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Q8N9I0 (SYT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-2
Alternative name(s):
Synaptotagmin II
Short name=SytII
Gene names
Name:SYT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone By similarity.

Cofactor

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

Subunit structure

Homotetramer Probable. Interacts with stonin 2 By similarity. Interacts with SCAMP5. Ref.3

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass membrane protein By similarity. Cytoplasmic vesiclesecretory vesiclechromaffin granule membrane; Single-pass membrane protein By similarity. Note: Synaptic vesicles and chromaffin granules By similarity.

Domain

The first C2 domain mediates Ca2+-dependent phospholipid binding By similarity.

The second C2 domain mediates interaction with Stonin 2 By similarity.

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Synaptotagmin-2
PRO_0000183942

Regions

Topological domain1 – 6262Vesicular Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 419336Cytoplasmic Potential
Domain141 – 242102C2 1
Domain272 – 375104C2 2
Region133 – 379247Phospholipid binding By similarity

Sites

Metal binding1691Calcium 2; via carbonyl oxygen By similarity
Metal binding1701Calcium 1 By similarity
Metal binding1701Calcium 2 By similarity
Metal binding1761Calcium 1 By similarity
Metal binding2281Calcium 1 By similarity
Metal binding2281Calcium 2 By similarity
Metal binding2291Calcium 1; via carbonyl oxygen By similarity
Metal binding2301Calcium 1 By similarity
Metal binding2301Calcium 2 By similarity
Metal binding2301Calcium 3 By similarity
Metal binding2331Calcium 3 By similarity
Metal binding2341Calcium 3; via carbonyl oxygen By similarity
Metal binding2361Calcium 2 By similarity
Metal binding2361Calcium 3 By similarity

Amino acid modifications

Modified residue2271Phosphotyrosine By similarity
Glycosylation291N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3101V → G in BAC04354. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8N9I0 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: BE3855E9CDE2D76E

FASTA41946,872
        10         20         30         40         50         60 
MRNIFKRNQE PIVAPATTTA TMPIGPVDNS TESGGAGESQ EDMFAKLKEK LFNEINKIPL 

        70         80         90        100        110        120 
PPWALIAIAV VAGLLLLTCC FCICKKCCCK KKKNKKEKGK GMKNAMNMKD MKGGQDDDDA 

       130        140        150        160        170        180 
ETGLTEGEGE GEEEKEPENL GKLQFSLDYD FQANQLTVGV LQAAELPALD MGGTSDPYVK 

       190        200        210        220        230        240 
VFLLPDKKKK YETKVHRKTL NPAFNETFTF KVPYQELGGK TLVMAIYDFD RFSKHDIIGE 

       250        260        270        280        290        300 
VKVPMNTVDL GQPIEEWRDL QGGEKEEPEK LGDICTSLRY VPTAGKLTVC ILEAKNLKKM 

       310        320        330        340        350        360 
DVGGLSDPYV KIHLMQNGKR LKKKKTTVKK KTLNPYFNES FSFEIPFEQI QKVQVVVTVL 

       370        380        390        400        410 
DYDKLGKNEA IGKIFVGSNA TGTELRHWSD MLANPRRPIA QWHSLKPEEE VDALLGKNK 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Tissue: Cerebellum.
[2]"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].
[3]"Human SCAMP5, a novel secretory carrier membrane protein, facilitates calcium-triggered cytokine secretion by interaction with SNARE machinery."
Han C., Chen T., Yang M., Li N., Liu H., Cao X.
J. Immunol. 182:2986-2996(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCAMP5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK090672 mRNA. Translation: BAC03500.1.
AK094430 mRNA. Translation: BAC04354.1.
BC100814 mRNA. Translation: AAI00815.1.
BC100815 mRNA. Translation: AAI00816.1.
BC100817 mRNA. Translation: AAI00818.1.
CCDSCCDS1427.1.
RefSeqNP_001129976.1. NM_001136504.1.
NP_796376.2. NM_177402.4.
UniGeneHs.25422.

3D structure databases

ProteinModelPortalQ8N9I0.
SMRQ8N9I0. Positions 138-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126085. 4 interactions.
IntActQ8N9I0. 4 interactions.
MINTMINT-2810903.
STRING9606.ENSP00000356236.

Chemistry

DrugBankDB00042. Botulinum Toxin Type B.

PTM databases

PhosphoSiteQ8N9I0.

Polymorphism databases

DMDM116242811.

Proteomic databases

PaxDbQ8N9I0.
PRIDEQ8N9I0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367267; ENSP00000356236; ENSG00000143858.
ENST00000367268; ENSP00000356237; ENSG00000143858.
GeneID127833.
KEGGhsa:127833.
UCSCuc001gye.3. human.

Organism-specific databases

CTD127833.
GeneCardsGC01M202559.
HGNCHGNC:11510. SYT2.
HPAHPA030372.
MIM600104. gene.
neXtProtNX_Q8N9I0.
PharmGKBPA36291.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5038.
HOGENOMHOG000232127.
HOVERGENHBG005010.
InParanoidQ8N9I0.
OMACCIRRCC.
OrthoDBEOG78PV8W.
PhylomeDBQ8N9I0.
TreeFamTF315600.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

BgeeQ8N9I0.
CleanExHS_SYT2.
GenevestigatorQ8N9I0.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR001565. Synaptotagmin.
[Graphical view]
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYT2. human.
GeneWikiSYT2.
GenomeRNAi127833.
NextBio82195.
PROQ8N9I0.
SOURCESearch...

Entry information

Entry nameSYT2_HUMAN
AccessionPrimary (citable) accession number: Q8N9I0
Secondary accession number(s): Q496K5, Q8NBE5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM