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Protein

Synaptotagmin-1

Gene

SYT1

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

Functioni

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. A Ca2+-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca2+-independent manner; these are neurexins, syntaxin and AP2.

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 bindingi172 – 1721Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi173 – 1731Calcium 1By similarity
Metal bindingi173 – 1731Calcium 2By similarity
Metal bindingi179 – 1791Calcium 1By similarity
Metal bindingi231 – 2311Calcium 1By similarity
Metal bindingi231 – 2311Calcium 2By similarity
Metal bindingi232 – 2321Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi233 – 2331Calcium 1By similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi233 – 2331Calcium 3By similarity
Metal bindingi236 – 2361Calcium 3By similarity
Metal bindingi237 – 2371Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi239 – 2391Calcium 2By similarity
Metal bindingi239 – 2391Calcium 3By similarity

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: UniProtKB
  • calcium-dependent phospholipid binding Source: ParkinsonsUK-UCL
  • calcium ion binding Source: GO_Central
  • clathrin binding Source: GO_Central
  • low-density lipoprotein particle receptor binding Source: MGI
  • phosphatidylinositol-4,5-bisphosphate binding Source: GO_Central
  • phosphatidylserine binding Source: Ensembl
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin-1 binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_264271. Toxicity of botulinum toxin type G (BoNT/G).
REACT_264609. Toxicity of botulinum toxin type B (BoNT/B).

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name:
SytI
p65
Gene namesi
Name:SYT1
Synonyms:SVP65, SYT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:11509. SYT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757VesicularSequence AnalysisAdd
BLAST
Transmembranei58 – 8023HelicalSequence AnalysisAdd
BLAST
Topological domaini81 – 422342CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

A SYT1 rare mutation has been found in a child with a severe neuro-developmental disorder. The individual harboring this variant shows early onset dyskinetic movement disorder, severe motor delay and profound cognitive impairment, suggesting that SYT1 may play a role in the pathogenesis of this neuro-developmental disorder.

Keywords - Diseasei

Disease mutation

Organism-specific databases

PharmGKBiPA36290.

Polymorphism and mutation databases

BioMutaiSYT1.
DMDMi135086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Synaptotagmin-1PRO_0000183936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Lipidationi75 – 751S-palmitoyl cysteineBy similarity
Lipidationi76 – 761S-palmitoyl cysteineBy similarity
Lipidationi78 – 781S-palmitoyl cysteineBy similarity
Lipidationi80 – 801S-palmitoyl cysteineBy similarity
Lipidationi83 – 831S-palmitoyl cysteineBy similarity
Modified residuei129 – 1291Phosphothreonine1 Publication
Modified residuei230 – 2301PhosphotyrosineBy similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP21579.
PRIDEiP21579.

PTM databases

PhosphoSiteiP21579.

Miscellaneous databases

PMAP-CutDBP21579.

Expressioni

Gene expression databases

BgeeiP21579.
CleanExiHS_SYT1.
ExpressionAtlasiP21579. baseline and differential.
GenevestigatoriP21579.

Organism-specific databases

HPAiHPA008394.
HPA064788.

Interactioni

Subunit structurei

Homotetramer (Probable). Interacts with SCAMP5, STON2, SV2A, SV2B, SV2C and RIMS1. Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity).By similarityCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
CACNB4O00305-22EBI-524909,EBI-714855
IKBKGQ9Y6K93EBI-524909,EBI-81279

Protein-protein interaction databases

BioGridi112723. 37 interactions.
DIPiDIP-34042N.
IntActiP21579. 16 interactions.
MINTiMINT-1400342.
STRINGi9606.ENSP00000261205.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 4711Combined sources
Beta strandi145 – 1539Combined sources
Turni154 – 1574Combined sources
Beta strandi158 – 16710Combined sources
Helixi173 – 1753Combined sources
Beta strandi180 – 1889Combined sources
Beta strandi206 – 2138Combined sources
Helixi217 – 2204Combined sources
Beta strandi224 – 2318Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi239 – 2479Combined sources
Helixi248 – 2503Combined sources
Beta strandi257 – 2626Combined sources
Beta strandi276 – 2849Combined sources
Turni285 – 2884Combined sources
Beta strandi289 – 29911Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi322 – 3287Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi339 – 3479Combined sources
Helixi350 – 3523Combined sources
Turni353 – 3553Combined sources
Beta strandi357 – 3648Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi373 – 3808Combined sources
Helixi385 – 39612Combined sources
Beta strandi402 – 4076Combined sources
Helixi411 – 4177Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K45NMR-A141-268[»]
2K4ANMR-A141-268[»]
2K8MNMR-A/D141-268[»]
2KI6NMR-A/F141-268[»]
2LHANMR-A272-422[»]
2R83X-ray2.70A/B141-422[»]
3F00X-ray1.36A141-266[»]
3F01X-ray1.70A141-266[»]
3F04X-ray1.35A141-266[»]
3F05X-ray1.40A141-266[»]
4ISQX-ray2.65D/E/F33-53[»]
4V11X-ray1.95A273-422[»]
ProteinModelPortaliP21579.
SMRiP21579. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21579.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 24589C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini287 – 37892C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 382247Phospholipid bindingCuratedAdd
BLAST

Domaini

The first C2 domain mediates Ca2+-dependent phospholipid binding.
The second C2 domain mediates interaction with SV2A and STN2.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292488.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP21579.
KOiK15290.
OMAiHDIIGEY.
PhylomeDBiP21579.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF183. PTHR10024:SF183. 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]

Sequencei

Sequence statusi: Complete.

P21579-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSESHHEAL AAPPVTTVAT VLPSNATEPA SPGEGKEDAF SKLKEKFMNE
60 70 80 90 100
LHKIPLPPWA LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN
110 120 130 140 150
AINMKDVKDL GKTMKDQALK DDDAETGLTD GEEKEEPKEE EKLGKLQYSL
160 170 180 190 200
DYDFQNNQLL VGIIQAAELP ALDMGGTSDP YVKVFLLPDK KKKFETKVHR
210 220 230 240 250
KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI IGEFKVPMNT
260 270 280 290 300
VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL
310 320 330 340 350
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF
360 370 380 390 400
EQIQKVQVVV TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR
410 420
PIAQWHTLQV EEEVDAMLAV KK
Length:422
Mass (Da):47,573
Last modified:May 1, 1991 - v1
Checksum:i467F7C58E411AFA9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti368 – 3681I → T Probable disease-associated mutation found in a patient with an early onset dyskinetic movement disorder, severe motor delay and profound cognitive impairment. 1 Publication
VAR_072911

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55047 mRNA. Translation: AAA60609.1.
AK094616 mRNA. Translation: BAG52897.1.
AK126908 mRNA. Translation: BAG54392.1.
CR627387 mRNA. Translation: CAH10483.1.
CH471054 Genomic DNA. Translation: EAW97343.1.
BC058917 mRNA. Translation: AAH58917.1.
CCDSiCCDS9017.1.
PIRiA39052. BMHU1Y.
RefSeqiNP_001129277.1. NM_001135805.1.
NP_001129278.1. NM_001135806.1.
NP_005630.1. NM_005639.2.
UniGeneiHs.310545.

Genome annotation databases

EnsembliENST00000261205; ENSP00000261205; ENSG00000067715.
ENST00000393240; ENSP00000376932; ENSG00000067715.
ENST00000552744; ENSP00000447575; ENSG00000067715.
GeneIDi6857.
KEGGihsa:6857.
UCSCiuc001sys.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55047 mRNA. Translation: AAA60609.1.
AK094616 mRNA. Translation: BAG52897.1.
AK126908 mRNA. Translation: BAG54392.1.
CR627387 mRNA. Translation: CAH10483.1.
CH471054 Genomic DNA. Translation: EAW97343.1.
BC058917 mRNA. Translation: AAH58917.1.
CCDSiCCDS9017.1.
PIRiA39052. BMHU1Y.
RefSeqiNP_001129277.1. NM_001135805.1.
NP_001129278.1. NM_001135806.1.
NP_005630.1. NM_005639.2.
UniGeneiHs.310545.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K45NMR-A141-268[»]
2K4ANMR-A141-268[»]
2K8MNMR-A/D141-268[»]
2KI6NMR-A/F141-268[»]
2LHANMR-A272-422[»]
2R83X-ray2.70A/B141-422[»]
3F00X-ray1.36A141-266[»]
3F01X-ray1.70A141-266[»]
3F04X-ray1.35A141-266[»]
3F05X-ray1.40A141-266[»]
4ISQX-ray2.65D/E/F33-53[»]
4V11X-ray1.95A273-422[»]
ProteinModelPortaliP21579.
SMRiP21579. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112723. 37 interactions.
DIPiDIP-34042N.
IntActiP21579. 16 interactions.
MINTiMINT-1400342.
STRINGi9606.ENSP00000261205.

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteiP21579.

Polymorphism and mutation databases

BioMutaiSYT1.
DMDMi135086.

Proteomic databases

PaxDbiP21579.
PRIDEiP21579.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261205; ENSP00000261205; ENSG00000067715.
ENST00000393240; ENSP00000376932; ENSG00000067715.
ENST00000552744; ENSP00000447575; ENSG00000067715.
GeneIDi6857.
KEGGihsa:6857.
UCSCiuc001sys.3. human.

Organism-specific databases

CTDi6857.
GeneCardsiGC12P079232.
HGNCiHGNC:11509. SYT1.
HPAiHPA008394.
HPA064788.
MIMi185605. gene.
neXtProtiNX_P21579.
PharmGKBiPA36290.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292488.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP21579.
KOiK15290.
OMAiHDIIGEY.
PhylomeDBiP21579.
TreeFamiTF315600.

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_264271. Toxicity of botulinum toxin type G (BoNT/G).
REACT_264609. Toxicity of botulinum toxin type B (BoNT/B).

Miscellaneous databases

ChiTaRSiSYT1. human.
EvolutionaryTraceiP21579.
GeneWikiiSYT1.
GenomeRNAii6857.
NextBioi26767.
PMAP-CutDBP21579.
PROiP21579.
SOURCEiSearch...

Gene expression databases

BgeeiP21579.
CleanExiHS_SYT1.
ExpressionAtlasiP21579. baseline and differential.
GenevestigatoriP21579.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF183. PTHR10024:SF183. 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. "Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans."
    Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., Suedhof T.C.
    J. Biol. Chem. 266:615-622(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Amygdala and Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: PNS.
  6. "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.
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: VARIANT THR-368, POSSIBLE INVOLVEMENT IN NEURO-DEVELOPMENTAL DISORDER.

Entry informationi

Entry nameiSYT1_HUMAN
AccessioniPrimary (citable) accession number: P21579
Secondary accession number(s): Q6AI31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 27, 2015
This is version 164 of the entry and version 1 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 12
    Human chromosome 12: 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

External Data

Dasty 3

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 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.