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Protein

Alpha-synuclein

Gene

SNCA

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

Functioni

May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi2CopperCurated1
Metal bindingi50CopperCurated1

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: Ensembl
  • calcium ion binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • cuprous ion binding Source: CAFA
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • dynein complex binding Source: UniProtKB
  • ferrous iron binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • kinesin binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • microtubule binding Source: Ensembl
  • oxidoreductase activity Source: UniProtKB
  • phospholipase binding Source: Ensembl
  • phospholipid binding Source: ParkinsonsUK-UCL
  • phosphoprotein binding Source: BHF-UCL
  • protein domain specific binding Source: Ensembl
  • protein N-terminus binding Source: Ensembl
  • tau protein binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: ParkinsonsUK-UCL
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  • adult locomotory behavior Source: Ensembl
  • aging Source: Ensembl
  • behavioral response to cocaine Source: Ensembl
  • cellular protein metabolic process Source: Reactome
  • cellular response to copper ion Source: UniProtKB
  • cellular response to epinephrine stimulus Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: Ensembl
  • cellular response to oxidative stress Source: ParkinsonsUK-UCL
  • dopamine biosynthetic process Source: UniProtKB
  • dopamine uptake involved in synaptic transmission Source: UniProtKB
  • excitatory postsynaptic potential Source: Ensembl
  • fatty acid metabolic process Source: Ensembl
  • long-term synaptic potentiation Source: Ensembl
  • microglial cell activation Source: ParkinsonsUK-UCL
  • mitochondrial ATP synthesis coupled electron transport Source: Ensembl
  • mitochondrial membrane organization Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of dopamine metabolic process Source: Ensembl
  • negative regulation of dopamine uptake involved in synaptic transmission Source: UniProtKB
  • negative regulation of exocytosis Source: UniProtKB
  • negative regulation of histone acetylation Source: UniProtKB
  • negative regulation of microtubule polymerization Source: BHF-UCL
  • negative regulation of mitochondrial electron transport, NADH to ubiquinone Source: ParkinsonsUK-UCL
  • negative regulation of monooxygenase activity Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of neuron death Source: ParkinsonsUK-UCL
  • negative regulation of norepinephrine uptake Source: UniProtKB
  • negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  • negative regulation of protein phosphorylation Source: Ensembl
  • negative regulation of serotonin uptake Source: UniProtKB
  • negative regulation of thrombin-activated receptor signaling pathway Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: ParkinsonsUK-UCL
  • negative regulation of transporter activity Source: UniProtKB
  • neutral lipid metabolic process Source: Ensembl
  • oxidation-reduction process Source: UniProtKB
  • phospholipid metabolic process Source: Ensembl
  • positive regulation of apoptotic process Source: ParkinsonsUK-UCL
  • positive regulation of endocytosis Source: UniProtKB
  • positive regulation of glutathione peroxidase activity Source: ParkinsonsUK-UCL
  • positive regulation of hydrogen peroxide catabolic process Source: ParkinsonsUK-UCL
  • positive regulation of inflammatory response Source: ParkinsonsUK-UCL
  • positive regulation of inositol phosphate biosynthetic process Source: UniProtKB
  • positive regulation of neuron death Source: ParkinsonsUK-UCL
  • positive regulation of neurotransmitter secretion Source: Ensembl
  • positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of protein serine/threonine kinase activity Source: BHF-UCL
  • positive regulation of receptor recycling Source: UniProtKB
  • positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • receptor internalization Source: UniProtKB
  • regulation of acyl-CoA biosynthetic process Source: Ensembl
  • regulation of dopamine secretion Source: UniProtKB
  • regulation of glutamate secretion Source: Ensembl
  • regulation of locomotion Source: Ensembl
  • regulation of long-term neuronal synaptic plasticity Source: Ensembl
  • regulation of macrophage activation Source: Ensembl
  • regulation of phospholipase activity Source: UniProtKB
  • regulation of presynapse assembly Source: ParkinsonsUK-UCL
  • regulation of reactive oxygen species biosynthetic process Source: ParkinsonsUK-UCL
  • regulation of synaptic vesicle recycling Source: ParkinsonsUK-UCL
  • response to interferon-gamma Source: UniProtKB
  • response to interleukin-1 Source: UniProtKB
  • response to iron(II) ion Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • response to magnesium ion Source: UniProtKB
  • supramolecular fiber organization Source: UniProtKB
  • synapse organization Source: Ensembl
  • synaptic vesicle endocytosis Source: UniProtKB
  • synaptic vesicle transport Source: Ensembl

Keywordsi

LigandCopper, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-977225 Amyloid fiber formation
SignaLinkiP37840
SIGNORiP37840

Protein family/group databases

TCDBi1.C.77.1.1 the synuclein (synuclein) family

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-synuclein
Alternative name(s):
Non-A beta component of AD amyloid
Non-A4 component of amyloid precursor
Short name:
NACP
Gene namesi
Name:SNCA
Synonyms:NACP, PARK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000145335.15
HGNCiHGNC:11138 SNCA
MIMi163890 gene
neXtProtiNX_P37840

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cell junction, Cytoplasm, Membrane, Nucleus, Secreted, Synapse

Pathology & Biotechi

Involvement in diseasei

Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.
Parkinson disease 1, autosomal dominant (PARK1)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.
See also OMIM:168601
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00795730A → P in PARK1; no effect on oligomerization. 2 PublicationsCorresponds to variant dbSNP:rs104893878Ensembl.1
Natural variantiVAR_07017150H → Q in PARK1; no effect on protein structure; no effect on phosphorylation of the protein; no effect on membrane- and lipid-binding; increases oligomerization; increases fibril formation; increases secretion of the protein; impairs copper-binding. 4 PublicationsCorresponds to variant dbSNP:rs201106962Ensembl.1
Natural variantiVAR_00745453A → T in PARK1; no effect on osmotic stress-induced phosphorylation; increases oligomerization. 3 PublicationsCorresponds to variant dbSNP:rs104893877Ensembl.1
Parkinson disease 4, autosomal dominant (PARK4)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (resting tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia.
See also OMIM:605543
Dementia Lewy body (DLB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder characterized by mental impairment leading to dementia, parkinsonism, fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.
See also OMIM:127750

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2D → A: Impairs copper-binding. 1 Publication1
Mutagenesisi35E → K: No effect on oligomerization. 1 Publication1
Mutagenesisi39Y → F: No effect on osmotic stress-induced phosphorylation. 1 Publication1
Mutagenesisi50H → A: Impairs copper-binding. 1 Publication1
Mutagenesisi57E → K: Increases oligomerization. 1 Publication1
Mutagenesisi67 – 71Missing : Reduces polymerization into amyloid fibrils. 1 Publication5
Mutagenesisi71 – 82Missing : Impairs polymerization into amyloid fibrils. 1 PublicationAdd BLAST12
Mutagenesisi76 – 77Missing : Impairs polymerization into amyloid fibrils. 1 Publication2
Mutagenesisi76Missing : Does not affect polymerization into amyloid fibrils. 1
Mutagenesisi77Missing : Does not affect polymerization into amyloid fibrils. 1 Publication1
Mutagenesisi78Missing : Does not affect polymerization into amyloid fibrils. 1 Publication1
Mutagenesisi85 – 94Missing : Reduces polymerization into amyloid fibrils. 1 Publication10
Mutagenesisi125Y → F: Abolishes osmotic stress-induced phosphorylation. 1 Publication1
Mutagenesisi133Y → F: No effect on osmotic stress-induced phosphorylation. 1 Publication1
Mutagenesisi136Y → F: No effect on osmotic stress-induced phosphorylation. 1 Publication1

Keywords - Diseasei

Alzheimer disease, Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

DisGeNETi6622
GeneReviewsiSNCA
MalaCardsiSNCA
MIMi127750 phenotype
168600 phenotype
168601 phenotype
605543 phenotype
OpenTargetsiENSG00000145335
Orphaneti1648 Dementia with Lewy body
171695 Parkinsonian-pyramidal syndrome
2828 Young adult-onset Parkinsonism
PharmGKBiPA35986

Chemistry databases

ChEMBLiCHEMBL6152

Polymorphism and mutation databases

BioMutaiSNCA
DMDMi586067

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840221 – 140Alpha-synucleinAdd BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei87Phosphoserine1 Publication1
Modified residuei125Phosphotyrosine; by FYN2 Publications1
Modified residuei129Phosphoserine; by BARK1, PLK2, CK2, CK1 and GRK53 Publications1

Post-translational modificationi

Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.6 Publications
Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.
Ubiquitinated. The predominant conjugate is the diubiquitinated form (By similarity).By similarity
Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP37840
MaxQBiP37840
PaxDbiP37840
PeptideAtlasiP37840
PRIDEiP37840
TopDownProteomicsiP37840-1 [P37840-1]

PTM databases

iPTMnetiP37840
PhosphoSitePlusiP37840

Miscellaneous databases

PMAP-CutDBiP37840

Expressioni

Tissue specificityi

Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.

Gene expression databases

BgeeiENSG00000145335
CleanExiHS_SNCA
ExpressionAtlasiP37840 baseline and differential
GenevisibleiP37840 HS

Organism-specific databases

HPAiCAB010877
HPA005459

Interactioni

Subunit structurei

Soluble monomer which can form filamentous aggregates. Interacts with UCHL1 (By similarity). Interacts with phospholipase D and histones.By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: Ensembl
  • histone binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • kinesin binding Source: UniProtKB
  • microtubule binding Source: Ensembl
  • phospholipase binding Source: Ensembl
  • phosphoprotein binding Source: BHF-UCL
  • protein domain specific binding Source: Ensembl
  • protein N-terminus binding Source: Ensembl
  • tau protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112506, 473 interactors
CORUMiP37840
DIPiDIP-35354N
IntActiP37840, 262 interactors
MINTiP37840
STRINGi9606.ENSP00000338345

Chemistry databases

BindingDBiP37840

Structurei

Secondary structure

1140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Helixi17 – 19Combined sources3
Helixi21 – 32Combined sources12
Helixi41 – 44Combined sources4
Beta strandi45 – 47Combined sources3
Helixi52 – 55Combined sources4
Helixi66 – 68Combined sources3
Beta strandi70 – 78Combined sources9
Beta strandi80 – 83Combined sources4
Beta strandi88 – 98Combined sources11
Beta strandi110 – 113Combined sources4
Turni120 – 122Combined sources3
Turni124 – 126Combined sources3
Turni133 – 136Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XQ8NMR-A1-140[»]
2JN5NMR-A1-12[»]
2KKWNMR-A1-140[»]
2M55NMR-B1-19[»]
2N0ANMR-A/B/C/D/E/F/G/H/I/J1-140[»]
2X6MX-ray1.62B132-140[»]
3Q25X-ray1.90A1-19[»]
3Q26X-ray1.54A10-42[»]
3Q27X-ray1.30A32-57[»]
3Q28X-ray1.60A58-79[»]
3Q29X-ray2.30A/C1-19[»]
4BXLNMR-C35-56[»]
4R0UX-ray1.38A72-78[»]
4R0WX-ray1.50A70-76[»]
4RIKX-ray1.85A69-77[»]
4RILelectron microscopy1.43A68-78[»]
4ZNNelectron microscopy1.41A47-56[»]
5CRWX-ray1.60B31-41[»]
DisProtiDP00070
ProteinModelPortaliP37840
SMRiP37840
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37840

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati20 – 301Add BLAST11
Repeati31 – 412Add BLAST11
Repeati42 – 563; approximateAdd BLAST15
Repeati57 – 674Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 674 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)Add BLAST48

Domaini

The 'non A-beta component of Alzheimer disease amyloid plaque' domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments.1 Publication

Sequence similaritiesi

Belongs to the synuclein family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IWI2 Eukaryota
ENOG4111TDZ LUCA
GeneTreeiENSGT00390000016161
HOGENOMiHOG000008691
HOVERGENiHBG000481
InParanoidiP37840
KOiK04528
OMAiSEAYEMP
OrthoDBiEOG091G11PA
PhylomeDBiP37840
TreeFamiTF332776

Family and domain databases

InterProiView protein in InterPro
IPR001058 Synuclein
IPR002460 Synuclein_alpha
PANTHERiPTHR13820 PTHR13820, 1 hit
PTHR13820:SF5 PTHR13820:SF5, 1 hit
PfamiView protein in Pfam
PF01387 Synuclein, 1 hit
PRINTSiPR01212 ASYNUCLEIN
PR01211 SYNUCLEIN

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P37840-1) [UniParc]FASTAAdd to basket
Also known as: NACP140

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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH
60 70 80 90 100
GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL
110 120 130 140
GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA
Length:140
Mass (Da):14,460
Last modified:October 1, 1994 - v1
Checksum:i6BB2F12128931663
GO
Isoform 2-4 (identifier: P37840-2) [UniParc]FASTAAdd to basket
Also known as: NACP112

The sequence of this isoform differs from the canonical sequence as follows:
     103-130: Missing.

Show »
Length:112
Mass (Da):11,372
Checksum:i16EA234777EFA89E
GO
Isoform 2-5 (identifier: P37840-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-54: Missing.

Show »
Length:126
Mass (Da):13,109
Checksum:i0F87D9A60E831E02
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00795730A → P in PARK1; no effect on oligomerization. 2 PublicationsCorresponds to variant dbSNP:rs104893878Ensembl.1
Natural variantiVAR_02270346E → K in PARK1 and DLB; significant increase in binding to negatively charged phospholipid liposomes; increases oligomerization. 3 PublicationsCorresponds to variant dbSNP:rs104893875Ensembl.1
Natural variantiVAR_07017150H → Q in PARK1; no effect on protein structure; no effect on phosphorylation of the protein; no effect on membrane- and lipid-binding; increases oligomerization; increases fibril formation; increases secretion of the protein; impairs copper-binding. 4 PublicationsCorresponds to variant dbSNP:rs201106962Ensembl.1
Natural variantiVAR_00745453A → T in PARK1; no effect on osmotic stress-induced phosphorylation; increases oligomerization. 3 PublicationsCorresponds to variant dbSNP:rs104893877Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00636341 – 54Missing in isoform 2-5. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_006364103 – 130Missing in isoform 2-4. 2 PublicationsAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08850 mRNA Translation: AAA16117.1
L36674 mRNA Translation: AAA98493.1
L36675 mRNA Translation: AAA98487.1
D31839 mRNA Translation: BAA06625.1
U46901
, U46897, U46898, U46899 Genomic DNA Translation: AAC02114.1
AF163864 Genomic DNA Translation: AAG30302.1
AF163864 Genomic DNA Translation: AAG30303.1
AY049786 mRNA Translation: AAL15443.1
AK290169 mRNA Translation: BAF82858.1
CR457058 mRNA Translation: CAG33339.1
DQ088379 Genomic DNA Translation: AAY88735.1
CH471057 Genomic DNA Translation: EAX06036.1
BC013293 mRNA Translation: AAH13293.1
BC108275 mRNA Translation: AAI08276.1
CCDSiCCDS3634.1 [P37840-1]
CCDS43252.1 [P37840-2]
PIRiA49669
S56746
RefSeqiNP_000336.1, NM_000345.3 [P37840-1]
NP_001139526.1, NM_001146054.1 [P37840-1]
NP_001139527.1, NM_001146055.1 [P37840-1]
NP_009292.1, NM_007308.2 [P37840-2]
XP_011530510.1, XM_011532208.2 [P37840-1]
XP_016864051.1, XM_017008562.1 [P37840-1]
XP_016864052.1, XM_017008563.1 [P37840-1]
UniGeneiHs.21374

Genome annotation databases

EnsembliENST00000336904; ENSP00000338345; ENSG00000145335 [P37840-1]
ENST00000345009; ENSP00000343683; ENSG00000145335 [P37840-2]
ENST00000394986; ENSP00000378437; ENSG00000145335 [P37840-1]
ENST00000394989; ENSP00000378440; ENSG00000145335 [P37840-3]
ENST00000394991; ENSP00000378442; ENSG00000145335 [P37840-1]
ENST00000420646; ENSP00000396241; ENSG00000145335 [P37840-2]
ENST00000505199; ENSP00000421485; ENSG00000145335 [P37840-3]
ENST00000506244; ENSP00000422238; ENSG00000145335 [P37840-1]
ENST00000508895; ENSP00000426955; ENSG00000145335 [P37840-1]
ENST00000618500; ENSP00000484044; ENSG00000145335 [P37840-3]
GeneIDi6622
KEGGihsa:6622
UCSCiuc003hso.3 human [P37840-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSYUA_HUMAN
AccessioniPrimary (citable) accession number: P37840
Secondary accession number(s): A8K2A4
, Q13701, Q4JHI3, Q6IAU6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 25, 2018
This is version 212 of the entry and version 1 of the sequence. See 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, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health