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Protein

Ganglioside GM2 activator

Gene

GM2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BioCyciZFISH:G66-31594-MONOMER.
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

HGNCiHGNC:4367. GM2A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 rs137852797dbSNPEnsembl.1
Natural variantiVAR_011698169R → P in GM2GAB. 1 PublicationCorresponds to variant rs104893892dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Gangliosidosis

Organism-specific databases

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

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

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...)1
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.

Expressioni

Gene expression databases

BgeeiENSG00000196743.
CleanExiHS_GM2A.
ExpressionAtlasiP17900. baseline and differential.
GenevisibleiP17900. HS.

Organism-specific databases

HPAiHPA008063.

Interactioni

Protein-protein interaction databases

BioGridi109022. 22 interactors.
IntActiP17900. 2 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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G13X-ray2.00A/B/C32-193[»]
1PU5X-ray1.90A/B/C32-193[»]
1PUBX-ray2.51A32-193[»]
1TJJX-ray2.00A/B/C32-193[»]
2AF9X-ray2.00A32-193[»]
2AG2X-ray2.00A/B/C32-193[»]
2AG4X-ray1.80A/B32-193[»]
2AG9X-ray2.20A/B32-193[»]
ProteinModelPortaliP17900.
SMRiP17900.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17900.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

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

Family and domain databases

InterProiIPR028996. GM2-AP.
IPR003172. ML_dom.
[Graphical view]
PANTHERiPTHR17357. PTHR17357. 1 hit.
PfamiPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTiSM00737. ML. 1 hit.
[Graphical view]

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 → T.5 PublicationsCorresponds to variant rs1048719dbSNPEnsembl.1
Natural variantiVAR_03689259I → V.6 PublicationsCorresponds to variant rs153477dbSNPEnsembl.1
Natural variantiVAR_03689369M → V.7 PublicationsCorresponds to variant rs153478dbSNPEnsembl.1
Natural variantiVAR_01169788Missing in GM2GAB. 1 Publication1
Natural variantiVAR_006947138C → R in GM2GAB. 1 PublicationCorresponds to variant rs137852797dbSNPEnsembl.1
Natural variantiVAR_011698169R → P in GM2GAB. 1 PublicationCorresponds to variant rs104893892dbSNPEnsembl.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

Cross-referencesi

Web resourcesi

GM2Adb

GM2A mutation database

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G13X-ray2.00A/B/C32-193[»]
1PU5X-ray1.90A/B/C32-193[»]
1PUBX-ray2.51A32-193[»]
1TJJX-ray2.00A/B/C32-193[»]
2AF9X-ray2.00A32-193[»]
2AG2X-ray2.00A/B/C32-193[»]
2AG4X-ray1.80A/B32-193[»]
2AG9X-ray2.20A/B32-193[»]
ProteinModelPortaliP17900.
SMRiP17900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109022. 22 interactors.
IntActiP17900. 2 interactors.
STRINGi9606.ENSP00000349687.

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.
SwissLipidsiSLP:000000476.

Polymorphism and mutation databases

BioMutaiGM2A.
DMDMi160331912.

Proteomic databases

EPDiP17900.
MaxQBiP17900.
PaxDbiP17900.
PeptideAtlasiP17900.
PRIDEiP17900.

Protocols and materials databases

DNASUi2760.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2760.
DisGeNETi2760.
GeneCardsiGM2A.
H-InvDBHIX0005327.
HGNCiHGNC:4367. GM2A.
HPAiHPA008063.
MalaCardsiGM2A.
MIMi272750. phenotype.
613109. gene.
neXtProtiNX_P17900.
OpenTargetsiENSG00000196743.
Orphaneti309246. GM2-gangliosidosis, AB variant.
PharmGKBiPA28752.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:G66-31594-MONOMER.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiGM2A. human.
EvolutionaryTraceiP17900.
GeneWikiiGM2A.
GenomeRNAii2760.
PROiP17900.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196743.
CleanExiHS_GM2A.
ExpressionAtlasiP17900. baseline and differential.
GenevisibleiP17900. HS.

Family and domain databases

InterProiIPR028996. GM2-AP.
IPR003172. ML_dom.
[Graphical view]
PANTHERiPTHR17357. PTHR17357. 1 hit.
PfamiPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTiSM00737. ML. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAP3_HUMAN
AccessioniPrimary (citable) accession number: P17900
Secondary accession number(s): B2R699
, D3DQH6, Q14426, Q14428, Q6LBL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 13, 2007
Last modified: November 30, 2016
This is version 169 of the entry and version 4 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, 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

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.