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Q9HCI7

- MSL2_HUMAN

UniProt

Q9HCI7 - MSL2_HUMAN

Protein

E3 ubiquitin-protein ligase MSL2

Gene

MSL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri44 – 8542RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H4-K16 acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase MSL2 (EC:6.3.2.-)
    Alternative name(s):
    Male-specific lethal 2-like 1
    Short name:
    MSL2-like 1
    Male-specific lethal-2 homolog
    Short name:
    MSL-2
    Male-specific lethal-2 homolog 1
    RING finger protein 184
    Gene namesi
    Name:MSL2
    Synonyms:KIAA1585, MSL2L1, RNF184
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:25544. MSL2.

    Subcellular locationi

    GO - Cellular componenti

    1. MSL complex Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641H → Y: Great redution in H2B ubiquitination. No effect on MSL1-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA164723152.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 577577E3 ubiquitin-protein ligase MSL2PRO_0000299536Add
    BLAST

    Proteomic databases

    MaxQBiQ9HCI7.
    PaxDbiQ9HCI7.
    PRIDEiQ9HCI7.

    PTM databases

    PhosphoSiteiQ9HCI7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HCI7.
    BgeeiQ9HCI7.
    CleanExiHS_MSL2.
    GenevestigatoriQ9HCI7.

    Organism-specific databases

    HPAiHPA003413.

    Interactioni

    Subunit structurei

    Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and MSL3. Forms a MSL heterotetrameric core with MSL1.1 Publication

    Protein-protein interaction databases

    BioGridi120467. 21 interactions.
    IntActiQ9HCI7. 7 interactions.
    STRINGi9606.ENSP00000311827.

    Structurei

    Secondary structure

    1
    577
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Helixi25 – 4016
    Turni45 – 473
    Beta strandi48 – 503
    Helixi68 – 703
    Beta strandi77 – 793
    Turni82 – 843
    Helixi94 – 11421

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B7YX-ray3.25C/D1-116[»]
    4B86X-ray3.50C/D/G/H/K/L1-116[»]
    ProteinModelPortaliQ9HCI7.
    SMRiQ9HCI7. Positions 1-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 116116Sufficient for interaction with MSL1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi396 – 46368Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MSL2 family.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri44 – 8542RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG86640.
    HOGENOMiHOG000043091.
    HOVERGENiHBG108149.
    InParanoidiQ9HCI7.
    KOiK13164.
    OMAiNVMPGSP.
    OrthoDBiEOG7JX33Z.
    PhylomeDBiQ9HCI7.
    TreeFamiTF328848.

    Family and domain databases

    InterProiIPR001841. Znf_RING.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HCI7-1) [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

    MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL    50
    LQDPIAPTNS TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV 100
    NCYKKLCEYI TQTTLARDII EAVDCSSDIL ALLNDGSLFC EETEKPSDSS 150
    FTLCLTHSPL PSTSEPTTDP QASLSPMSES TLSIAIGSSV INGLPTYNGL 200
    SIDRFGINIP SPEHSNTIDV CNTVDIKTED LSDSLPPVCD TVATDLCSTG 250
    IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN 300
    GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKIAKLNR KRSRSESDSE 350
    KVQPLPISTI IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT 400
    VLLSTKSMKK SHEHGSKKSH SKTKPGILKK DKAVKEKIPS HHFMPGSPTK 450
    TVYKKPQEKK GCKCGRATQN PSVLTCRGQR CPCYSNRKAC LDCICRGCQN 500
    SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS TSTSVINVTG 550
    SPVTTFLAAS THDDKSLDEA IDMRFDC 577
    Length:577
    Mass (Da):62,541
    Last modified:September 11, 2007 - v2
    Checksum:i756C7625E0AF1CA6
    GO
    Isoform 2 (identifier: Q9HCI7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:503
    Mass (Da):54,339
    Checksum:iF591F7182AA9937D
    GO

    Sequence cautioni

    The sequence AAH32719.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA91673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB13411.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti348 – 3481D → E in BAG63776. (PubMed:14702039)Curated
    Sequence conflicti411 – 4111S → G in BAA91673. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7474Missing in isoform 2. 1 PublicationVSP_046200Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046805 mRNA. Translation: BAB13411.1. Different initiation.
    AK001408 mRNA. Translation: BAA91673.1. Different initiation.
    AK302491 mRNA. Translation: BAG63776.1.
    AL834289 mRNA. Translation: CAD38963.2.
    AC092991 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79119.1.
    CH471052 Genomic DNA. Translation: EAW79120.1.
    BC032719 mRNA. Translation: AAH32719.1. Different initiation.
    BC093764 mRNA. Translation: AAH93764.1.
    BC093790 mRNA. Translation: AAH93790.1.
    CCDSiCCDS33861.1. [Q9HCI7-1]
    CCDS46922.1. [Q9HCI7-2]
    RefSeqiNP_001138889.1. NM_001145417.1. [Q9HCI7-2]
    NP_060603.2. NM_018133.3. [Q9HCI7-1]
    XP_005247628.1. XM_005247571.1. [Q9HCI7-2]
    XP_005247629.1. XM_005247572.1. [Q9HCI7-2]
    XP_006713747.1. XM_006713684.1. [Q9HCI7-2]
    UniGeneiHs.18631.

    Genome annotation databases

    EnsembliENST00000309993; ENSP00000311827; ENSG00000174579. [Q9HCI7-1]
    ENST00000434835; ENSP00000387948; ENSG00000174579. [Q9HCI7-2]
    GeneIDi55167.
    KEGGihsa:55167.
    UCSCiuc003eqx.1. human. [Q9HCI7-1]

    Polymorphism databases

    DMDMi158564022.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046805 mRNA. Translation: BAB13411.1 . Different initiation.
    AK001408 mRNA. Translation: BAA91673.1 . Different initiation.
    AK302491 mRNA. Translation: BAG63776.1 .
    AL834289 mRNA. Translation: CAD38963.2 .
    AC092991 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79119.1 .
    CH471052 Genomic DNA. Translation: EAW79120.1 .
    BC032719 mRNA. Translation: AAH32719.1 . Different initiation.
    BC093764 mRNA. Translation: AAH93764.1 .
    BC093790 mRNA. Translation: AAH93790.1 .
    CCDSi CCDS33861.1. [Q9HCI7-1 ]
    CCDS46922.1. [Q9HCI7-2 ]
    RefSeqi NP_001138889.1. NM_001145417.1. [Q9HCI7-2 ]
    NP_060603.2. NM_018133.3. [Q9HCI7-1 ]
    XP_005247628.1. XM_005247571.1. [Q9HCI7-2 ]
    XP_005247629.1. XM_005247572.1. [Q9HCI7-2 ]
    XP_006713747.1. XM_006713684.1. [Q9HCI7-2 ]
    UniGenei Hs.18631.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B7Y X-ray 3.25 C/D 1-116 [» ]
    4B86 X-ray 3.50 C/D/G/H/K/L 1-116 [» ]
    ProteinModelPortali Q9HCI7.
    SMRi Q9HCI7. Positions 1-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120467. 21 interactions.
    IntActi Q9HCI7. 7 interactions.
    STRINGi 9606.ENSP00000311827.

    PTM databases

    PhosphoSitei Q9HCI7.

    Polymorphism databases

    DMDMi 158564022.

    Proteomic databases

    MaxQBi Q9HCI7.
    PaxDbi Q9HCI7.
    PRIDEi Q9HCI7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309993 ; ENSP00000311827 ; ENSG00000174579 . [Q9HCI7-1 ]
    ENST00000434835 ; ENSP00000387948 ; ENSG00000174579 . [Q9HCI7-2 ]
    GeneIDi 55167.
    KEGGi hsa:55167.
    UCSCi uc003eqx.1. human. [Q9HCI7-1 ]

    Organism-specific databases

    CTDi 55167.
    GeneCardsi GC03M135867.
    HGNCi HGNC:25544. MSL2.
    HPAi HPA003413.
    MIMi 614802. gene.
    neXtProti NX_Q9HCI7.
    PharmGKBi PA164723152.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86640.
    HOGENOMi HOG000043091.
    HOVERGENi HBG108149.
    InParanoidi Q9HCI7.
    KOi K13164.
    OMAi NVMPGSP.
    OrthoDBi EOG7JX33Z.
    PhylomeDBi Q9HCI7.
    TreeFami TF328848.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi MSL2. human.
    GenomeRNAii 55167.
    NextBioi 35476248.
    PROi Q9HCI7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCI7.
    Bgeei Q9HCI7.
    CleanExi HS_MSL2.
    Genevestigatori Q9HCI7.

    Family and domain databases

    InterProi IPR001841. Znf_RING.
    [Graphical view ]
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 339-577 (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph node.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain and Uterus.
    7. "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16."
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 25:9175-9188(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF MSL COMPLEX COMPONENTS, IDENTIFICATION BY MASS SPECTROMETRY.
    8. Erratum
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 26:387-387(2006)
    9. "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation."
      Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.
      Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS E3 UBIQUITIN LIGASE, MUTAGENESIS OF HIS-64.
    10. "Msl1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila."
      Hallacli E., Lipp M., Georgiev P., Spielman C., Cusack S., Akhtar A., Kadlec J.
      Mol. Cell 48:587-600(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-116 IN COMPLEX WITH MSL1 AND ZINC IONS, SUBUNIT, INTERACTION WITH MSL1.

    Entry informationi

    Entry nameiMSL2_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCI7
    Secondary accession number(s): B4DYL4
    , G5E9I1, Q0D2P1, Q8NDB4, Q9NVS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 89 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3