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Q9BT40

- INP5K_HUMAN

UniProt

Q9BT40 - INP5K_HUMAN

Protein

Inositol polyphosphate 5-phosphatase K

Gene

INPP5K

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. May negatively regulate assembly of the actin cytoskeleton.1 Publication

    Catalytic activityi

    D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate.1 Publication

    GO - Molecular functioni

    1. inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Source: UniProtKB-EC
    2. inositol-1,4,5-trisphosphate 5-phosphatase activity Source: UniProtKB-EC
    3. inositol bisphosphate phosphatase activity Source: MGI
    4. inositol-polyphosphate 5-phosphatase activity Source: UniProtKB-EC
    5. inositol trisphosphate phosphatase activity Source: MGI
    6. lipid phosphatase activity Source: UniProtKB
    7. phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Source: UniProtKB
    8. phosphatidylinositol phosphate 5-phosphatase activity Source: UniProtKB
    9. phosphatidylinositol trisphosphate phosphatase activity Source: UniProtKB
    10. protein binding Source: UniProtKB
    11. vasopressin receptor activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. cellular response to cAMP Source: UniProtKB
    3. cellular response to epidermal growth factor stimulus Source: UniProtKB
    4. cellular response to hormone stimulus Source: UniProtKB
    5. cellular response to insulin stimulus Source: UniProtKB
    6. cellular response to tumor necrosis factor Source: UniProtKB
    7. dephosphorylation Source: GOC
    8. glucose homeostasis Source: UniProtKB
    9. G-protein coupled receptor signaling pathway Source: UniProtKB
    10. inositol phosphate dephosphorylation Source: MGI
    11. in utero embryonic development Source: Ensembl
    12. negative regulation by host of viral transcription Source: UniProtKB
    13. negative regulation of calcium ion transport Source: UniProtKB
    14. negative regulation of dephosphorylation Source: UniProtKB
    15. negative regulation of glucose transport Source: UniProtKB
    16. negative regulation of glycogen (starch) synthase activity Source: UniProtKB
    17. negative regulation of glycogen biosynthetic process Source: UniProtKB
    18. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    19. negative regulation of MAP kinase activity Source: UniProtKB
    20. negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
    21. negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
    22. negative regulation of protein kinase activity Source: UniProtKB
    23. negative regulation of protein kinase B signaling Source: UniProtKB
    24. negative regulation of protein phosphorylation Source: UniProtKB
    25. negative regulation of protein targeting to membrane Source: UniProtKB
    26. negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
    27. negative regulation of stress fiber assembly Source: UniProtKB
    28. negative regulation of transcription, DNA-templated Source: UniProtKB
    29. phosphatidylinositol biosynthetic process Source: Reactome
    30. phosphatidylinositol dephosphorylation Source: UniProtKB
    31. phospholipid metabolic process Source: Reactome
    32. positive regulation of renal water transport Source: UniProtKB
    33. positive regulation of transcription, DNA-templated Source: UniProtKB
    34. positive regulation of urine volume Source: UniProtKB
    35. protein targeting to plasma membrane Source: UniProtKB
    36. regulation of glycogen biosynthetic process Source: UniProtKB
    37. ruffle assembly Source: UniProtKB
    38. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05626-MONOMER.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol polyphosphate 5-phosphatase K (EC:3.1.3.56)
    Alternative name(s):
    Skeletal muscle and kidney-enriched inositol phosphatase
    Gene namesi
    Name:INPP5K
    Synonyms:PPS, SKIP
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:33882. INPP5K.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication
    Note: Following stimulation with EGF, translocates to membrane ruffles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. membrane Source: UniProtKB
    5. neuron projection Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. plasma membrane Source: UniProtKB
    9. ruffle Source: MGI
    10. ruffle membrane Source: UniProtKB
    11. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi349 – 3491Y → A or F: No effect on EGF-induced ruffle localization. 1 Publication
    Mutagenesisi361 – 3611D → A: Significant decrease in EGF-induced ruffle localization. 1 Publication
    Mutagenesisi362 – 3621W → A: Significant decrease in EGF-induced ruffle localization. 1 Publication
    Mutagenesisi376 – 3761Y → A or F: No effect on EGF-induced ruffle localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA164720951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Inositol polyphosphate 5-phosphatase KPRO_0000209727Add
    BLAST

    Proteomic databases

    MaxQBiQ9BT40.
    PaxDbiQ9BT40.
    PRIDEiQ9BT40.

    PTM databases

    PhosphoSiteiQ9BT40.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels in skeletal muscle, heart and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9BT40.
    BgeeiQ9BT40.
    CleanExiHS_INPP5K.
    GenevestigatoriQ9BT40.

    Organism-specific databases

    HPAiHPA031044.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LNX1Q8TBB13EBI-749162,EBI-739832

    Protein-protein interaction databases

    BioGridi119720. 17 interactions.
    IntActiQ9BT40. 13 interactions.
    MINTiMINT-1445023.
    STRINGi9606.ENSP00000254712.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BT40.
    SMRiQ9BT40. Positions 20-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni16 – 318303CatalyticSequence AnalysisAdd
    BLAST
    Regioni321 – 448128Required for ruffle localizationAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5411.
    HOGENOMiHOG000046051.
    HOVERGENiHBG082135.
    InParanoidiQ9BT40.
    KOiK01106.
    OMAiGLYGYWG.
    PhylomeDBiQ9BT40.
    TreeFamiTF317034.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    [Graphical view]
    SMARTiSM00128. IPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9BT40-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSRKLSGPK GRRLSIHVVT WNVASAAPPL DLSDLLQLNN RNLNLDIYVI    50
    GLQELNSGII SLLSDAAFND SWSSFLMDVL SPLSFIKVSH VRMQGILLLV 100
    FAKYQHLPYI QILSTKSTPT GLFGYWGNKG GVNICLKLYG YYVSIINCHL 150
    PPHISNNYQR LEHFDRILEM QNCEGRDIPN ILDHDLIIWF GDMNFRIEDF 200
    GLHFVRESIK NRCYGGLWEK DQLSIAKKHD PLLREFQEGR LLFPPTYKFD 250
    RNSNDYDTSE KKRKPAWTDR ILWRLKRQPC AGPDTPIPPA SHFSLSLRGY 300
    SSHMTYGISD HKPVSGTFDL ELKPLVSAPL IVLMPEDLWT VENDMMVSYS 350
    STSDFPSSPW DWIGLYKVGL RDVNDYVSYA WVGDSKVSCS DNLNQVYIDI 400
    SNIPTTEDEF LLCYYSNSLR SVVGISRPFQ IPPGSLREDP LGEAQPQI 448
    Length:448
    Mass (Da):51,090
    Last modified:October 17, 2006 - v3
    Checksum:i46FAA48C6E2EEAD4
    GO
    Isoform 21 Publication (identifier: Q9BT40-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-76: Missing.

    Show »
    Length:372
    Mass (Da):42,784
    Checksum:iE257B4890DCD44F3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201T → A in AAB03214. 1 PublicationCurated
    Sequence conflicti416 – 4161S → R in BAA92340. (PubMed:10753883)Curated
    Sequence conflicti416 – 4161S → R in BAA92341. (PubMed:10753883)Curated
    Sequence conflicti416 – 4161S → R in BAA92342. (PubMed:10753883)Curated
    Sequence conflicti416 – 4161S → R in AAB03214. 1 PublicationCurated
    Sequence conflicti426 – 4261S → R in BAA92340. (PubMed:10753883)Curated
    Sequence conflicti426 – 4261S → R in BAA92341. (PubMed:10753883)Curated
    Sequence conflicti426 – 4261S → R in BAA92342. (PubMed:10753883)Curated
    Sequence conflicti426 – 4261S → R in AAB03214. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti315 – 3151S → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036497

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7676Missing in isoform 2. 2 PublicationsVSP_050612Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB036829 mRNA. Translation: BAA92340.1.
    AB036830 mRNA. Translation: BAA92341.1.
    AB036831 Genomic DNA. Translation: BAA92342.1.
    AK312585 mRNA. Translation: BAG35479.1.
    AK312844 mRNA. Translation: BAG35697.1.
    CH471108 Genomic DNA. Translation: EAW90614.1.
    CH471108 Genomic DNA. Translation: EAW90615.1.
    CH471108 Genomic DNA. Translation: EAW90618.1.
    BC004362 mRNA. Translation: AAH04362.1.
    U45973 mRNA. Translation: AAB03214.1.
    CCDSiCCDS11004.1. [Q9BT40-1]
    CCDS11005.1. [Q9BT40-2]
    RefSeqiNP_001129114.1. NM_001135642.1. [Q9BT40-2]
    NP_057616.2. NM_016532.3. [Q9BT40-1]
    NP_570122.1. NM_130766.2. [Q9BT40-2]
    XP_005256740.1. XM_005256683.1. [Q9BT40-2]
    XP_006721608.1. XM_006721545.1. [Q9BT40-2]
    UniGeneiHs.632238.

    Genome annotation databases

    EnsembliENST00000320345; ENSP00000318476; ENSG00000132376. [Q9BT40-2]
    ENST00000406424; ENSP00000385177; ENSG00000132376. [Q9BT40-2]
    ENST00000421807; ENSP00000413937; ENSG00000132376. [Q9BT40-1]
    GeneIDi51763.
    KEGGihsa:51763.
    UCSCiuc002fsq.3. human. [Q9BT40-1]

    Polymorphism databases

    DMDMi116242791.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB036829 mRNA. Translation: BAA92340.1 .
    AB036830 mRNA. Translation: BAA92341.1 .
    AB036831 Genomic DNA. Translation: BAA92342.1 .
    AK312585 mRNA. Translation: BAG35479.1 .
    AK312844 mRNA. Translation: BAG35697.1 .
    CH471108 Genomic DNA. Translation: EAW90614.1 .
    CH471108 Genomic DNA. Translation: EAW90615.1 .
    CH471108 Genomic DNA. Translation: EAW90618.1 .
    BC004362 mRNA. Translation: AAH04362.1 .
    U45973 mRNA. Translation: AAB03214.1 .
    CCDSi CCDS11004.1. [Q9BT40-1 ]
    CCDS11005.1. [Q9BT40-2 ]
    RefSeqi NP_001129114.1. NM_001135642.1. [Q9BT40-2 ]
    NP_057616.2. NM_016532.3. [Q9BT40-1 ]
    NP_570122.1. NM_130766.2. [Q9BT40-2 ]
    XP_005256740.1. XM_005256683.1. [Q9BT40-2 ]
    XP_006721608.1. XM_006721545.1. [Q9BT40-2 ]
    UniGenei Hs.632238.

    3D structure databases

    ProteinModelPortali Q9BT40.
    SMRi Q9BT40. Positions 20-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119720. 17 interactions.
    IntActi Q9BT40. 13 interactions.
    MINTi MINT-1445023.
    STRINGi 9606.ENSP00000254712.

    PTM databases

    PhosphoSitei Q9BT40.

    Polymorphism databases

    DMDMi 116242791.

    Proteomic databases

    MaxQBi Q9BT40.
    PaxDbi Q9BT40.
    PRIDEi Q9BT40.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320345 ; ENSP00000318476 ; ENSG00000132376 . [Q9BT40-2 ]
    ENST00000406424 ; ENSP00000385177 ; ENSG00000132376 . [Q9BT40-2 ]
    ENST00000421807 ; ENSP00000413937 ; ENSG00000132376 . [Q9BT40-1 ]
    GeneIDi 51763.
    KEGGi hsa:51763.
    UCSCi uc002fsq.3. human. [Q9BT40-1 ]

    Organism-specific databases

    CTDi 51763.
    GeneCardsi GC17M001397.
    HGNCi HGNC:33882. INPP5K.
    HPAi HPA031044.
    MIMi 607875. gene.
    neXtProti NX_Q9BT40.
    PharmGKBi PA164720951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5411.
    HOGENOMi HOG000046051.
    HOVERGENi HBG082135.
    InParanoidi Q9BT40.
    KOi K01106.
    OMAi GLYGYWG.
    PhylomeDBi Q9BT40.
    TreeFami TF317034.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05626-MONOMER.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    GeneWikii SKIP.
    GenomeRNAii 51763.
    NextBioi 55878.
    PROi Q9BT40.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BT40.
    Bgeei Q9BT40.
    CleanExi HS_INPP5K.
    Genevestigatori Q9BT40.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    [Graphical view ]
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    SMARTi SM00128. IPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel inositol polyphosphate 5-phosphatase."
      Ijuin T., Mochizuki Y., Fukami K., Funaki M., Asano T., Takenawa T.
      J. Biol. Chem. 275:10870-10875(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Testis1 Publication.
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: EyeImported.
    5. Nussbaum R.L.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 120-448.
      Tissue: BrainImported.
    6. "Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase SKIP localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation."
      Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D., Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.
      J. Biol. Chem. 278:11376-11385(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-349; ASP-361; TRP-362 AND TYR-376.
    7. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-315.

    Entry informationi

    Entry nameiINP5K_HUMAN
    AccessioniPrimary (citable) accession number: Q9BT40
    Secondary accession number(s): B2R6I2
    , B2R750, D3DTH8, Q15733, Q9NPJ5, Q9P2R5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3