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Q9UHD1

- CHRD1_HUMAN

UniProt

Q9UHD1 - CHRD1_HUMAN

Protein

Cysteine and histidine-rich domain-containing protein 1

Gene

CHORDC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi5 – 51Zinc 1
    Metal bindingi10 – 101Zinc 1
    Metal bindingi24 – 241Zinc 1
    Metal bindingi27 – 271Zinc 2
    Metal bindingi42 – 421Zinc 2
    Metal bindingi43 – 431Zinc 2
    Metal bindingi59 – 591Zinc 2
    Metal bindingi64 – 641Zinc 1
    Metal bindingi157 – 1571Zinc 3PROSITE-ProRule annotation
    Metal bindingi162 – 1621Zinc 3PROSITE-ProRule annotation
    Metal bindingi176 – 1761Zinc 3PROSITE-ProRule annotation
    Metal bindingi179 – 1791Zinc 4PROSITE-ProRule annotation
    Metal bindingi194 – 1941Zinc 4PROSITE-ProRule annotation
    Metal bindingi195 – 1951Zinc 4PROSITE-ProRule annotation
    Metal bindingi211 – 2111Zinc 4PROSITE-ProRule annotation
    Metal bindingi216 – 2161Zinc 3PROSITE-ProRule annotation

    GO - Molecular functioni

    1. Hsp90 protein binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. chaperone-mediated protein folding Source: UniProtKB
    2. negative regulation of Rho-dependent protein serine/threonine kinase activity Source: Ensembl
    3. regulation of cellular response to heat Source: UniProtKB
    4. regulation of centrosome duplication Source: Ensembl
    5. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine and histidine-rich domain-containing protein 1
    Alternative name(s):
    CHORD domain-containing protein 1
    Short name:
    CHORD-containing protein 1
    Short name:
    CHP-1
    Protein morgana
    Gene namesi
    Name:CHORDC1
    Synonyms:CHP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14525. CHORDC1.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26476.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 332331Cysteine and histidine-rich domain-containing protein 1PRO_0000317770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei47 – 471Phosphothreonine1 Publication
    Modified residuei51 – 511Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHD1.
    PaxDbiQ9UHD1.
    PeptideAtlasiQ6IN49.
    PRIDEiQ9UHD1.

    Expressioni

    Tissue specificityi

    Underexpressed in many breast and lung cancers.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHD1.
    BgeeiQ9UHD1.
    CleanExiHS_CHORDC1.
    GenevestigatoriQ9UHD1.

    Organism-specific databases

    HPAiHPA041040.

    Interactioni

    Subunit structurei

    Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with HSP90AB1 and PPP5C By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AA1P079008EBI-2550959,EBI-296047

    Protein-protein interaction databases

    BioGridi117929. 17 interactions.
    IntActiQ9UHD1. 17 interactions.
    STRINGi9606.ENSP00000319255.

    Structurei

    Secondary structure

    1
    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 103
    Turni16 – 183
    Turni21 – 233
    Beta strandi31 – 344
    Beta strandi37 – 448
    Beta strandi46 – 494
    Helixi50 – 534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YRTNMR-A1-68[»]
    ProteinModelPortaliQ9UHD1.
    SMRiQ9UHD1. Positions 1-68, 157-216, 231-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHD1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 6460CHORD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini157 – 21660CHORD 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini227 – 31690CSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 7776Interaction with PPP5CBy similarityAdd
    BLAST
    Regioni65 – 316252Interaction with HSP90AA1 and HSP90AB1By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 2 CHORD domains.PROSITE-ProRule annotation
    Contains 1 CS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG282821.
    HOGENOMiHOG000207093.
    HOVERGENiHBG052156.
    InParanoidiQ9UHD1.
    KOiK16729.
    OMAiLSQEGCT.
    OrthoDBiEOG7X6M0X.
    PhylomeDBiQ9UHD1.
    TreeFamiTF105394.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007051. CHORD.
    IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    [Graphical view]
    PfamiPF04968. CHORD. 2 hits.
    PF04969. CS. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51401. CHORD. 2 hits.
    PS51203. CS. 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: Q9UHD1-1) [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

    MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF    50
    SDFLSIVGCT KGRHNSEKPP EPVKPEVKTT EKKELCELKP KFQEHIIQAP 100
    KPVEAIKRPS PDEPMTNLEL KISASLKQAL DKLKLSSGNE ENKKEEDNDE 150
    IKIGTSCKNG GCSKTYQGLE SLEEVCVYHS GVPIFHEGMK YWSCCRRKTS 200
    DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE VTISVYAKNS 250
    LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI 300
    EITMRKAEPM QWASLELPAA KKQEKQKDAT TD 332
    Length:332
    Mass (Da):37,490
    Last modified:February 5, 2008 - v2
    Checksum:i3142D8EC8A879155
    GO
    Isoform 2 (identifier: Q9UHD1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         39-57: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:313
    Mass (Da):35,286
    Checksum:i3347F35622425A90
    GO

    Sequence cautioni

    The sequence AAH17789.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2341W → L in AAF18437. (PubMed:10571178)Curated
    Sequence conflicti267 – 2671H → I in AAF18437. (PubMed:10571178)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti329 – 3291A → D.4 Publications
    Corresponds to variant rs1045861 [ dbSNP | Ensembl ].
    VAR_038676

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei39 – 5719Missing in isoform 2. 1 PublicationVSP_031150Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF192466 mRNA. Translation: AAF18437.1.
    AF123249 mRNA. Translation: AAG43237.1.
    AK290231 mRNA. Translation: BAF82920.1.
    AK312663 mRNA. Translation: BAG35545.1.
    AP002364 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW66868.1.
    CH471065 Genomic DNA. Translation: EAW66870.1.
    BC017789 mRNA. Translation: AAH17789.1. Different initiation.
    BC072461 mRNA. Translation: AAH72461.1.
    CCDSiCCDS44705.1. [Q9UHD1-2]
    CCDS8289.1. [Q9UHD1-1]
    RefSeqiNP_001137545.1. NM_001144073.1. [Q9UHD1-2]
    NP_036256.2. NM_012124.2. [Q9UHD1-1]
    UniGeneiHs.22857.

    Genome annotation databases

    EnsembliENST00000320585; ENSP00000319255; ENSG00000110172. [Q9UHD1-1]
    ENST00000457199; ENSP00000401080; ENSG00000110172. [Q9UHD1-2]
    GeneIDi26973.
    KEGGihsa:26973.
    UCSCiuc001pdg.2. human. [Q9UHD1-1]
    uc009yvz.2. human. [Q9UHD1-2]

    Polymorphism databases

    DMDMi167008724.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF192466 mRNA. Translation: AAF18437.1 .
    AF123249 mRNA. Translation: AAG43237.1 .
    AK290231 mRNA. Translation: BAF82920.1 .
    AK312663 mRNA. Translation: BAG35545.1 .
    AP002364 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW66868.1 .
    CH471065 Genomic DNA. Translation: EAW66870.1 .
    BC017789 mRNA. Translation: AAH17789.1 . Different initiation.
    BC072461 mRNA. Translation: AAH72461.1 .
    CCDSi CCDS44705.1. [Q9UHD1-2 ]
    CCDS8289.1. [Q9UHD1-1 ]
    RefSeqi NP_001137545.1. NM_001144073.1. [Q9UHD1-2 ]
    NP_036256.2. NM_012124.2. [Q9UHD1-1 ]
    UniGenei Hs.22857.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YRT NMR - A 1-68 [» ]
    ProteinModelPortali Q9UHD1.
    SMRi Q9UHD1. Positions 1-68, 157-216, 231-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117929. 17 interactions.
    IntActi Q9UHD1. 17 interactions.
    STRINGi 9606.ENSP00000319255.

    Polymorphism databases

    DMDMi 167008724.

    Proteomic databases

    MaxQBi Q9UHD1.
    PaxDbi Q9UHD1.
    PeptideAtlasi Q6IN49.
    PRIDEi Q9UHD1.

    Protocols and materials databases

    DNASUi 26973.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320585 ; ENSP00000319255 ; ENSG00000110172 . [Q9UHD1-1 ]
    ENST00000457199 ; ENSP00000401080 ; ENSG00000110172 . [Q9UHD1-2 ]
    GeneIDi 26973.
    KEGGi hsa:26973.
    UCSCi uc001pdg.2. human. [Q9UHD1-1 ]
    uc009yvz.2. human. [Q9UHD1-2 ]

    Organism-specific databases

    CTDi 26973.
    GeneCardsi GC11M089933.
    H-InvDB HIX0010016.
    HGNCi HGNC:14525. CHORDC1.
    HPAi HPA041040.
    MIMi 604353. gene.
    neXtProti NX_Q9UHD1.
    PharmGKBi PA26476.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282821.
    HOGENOMi HOG000207093.
    HOVERGENi HBG052156.
    InParanoidi Q9UHD1.
    KOi K16729.
    OMAi LSQEGCT.
    OrthoDBi EOG7X6M0X.
    PhylomeDBi Q9UHD1.
    TreeFami TF105394.

    Miscellaneous databases

    ChiTaRSi CHORDC1. human.
    EvolutionaryTracei Q9UHD1.
    GenomeRNAii 26973.
    NextBioi 49424.
    PROi Q9UHD1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHD1.
    Bgeei Q9UHD1.
    CleanExi HS_CHORDC1.
    Genevestigatori Q9UHD1.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR007051. CHORD.
    IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    [Graphical view ]
    Pfami PF04968. CHORD. 2 hits.
    PF04969. CS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS51401. CHORD. 2 hits.
    PS51203. CS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans."
      Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P.
      Cell 99:355-366(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-329.
    2. "Isolation and characterization the chymotrypsin-like protein gene from human heart cDNA library."
      Zhao Y., Cao H., Jiang Y., Meng X., Zhao X., Liu D., Ding J.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-329.
      Tissue: Heart.
    3. "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 1), VARIANT ASP-329.
      Tissue: Thalamus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-329.
    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. Bienvenut W.V., Bilsland A.E., Keith W.N.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-8; 47-61; 108-121; 249-256; 282-289; 291-299 AND 306-321, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: FUNCTION, INTERACTION WITH ROCK1 AND ROCK2, TISSUE SPECIFICITY.
    11. "A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein."
      Gano J.J., Simon J.A.
      Mol. Cell. Proteomics 9:255-270(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSP90AA1.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of the CHORD domain of human CHORD-containing protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-68.

    Entry informationi

    Entry nameiCHRD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHD1
    Secondary accession number(s): B2R6P8
    , Q6IN49, Q8WVL9, Q9H3D6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 95 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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