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Protein

Synaptotagmin-7

Gene

Syt7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ca2+ sensor involved in Ca2+-dependent exocytosis of secretory and synaptic vesicles through Ca2+ and phospholipid binding to the C2 domain. Ca2+ induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis. SYT7 binds Ca2+ with high affinity and slow kinetics compared to other synaptotagmins (PubMed:26738595). Involved in Ca2+-triggered lysosomal exocytosis, a major component of the plasma membrane repair (By similarity). Ca2+-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages (PubMed:16982801, PubMed:21041449). Ca2+-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts (PubMed:18539119). Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes (PubMed:25860611). Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca2+ into the axon terminal after spike generation, increasing the release probability of neurotransmitters (PubMed:24569478, PubMed:26738595). Probably mediates synaptic facilitation by directly increasing the probability of release (PubMed:26738595). May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca2+ and by forming a complex with calmodulin (PubMed:24569478). Also acts as a regulator of Ca2+-dependent insulin and glucagon secretion in beta-cells (PubMed:18308938, PubMed:19171650). Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (PubMed:20956309). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (By similarity).By similarity9 Publications

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per C2 domain.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi166 – 1661Calcium 1By similarity
Metal bindingi166 – 1661Calcium 2By similarity
Metal bindingi172 – 1721Calcium 1By similarity
Metal bindingi225 – 2251Calcium 11 Publication
Metal bindingi225 – 2251Calcium 21 Publication
Metal bindingi227 – 2271Calcium 11 Publication
Metal bindingi227 – 2271Calcium 21 Publication
Metal bindingi227 – 2271Calcium 31 Publication
Metal bindingi230 – 2301Calcium 3By similarity
Metal bindingi233 – 2331Calcium 21 Publication
Metal bindingi233 – 2331Calcium 31 Publication
Metal bindingi297 – 2971Calcium 4Combined sources1 Publication
Metal bindingi297 – 2971Calcium 5Combined sources1 Publication
Metal bindingi303 – 3031Calcium 5Combined sources1 Publication
Metal bindingi357 – 3571Calcium 4Combined sources1 Publication
Metal bindingi357 – 3571Calcium 5Combined sources1 Publication
Metal bindingi359 – 3591Calcium 4Combined sources1 Publication
Metal bindingi359 – 3591Calcium 5Combined sources1 Publication
Metal bindingi359 – 3591Calcium 6Combined sources1 Publication
Metal bindingi362 – 3621Calcium 6Combined sources1 Publication
Metal bindingi365 – 3651Calcium 4Combined sources1 Publication
Metal bindingi365 – 3651Calcium 6Combined sources1 Publication

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: GO_Central
  • calmodulin binding Source: UniProtKB
  • clathrin binding Source: GO_Central
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • phosphatidylserine binding Source: ParkinsonsUK-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: GO_Central

GO - Biological processi

  • calcium ion-regulated exocytosis of neurotransmitter Source: UniProtKB
  • calcium ion regulated lysosome exocytosis Source: UniProtKB
  • phagocytosis Source: UniProtKB
  • phagosome-lysosome fusion Source: UniProtKB
  • plasma membrane repair Source: MGI
  • regulation of bone remodeling Source: UniProtKB
  • regulation of calcium ion-dependent exocytosis Source: ParkinsonsUK-UCL
  • regulation of glucagon secretion Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of phagocytosis Source: UniProtKB
  • short-term synaptic potentiation Source: UniProtKB
  • synaptic vesicle recycling Source: UniProtKB
  • vesicle-mediated cholesterol transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

Calcium, Calmodulin-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-7Curated
Alternative name(s):
Synaptotagmin VII1 Publication
Short name:
SytVII1 Publication
Gene namesi
Name:Syt7Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1859545. Syt7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616VesicularSequence analysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence analysisAdd
BLAST
Topological domaini38 – 403366CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: GOC
  • early phagosome Source: UniProtKB
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB-SubCell
  • lysosome Source: UniProtKB
  • peroxisomal membrane Source: UniProtKB-SubCell
  • peroxisome Source: UniProtKB
  • phagocytic vesicle membrane Source: UniProtKB-SubCell
  • presynaptic membrane Source: UniProtKB
  • synaptic vesicle Source: UniProtKB
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Peroxisome, Synapse

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice were born at the expected Mendelian ratio and do not show gross abnormalities and/or obvious neurological defects. Mice have a normal life span and are fertile, although reproductive capacity is declining faster with age (PubMed:12925704). Embryonic fibroblasts from Syt7 deficient mice are less susceptible to Trypanosoma cruzi invasion, and display impaired lysosomal exocytosis and resealing after wounding (PubMed:12925704). Mutant mice display impaired insulin secretion: they exhibit normal insulin sensitivity and normal metabolic and Ca2+ responses but impaired insulin release, due to Ca2+-sensing defects (PubMed:18308938). Impaired glucagon secretion (PubMed:19171650). Neurons show enhanced synaptic depression: spontaneous synaptic vesicle release is unaffected, while replenishment is impaired (PubMed:24569478). Abolished synaptic facilitation at all synapses except for mossy fiber synapses, where the remaining enhancement is consistent with use-dependent spike broadening that occurs at this synapse (PubMed:26738595). The loss of facilitation is not due to slowed recovery from depression. The initial probability of release and the presynaptic residual Ca2+ signals are not affected (PubMed:26738595).5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 417CGLCHWC → SGLSHWS: Abolishes palmitoylation. Impaired phagocytosis and localization to lysosomes. 1 Publication
Mutagenesisi225 – 2339DYDRFSRND → AYARFSRNA in C2A*; loss of function due to abolished Ca(2+)-binding to the first C2 domain. Impaired ability to mediate synaptic facilitation. 1 Publication
Mutagenesisi225 – 2273DYD → NYN: Loss of Ca(2+)-binding in the first C2 domain. Impaired delivery of lysosomal membrane to nascent phagosomes; when associated with 357-N--N-359. Impaired synaptic vesicle replenishment; when associated with 357-N--N-359. 2 Publications
Mutagenesisi357 – 3593DKD → NKN: Loss of Ca(2+)-binding in the second C2 domain. Impaired delivery of lysosomal membrane to nascent phagosomes; when associated with 225-N--N-227. Impaired synaptic vesicle replenishment; when associated with 225-N--N-227. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Synaptotagmin-7PRO_0000183958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei58 – 581PhosphothreonineCombined sources
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei119 – 1191PhosphoserineBy similarity
Modified residuei122 – 1221PhosphoserineCombined sources

Post-translational modificationi

Palmitoylated at its vesicular N-terminus; palmitoylation is required for localization to lysosome and phagocytosis in macrophages.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ9R0N7.
PaxDbiQ9R0N7.
PRIDEiQ9R0N7.

PTM databases

iPTMnetiQ9R0N7.
PhosphoSiteiQ9R0N7.
SwissPalmiQ9R0N7.

Expressioni

Tissue specificityi

Widely expressed. Expressed in insulin-secreting cells (PubMed:18308938). Present in glucagon-secreting cells (at protein level) (PubMed:19171650).2 Publications

Gene expression databases

BgeeiENSMUSG00000024743.
CleanExiMM_SYT7.
ExpressionAtlasiQ9R0N7. baseline and differential.
GenevisibleiQ9R0N7. MM.

Interactioni

Subunit structurei

Homodimer (PubMed:10871604). Can also form heterodimers with SYT6, SYT9 and SYT10 (PubMed:10871604). Interacts with calmodulin (CALM1, CALM2 or CALM3) (PubMed:24569478). Interacts with CD63; required for localization to lysosomes (PubMed:21041449).3 Publications

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • clathrin binding Source: GO_Central
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: GO_Central

Protein-protein interaction databases

IntActiQ9R0N7. 1 interaction.
MINTiMINT-4998417.
STRINGi10090.ENSMUSP00000127973.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi269 – 2779Combined sources
Turni278 – 2814Combined sources
Beta strandi282 – 29211Combined sources
Turni298 – 3003Combined sources
Beta strandi304 – 3129Combined sources
Beta strandi315 – 3217Combined sources
Beta strandi332 – 3409Combined sources
Helixi343 – 3486Combined sources
Beta strandi349 – 3579Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi365 – 37612Combined sources
Helixi378 – 38912Combined sources
Beta strandi395 – 4006Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N5AX-ray1.44A266-403[»]
ProteinModelPortaliQ9R0N7.
SMRiQ9R0N7. Positions 101-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini137 – 239103C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini268 – 371104C2 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The C2 domains bind Ca2+ and membranes. Binding to membranes involves Ca2+-dependent phospholipid binding. Compared to other members of the family, the C2 domains of SYT7 dock and insert into cellular membranes in response to intracellular Ca2+ concentrations that are lower than those required for other synaptotagmins. The two C2 domains bind independently to planar membranes, without interdomain cooperativity. Moreover, SYT7 C2 domains insert more deeply into membranes compared to other synaptotagmins.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

eggNOGiENOG410IT3N. Eukaryota.
ENOG410XS7N. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiQ9R0N7.
KOiK19907.
OMAiTAVAQWH.
OrthoDBiEOG091G08NG.
PhylomeDBiQ9R0N7.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015427. Synaptotagmin7.
[Graphical view]
PANTHERiPTHR10024:SF230. PTHR10024:SF230. 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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R0N7-1) [UniParc]FASTAAdd to basket
Also known as: Synaptotagmin VIIalpha1 Publication, Syt7alphaCurated

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK
60 70 80 90 100
NSLETVGTPD SGRGRGEKKA IKLPAGGKAV NTAPVPGQTP HDESDRRTET
110 120 130 140 150
RSSVSDLVNS LTSEMLMLSP GSEEDEAHEG CSRENLGRIQ FSVGYNFQES
160 170 180 190 200
TLTVKVMKAQ ELPAKDFSGT SDPFVKIYLL PDKKHKLETK VKRKNLNPHW
210 220 230 240 250
NETFLFEGFP YEKVVQRVLY LQVLDYDRFS RNDPIGEVSI PLNKVDLTQM
260 270 280 290 300
QTFWKDLKPC SDGSGSRGEL LLSLCYNPSA NSIIVNIIKA RNLKAMDIGG
310 320 330 340 350
TSDPYVKVWL MYKDKRVEKK KTVTKKRNLN PIFNESFAFD IPTEKLRETT
360 370 380 390 400
IIITVMDKDK LSRNDVIGKI YLSWKSGPGE VKHWKDMIAR PRQPVAQWHQ

LKA
Note: Major isoform.1 Publication
Length:403
Mass (Da):45,472
Last modified:May 1, 2000 - v1
Checksum:i4E63C5779C2ED43E
GO
Isoform 2 (identifier: Q9R0N7-2) [UniParc]FASTAAdd to basket
Also known as: Synaptotagmin VIIgamma1 Publication, Syt7gammaCurated

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NFEDSTLSTA...QNQNAQGDKR

Show »
Length:518
Mass (Da):58,260
Checksum:i98E550CE940B10FA
GO
Isoform 3 (identifier: Q9R0N7-3) [UniParc]FASTAAdd to basket
Also known as: Synaptotagmin VIIbeta1 Publication, Syt7betaCurated

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: I → INDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYAPYGDPRLSL

Show »
Length:447
Mass (Da):50,671
Checksum:iC1968D5EAAEF07B7
GO
Isoform 4 (identifier: Q9R0N7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NFEDSTLSTA...QNQNAQGDKR

Show »
Length:567
Mass (Da):63,099
Checksum:iF612EDF43F34EB79
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 711I → INDLDRDFWNNNESTVQQKW SSYPPKEFILNISPYAPYGD PRLSL in isoform 3. VSP_058235
Alternative sequencei72 – 721K → NFEDSTLSTATTLESIPSSA GEPKCQRPRTLMRQQSLQQP LSQNQRGRQPSQPTTSWDHV VGQIRNRGLDMKSFLEGRMV VLSLVLGLSEQDDFANIPDL QNPGTQQNQNAQGDKR in isoform 2. VSP_058236
Alternative sequencei72 – 721K → NFEDSTLSTATTLESIPSSA GEPKCQRPRTLMRQQSLQQP LSQNQQGRQPSQPTTSQSLG QLQAHAASAPGSNPRAYGRG QARQGTSAGSKYRAAGGRSR SNPGSWDHVVGQIRNRGLDM KSFLEGRMVVLSLVLGLSEQ DDFANIPDLQNPGTQQNQNA QGDKR in isoform 4. VSP_058237

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026804 mRNA. Translation: BAA85776.1.
AB075900 mRNA. Translation: BAC44832.1.
AB075901 mRNA. Translation: BAC44833.1.
AC124169 Genomic DNA. No translation available.
BC105660 mRNA. Translation: AAI05661.1.
BC139806 mRNA. Translation: AAI39807.1.
CCDSiCCDS29575.1. [Q9R0N7-1]
CCDS29576.1. [Q9R0N7-3]
CCDS50388.1. [Q9R0N7-4]
RefSeqiNP_061271.1. NM_018801.3. [Q9R0N7-1]
NP_775090.1. NM_173067.3. [Q9R0N7-3]
NP_775091.2. NM_173068.2. [Q9R0N7-4]
UniGeneiMm.182654.

Genome annotation databases

EnsembliENSMUST00000073899; ENSMUSP00000073560; ENSMUSG00000024743. [Q9R0N7-1]
ENSMUST00000076968; ENSMUSP00000076234; ENSMUSG00000024743. [Q9R0N7-3]
ENSMUST00000169121; ENSMUSP00000127973; ENSMUSG00000024743. [Q9R0N7-4]
GeneIDi54525.
KEGGimmu:54525.
UCSCiuc008gpp.2. mouse.
uc008gpq.2. mouse. [Q9R0N7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026804 mRNA. Translation: BAA85776.1.
AB075900 mRNA. Translation: BAC44832.1.
AB075901 mRNA. Translation: BAC44833.1.
AC124169 Genomic DNA. No translation available.
BC105660 mRNA. Translation: AAI05661.1.
BC139806 mRNA. Translation: AAI39807.1.
CCDSiCCDS29575.1. [Q9R0N7-1]
CCDS29576.1. [Q9R0N7-3]
CCDS50388.1. [Q9R0N7-4]
RefSeqiNP_061271.1. NM_018801.3. [Q9R0N7-1]
NP_775090.1. NM_173067.3. [Q9R0N7-3]
NP_775091.2. NM_173068.2. [Q9R0N7-4]
UniGeneiMm.182654.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N5AX-ray1.44A266-403[»]
ProteinModelPortaliQ9R0N7.
SMRiQ9R0N7. Positions 101-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0N7. 1 interaction.
MINTiMINT-4998417.
STRINGi10090.ENSMUSP00000127973.

PTM databases

iPTMnetiQ9R0N7.
PhosphoSiteiQ9R0N7.
SwissPalmiQ9R0N7.

Proteomic databases

MaxQBiQ9R0N7.
PaxDbiQ9R0N7.
PRIDEiQ9R0N7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073899; ENSMUSP00000073560; ENSMUSG00000024743. [Q9R0N7-1]
ENSMUST00000076968; ENSMUSP00000076234; ENSMUSG00000024743. [Q9R0N7-3]
ENSMUST00000169121; ENSMUSP00000127973; ENSMUSG00000024743. [Q9R0N7-4]
GeneIDi54525.
KEGGimmu:54525.
UCSCiuc008gpp.2. mouse.
uc008gpq.2. mouse. [Q9R0N7-1]

Organism-specific databases

CTDi9066.
MGIiMGI:1859545. Syt7.

Phylogenomic databases

eggNOGiENOG410IT3N. Eukaryota.
ENOG410XS7N. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiQ9R0N7.
KOiK19907.
OMAiTAVAQWH.
OrthoDBiEOG091G08NG.
PhylomeDBiQ9R0N7.

Miscellaneous databases

ChiTaRSiSyt7. mouse.
PROiQ9R0N7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024743.
CleanExiMM_SYT7.
ExpressionAtlasiQ9R0N7. baseline and differential.
GenevisibleiQ9R0N7. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015427. Synaptotagmin7.
[Graphical view]
PANTHERiPTHR10024:SF230. PTHR10024:SF230. 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...

Entry informationi

Entry nameiSYT7_MOUSE
AccessioniPrimary (citable) accession number: Q9R0N7
Secondary accession number(s): A4QPF1
, E9PZA8, Q0D2K7, Q8CF95, Q8CF96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.