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Protein

Ganglioside GM2 activator

Gene

GM2A

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

Functioni

The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-1660662 Glycosphingolipid metabolism
R-HSA-6798695 Neutrophil degranulation

Chemistry databases

SwissLipidsiSLP:000000476

Names & Taxonomyi

Protein namesi
Recommended name:
Ganglioside GM2 activator
Alternative name(s):
Cerebroside sulfate activator protein
GM2-AP
Sphingolipid activator protein 3
Short name:
SAP-3
Cleaved into the following chain:
Gene namesi
Name:GM2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000196743.8
HGNCiHGNC:4367 GM2A
MIMi613109 gene
neXtProtiNX_P17900

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

Lysosome

Pathology & Biotechi

Involvement in diseasei

GM2-gangliosidosis AB (GM2GAB)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the presence of both normal hexosaminidase A and B.
See also OMIM:272750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01169788Missing in GM2GAB. 1 Publication1
Natural variantiVAR_006947138C → R in GM2GAB. 1 PublicationCorresponds to variant dbSNP:rs137852797EnsemblClinVar.1
Natural variantiVAR_011698169R → P in GM2GAB. 1 PublicationCorresponds to variant dbSNP:rs104893892EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Gangliosidosis

Organism-specific databases

DisGeNETi2760
MalaCardsiGM2A
MIMi272750 phenotype
OpenTargetsiENSG00000196743
Orphaneti309246 GM2-gangliosidosis, AB variant
PharmGKBiPA28752

Chemistry databases

DrugBankiDB04660 Choline alfoscerate
DB02325 Isopropyl Alcohol
DB03017 Lauric Acid
DB03633 Lpc-Ether
DB08231 MYRISTIC ACID
DB02261 Platelet Activating Factor

Polymorphism and mutation databases

BioMutaiGM2A
DMDMi160331912

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000003163924 – 311 Publication8
ChainiPRO_000003164032 – 193Ganglioside GM2 activatorAdd BLAST162
ChainiPRO_000003164134 – 193Ganglioside GM2 activator isoform shortAdd BLAST160

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 183
Glycosylationi63N-linked (GlcNAc...) asparagine1
Disulfide bondi99 ↔ 106
Disulfide bondi112 ↔ 138
Disulfide bondi125 ↔ 136

Post-translational modificationi

The serines in positions 32 and 33 are absent in 80% of the sequenced protein.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP17900
MaxQBiP17900
PaxDbiP17900
PeptideAtlasiP17900
PRIDEiP17900
ProteomicsDBi53524

Expressioni

Gene expression databases

BgeeiENSG00000196743
CleanExiHS_GM2A
ExpressionAtlasiP17900 baseline and differential
GenevisibleiP17900 HS

Organism-specific databases

HPAiHPA008063

Interactioni

Protein-protein interaction databases

BioGridi109022, 27 interactors
IntActiP17900, 3 interactors
STRINGi9606.ENSP00000349687

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 40Combined sources6
Turni41 – 43Combined sources3
Beta strandi45 – 74Combined sources30
Beta strandi81 – 90Combined sources10
Beta strandi93 – 96Combined sources4
Beta strandi103 – 105Combined sources3
Beta strandi107 – 109Combined sources3
Helixi111 – 118Combined sources8
Beta strandi121 – 123Combined sources3
Helixi129 – 132Combined sources4
Beta strandi137 – 140Combined sources4
Beta strandi142 – 154Combined sources13
Turni161 – 163Combined sources3
Beta strandi164 – 176Combined sources13
Beta strandi179 – 192Combined sources14

3D structure databases

ProteinModelPortaliP17900
SMRiP17900
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17900

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IX9N Eukaryota
ENOG4111JSM LUCA
GeneTreeiENSGT00390000003288
HOGENOMiHOG000031350
HOVERGENiHBG000260
InParanoidiP17900
KOiK12383
OMAiWLSTGNY
OrthoDBiEOG091G0VEB
PhylomeDBiP17900
TreeFamiTF353575

Family and domain databases

Gene3Di2.70.220.10, 1 hit
InterProiView protein in InterPro
IPR028996 GM2-AP
IPR036846 GM2-AP_sf
IPR003172 ML_dom
PANTHERiPTHR17357 PTHR17357, 1 hit
PfamiView protein in Pfam
PF02221 E1_DerP2_DerF2, 1 hit
SMARTiView protein in SMART
SM00737 ML, 1 hit
SUPFAMiSSF63707 SSF63707, 1 hit

Sequencei

Sequence statusi: Complete.

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

P17900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSLMQAPLL IALGLLLAAP AQAHLKKPSQ LSSFSWDNCD EGKDPAVIRS
60 70 80 90 100
LTLEPDPIIV PGNVTLSVMG STSVPLSSPL KVDLVLEKEV AGLWIKIPCT
110 120 130 140 150
DYIGSCTFEH FCDVLDMLIP TGEPCPEPLR TYGLPCHCPF KEGTYSLPKS
160 170 180 190
EFVVPDLELP SWLTTGNYRI ESVLSSSGKR LGCIKIAASL KGI
Length:193
Mass (Da):20,838
Last modified:November 13, 2007 - v4
Checksum:i4EB1119945365F7E
GO

Sequence cautioni

The sequence CAA43408 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA43994 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39C → R in BAG35396 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01383019A → T5 PublicationsCorresponds to variant dbSNP:rs1048719EnsemblClinVar.1
Natural variantiVAR_03689259I → V6 PublicationsCorresponds to variant dbSNP:rs153477EnsemblClinVar.1
Natural variantiVAR_03689369M → V7 PublicationsCorresponds to variant dbSNP:rs153478EnsemblClinVar.1
Natural variantiVAR_01169788Missing in GM2GAB. 1 Publication1
Natural variantiVAR_006947138C → R in GM2GAB. 1 PublicationCorresponds to variant dbSNP:rs137852797EnsemblClinVar.1
Natural variantiVAR_011698169R → P in GM2GAB. 1 PublicationCorresponds to variant dbSNP:rs104893892EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76477 mRNA Translation: AAA35907.1
X62078 mRNA Translation: CAA43993.1
X62078 mRNA Translation: CAA43994.1 Different initiation.
X61095 mRNA Translation: CAA43408.1 Different initiation.
L01439 mRNA Translation: AAA52767.1
AF124719, AF124717, AF124718 Genomic DNA Translation: AAD25741.1
AK312494 mRNA Translation: BAG35396.1
AC008385 Genomic DNA No translation available.
CH471062 Genomic DNA Translation: EAW61680.1
CH471062 Genomic DNA Translation: EAW61681.1
BC009273 mRNA Translation: AAH09273.1
X16087 mRNA Translation: CAA34215.1
CCDSiCCDS4313.1
PIRiI54178
S13195
S22411
RefSeqiNP_000396.2, NM_000405.4
UniGeneiHs.483873

Genome annotation databases

EnsembliENST00000357164; ENSP00000349687; ENSG00000196743
GeneIDi2760
KEGGihsa:2760
UCSCiuc003ltr.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSAP3_HUMAN
AccessioniPrimary (citable) accession number: P17900
Secondary accession number(s): B2R699
, D3DQH6, Q14426, Q14428, Q6LBL5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 13, 2007
Last modified: July 18, 2018
This is version 183 of the entry and version 4 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

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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