Q9BT88 (SYT11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Synaptotagmin-11

Alternative name(s):
Synaptotagmin XI
Short name=SytXI

Gene names

Name:	SYT11
Synonyms:	KIAA0080

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Cofactor	Binds 3 calcium ions per subunit. The ions are bound to the C2 domains By similarity.
Subunit structure	Homodimer. Can also form heterodimers By similarity. Interacts with PARK2. Ref.7
Subcellular location	Membrane; Single-pass membrane protein. Cell junction › synapse By similarity. Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane; Single-pass membrane protein By similarity. Note: In substantia nigra, observed in neuronal cell bodies and neurites. Found in the core of the Lewy bodies in the brain of sporadic Parkinson disease patients. Ref.7
Post-translational modification	Ubiquitinated and targeted to the proteasome complex for degradation. Ref.7
Sequence similarities	Belongs to the synaptotagmin family. Contains 2 C2 domains.
Sequence caution	The sequence BAA07527.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasmic vesicle Membrane Synapse
Coding sequence diversity	Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Inferred from electronic annotation. Source: Compara synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APPBP2	Q92624	3	EBI-751770,EBI-743771
ATP13A2	Q9NQ11	2	EBI-751770,EBI-6308763

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Synaptotagmin-11		PRO_0000183969
Regions
	Topological domain	1 – 15	15	Vesicular Potential
	Transmembrane	16 – 36	21	Helical; Potential
	Topological domain	37 – 431	395	Cytoplasmic Potential
	Domain	174 – 262	89	C2 1
	Domain	304 – 397	94	C2 2
Sites
	Metal binding	188	1	Calcium 1 By similarity
	Metal binding	188	1	Calcium 2 By similarity
	Metal binding	195	1	Calcium 1 By similarity
	Metal binding	249	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	250	1	Calcium 1 By similarity
	Metal binding	250	1	Calcium 2 By similarity
	Metal binding	250	1	Calcium 3 By similarity
	Metal binding	253	1	Calcium 3 By similarity
	Metal binding	256	1	Calcium 2 By similarity
	Metal binding	256	1	Calcium 3 By similarity
Natural variations
	Natural variant	48	1	Q → H. Ref.1 Ref.3 Ref.4 Ref.6 Corresponds to variant rs822522 [ dbSNP | Ensembl ].		VAR_047656
	Natural variant	231	1	G → V. Ref.6 Corresponds to variant rs17853892 [ dbSNP | Ensembl ].		VAR_047657
Experimental info
	Sequence conflict	50	1	N → S in BAB55186. Ref.3
	Sequence conflict	268	1	V → A in BAB55186. Ref.3
	Sequence conflict	359	1	F → L in CAH18653. Ref.4
	Sequence conflict	370	1	D → G in CAH18653. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9BT88 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 5C8667D2C23D758E	FASTA	431	48,297
	10 20 30 40 50 60 MAEITNIRPS FDVSPVVAGL IGASVLVVCV SVTVFVWSCC HQQAEKKQKN PPYKFIHMLK 70 80 90 100 110 120 GISIYPETLS NKKKIIKVRR DKDGPGREGG RRNLLVDAAE AGLLSRDKDP RGPSSGSCID 130 140 150 160 170 180 QLPIKMDYGE ELRSPITSLT PGESKTTSPS SPEEDVMLGS LTFSVDYNFP KKALVVTIQE 190 200 210 220 230 240 AHGLPVMDDQ TQGSDPYIKM TILPDKRHRV KTRVLRKTLD PVFDETFTFY GIPYSQLQDL 250 260 270 280 290 300 VLHFLVLSFD RFSRDDVIGE VMVPLAGVDP STGKVQLTRD IIKRNIQKCI SRGELQVSLS 310 320 330 340 350 360 YQPVAQRMTV VVLKARHLPK MDITGLSGNP YVKVNVYYGR KRIAKKKTHV KKCTLNPIFN 370 380 390 400 410 420 ESFIYDIPTD LLPDISIEFL VIDFDRTTKN EVVGRLILGA HSVTASGAEH WREVCESPRK 430 PVAKWHSLSE Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-48. Tissue: Bone marrow.
[2]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-48.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-48. Tissue: Amygdala.
[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]	"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], VARIANTS HIS-48 AND VAL-231. Tissue: Brain and Lymph.
[7]	"The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI." Huynh D.P., Scoles D.R., Nguyen D., Pulst S.M. Hum. Mol. Genet. 12:2587-2597(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARK2, UBIQUITINATION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D38522 mRNA. Translation: BAA07527.2. Different initiation. AK027540 mRNA. Translation: BAB55186.1. AK074931 mRNA. Translation: BAC11300.1. CR749792 mRNA. Translation: CAH18653.1. AL139128 Genomic DNA. Translation: CAH69948.1. BC004291 mRNA. Translation: AAH04291.1. BC013690 mRNA. Translation: AAH13690.1. BC039205 mRNA. Translation: AAH39205.1.
IPI	IPI00027875.
RefSeq	NP_689493.3. NM_152280.4.
UniGene	Hs.32984.
3D structure databases
ProteinModelPortal	Q9BT88.
SMR	Q9BT88. Positions 158-430.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BT88. 2 interactions.
MINT	MINT-240234.
STRING	9606.ENSP00000357307.
PTM databases
PhosphoSite	Q9BT88.
Polymorphism databases
DMDM	215273917.
Proteomic databases
PaxDb	Q9BT88.
PRIDE	Q9BT88.
Protocols and materials databases
DNASU	23208.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368324; ENSP00000357307; ENSG00000132718.
GeneID	23208.
KEGG	hsa:23208.
UCSC	uc001fmg.3. human.
Organism-specific databases
CTD	23208.
GeneCards	GC01P155829.
H-InvDB	HIX0001138.
HGNC	HGNC:19239. SYT11.
MIM	608741. gene.
neXtProt	NX_Q9BT88.
PharmGKB	PA134898675.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG292488.
HOGENOM	HOG000232126.
HOVERGEN	HBG005010.
InParanoid	Q9BT88.
OMA	IKVDYGD.
OrthoDB	EOG4894MK.
PhylomeDB	Q9BT88.
Gene expression databases
ArrayExpress	Q9BT88.
Bgee	Q9BT88.
CleanEx	HS_SYT11.
Genevestigator	Q9BT88.
GermOnline	ENSG00000132718. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR001565. Synaptotagmin. [Graphical view]
Pfam	PF00168. C2. 2 hits. [Graphical view]
PRINTS	PR00399. SYNAPTOTAGMN.
SMART	SM00239. C2. 2 hits. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 2 hits.
PROSITE	PS50004. C2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SYT11. human.
GenomeRNAi	23208.
NextBio	44743.
SOURCE	Search...

Entry information

Entry name

SYT11_HUMAN

Accession

Primary (citable) accession number: Q9BT88
Secondary accession number(s): Q14998 , Q5W0D4, Q68CT5, Q8IXU3, Q96SU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.