Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9HD42

- CHM1A_HUMAN

UniProt

Q9HD42 - CHM1A_HUMAN

Protein

Charged multivesicular body protein 1a

Gene

CHMP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. May also be involved in chromosome condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of condensed chromatin. May play a role in stable cell cycle progression and in PcG gene silencing.4 Publications

    GO - Molecular functioni

    1. metallopeptidase activity Source: ProtInc
    2. protein binding Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProt
    5. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. gene silencing Source: UniProtKB
    3. mitotic chromosome condensation Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. negative regulation of transcription by glucose Source: UniProtKB
    6. protein transport Source: UniProtKB-KW
    7. proteolysis Source: GOC
    8. transcription, DNA-templated Source: UniProtKB-KW
    9. vesicle-mediated transport Source: UniProtKB

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Cell cycle, Cell division, Protein transport, Transcription, Transcription regulation, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Charged multivesicular body protein 1a
    Alternative name(s):
    Chromatin-modifying protein 1a
    Short name:
    CHMP1a
    Vacuolar protein sorting-associated protein 46-1
    Short name:
    Vps46-1
    Short name:
    hVps46-1
    Gene namesi
    Name:CHMP1A
    Synonyms:CHMP11 Publication, KIAA00471 Publication, PCOLN3, PRSM11 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:8740. CHMP1A.

    Subcellular locationi

    Cytoplasm. Endosome membrane; Peripheral membrane protein. Nucleus matrix
    Note: The cytoplasmic form is partially membrane-associated and localizes to early endosomes. The nuclear form remains associated with the chromosome scaffold during mitosis. On overexpression, it localizes to nuclear bodies characterized by nuclease-resistant condensed chromatin.

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: UniProtKB
    2. early endosome Source: UniProtKB
    3. endomembrane system Source: UniProtKB
    4. endosome membrane Source: UniProtKB-SubCell
    5. extracellular vesicular exosome Source: UniProt
    6. microtubule organizing center Source: UniProtKB
    7. nuclear matrix Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Pontocerebellar hypoplasia 8 (PCH8) [MIM:614961]: An autosomal recessive neurodevelopmental disorder characterized by severe psychomotor retardation, abnormal movements, hypotonia, spasticity, and variable visual defects. Brain MRI shows pontocerebellar hypoplasia, decreased cerebral white matter, and a thin corpus callosum.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi191 – 1911L → A: No effect on interaction with IST1; when associated with L-194. 1 Publication
    Mutagenesisi194 – 1941L → A: No effect on interaction with IST1; when associated with L-194. 1 Publication

    Organism-specific databases

    MIMi614961. phenotype.
    Orphaneti324569. Pontocerebellar hypoplasia type 8.
    PharmGKBiPA33085.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 196196Charged multivesicular body protein 1aPRO_0000211448Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9HD42.
    PaxDbiQ9HD42.
    PRIDEiQ9HD42.

    PTM databases

    PhosphoSiteiQ9HD42.

    Expressioni

    Tissue specificityi

    Expressed in placenta, cultured skin fibroblasts and in osteoblast cell line MG-63.1 Publication

    Inductioni

    By muristerone.1 Publication

    Gene expression databases

    ArrayExpressiQ9HD42.
    BgeeiQ9HD42.
    CleanExiHS_CHMP1A.
    GenevestigatoriQ9HD42.

    Interactioni

    Subunit structurei

    Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Self-associates. Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B. Interacts with PHF1. Interacts with IST1. Interacts with MITD1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAMBPO956303EBI-1057156,EBI-396676
    USP8P408183EBI-1057156,EBI-1050865

    Protein-protein interaction databases

    BioGridi111148. 14 interactions.
    DIPiDIP-50647N.
    IntActiQ9HD42. 5 interactions.
    MINTiMINT-6946738.
    STRINGi9606.ENSP00000253475.

    Structurei

    Secondary structure

    1
    196
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi184 – 19512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JQ9NMR-B180-196[»]
    2YMBX-ray3.40F/H184-196[»]
    4A5XX-ray1.91C/D184-196[»]
    ProteinModelPortaliQ9HD42.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HD42.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili5 – 4743Sequence AnalysisAdd
    BLAST
    Coiled coili102 – 12423Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi185 – 19511MIT-interacting motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNF7 family.Sequence Analysis

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG331649.
    HOGENOMiHOG000241980.
    HOVERGENiHBG080200.
    OrthoDBiEOG7BP843.
    PhylomeDBiQ9HD42.
    TreeFamiTF300076.

    Family and domain databases

    InterProiIPR005024. Snf7.
    [Graphical view]
    PfamiPF03357. Snf7. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9HD42-1) [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

    MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALLQK NVECARVYAE    50
    NAIRKKNEGV NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL 100
    STMDLQKVSS VMDRFEQQVQ NLDVHTSVME DSMSSATTLT TPQEQVDSLI 150
    MQIAEENGLE VLDQLSQLPE GASAVGESSV RSQEDQLSRR LAALRN 196
    Length:196
    Mass (Da):21,703
    Last modified:March 1, 2001 - v1
    Checksum:i85D0ED7D10828D60
    GO
    Isoform 2Curated (identifier: Q9HD42-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-128: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:68
    Mass (Da):7,363
    Checksum:iF58834B1C0E254DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771Q → D in AAC50775. (PubMed:8863740)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 128128Missing in isoform 2. 1 PublicationVSP_051716Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58048 mRNA. Translation: AAC50775.1. Sequence problems.
    AF281063 mRNA. Translation: AAG01448.1.
    D38554 mRNA. Translation: BAA07557.1. Sequence problems.
    BT006841 mRNA. Translation: AAP35487.1.
    AC010538 Genomic DNA. No translation available.
    BC007527 mRNA. No translation available.
    BC010000 mRNA. Translation: AAH10000.2.
    BC132711 mRNA. Translation: AAI32712.1.
    BC132713 mRNA. Translation: AAI32714.1.
    CCDSiCCDS45552.1. [Q9HD42-1]
    PIRiJC4963.
    RefSeqiNP_002759.2. NM_002768.4. [Q9HD42-1]
    UniGeneiHs.589427.

    Genome annotation databases

    EnsembliENST00000397901; ENSP00000380998; ENSG00000131165. [Q9HD42-1]
    GeneIDi5119.
    KEGGihsa:5119.
    UCSCiuc002fnu.4. human. [Q9HD42-1]

    Polymorphism databases

    DMDMi62510514.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58048 mRNA. Translation: AAC50775.1 . Sequence problems.
    AF281063 mRNA. Translation: AAG01448.1 .
    D38554 mRNA. Translation: BAA07557.1 . Sequence problems.
    BT006841 mRNA. Translation: AAP35487.1 .
    AC010538 Genomic DNA. No translation available.
    BC007527 mRNA. No translation available.
    BC010000 mRNA. Translation: AAH10000.2 .
    BC132711 mRNA. Translation: AAI32712.1 .
    BC132713 mRNA. Translation: AAI32714.1 .
    CCDSi CCDS45552.1. [Q9HD42-1 ]
    PIRi JC4963.
    RefSeqi NP_002759.2. NM_002768.4. [Q9HD42-1 ]
    UniGenei Hs.589427.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JQ9 NMR - B 180-196 [» ]
    2YMB X-ray 3.40 F/H 184-196 [» ]
    4A5X X-ray 1.91 C/D 184-196 [» ]
    ProteinModelPortali Q9HD42.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111148. 14 interactions.
    DIPi DIP-50647N.
    IntActi Q9HD42. 5 interactions.
    MINTi MINT-6946738.
    STRINGi 9606.ENSP00000253475.

    PTM databases

    PhosphoSitei Q9HD42.

    Polymorphism databases

    DMDMi 62510514.

    Proteomic databases

    MaxQBi Q9HD42.
    PaxDbi Q9HD42.
    PRIDEi Q9HD42.

    Protocols and materials databases

    DNASUi 5119.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397901 ; ENSP00000380998 ; ENSG00000131165 . [Q9HD42-1 ]
    GeneIDi 5119.
    KEGGi hsa:5119.
    UCSCi uc002fnu.4. human. [Q9HD42-1 ]

    Organism-specific databases

    CTDi 5119.
    GeneCardsi GC16M089710.
    H-InvDB HIX0013363.
    HGNCi HGNC:8740. CHMP1A.
    MIMi 164010. gene.
    614961. phenotype.
    neXtProti NX_Q9HD42.
    Orphaneti 324569. Pontocerebellar hypoplasia type 8.
    PharmGKBi PA33085.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331649.
    HOGENOMi HOG000241980.
    HOVERGENi HBG080200.
    OrthoDBi EOG7BP843.
    PhylomeDBi Q9HD42.
    TreeFami TF300076.

    Miscellaneous databases

    ChiTaRSi CHMP1A. human.
    EvolutionaryTracei Q9HD42.
    GeneWikii CHMP1A.
    GenomeRNAii 5119.
    NextBioi 19738.
    PROi Q9HD42.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HD42.
    Bgeei Q9HD42.
    CleanExi HS_CHMP1A.
    Genevestigatori Q9HD42.

    Family and domain databases

    InterProi IPR005024. Snf7.
    [Graphical view ]
    Pfami PF03357. Snf7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)."
      Scott I.C., Halila R., Jenkins J.M., Mehan S., Apostolou S., Winqvist R., Callen D.F., Prockop D.J., Peltonen L., Kadler K.E.
      Gene 174:135-143(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, TISSUE SPECIFICITY.
      Tissue: Fibroblast and Placenta.
    2. "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
      Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
      J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
      Tissue: Placenta1 Publication.
    3. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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].
    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] (ISOFORMS 1 AND 2).
      Tissue: BrainImported and Kidney1 Publication.
    7. "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
      Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
      J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A.
    8. Cited for: INTERACTION WITH CHMP1B; VPS4A AND VPS4B.
    9. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH CHMP1B AND VPS4A.
    10. Erratum
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
    11. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: INTERACTION WITH IST1.
    13. "Biochemical analyses of human IST1 and its function in cytokinesis."
      Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
      Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IST1, MUTAGENESIS OF LEU-191 AND LEU-194.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: INVOLVEMENT IN PCH8.
    16. Cited for: STRUCTURE BY NMR OF 180-196 IN COMPLEX WITH VPS4A.
    17. "ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes."
      Hadders M.A., Agromayor M., Obita T., Perisic O., Caballe A., Kloc M., Lamers M.H., Williams R.L., Martin-Serrano J.
      Proc. Natl. Acad. Sci. U.S.A. 109:17424-17429(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 184-196 IN COMPLEX WITH MITD1, FUNCTION, INTERACTION WITH MITD1.

    Entry informationi

    Entry nameiCHM1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9HD42
    Secondary accession number(s): A2RU09
    , Q14468, Q15779, Q96G31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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. 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