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P17900

- SAP3_HUMAN

UniProt

P17900 - SAP3_HUMAN

Protein

Ganglioside GM2 activator

Gene

GM2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (13 Nov 2007)
      Previous versions | rss
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    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

    1. beta-N-acetylhexosaminidase activity Source: Ensembl
    2. lipid transporter activity Source: Ensembl
    3. phospholipase activator activity Source: Ensembl

    GO - Biological processi

    1. ganglioside catabolic process Source: Ensembl
    2. glycosphingolipid metabolic process Source: Reactome
    3. learning or memory Source: Ensembl
    4. lipid storage Source: Ensembl
    5. neuromuscular process controlling balance Source: Ensembl
    6. oligosaccharide catabolic process Source: Ensembl
    7. positive regulation of hydrolase activity Source: Ensembl
    8. small molecule metabolic process Source: Reactome
    9. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Sphingolipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_116105. Glycosphingolipid metabolism.

    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
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4367. GM2A.

    Subcellular locationi

    GO - Cellular componenti

    1. apical cortex Source: Ensembl
    2. cytoplasmic side of plasma membrane Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. lysosomal lumen Source: Reactome
    5. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881Missing in GM2GAB. 1 Publication
    VAR_011697
    Natural varianti138 – 1381C → R in GM2GAB. 1 Publication
    VAR_006947
    Natural varianti169 – 1691R → P in GM2GAB. 1 Publication
    VAR_011698

    Keywords - Diseasei

    Disease mutation, Gangliosidosis

    Organism-specific databases

    MIMi272750. phenotype.
    Orphaneti309246. GM2-gangliosidosis, AB variant.
    PharmGKBiPA28752.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 3181 PublicationPRO_0000031639
    Chaini32 – 193162Ganglioside GM2 activatorPRO_0000031640Add
    BLAST
    Chaini34 – 193160Ganglioside GM2 activator isoform shortPRO_0000031641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 183
    Glycosylationi63 – 631N-linked (GlcNAc...)
    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

    MaxQBiP17900.
    PaxDbiP17900.
    PRIDEiP17900.

    Expressioni

    Gene expression databases

    ArrayExpressiP17900.
    BgeeiP17900.
    CleanExiHS_GM2A.
    GenevestigatoriP17900.

    Organism-specific databases

    HPAiHPA008063.

    Interactioni

    Protein-protein interaction databases

    BioGridi109022. 3 interactions.
    IntActiP17900. 1 interaction.
    STRINGi9606.ENSP00000349687.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 406
    Turni41 – 433
    Beta strandi45 – 7430
    Beta strandi81 – 9010
    Beta strandi93 – 964
    Beta strandi103 – 1053
    Beta strandi107 – 1093
    Helixi111 – 1188
    Beta strandi121 – 1233
    Helixi129 – 1324
    Beta strandi137 – 1404
    Beta strandi142 – 15413
    Turni161 – 1633
    Beta strandi164 – 17613
    Beta strandi179 – 19214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 32-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17900.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47814.
    HOGENOMiHOG000031350.
    HOVERGENiHBG000260.
    InParanoidiP17900.
    KOiK12383.
    OMAiFSWENCD.
    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

    MQSLMQAPLL IALGLLLAAP AQAHLKKPSQ LSSFSWDNCD EGKDPAVIRS    50
    LTLEPDPIIV PGNVTLSVMG STSVPLSSPL KVDLVLEKEV AGLWIKIPCT 100
    DYIGSCTFEH FCDVLDMLIP TGEPCPEPLR TYGLPCHCPF KEGTYSLPKS 150
    EFVVPDLELP SWLTTGNYRI ESVLSSSGKR LGCIKIAASL KGI 193
    Length:193
    Mass (Da):20,838
    Last modified:November 13, 2007 - v4
    Checksum:i4EB1119945365F7E
    GO

    Sequence cautioni

    The sequence CAA43408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA43994.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391C → R in BAG35396. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191A → T.5 Publications
    Corresponds to variant rs1048719 [ dbSNP | Ensembl ].
    VAR_013830
    Natural varianti59 – 591I → V.6 Publications
    Corresponds to variant rs153477 [ dbSNP | Ensembl ].
    VAR_036892
    Natural varianti69 – 691M → V.7 Publications
    Corresponds to variant rs153478 [ dbSNP | Ensembl ].
    VAR_036893
    Natural varianti88 – 881Missing in GM2GAB. 1 Publication
    VAR_011697
    Natural varianti138 – 1381C → R in GM2GAB. 1 Publication
    VAR_006947
    Natural varianti169 – 1691R → P in GM2GAB. 1 Publication
    VAR_011698

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.4. human.

    Polymorphism databases

    DMDMi160331912.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GM2Adb

    GM2A mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4313.1.
    PIRi I54178.
    S13195.
    S22411.
    RefSeqi NP_000396.2. NM_000405.4.
    UniGenei Hs.483873.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G13 X-ray 2.00 A/B/C 32-193 [» ]
    1PU5 X-ray 1.90 A/B/C 32-193 [» ]
    1PUB X-ray 2.51 A 32-193 [» ]
    1TJJ X-ray 2.00 A/B/C 32-193 [» ]
    2AF9 X-ray 2.00 A 32-193 [» ]
    2AG2 X-ray 2.00 A/B/C 32-193 [» ]
    2AG4 X-ray 1.80 A/B 32-193 [» ]
    2AG9 X-ray 2.20 A/B 32-193 [» ]
    ProteinModelPortali P17900.
    SMRi P17900. Positions 32-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109022. 3 interactions.
    IntActi P17900. 1 interaction.
    STRINGi 9606.ENSP00000349687.

    Polymorphism databases

    DMDMi 160331912.

    Proteomic databases

    MaxQBi P17900.
    PaxDbi P17900.
    PRIDEi P17900.

    Protocols and materials databases

    DNASUi 2760.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357164 ; ENSP00000349687 ; ENSG00000196743 .
    GeneIDi 2760.
    KEGGi hsa:2760.
    UCSCi uc003ltr.4. human.

    Organism-specific databases

    CTDi 2760.
    GeneCardsi GC05P150612.
    H-InvDB HIX0005327.
    HGNCi HGNC:4367. GM2A.
    HPAi HPA008063.
    MIMi 272750. phenotype.
    613109. gene.
    neXtProti NX_P17900.
    Orphaneti 309246. GM2-gangliosidosis, AB variant.
    PharmGKBi PA28752.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47814.
    HOGENOMi HOG000031350.
    HOVERGENi HBG000260.
    InParanoidi P17900.
    KOi K12383.
    OMAi FSWENCD.
    PhylomeDBi P17900.
    TreeFami TF353575.

    Enzyme and pathway databases

    Reactomei REACT_116105. Glycosphingolipid metabolism.

    Miscellaneous databases

    ChiTaRSi GM2A. human.
    EvolutionaryTracei P17900.
    GeneWikii GM2A.
    GenomeRNAii 2760.
    NextBioi 10860.
    PROi P17900.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17900.
    Bgeei P17900.
    CleanExi HS_GM2A.
    Genevestigatori P17900.

    Family and domain databases

    InterProi IPR028996. GM2-AP.
    IPR003172. ML_dom.
    [Graphical view ]
    PANTHERi PTHR17357. PTHR17357. 1 hit.
    Pfami PF02221. E1_DerP2_DerF2. 1 hit.
    [Graphical view ]
    SMARTi SM00737. ML. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and expression of a full-length cDNA encoding the human G-M2 activator protein."
      Xie B., McInnes B., Neote K., Lamhonwah A.-M., Mahuran D.
      Biochem. Biophys. Res. Commun. 177:1217-1223(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-59 AND VAL-69.
    2. "Characterization of full-length cDNAs and the gene coding for the human GM2 activator protein."
      Klima H., Tanaka A., Schnabel D., Nakano T., Schroeder M., Suzuki K., Sandhoff K.
      FEBS Lett. 289:260-264(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-19; VAL-59 AND VAL-69.
    3. "Evidence for two cDNAs encoding human GM2-activator protein."
      Nagarajan S., Chen H.C., Li S.C., Li Y.T., Lockyer J.
      Biochem. J. 282:807-813(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    4. "Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5."
      Xie B., Kennedy J.L., McInnes B., Auger D., Mahuran D.J.
      Genomics 14:796-798(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-19; VAL-59 AND VAL-69.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-19 AND VAL-69.
      Tissue: Substantia nigra.
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Structure of the GM2A gene: identification of an exon 2 nonsense mutation and a naturally occurring transcript with an in-frame deletion of exon 2."
      Chen B., Rigat B., Curry C., Mahuran D.J.
      Am. J. Hum. Genet. 65:77-87(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-19; VAL-59 AND VAL-69.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-59 AND VAL-69.
      Tissue: Uterus.
    10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-193, VARIANTS THR-19; VAL-59 AND VAL-69.
    11. "The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein."
      Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.
      Eur. J. Biochem. 192:709-714(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-193.
      Tissue: Kidney.
    12. "Crystal structure of human GM2-activator protein with a novel beta-cup topology."
      Wright C.S., Li S.-C., Rastinejad F.
      J. Mol. Biol. 304:411-422(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    13. "A mutation in the gene of a glycolipid-binding protein (GM2 activator) that causes GM2-gangliosidosis variant AB."
      Schroeder M., Schnabel D., Suzuki K., Sandhoff K.
      FEBS Lett. 290:1-3(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2GAB ARG-138.
    14. "Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation and expression in BHK cells."
      Schroder M., Schnabel D., Hurwitz R., Young E., Suzuki K., Sandhoff K.
      Hum. Genet. 92:437-440(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2GAB PRO-169.
    15. "Molecular analysis of a GM2-activator deficiency in two patients with GM2-gangliosidosis AB variant."
      Schepers U., Glombitza G., Lemm T., Hoffmann A., Chabas A., Ozand P., Sandhoff K.
      Am. J. Hum. Genet. 59:1048-1056(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2GAB LYS-88 DEL.

    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: October 1, 2014
    This is version 151 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

    External Data

    Dasty 3