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Protein

Vesicle-associated membrane protein 2

Gene

VAMP2

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

Functioni

Involved in the targeting and/or fusion of transport vesicles to their target membrane.

GO - Molecular functioni

  1. calcium-dependent protein binding Source: ParkinsonsUK-UCL
  2. calmodulin binding Source: ParkinsonsUK-UCL
  3. phospholipid binding Source: ParkinsonsUK-UCL
  4. protein self-association Source: ParkinsonsUK-UCL
  5. SNAP receptor activity Source: GO_Central
  6. SNARE binding Source: ParkinsonsUK-UCL
  7. syntaxin-1 binding Source: ParkinsonsUK-UCL
  8. syntaxin binding Source: UniProtKB

GO - Biological processi

  1. calcium ion-dependent exocytosis Source: ParkinsonsUK-UCL
  2. cellular protein metabolic process Source: Reactome
  3. cellular response to insulin stimulus Source: ParkinsonsUK-UCL
  4. energy reserve metabolic process Source: Reactome
  5. eosinophil degranulation Source: UniProtKB
  6. exocytosis Source: ParkinsonsUK-UCL
  7. glutamate secretion Source: Reactome
  8. Golgi to plasma membrane protein transport Source: ParkinsonsUK-UCL
  9. long-term synaptic potentiation Source: ParkinsonsUK-UCL
  10. membrane fusion Source: ParkinsonsUK-UCL
  11. membrane organization Source: Reactome
  12. neurotransmitter secretion Source: Reactome
  13. pathogenesis Source: Reactome
  14. positive regulation of intracellular protein transport Source: ParkinsonsUK-UCL
  15. post-Golgi vesicle-mediated transport Source: Reactome
  16. protein complex assembly Source: ParkinsonsUK-UCL
  17. protein transport Source: ParkinsonsUK-UCL
  18. regulation of exocytosis Source: ParkinsonsUK-UCL
  19. regulation of insulin secretion Source: Reactome
  20. regulation of vesicle-mediated transport Source: ParkinsonsUK-UCL
  21. response to glucose Source: ParkinsonsUK-UCL
  22. small molecule metabolic process Source: Reactome
  23. synaptic transmission Source: Reactome
  24. synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  25. vesicle fusion Source: GO_Central
  26. vesicle-mediated transport Source: ParkinsonsUK-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
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_15550. Insulin processing.
REACT_18325. Regulation of insulin secretion.
REACT_19187. Clathrin derived vesicle budding.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_263857. Toxicity of botulinum toxin type F (BoNT/F).
REACT_263924. Toxicity of botulinum toxin type D (BoNT/D).
REACT_264271. Toxicity of botulinum toxin type G (BoNT/G).
REACT_264609. Toxicity of botulinum toxin type B (BoNT/B).
REACT_268602. Toxicity of tetanus toxin (TeNT).

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 2
Short name:
VAMP-2
Alternative name(s):
Synaptobrevin-2
Gene namesi
Name:VAMP2
Synonyms:SYB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12643. VAMP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 9493CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei95 – 11420Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini115 – 1162VesicularSequence Analysis

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. clathrin-coated vesicle Source: UniProtKB
  3. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  4. clathrin-sculpted glutamate transport vesicle membrane Source: Reactome
  5. clathrin-sculpted monoamine transport vesicle membrane Source: Reactome
  6. cytoplasmic vesicle Source: ParkinsonsUK-UCL
  7. cytosol Source: Reactome
  8. extracellular vesicular exosome Source: UniProtKB
  9. integral component of plasma membrane Source: ProtInc
  10. intracellular membrane-bounded organelle Source: ParkinsonsUK-UCL
  11. membrane Source: UniProtKB
  12. neuron projection Source: ParkinsonsUK-UCL
  13. neuron projection terminus Source: ParkinsonsUK-UCL
  14. perinuclear region of cytoplasm Source: ParkinsonsUK-UCL
  15. plasma membrane Source: ParkinsonsUK-UCL
  16. secretory granule Source: ParkinsonsUK-UCL
  17. secretory granule membrane Source: Reactome
  18. SNARE complex Source: UniProtKB
  19. synapse Source: ParkinsonsUK-UCL
  20. synaptic vesicle Source: ParkinsonsUK-UCL
  21. synaptic vesicle membrane Source: ParkinsonsUK-UCL
  22. synaptobrevin 2-SNAP-25-syntaxin-1a complex Source: ParkinsonsUK-UCL
  23. synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Source: ParkinsonsUK-UCL
  24. synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex Source: ParkinsonsUK-UCL
  25. trans-Golgi network Source: ParkinsonsUK-UCL
  26. zymogen granule membrane Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37267.

Chemistry

DrugBankiDB00042. Botulinum Toxin Type B.

Polymorphism and mutation databases

BioMutaiVAMP2.
DMDMi288558837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 116115Vesicle-associated membrane protein 2PRO_0000206723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP63027.
PRIDEiP63027.

PTM databases

PhosphoSiteiP63027.

Expressioni

Tissue specificityi

Nervous system and skeletal muscle.1 Publication

Gene expression databases

BgeeiP63027.
CleanExiHS_VAMP2.
ExpressionAtlasiP63027. baseline and differential.
GenevestigatoriP63027.

Interactioni

Subunit structurei

Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds to CPLX1. Interacts with BVES and STX4 (By similarity). Interacts with VAPA and VAPB.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
D2KHQ92EBI-520113,EBI-7604762From a different organism.
FA7GBG32EBI-520113,EBI-7604673From a different organism.
PicalmO550122EBI-520113,EBI-915601From a different organism.
PRKD3O948067EBI-520113,EBI-1255366
SNAP29O957213EBI-520113,EBI-490676
STX4Q128463EBI-520113,EBI-744942

Protein-protein interaction databases

BioGridi112711. 72 interactions.
DIPiDIP-39072N.
IntActiP63027. 10 interactions.
MINTiMINT-4824900.
STRINGi9606.ENSP00000314214.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Turni47 – 493Combined sources
Helixi50 – 534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FIEX-ray2.10C/D22-57[»]
3FIIX-ray2.17B27-57[»]
3RK2X-ray2.20A/E28-60[»]
3RK3X-ray3.50A28-60[»]
3RL0X-ray3.80A/E/I/M/Q/U/Y/c28-60[»]
DisProtiDP00069.
ProteinModelPortaliP63027.
SMRiP63027. Positions 30-116.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63027.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 9161v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP63027.
KOiK13504.
OrthoDBiEOG7MSMRJ.
PhylomeDBiP63027.
TreeFamiTF313666.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV
60 70 80 90 100
DKVLERDQKL SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG
110
VICAIILIII IVYFST
Length:116
Mass (Da):12,663
Last modified:February 9, 2010 - v3
Checksum:i9CD679C4F6F1B5A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161T → S in AAA60604 (PubMed:1976629).Curated
Sequence conflicti116 – 1161T → S in CAA12385 (Ref. 2) Curated
Sequence conflicti116 – 1161T → S in AAF15551 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36205
, M36201, M36202, M36203, M36204 Genomic DNA. Translation: AAA60604.1.
AJ225044 mRNA. Translation: CAA12385.1.
AF135372 Genomic DNA. Translation: AAF15551.1.
AK289555 mRNA. Translation: BAF82244.1.
CH471108 Genomic DNA. Translation: EAW90087.1.
BC002737 mRNA. Translation: AAH02737.3.
BC019608 mRNA. Translation: AAH19608.1.
BC033870 mRNA. Translation: AAH33870.1.
CCDSiCCDS32561.1.
PIRiB38315.
RefSeqiNP_055047.2. NM_014232.2.
UniGeneiHs.25348.

Genome annotation databases

EnsembliENST00000316509; ENSP00000314214; ENSG00000220205.
GeneIDi6844.
KEGGihsa:6844.
UCSCiuc010cnt.1. human.

Polymorphism and mutation databases

BioMutaiVAMP2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36205
, M36201, M36202, M36203, M36204 Genomic DNA. Translation: AAA60604.1.
AJ225044 mRNA. Translation: CAA12385.1.
AF135372 Genomic DNA. Translation: AAF15551.1.
AK289555 mRNA. Translation: BAF82244.1.
CH471108 Genomic DNA. Translation: EAW90087.1.
BC002737 mRNA. Translation: AAH02737.3.
BC019608 mRNA. Translation: AAH19608.1.
BC033870 mRNA. Translation: AAH33870.1.
CCDSiCCDS32561.1.
PIRiB38315.
RefSeqiNP_055047.2. NM_014232.2.
UniGeneiHs.25348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FIEX-ray2.10C/D22-57[»]
3FIIX-ray2.17B27-57[»]
3RK2X-ray2.20A/E28-60[»]
3RK3X-ray3.50A28-60[»]
3RL0X-ray3.80A/E/I/M/Q/U/Y/c28-60[»]
DisProtiDP00069.
ProteinModelPortaliP63027.
SMRiP63027. Positions 30-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112711. 72 interactions.
DIPiDIP-39072N.
IntActiP63027. 10 interactions.
MINTiMINT-4824900.
STRINGi9606.ENSP00000314214.

Chemistry

ChEMBLiCHEMBL2364160.
DrugBankiDB00042. Botulinum Toxin Type B.

Protein family/group databases

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

PTM databases

PhosphoSiteiP63027.

Polymorphism and mutation databases

BioMutaiVAMP2.
DMDMi288558837.

Proteomic databases

MaxQBiP63027.
PRIDEiP63027.

Protocols and materials databases

DNASUi6844.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316509; ENSP00000314214; ENSG00000220205.
GeneIDi6844.
KEGGihsa:6844.
UCSCiuc010cnt.1. human.

Organism-specific databases

CTDi6844.
GeneCardsiGC17M008062.
HGNCiHGNC:12643. VAMP2.
MIMi185881. gene.
neXtProtiNX_P63027.
PharmGKBiPA37267.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP63027.
KOiK13504.
OrthoDBiEOG7MSMRJ.
PhylomeDBiP63027.
TreeFamiTF313666.

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
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_15550. Insulin processing.
REACT_18325. Regulation of insulin secretion.
REACT_19187. Clathrin derived vesicle budding.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_263857. Toxicity of botulinum toxin type F (BoNT/F).
REACT_263924. Toxicity of botulinum toxin type D (BoNT/D).
REACT_264271. Toxicity of botulinum toxin type G (BoNT/G).
REACT_264609. Toxicity of botulinum toxin type B (BoNT/B).
REACT_268602. Toxicity of tetanus toxin (TeNT).

Miscellaneous databases

ChiTaRSiVAMP2. human.
EvolutionaryTraceiP63027.
GeneWikiiVAMP2.
GenomeRNAii6844.
NextBioi26719.
PROiP63027.
SOURCEiSearch...

Gene expression databases

BgeeiP63027.
CleanExiHS_VAMP2.
ExpressionAtlasiP63027. baseline and differential.
GenevestigatoriP63027.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2."
    Archer B.T. III, Oezcelik T., Jahn R., Francke U., Suedhof T.C.
    J. Biol. Chem. 265:17267-17273(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Expression of VAMP genes in human neutrophils."
    Nabokina S.M., Lazo P.A., Mollinedo F.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peripheral blood.
  3. "Genomic structure of human SYB2 gene."
    Taruscio D., Zoraqi K.G., Falbo V.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  4. "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: Cerebellum.
  5. 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].
    Tissue: Neuroblastoma and Testis.
  7. "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2."
    Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H., Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J., Ward C.W.
    Biochem. J. 317:945-954(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane."
    Kutay U., Ahnert-Hilger G., Hartmann E., Wiedenmann B., Rapoport T.A.
    EMBO J. 14:217-223(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  9. "Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution."
    Hanson M.A., Stevens R.C.
    Nat. Struct. Biol. 7:687-692(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-89 IN COMPLEX WITH BOTB.

Entry informationi

Entry nameiVAMP2_HUMAN
AccessioniPrimary (citable) accession number: P63027
Secondary accession number(s): P19065, Q9BUC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 9, 2010
Last modified: April 29, 2015
This is version 113 of the entry and version 3 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.