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P17900

- SAP3_HUMAN

UniProt

P17900 - SAP3_HUMAN

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Protein

Ganglioside GM2 activator

Gene

GM2A

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  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
Complete GO annotation...

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: UniProtKB
  4. lysosomal lumen Source: Reactome
  5. mitochondrion Source: Ensembl
Complete GO annotation...

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

BgeeiP17900.
CleanExiHS_GM2A.
ExpressionAtlasiP17900. baseline and differential.
GenevestigatoriP17900.

Organism-specific databases

HPAiHPA008063.

Interactioni

Protein-protein interaction databases

BioGridi109022. 12 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.
GeneTreeiENSGT00390000003288.
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

        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 CAA43408.1 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. 12 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.
GeneTreei ENSGT00390000003288.
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

Bgeei P17900.
CleanExi HS_GM2A.
ExpressionAtlasi P17900. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 152 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