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P07305

- H10_HUMAN

UniProt

P07305 - H10_HUMAN

Protein

Histone H1.0

Gene

H1F0

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The H1F0 histones are found in cells that are in terminal stages of differentiation or that have low rates of cell division.

    GO - Molecular functioni

    1. chromatin DNA binding Source: UniProt
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic DNA fragmentation Source: Reactome
    2. apoptotic process Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_13462. Activation of DNA fragmentation factor.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H1.0
    Alternative name(s):
    Histone H1'
    Histone H1(0)
    Cleaved into the following chain:
    Gene namesi
    Name:H1F0
    Synonyms:H1FV
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4714. H1F0.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Chromosome 1 PublicationPROSITE-ProRule annotation
    Note: The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. Golgi apparatus Source: HPA
    3. nuclear chromatin Source: UniProtKB
    4. nuclear euchromatin Source: UniProt
    5. nucleoplasm Source: Reactome
    6. nucleosome Source: InterPro
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29092.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194Histone H1.0PRO_0000423207Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 194193Histone H1.0, N-terminally processedPRO_0000195904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; partial; in Histone H1.0, N-terminally processed2 Publications
    Modified residuei4 – 41Deamidated asparagine; partial1 Publication
    Modified residuei42 – 421CitrullineBy similarity

    Post-translational modificationi

    Phosphorylated on Ser-17 in RNA edited version.

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiP07305.
    PaxDbiP07305.
    PeptideAtlasiP07305.
    PRIDEiP07305.

    PTM databases

    PhosphoSiteiP07305.

    Expressioni

    Inductioni

    Both the unedited and the RNA edited versions are induced by butyrate (at protein level). Only RNA edited version is induced by DTT, vinblastine or TNF (at protein level).1 Publication

    Gene expression databases

    BgeeiP07305.
    CleanExiHS_H1F0.
    GenevestigatoriP07305.

    Organism-specific databases

    HPAiHPA000843.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E1P040142EBI-725224,EBI-7014446From a different organism.

    Protein-protein interaction databases

    BioGridi109260. 27 interactions.
    DIPiDIP-41775N.
    IntActiP07305. 8 interactions.
    MINTiMINT-276185.
    STRINGi9606.ENSP00000344504.

    Structurei

    3D structure databases

    ProteinModelPortaliP07305.
    SMRiP07305. Positions 25-97.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 9774H15PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the histone H1/H5 family.PROSITE-ProRule annotation
    Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG126832.
    HOGENOMiHOG000251627.
    HOVERGENiHBG069502.
    InParanoidiP07305.
    KOiK11275.
    OMAiDEPKRSV.
    OrthoDBiEOG75QR72.
    PhylomeDBiP07305.
    TreeFamiTF313664.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR005818. Histone_H1/H5_H15.
    IPR005819. Histone_H5.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00538. Linker_histone. 1 hit.
    [Graphical view]
    PRINTSiPR00624. HISTONEH5.
    SMARTiSM00526. H15. 1 hit.
    [Graphical view]
    PROSITEiPS51504. H15. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07305-1) [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

    MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI    50
    QKYIKSHYKV GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE 100
    PKKSVAFKKT KKEIKKVATP KKASKPKKAA SKAPTKKPKA TPVKKAKKKL 150
    AATPKKAKKP KTVKAKPVKA SKPKKAKPVK PKAKSSAKRA GKKK 194
    Length:194
    Mass (Da):20,863
    Last modified:January 23, 2007 - v3
    Checksum:i03ED6F01919F8BE1
    GO
    Isoform 2 (identifier: P07305-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3-19: Missing.

    Show »
    Length:177
    Mass (Da):19,167
    Checksum:i8CD558F288DB593A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651D → H in AAH29046. (PubMed:15489334)Curated

    RNA editingi

    Partially edited. In approximately 3.6% of the mRNA molecules, a new initiator methionine is created by a single uridine insertion in the 5'-UTR, causing an N-terminal extension of 99 amino acids. The existence of the RNA edited version is supported by direct protein sequencing by MS/MS of the following peptides specific to that version: 12-21; 22-33; 37-47; 48-67; 68-83; 84-94 and 97-113. The RNA edited version is called ET-H1.0.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 11M → MLGKGRQRRRRQRQRQSPVP RPSDRPAGLGLAKPARRALP TPEPGRKSSDSSLASPGAAL QTGPVVRGSGADPEAGFAQP PTRAGPLEGAFNSRTRQATM in RNA edited version.
    VAR_054789

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei3 – 1917Missing in isoform 2. 1 PublicationVSP_042163Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03473 Genomic DNA. Translation: CAA27190.1.
    CR456502 mRNA. Translation: CAG30388.1.
    CR542220 mRNA. Translation: CAG47016.1.
    AK299209 mRNA. Translation: BAG61248.1.
    AK312583 mRNA. Translation: BAG35477.1.
    Z97630 Genomic DNA. Translation: CAB42829.1.
    CH471095 Genomic DNA. Translation: EAW60188.1.
    BC000145 mRNA. Translation: AAH00145.1.
    BC029046 mRNA. Translation: AAH29046.1.
    CCDSiCCDS13956.1. [P07305-1]
    PIRiA24850. HSHU10.
    RefSeqiNP_005309.1. NM_005318.3. [P07305-1]
    UniGeneiHs.745024.

    Genome annotation databases

    EnsembliENST00000340857; ENSP00000344504; ENSG00000189060. [P07305-1]
    GeneIDi3005.
    KEGGihsa:3005.
    UCSCiuc003aty.3. human. [P07305-1]

    Polymorphism databases

    DMDMi121897.

    Keywords - Coding sequence diversityi

    Alternative splicing, RNA editing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Histone H1 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03473 Genomic DNA. Translation: CAA27190.1 .
    CR456502 mRNA. Translation: CAG30388.1 .
    CR542220 mRNA. Translation: CAG47016.1 .
    AK299209 mRNA. Translation: BAG61248.1 .
    AK312583 mRNA. Translation: BAG35477.1 .
    Z97630 Genomic DNA. Translation: CAB42829.1 .
    CH471095 Genomic DNA. Translation: EAW60188.1 .
    BC000145 mRNA. Translation: AAH00145.1 .
    BC029046 mRNA. Translation: AAH29046.1 .
    CCDSi CCDS13956.1. [P07305-1 ]
    PIRi A24850. HSHU10.
    RefSeqi NP_005309.1. NM_005318.3. [P07305-1 ]
    UniGenei Hs.745024.

    3D structure databases

    ProteinModelPortali P07305.
    SMRi P07305. Positions 25-97.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109260. 27 interactions.
    DIPi DIP-41775N.
    IntActi P07305. 8 interactions.
    MINTi MINT-276185.
    STRINGi 9606.ENSP00000344504.

    PTM databases

    PhosphoSitei P07305.

    Polymorphism databases

    DMDMi 121897.

    Proteomic databases

    MaxQBi P07305.
    PaxDbi P07305.
    PeptideAtlasi P07305.
    PRIDEi P07305.

    Protocols and materials databases

    DNASUi 3005.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340857 ; ENSP00000344504 ; ENSG00000189060 . [P07305-1 ]
    GeneIDi 3005.
    KEGGi hsa:3005.
    UCSCi uc003aty.3. human. [P07305-1 ]

    Organism-specific databases

    CTDi 3005.
    GeneCardsi GC22P038201.
    H-InvDB HIX0016454.
    HGNCi HGNC:4714. H1F0.
    HPAi HPA000843.
    MIMi 142708. gene.
    neXtProti NX_P07305.
    PharmGKBi PA29092.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG126832.
    HOGENOMi HOG000251627.
    HOVERGENi HBG069502.
    InParanoidi P07305.
    KOi K11275.
    OMAi DEPKRSV.
    OrthoDBi EOG75QR72.
    PhylomeDBi P07305.
    TreeFami TF313664.

    Enzyme and pathway databases

    Reactomei REACT_13462. Activation of DNA fragmentation factor.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

    Miscellaneous databases

    ChiTaRSi H1F0. human.
    GenomeRNAii 3005.
    NextBioi 11916.
    PROi P07305.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07305.
    CleanExi HS_H1F0.
    Genevestigatori P07305.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR005818. Histone_H1/H5_H15.
    IPR005819. Histone_H5.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00538. Linker_histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00624. HISTONEH5.
    SMARTi SM00526. H15. 1 hit.
    [Graphical view ]
    PROSITEi PS51504. H15. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential distribution of lysine and arginine residues in the closely related histones H1 and H5. Analysis of a human H1 gene."
      Doenecke D., Tonjes R.
      J. Mol. Biol. 187:461-464(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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.
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Colon and Placenta.
    8. Cited for: PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), IDENTIFICATION BY MASS SPECTROMETRY, RNA EDITING, SUBCELLULAR LOCATION, INDUCTION.
    9. "The microheterogeneity of the mammalian H1(0) histone. Evidence for an age-dependent deamidation."
      Lindner H., Sarg B., Hoertnagl B., Helliger W.
      J. Biol. Chem. 273:13324-13330(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT THR-2, CLEAVAGE OF INITIATOR METHIONINE, DEAMIDATION AT ASN-4.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiH10_HUMAN
    AccessioniPrimary (citable) accession number: P07305
    Secondary accession number(s): B2R6I0
    , B4DRD6, Q6FG88, Q8N6R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3