Protein detail
SPTN2
Spectrin beta chain, non-erythrocytic 2 (Beta-III spectrin) (Spinocerebellar ataxia 5 protein)
Entry name SPTN2 | UniProt ID | EVMP confidence score 0.28 |
Supporting publications (n) 1 | Transmembrane count | Protein classification Disease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
Protein Names
Spectrin beta chain, non-erythrocytic 2 (Beta-III spectrin) (Spinocerebellar ataxia 5 protein)
Protein Class (4)
Disease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
Protein Function (3)
- Human disease related genes:Nervous system diseases:Neurodegenerative diseases
- Disease related genes
- Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
SCA5
Gene Description
Spectrin beta, non-erythrocytic 2
Chromosome
11
Position
66682497-66744670
Supporting publications (n)
1
EVMP confidence score
0.28
Fluorescence & Localization
Tissue Specificskeletal muscleCell SpecificAdrenal cortex cellsSingle-Nuclei Brain Specificendothelial cell
Function & Pathway
Protein Function (3)
- Human disease related genes:Nervous system diseases:Neurodegenerative diseases
- Disease related genes
- Predicted intracellular proteins
Cellular Component (15)
- GO:0005615 extracellular space
- GO:0005829 cytosol
- GO:0005886 plasma membrane
- GO:0008091 spectrin
- GO:0016324 apical plasma membrane
- GO:0030054 cell junction
- GO:0030864 cortical actin cytoskeleton
- GO:0033010 paranodal junction
- GO:0042995 cell projection
- GO:0043025 neuronal cell body
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Molecular Function (7)
KEGG (4)
Reactome (15)
- R-hsa-1280218 adaptive immune system
- R-hsa-446203 asparagine n linked glycosylation
- R-hsa-6807878 copi mediated anterograde transport
- R-hsa-199977 er to golgi anterograde transport
- R-hsa-445095 interaction between l1 and ankyrins
- R-hsa-373760 l1cam interactions
- R-hsa-5684996 mapk1 mapk3 signaling
- R-hsa-5683057 mapk family signaling cascades
- R-hsa-199991 membrane trafficking
- R-hsa-2132295 mhc class ii antigen presentation
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Mediation Categories (4)
Fusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence21
Enzyme-Mediated Modification (1)
1 record.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| SPTBN2 | EGF | P01133 | S | 2,171 | phosphorylation | BEL-Large-Corpus_ProtMapperProtMapper | ProtMapper:17081983 |
Ligand-Receptor Signaling (9)
9 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| ecm | ecm | GO_Intercell | Yes | ||||
| ecm | ecm | OmniPath | Yes | ||||
| extracellular | extracellular | OmniPath | |||||
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath | |||||
| ligand | ligand | CellTalkDB | Yes | ||||
| ligand | ligand | OmniPath | Yes |
Protein Complex Composition (10)
10 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| Non-erythrocytic spectrin | SPTAN1SPTBN2 | O15020Q13813 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C385 | |
| LSM1LSM2LSM3LSM4LSM5SPTBN2 | O15020O15116P62310Q9Y333Q9Y4Y9Q9Y4Z0 | 0:0:0:0:0:0 | hu.MAP | |||
| LSM4LSM5LSM8SLU7SPTBSPTBN2 | O15020O95391O95777P11277Q9Y4Y9Q9Y4Z0 | 0:0:0:0:0:0 | hu.MAP | |||
| CRELD2LSM4LSM8MAGOHSLU7SPTBN2 | O15020O95391O95777P61326Q6UXH1Q9Y4Z0 | 0:0:0:0:0:0 | hu.MAP | |||
| KDM5CPBKSPTBN2THTPAUBA5USP5ZFP91 | O15020P41229P45974Q96JP5Q96KB5Q9BU02Q9GZZ9 | 0:0:0:0:0:0:0 | Havugimana2012 | Havugimana2012:C_533 | ||
| LSM7RAD23ASPTBN2 | O15020P54725Q9UK45 | 0:0:0 | hu.MAP | |||
| ACTBSPTBN2 | O15020P60709 | 6:6 | PDB | PDB:6anu | ||
| MAGOHSPTBN2 | O15020P61326 | 0:0 | hu.MAP | |||
| SPTAN1SPTBN1SPTBN2 | O15020Q01082Q13813 | 0:0:0 | hu.MAP2 | |||
| SPTBN2TCEA2 | O15020Q15560 | 0:0 | hu.MAP2 |
Isolation & Detection Technology (1)
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationSize Exclusion Chromatography | Mass spectrometry | 1 | 30550287 |
Sequence, Structure & Domains
Sequences
Length
2,390
Mass
271,325
Sequence
MSSTLSPTDFDSLEIQGQYSDINNRWDLPDSDWDNDSSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRVGDLYSDLRDGRNLLRLLEVLSGEILPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLVWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLLDFESLKKCNAHYNLQNAFNLAEKELGLTKLLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGKRIGKVLDHAMEAERLVEKYESLASELLQWIEQTIVTLNDRQLANSLSGVQNQLQSFNSYRTVEKPPKFTEKGNLEVLLFTIQSKLRANNQKVYTPREGRLISDINKAWERLEKAEHERELALRTELIRQEKLEQLAARFDRKAAMRETWLSENQRLVSQDNFGLELAAVEAAVRKHEAIETDIVAYSGRVQAVDAVAAELAAERYHDIKRIAARQHNVARLWDFLRQMVAARRERLLLNLELQKVFQDLLYLMDWMEEMKGRLQSQDLGRHLAGVEDLLQLHELVEADIAVQAERVRAVSASALRFCNPGKEYRPCDPQLVSERVAKLEQSYEALCELAAARRARLEESRRLWRFLWEVGEAEAWVREQQHLLASADTGRDLTGALRLLNKHTALRGEMSGRLGPLKLTLEQGQQLVAEGHPGASQASARAAELQAQWERLEALAEERAQRLAQAASLYQFQADANDMEAWLVDALRLVSSPELGHDEFSTQALARQHRALEEEIRSHRPTLDALREQAAALPPTLSRTPEVQSRVPTLERHYEELQARAGERARALEAALALYTMLSEAGACGLWVEEKEQWLNGLALPERLEDLEVVQQRFETLEPEMNTLAAQITAVNDIAEQLLKANPPGKDRIVNTQEQLNHRWQQFRRLADGKKAALTSALSIQNYHLECTETQAWMREKTKVIESTQGLGNDLAGVLALQRKLAGTERDLEAIAARVGELTREANALAAGHPAQAVAINARLREVQTGWEDLRATMRRREESLGEARRLQDFLRSLDDFQAWLGRTQTAVASEEGPATLPEAEALLAQHAALRGEVERAQSEYSRLRALGEEVTRDQADPQCLFLRQRLEALGTGWEELGRMWESRQGRLAQAHGFQGFLRDARQAEGVLSSQEYVLSHTEMPGTLQAADAAIKKLEDFMSTMDANGERIHGLLEAGRQLVSEGNIHADKIREKADSIERRHKKNQDAAQQFLGRLRDNREQQHFLQDCHELKLWIDEKMLTAQDVSYDEARNLHTKWQKHQAFMAELAANKDWLDKVDKEGRELTLEKPELKALVSEKLRDLHRRWDELETTTQAKARSLFDANRAELFAQSCCALESWLESLQAQLHSDDYGKDLTSVNILLKKQQMLEWEMAVREKEVEAIQAQAKALAQEDQGAGEVERTSRAVEEKFRALCQPMRERCRRLQASREQHQFHRDVEDEILWVTERLPMASSMEHGKDLPSVQLLMKKNQTLQKEIQGHEPRIADLRERQRALGAAAAGPELAELQEMWKRLGHELELRGKRLEDALRAQQFYRDAAEAEAWMGEQELHMMGQEKAKDELSAQAEVKKHQVLEQALADYAQTIHQLAASSQDMIDHEHPESTRISIRQAQVDKLYAGLKELAGERRERLQEHLRLCQLRRELDDLEQWIQEREVVAASHELGQDYEHVTMLRDKFREFSRDTSTIGQERVDSANALANGLIAGGHAARATVAEWKDSLNEAWADLLELLDTRGQVLAAAYELQRFLHGARQALARVQHKQQQLPDGTGRDLNAAEALQRRHCAYEHDIQALSPQVQQVQDDGHRLQKAYAGDKAEEIGRHMQAVAEAWAQLQGSSAARRQLLLDTTDKFRFFKAVRELMLWMDEVNLQMDAQERPRDVSSADLVIKNQQGIKAEIEARADRFSSCIDMGKELLARSHYAAEEISEKLSQLQARRQETAEKWQEKMDWLQLVLEVLVFGRDAGMAEAWLCSQEPLVRSAELGCTVDEVESLIKRHEAFQKSAVAWEERFCALEKLTALEEREKERKRKREEEERRKQPPAPEPTASVPPGDLVGGQTASDTTWDGTQPRPPPSTQAPSVNGVCTDGEPSQPLLGQQRLEHSSFPEGPGPGSGDEANGPRGERQTRTRGPAPSAMPQSRSTESAHAATLPPRGPEPSAQEQMEGMLCRKQEMEAFGKKAANRSWQNVYCVLRRGSLGFYKDAKAASAGVPYHGEVPVSLARAQGSVAFDYRKRKHVFKLGLQDGKEYLFQAKDEAEMSSWLRVVNAAIATASSASGEPEEPVVPSTTRGMTRAMTMPPVSPVGAEGPVVLRSKDGREREREKRFSFFKKNK
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O15020-1; Sequence=Displayed; Name=2; IsoId=O15020-2; Sequence=VSP_000722
Alternative Sequence
2314..2390; AEMSSWLRVVNAAIATASSASGEPEEPVVPSTTRGMTRAMTMPPVSPVGAEGPVVLRSKDGREREREKRFSFFKKNK -> VSCPSCSSLSVPFQKLPAADSPSFPVLPLFPGLVLCGKTGCVRRPHQAALPV (in isoform 2)
3D Structural Models
Turn
220..222; 225..227; 256..258; 2265..2267
Helix
180..191; 209..218; 234..246; 266..282; 2261..2264; 2313..2328
Beta Strand
193..195; 205..208; 261..263; 283..285; 2221..2233; 2244..2251; 2254..2260; 2269..2272; 2282..2285; 2293..2299; 2301..2303; 2305..2309
3D Structure
Electron microscopy (1); NMR spectroscopy (2)
Domain & Motif Annotations
Compositional Bias
2081..2096; Basic and acidic residues; 2116..2125; Polar residues; 2370..2383; Basic and acidic residues
Repeat
306..414; Spectrin 1; 427..527; Spectrin 2; 532..639; Spectrin 3; 642..744; Spectrin 4; 749..849; Spectrin 5; 855..954; Spectrin 6; 960..1063; Spectrin 7; 1066..1169; Spectrin 8; 1174..1262; Spectrin 9; 1279..1379; Spectrin 10; 1384..1485; Spectrin 11; 1489..1586; Spectrin 12; 1589..1692; Spectrin 13; 1696..1797; Spectrin 14; 1801..1904; Spectrin 15; 1910..2010; Spectrin 16; 2017..2076; Spectrin 17
Domain (FT)
57..161; Calponin-homology (CH) 1; 176..281; Calponin-homology (CH) 2; 2218..2328; PH
Region
2..278; Actin-binding; 2081..2222; Disordered; 2331..2390; Disordered
Protein Families
Spectrin family
Sequence Similarities
Belongs to the spectrin family.
Clinical Relevance
Disease Involvement (3)
Disease variantNeurodegenerationSpinocerebellar ataxia
Related Diseases
Supporting Publications1
| PMID | Title | Related sentences |
|---|---|---|
| 27601599 | Comprehensive Proteomic Analysis of Human Milk-derived Extracellular Vesicles Unveils a Novel Functional Proteome Distinct from Other Milk Components. | No related sentences available |