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Q8IWY9

- CDAN1_HUMAN

UniProt

Q8IWY9 - CDAN1_HUMAN

Protein

Codanin-1

Gene

CDAN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    Functioni

    May acts as a negative regulator of ASF1 in chromatin assembly.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin assembly Source: UniProtKB
    2. chromatin organization Source: MGI
    3. negative regulation of DNA replication Source: UniProtKB
    4. protein localization Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Codanin-1
    Gene namesi
    Name:CDAN1
    ORF Names:UNQ664/PRO1295
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:1713. CDAN1.

    Subcellular locationi

    Cytoplasm. Nucleus. Membrane Curated; Multi-pass membrane protein Curated
    Note: Mainly detected as a cytoplasmic protein.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endomembrane system Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Anemia, congenital dyserythropoietic, 1A (CDAN1A) [MIM:224120]: An autosomal recessive blood disorder characterized by morphological abnormalities of erythroblasts, ineffective erythropoiesis, macrocytic anemia and secondary hemochromatosis. It is occasionally associated with bone abnormalities, especially of the hands and feet (acrodysostosis), nail hypoplasia, and scoliosis. Ultrastructural features include internuclear chromatin bridges connecting some nearly completely separated erythroblasts and an abnormal appearance (spongy or Swiss-cheese appearance) of the heterochromatin in a high proportion of the erythroblasts.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti599 – 5991N → S in CDAN1A. 1 Publication
    VAR_017218
    Natural varianti672 – 6721P → L in CDAN1A. 1 Publication
    VAR_017219
    Natural varianti698 – 6981E → K in CDAN1A. 1 Publication
    VAR_017220
    Natural varianti714 – 7141R → W in CDAN1A; partially disrupts ASF1 binding and loss the ability to arrest cells in S phase and inhibit DNA synthesis. 1 Publication
    Corresponds to variant rs80338696 [ dbSNP | Ensembl ].
    VAR_017221
    Natural varianti868 – 8681F → I in CDAN1A. 1 Publication
    VAR_017222
    Natural varianti869 – 8691V → M in CDAN1A. 1 Publication
    VAR_017223
    Natural varianti1042 – 10421R → W in CDAN1A; partially disrupts ASF1 binding. 1 Publication
    VAR_017224
    Natural varianti1043 – 10431D → V in CDAN1A. 1 Publication
    VAR_017225
    Natural varianti1130 – 11301P → L in CDAN1A. 1 Publication
    VAR_017226

    Keywords - Diseasei

    Congenital dyserythropoietic anemia, Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi224120. phenotype.
    Orphaneti98869. Congenital dyserythropoietic anemia type I.
    PharmGKBiPA26249.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 12271226Codanin-1PRO_0000089439Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8IWY9.
    PaxDbiQ8IWY9.
    PRIDEiQ8IWY9.

    PTM databases

    PhosphoSiteiQ8IWY9.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 3 is not found in erythroid cells.1 Publication

    Gene expression databases

    ArrayExpressiQ8IWY9.
    BgeeiQ8IWY9.
    CleanExiHS_CDAN1.
    GenevestigatoriQ8IWY9.

    Organism-specific databases

    HPAiHPA039404.
    HPA040787.

    Interactioni

    Subunit structurei

    Found in a cytosolic complex with ASF1A, ASF1B, IPO4 and histones H3.1 and H4.1 Publication

    Protein-protein interaction databases

    BioGridi126963. 8 interactions.
    DIPiDIP-24225N.
    IntActiQ8IWY9. 4 interactions.
    MINTiMINT-1377874.
    STRINGi9606.ENSP00000348564.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IWY9.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei312 – 33221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei626 – 64621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 20821Interaction with ASF1A/BAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG79208.
    HOGENOMiHOG000111492.
    HOVERGENiHBG107631.
    InParanoidiQ8IWY9.
    OMAiREQSSRV.
    OrthoDBiEOG715Q3S.
    PhylomeDBiQ8IWY9.
    TreeFamiTF328405.

    Family and domain databases

    InterProiIPR028171. Codanin-1_C.
    [Graphical view]
    PfamiPF15296. Codanin-1_C. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q8IWY9-2) [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

    MAAVLESLLR EEVSVAAVVR WIARSTQGSE DNAGEAAALS SLRALRKEFV     50
    PFLLNFLREQ SSRVLPQGPP TPAKTPGASA ALPGRPGGPP RGSRGARSQL 100
    FPPTEAQSTA AEAPLARRGG RRRGPGPARE RGGRGLEEGV SGESLPGAGG 150
    RRLRGSGSPS RPSLTLSDPP NLSNLEEFPP VGSVPPGPTG TKPSRRINPT 200
    PVSEERSLSK PKTCFTSPPI SCVPSSQPSA LDTSPWGLGL PPGCRSLQEE 250
    REMLRKERSK QLQQSPTPTC PTPELGSPLP SRTGSLTDEP ADPARVSSRQ 300
    RLELVALVYS SCIAENLVPN LFLELFFVFQ LLTARRMVTA KDSDPELSPA 350
    VLDSLESPLF QSIHDCVFFA VQVLECHFQV LSNLDKGTLK LLAENERLLC 400
    FSPALQGRLR AAYEGSVAKV SLVMPPSTQA VSFQPETDNR ANFSSDRAFH 450
    TFKKQRDVFY EVLREWEDHH EEPGWDFEKG LGSRIRAMMG QLSAACSHSH 500
    FVRLFQKQLL QMCQSPGGAG GTVLGEAPDV LSMLGADKLG RLWRLQERLM 550
    APQSSGGPCP PPTFPGCQGF FRDFILSASS FQFNQHLMDS LSLKIQELNG 600
    LALPQHEPND EDGESDVDWQ GERKQFAVVL LSLRLLAKFL GFVAFLPYRG 650
    PEPPPTGELQ DSILALRSQV PPVLDVRTLL QRGLQARRAV LTVPWLVEFL 700
    SFADHVVPLL EYYRDIFTLL LRLHRSLVLS QESEGKMCFL NKLLLLAVLG 750
    WLFQIPTVPE DLFFLEEGPS YAFEVDTVAP EHGLDNAPVV DQQLLYTCCP 800
    YIGELRKLLA SWVSGSSGRS GGFMRKITPT TTTSLGAQPS QTSQGLQAQL 850
    AQAFFHNQPP SLRRTVEFVA ERIGSNCVKH IKATLVADLV RQAESLLQEQ 900
    LVTQGEEGGD PAQLLEILCS QLCPHGAQAL ALGREFCQRK SPGAVRALLP 950
    EETPAAVLSS AENIAVGLAT EKACAWLSAN ITALIRREVK AAVSRTLRAQ 1000
    GPEPAARGER RGCSRACEHH APLPSHLISE IKDVLSLAVG PRDPDEGVSP 1050
    EHLEQLLGQL GQTLRCRQFL CPPAEQHLAK CSVELASLLV ADQIPILGPP 1100
    AQYRLERGQA RRLLHMLLSL WKEDFQGPVP LQLLLSPRNV GLLADTRPRE 1150
    WDLLLFLLRE LVEKGLMGRM EIEACLGSLH QAQWPGDFAE ELATLSNLFL 1200
    AEPHLPEPQL RACELVQPNR GTVLAQS 1227
    Length:1,227
    Mass (Da):134,120
    Last modified:May 18, 2010 - v4
    Checksum:iE2BC04ACD669DF6F
    GO
    Isoform 1 (identifier: Q8IWY9-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         190-190: G → GETQLSCRRWVPRRLWGVSHSSSALRSGAPGCR
         226-258: Missing.

    Show »
    Length:1,226
    Mass (Da):133,992
    Checksum:i0674D569F19BCD52
    GO
    Isoform 3 (identifier: Q8IWY9-3)

    Sequence is not available
    Length:
    Mass (Da):

    Sequence cautioni

    The sequence AAH52568.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAO14994.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAQ88832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 322DN → VT in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti39 – 391L → V in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti42 – 454LRAL → FGAW in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti51 – 522PF → RS in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti55 – 551N → T in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti73 – 731A → P in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti76 – 761P → R in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti82 – 821L → C in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti93 – 931S → T in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti380 – 3801V → F in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti421 – 4211S → F in AAH52568. (PubMed:15489334)Curated
    Sequence conflicti421 – 4211S → F in AAH66640. (PubMed:15489334)Curated
    Sequence conflicti669 – 6691Q → P in AAQ88832. (PubMed:12975309)Curated
    Sequence conflicti726 – 7261S → C in AAO14994. (PubMed:12434312)Curated
    Sequence conflicti946 – 9461R → W in AAH01092. (PubMed:15489334)Curated
    Sequence conflicti946 – 9461R → W in AAH08333. (PubMed:15489334)Curated
    Sequence conflicti946 – 9461R → W in AAH08334. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071Q → L.
    Corresponds to variant rs4265781 [ dbSNP | Ensembl ].
    VAR_059602
    Natural varianti596 – 5961Q → R.
    Corresponds to variant rs12917189 [ dbSNP | Ensembl ].
    VAR_056785
    Natural varianti599 – 5991N → S in CDAN1A. 1 Publication
    VAR_017218
    Natural varianti672 – 6721P → L in CDAN1A. 1 Publication
    VAR_017219
    Natural varianti698 – 6981E → K in CDAN1A. 1 Publication
    VAR_017220
    Natural varianti714 – 7141R → W in CDAN1A; partially disrupts ASF1 binding and loss the ability to arrest cells in S phase and inhibit DNA synthesis. 1 Publication
    Corresponds to variant rs80338696 [ dbSNP | Ensembl ].
    VAR_017221
    Natural varianti868 – 8681F → I in CDAN1A. 1 Publication
    VAR_017222
    Natural varianti869 – 8691V → M in CDAN1A. 1 Publication
    VAR_017223
    Natural varianti891 – 8911R → C.
    Corresponds to variant rs8023524 [ dbSNP | Ensembl ].
    VAR_056786
    Natural varianti1042 – 10421R → W in CDAN1A; partially disrupts ASF1 binding. 1 Publication
    VAR_017224
    Natural varianti1043 – 10431D → V in CDAN1A. 1 Publication
    VAR_017225
    Natural varianti1130 – 11301P → L in CDAN1A. 1 Publication
    VAR_017226

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei190 – 1901G → GETQLSCRRWVPRRLWGVSH SSSALRSGAPGCR in isoform 1. 1 PublicationVSP_027097
    Alternative sequencei226 – 25833Missing in isoform 1. 1 PublicationVSP_027098Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF525398 mRNA. Translation: AAO14994.1. Different initiation.
    AC090510 Genomic DNA. No translation available.
    BC001092 mRNA. Translation: AAH01092.1.
    BC008333 mRNA. Translation: AAH08333.1.
    BC008334 mRNA. Translation: AAH08334.1.
    BC052568 mRNA. Translation: AAH52568.1. Different initiation.
    BC066640 mRNA. Translation: AAH66640.1.
    AY358467 mRNA. Translation: AAQ88832.1. Different initiation.
    CCDSiCCDS32209.1. [Q8IWY9-2]
    RefSeqiNP_612486.2. NM_138477.2. [Q8IWY9-2]
    UniGeneiHs.599232.

    Genome annotation databases

    EnsembliENST00000356231; ENSP00000348564; ENSG00000140326. [Q8IWY9-2]
    GeneIDi146059.
    KEGGihsa:146059.
    UCSCiuc001zql.3. human. [Q8IWY9-2]

    Polymorphism databases

    DMDMi296439465.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF525398 mRNA. Translation: AAO14994.1 . Different initiation.
    AC090510 Genomic DNA. No translation available.
    BC001092 mRNA. Translation: AAH01092.1 .
    BC008333 mRNA. Translation: AAH08333.1 .
    BC008334 mRNA. Translation: AAH08334.1 .
    BC052568 mRNA. Translation: AAH52568.1 . Different initiation.
    BC066640 mRNA. Translation: AAH66640.1 .
    AY358467 mRNA. Translation: AAQ88832.1 . Different initiation.
    CCDSi CCDS32209.1. [Q8IWY9-2 ]
    RefSeqi NP_612486.2. NM_138477.2. [Q8IWY9-2 ]
    UniGenei Hs.599232.

    3D structure databases

    ProteinModelPortali Q8IWY9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126963. 8 interactions.
    DIPi DIP-24225N.
    IntActi Q8IWY9. 4 interactions.
    MINTi MINT-1377874.
    STRINGi 9606.ENSP00000348564.

    PTM databases

    PhosphoSitei Q8IWY9.

    Polymorphism databases

    DMDMi 296439465.

    Proteomic databases

    MaxQBi Q8IWY9.
    PaxDbi Q8IWY9.
    PRIDEi Q8IWY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356231 ; ENSP00000348564 ; ENSG00000140326 . [Q8IWY9-2 ]
    GeneIDi 146059.
    KEGGi hsa:146059.
    UCSCi uc001zql.3. human. [Q8IWY9-2 ]

    Organism-specific databases

    CTDi 146059.
    GeneCardsi GC15M043015.
    GeneReviewsi CDAN1.
    H-InvDB HIX0202162.
    HGNCi HGNC:1713. CDAN1.
    HPAi HPA039404.
    HPA040787.
    MIMi 224120. phenotype.
    607465. gene.
    neXtProti NX_Q8IWY9.
    Orphaneti 98869. Congenital dyserythropoietic anemia type I.
    PharmGKBi PA26249.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG79208.
    HOGENOMi HOG000111492.
    HOVERGENi HBG107631.
    InParanoidi Q8IWY9.
    OMAi REQSSRV.
    OrthoDBi EOG715Q3S.
    PhylomeDBi Q8IWY9.
    TreeFami TF328405.

    Miscellaneous databases

    ChiTaRSi CDAN1. human.
    GenomeRNAii 146059.
    NextBioi 85255.
    PROi Q8IWY9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IWY9.
    Bgeei Q8IWY9.
    CleanExi HS_CDAN1.
    Genevestigatori Q8IWY9.

    Family and domain databases

    InterProi IPR028171. Codanin-1_C.
    [Graphical view ]
    Pfami PF15296. Codanin-1_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, VARIANTS CDAN1A SER-599; LEU-672; LYS-698; TRP-714; ILE-868; MET-869; TRP-1042; VAL-1043 AND LEU-1130.
    2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 2).
      Tissue: Kidney and Ovary.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 669-1016 (ISOFORM 2).
    5. "Codanin-1 mutations in congenital dyserythropoietic anemia type 1 affect HP1-alpha localization in erythroblasts."
      Renella R., Roberts N.A., Brown J.M., De Gobbi M., Bird L.E., Hassanali T., Sharpe J.A., Sloane-Stanley J., Ferguson D.J., Cordell J., Buckle V.J., Higgs D.R., Wood W.G.
      Blood 117:6928-6938(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in S-phase histone supply."
      Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.
      EMBO J. 31:2013-2023(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ASF1A AND ASF1B, IDENTIFICATION IN A COMPLEX WITH ASF1A; ASF1B; IPO4; HISTONES H3.2 AND H4, CHARACTERIZATION OF VARIANTS TRP-714 AND TRP-1042, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCDAN1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IWY9
    Secondary accession number(s): Q6NYD0, Q7Z7L5, Q969N3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 100 of the entry and version 4 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 15
      Human chromosome 15: 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

    External Data

    Dasty 3