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Q08AH3

- ACS2A_HUMAN

UniProt

Q08AH3 - ACS2A_HUMAN

Protein

Acyl-coenzyme A synthetase ACSM2A, mitochondrial

Gene

ACSM2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 2 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C4 to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) By similarity.By similarity

    Catalytic activityi

    ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA.

    Cofactori

    Magnesium or manganese.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei139 – 1391Coenzyme A
    Binding sitei364 – 3641Substrate
    Binding sitei446 – 4461ATP
    Binding sitei461 – 4611ATP
    Binding sitei472 – 4721Substrate
    Binding sitei501 – 5011Coenzyme A
    Binding sitei532 – 5321Coenzyme A
    Binding sitei557 – 5571ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi221 – 2299ATP
    Nucleotide bindingi359 – 3646ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. butyrate-CoA ligase activity Source: BHF-UCL
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid metabolic process Source: UniProtKB-KW
    2. glucose homeostasis Source: BHF-UCL
    3. medium-chain fatty-acyl-CoA metabolic process Source: BHF-UCL
    4. triglyceride homeostasis Source: BHF-UCL

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_6812. Conjugation of salicylate with glycine.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A synthetase ACSM2A, mitochondrial (EC:6.2.1.2)
    Alternative name(s):
    Acyl-CoA synthetase medium-chain family member 2A
    Butyrate--CoA ligase 2A
    Butyryl-coenzyme A synthetase 2A
    Middle-chain acyl-CoA synthetase 2A
    Gene namesi
    Name:ACSM2A
    Synonyms:ACSM2, MACS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:32017. ACSM2A.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162375402.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4646MitochondrionSequence AnalysisAdd
    BLAST
    Chaini47 – 577531Acyl-coenzyme A synthetase ACSM2A, mitochondrialPRO_0000306093Add
    BLAST

    Proteomic databases

    MaxQBiQ08AH3.
    PaxDbiQ08AH3.
    PRIDEiQ08AH3.

    PTM databases

    PhosphoSiteiQ08AH3.

    Expressioni

    Gene expression databases

    BgeeiQ08AH3.
    GenevestigatoriQ08AH3.

    Organism-specific databases

    HPAiHPA057699.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000219054.

    Structurei

    Secondary structure

    1
    577
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni34 – 363
    Helixi46 – 494
    Helixi51 – 599
    Beta strandi67 – 726
    Beta strandi74 – 763
    Beta strandi78 – 825
    Helixi83 – 9816
    Turni99 – 1013
    Beta strandi108 – 1125
    Helixi117 – 12913
    Beta strandi132 – 1354
    Helixi142 – 15211
    Beta strandi155 – 1606
    Turni161 – 1633
    Helixi164 – 1707
    Helixi171 – 1733
    Beta strandi179 – 1868
    Beta strandi191 – 1933
    Helixi194 – 2007
    Beta strandi214 – 2207
    Beta strandi224 – 2274
    Beta strandi230 – 2345
    Helixi235 – 24511
    Turni246 – 2494
    Beta strandi256 – 2594
    Helixi266 – 2716
    Helixi274 – 2785
    Beta strandi282 – 2865
    Helixi293 – 30210
    Beta strandi307 – 3104
    Helixi312 – 3198
    Turni323 – 3253
    Beta strandi333 – 3397
    Helixi343 – 35311
    Beta strandi358 – 3636
    Turni364 – 3663
    Beta strandi367 – 3715
    Beta strandi392 – 3954
    Beta strandi408 – 4136
    Beta strandi415 – 4173
    Helixi430 – 4356
    Beta strandi441 – 45010
    Beta strandi456 – 4616
    Helixi462 – 4643
    Beta strandi466 – 4683
    Beta strandi471 – 4733
    Helixi475 – 4839
    Beta strandi488 – 49811
    Turni499 – 5013
    Beta strandi502 – 51110
    Helixi513 – 5153
    Helixi520 – 53415
    Helixi537 – 5393
    Beta strandi542 – 5487
    Helixi560 – 5678

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VZEX-ray2.45A/B/C32-577[»]
    2WD9X-ray2.60A/B/C32-576[»]
    3B7WX-ray2.00A32-577[»]
    3C5EX-ray1.60A32-577[»]
    3DAYX-ray1.95A32-577[»]
    3EQ6X-ray2.40A/B32-577[»]
    3GPCX-ray1.90A/B32-577[»]
    ProteinModelPortaliQ08AH3.
    SMRiQ08AH3. Positions 34-569.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08AH3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni469 – 4713Coenzyme A binding
    Regioni540 – 5423Coenzyme A binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229982.
    HOVERGENiHBG053031.
    InParanoidiQ08AH3.
    KOiK01896.
    OMAiTIQMKAK.
    OrthoDBiEOG7D85VZ.
    PhylomeDBiQ08AH3.
    TreeFamiTF354264.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q08AH3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV    50
    LDHWADMEKA GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANVLSGA 100
    CGLQRGDRVA VVLPRVPEWW LVILGCIRAG LIFMPGTIQM KSTDILYRLQ 150
    MSKAKAIVAG DEVIQEVDTV ASECPSLRIK LLVSEKSCDG WLNFKKLLNE 200
    ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL KAKMDAGWTG 250
    LQASDIMWTI SDTGWILNIL CSLMEPWALG ACTFVHLLPK FDPLVILKTL 300
    SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCVTVGES LLPETLENWR 350
    AQTGLDIRES YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQIIDDKGN 400
    VLPPGTEGDI GIRVKPIRPI GIFSGYVDNP DKTAANIRGD FWLLGDRGIK 450
    DEDGYFQFMG RANDIINSSG YRIGPSEVEN ALMEHPAVVE TAVISSPDPV 500
    RGEVVKAFVV LASQFLSHDP EQLTKELQQH VKSVTAPYKY PRKIEFVLNL 550
    PKTVTGKIQR AKLRDKEWKM SGKARAQ 577
    Length:577
    Mass (Da):64,223
    Last modified:September 1, 2009 - v2
    Checksum:i16167FC69562436F
    GO

    Sequence cautioni

    The sequence AAC23497.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti463 – 4631N → D in BAG53201. (PubMed:14702039)Curated
    Sequence conflicti463 – 4631N → D in AAI25177. (PubMed:15489334)Curated
    Sequence conflicti463 – 4631N → D in AAC23497. (PubMed:10493829)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti335 – 3351V → L.
    Corresponds to variant rs4643305 [ dbSNP | Ensembl ].
    VAR_058692
    Natural varianti336 – 3361T → A.
    Corresponds to variant rs5002299 [ dbSNP | Ensembl ].
    VAR_058693
    Natural varianti337 – 3371V → G.
    Corresponds to variant rs4586421 [ dbSNP | Ensembl ].
    VAR_058694
    Natural varianti513 – 5131S → L.3 Publications
    Corresponds to variant rs1133607 [ dbSNP | Ensembl ].
    VAR_035247
    Natural varianti561 – 5611A → T.
    Corresponds to variant rs1054977 [ dbSNP | Ensembl ].
    VAR_035248

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK096039 mRNA. Translation: BAG53201.1.
    AC137056 Genomic DNA. No translation available.
    BC125176 mRNA. Translation: AAI25177.1.
    AC003034 Genomic DNA. Translation: AAC23497.1. Sequence problems.
    CCDSiCCDS32401.1.
    RefSeqiNP_001010845.1. NM_001010845.2.
    XP_005255150.1. XM_005255093.1.
    UniGeneiHs.298252.
    Hs.656497.

    Genome annotation databases

    EnsembliENST00000219054; ENSP00000219054; ENSG00000183747.
    ENST00000396104; ENSP00000379411; ENSG00000183747.
    ENST00000573854; ENSP00000459451; ENSG00000183747.
    ENST00000575690; ENSP00000460349; ENSG00000183747.
    GeneIDi123876.
    KEGGihsa:123876.
    UCSCiuc002dhf.4. human.

    Polymorphism databases

    DMDMi257050995.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK096039 mRNA. Translation: BAG53201.1 .
    AC137056 Genomic DNA. No translation available.
    BC125176 mRNA. Translation: AAI25177.1 .
    AC003034 Genomic DNA. Translation: AAC23497.1 . Sequence problems.
    CCDSi CCDS32401.1.
    RefSeqi NP_001010845.1. NM_001010845.2.
    XP_005255150.1. XM_005255093.1.
    UniGenei Hs.298252.
    Hs.656497.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VZE X-ray 2.45 A/B/C 32-577 [» ]
    2WD9 X-ray 2.60 A/B/C 32-576 [» ]
    3B7W X-ray 2.00 A 32-577 [» ]
    3C5E X-ray 1.60 A 32-577 [» ]
    3DAY X-ray 1.95 A 32-577 [» ]
    3EQ6 X-ray 2.40 A/B 32-577 [» ]
    3GPC X-ray 1.90 A/B 32-577 [» ]
    ProteinModelPortali Q08AH3.
    SMRi Q08AH3. Positions 34-569.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000219054.

    PTM databases

    PhosphoSitei Q08AH3.

    Polymorphism databases

    DMDMi 257050995.

    Proteomic databases

    MaxQBi Q08AH3.
    PaxDbi Q08AH3.
    PRIDEi Q08AH3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219054 ; ENSP00000219054 ; ENSG00000183747 .
    ENST00000396104 ; ENSP00000379411 ; ENSG00000183747 .
    ENST00000573854 ; ENSP00000459451 ; ENSG00000183747 .
    ENST00000575690 ; ENSP00000460349 ; ENSG00000183747 .
    GeneIDi 123876.
    KEGGi hsa:123876.
    UCSCi uc002dhf.4. human.

    Organism-specific databases

    CTDi 123876.
    GeneCardsi GC16P020463.
    H-InvDB HIX0012859.
    HGNCi HGNC:32017. ACSM2A.
    HPAi HPA057699.
    MIMi 614358. gene.
    neXtProti NX_Q08AH3.
    PharmGKBi PA162375402.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000229982.
    HOVERGENi HBG053031.
    InParanoidi Q08AH3.
    KOi K01896.
    OMAi TIQMKAK.
    OrthoDBi EOG7D85VZ.
    PhylomeDBi Q08AH3.
    TreeFami TF354264.

    Enzyme and pathway databases

    Reactomei REACT_6812. Conjugation of salicylate with glycine.

    Miscellaneous databases

    EvolutionaryTracei Q08AH3.
    GenomeRNAii 123876.
    NextBioi 81177.
    PROi Q08AH3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q08AH3.
    Genevestigatori Q08AH3.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Kidney.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 299-577, VARIANT LEU-513.
    5. "Crystal structure of L64P mutant of human acyl-CoA synthetase medium-chain family member 2A."
      Structural genomics consortium (SGC)
      Submitted (FEB-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.
    6. "Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A."
      Kochan G., Pilka E.S., von Delft F., Oppermann U., Yue W.W.
      J. Mol. Biol. 388:997-1008(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 32-577 IN COMPLEXES WITH ATP; COENZYME A; IBUPROFEN AND MAGNESIUM.
    7. "An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors."
      Iwai N., Mannami T., Tomoike H., Ono K., Iwanaga Y.
      Hypertension 41:1041-1046(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-513.
    8. "The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population."
      Lindner I., Rubin D., Helwig U., Nitz I., Hampe J., Schreiber S., Schrezenmeir J., Doering F.
      Mol. Nutr. Food Res. 50:270-274(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-513.

    Entry informationi

    Entry nameiACS2A_HUMAN
    AccessioniPrimary (citable) accession number: Q08AH3
    Secondary accession number(s): B3KTT9, O75202
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 68 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3