mouse.

Organism-specific databases

CTDi 23208.
MGIi MGI:1859547. Syt11.

Phylogenomic databases

eggNOGi NOG292488.
GeneTreei ENSGT00750000117274.
HOGENOMi HOG000232126.
HOVERGENi HBG005010.
InParanoidi Q7TQG8.
OMAi IKVDYGD.
TreeFami TF315600.

Miscellaneous databases

ChiTaRSi SYT11. mouse.
NextBioi 379479.
PROi Q9R0N3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R0N3.
Bgeei Q9R0N3.
CleanExi MM_SYT11.
Genevestigatori Q9R0N3.

Family and domain databases

Gene3Di 2.60.40.150. 2 hits.
InterProi IPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028699. SYT11.
[Graphical view ]
PANTHERi PTHR10024:SF115. PTHR10024:SF115. 1 hit.
Pfami PF00168. C2. 2 hits.
[Graphical view ]
PRINTSi PR00399. SYNAPTOTAGMN.
SMARTi SM00239. C2. 2 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 2 hits.
PROSITEi PS50004. C2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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/6.
    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: September 3, 2014
This is version 119 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

External Data

Dasty 3

Similar proteinsi