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P16989

- YBOX3_HUMAN

UniProt

P16989 - YBOX3_HUMAN

Protein

Y-box-binding protein 3

Gene

YBX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 4 (16 May 2006)
      Previous versions | rss
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    Functioni

    Binds to the GM-CSF promoter. Seems to act as a repressor. Binds also to full length mRNA and to short RNA sequences containing the consensus site 5'-UCCAUCA-3'. May have a role in translation repression By similarity.By similarity

    GO - Molecular functioni

    1. double-stranded DNA binding Source: ProtInc
    2. mRNA 3'-UTR binding Source: BHF-UCL
    3. poly(A) RNA binding Source: UniProtKB
    4. Rho GTPase binding Source: BHF-UCL
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc
    6. single-stranded DNA binding Source: Ensembl
    7. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. 3'-UTR-mediated mRNA stabilization Source: BHF-UCL
    2. cellular hyperosmotic response Source: BHF-UCL
    3. cellular response to tumor necrosis factor Source: BHF-UCL
    4. fertilization Source: Ensembl
    5. in utero embryonic development Source: Ensembl
    6. male gonad development Source: Ensembl
    7. negative regulation of apoptotic process Source: Ensembl
    8. negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress Source: BHF-UCL
    9. negative regulation of necroptotic process Source: BHF-UCL
    10. negative regulation of skeletal muscle tissue development Source: Ensembl
    11. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    12. positive regulation of cytoplasmic translation Source: BHF-UCL
    13. positive regulation of organ growth Source: Ensembl
    14. response to cold Source: ProtInc
    15. spermatogenesis Source: Ensembl
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Y-box-binding protein 3
    Alternative name(s):
    Cold shock domain-containing protein A
    DNA-binding protein A
    Single-strand DNA-binding protein NF-GMB
    Gene namesi
    Name:YBX3
    Synonyms:CSDA, DBPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2428. YBX3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: BHF-UCL
    3. perinuclear region of cytoplasm Source: BHF-UCL
    4. polysome Source: Ensembl
    5. tight junction Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26929.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 372371Y-box-binding protein 3PRO_0000100214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei134 – 1341Phosphoserine1 Publication
    Modified residuei201 – 2011Phosphoserine2 Publications
    Modified residuei203 – 2031Phosphoserine2 Publications
    Modified residuei204 – 2041Phosphoserine3 Publications
    Modified residuei324 – 3241Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP16989.
    PaxDbiP16989.
    PRIDEiP16989.

    PTM databases

    PhosphoSiteiP16989.

    Miscellaneous databases

    PMAP-CutDBP16989.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle and heart.

    Gene expression databases

    BgeeiP16989.
    CleanExiHS_CSDA.
    GenevestigatoriP16989.

    Organism-specific databases

    HPAiHPA034838.

    Interactioni

    Subunit structurei

    Found in a mRNP complex with YBX2.By similarity

    Protein-protein interaction databases

    BioGridi114101. 62 interactions.
    DIPiDIP-42489N.
    IntActiP16989. 27 interactions.
    MINTiMINT-1152000.
    STRINGi9606.ENSP00000228251.

    Structurei

    3D structure databases

    ProteinModelPortaliP16989.
    SMRiP16989. Positions 84-160.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 15765CSDAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CSD (cold-shock) domain.Curated

    Phylogenomic databases

    eggNOGiCOG1278.
    HOGENOMiHOG000116439.
    HOVERGENiHBG008757.
    InParanoidiP16989.
    KOiK06099.
    OMAiLSFNRND.
    OrthoDBiEOG7TBC44.
    PhylomeDBiP16989.
    TreeFamiTF317306.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR019844. Cold-shock_CS.
    IPR011129. Cold_shock_prot.
    IPR002059. CSP_DNA-bd.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF00313. CSD. 1 hit.
    [Graphical view]
    PRINTSiPR00050. COLDSHOCK.
    SMARTiSM00357. CSP. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    PROSITEiPS00352. COLD_SHOCK. 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

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P16989-1) [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

    MSEAGEATTT TTTTLPQAPT EAAAAAPQDP APKSPVGSGA PQAAAPAPAA    50
    HVAGNPGGDA APAATGTAAA ASLATAAGSE DAEKKVLATK VLGTVKWFNV 100
    RNGYGFINRN DTKEDVFVHQ TAIKKNNPRK YLRSVGDGET VEFDVVEGEK 150
    GAEAANVTGP DGVPVEGSRY AADRRRYRRG YYGRRRGPPR NYAGEEEEEG 200
    SGSSEGFDPP ATDRQFSGAR NQLRRPQYRP QYRQRRFPPY HVGQTFDRRS 250
    RVLPHPNRIQ AGEIGEMKDG VPEGAQLQGP VHRNPTYRPR YRSRGPPRPR 300
    PAPAVGEAED KENQQATSGP NQPSVRRGYR RPYNYRRRPR PPNAPSQDGK 350
    EAKAGEAPTE NPAPPTQQSS AE 372
    Length:372
    Mass (Da):40,090
    Last modified:May 16, 2006 - v4
    Checksum:iAA8517AC3B7D35CC
    GO
    Isoform 2 (identifier: P16989-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         192-260: Missing.

    Show »
    Length:303
    Mass (Da):31,947
    Checksum:i29E708D6FCB442CD
    GO
    Isoform 3 (identifier: P16989-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         340-372: RPPNAPSQDGKEAKAGEAPTENPAPPTQQSSAE → PSS

    Show »
    Length:342
    Mass (Da):37,021
    Checksum:i255258C4B4E80A4F
    GO

    Sequence cautioni

    The sequence AAA35749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751T → A.3 Publications
    Corresponds to variant rs1126501 [ dbSNP | Ensembl ].
    VAR_013114

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei192 – 26069Missing in isoform 2. 1 PublicationVSP_001135Add
    BLAST
    Alternative sequencei340 – 37233RPPNA…QSSAE → PSS in isoform 3. 1 PublicationVSP_001136Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24069 mRNA. Translation: AAA35749.1. Different initiation.
    L29071
    , L29064, L29065, L29066, L29067, L29068, L29069, L29070 Genomic DNA. Translation: AAA79243.1.
    X95325 mRNA. Translation: CAA64631.1.
    X72712 mRNA. Translation: CAA51261.1.
    AK314846 mRNA. Translation: BAG37363.1.
    CH471094 Genomic DNA. Translation: EAW96201.1.
    CH471094 Genomic DNA. Translation: EAW96203.1.
    BC008801 mRNA. Translation: AAH08801.1.
    BC015564 mRNA. Translation: AAH15564.1.
    BC015913 mRNA. Translation: AAH15913.1.
    BC021926 mRNA. Translation: AAH21926.1.
    CCDSiCCDS44831.1. [P16989-2]
    CCDS8630.1. [P16989-1]
    PIRiI53354.
    S69501.
    RefSeqiNP_001138898.1. NM_001145426.1. [P16989-2]
    NP_003642.3. NM_003651.4. [P16989-1]
    UniGeneiHs.221889.

    Genome annotation databases

    EnsembliENST00000228251; ENSP00000228251; ENSG00000060138. [P16989-1]
    ENST00000279550; ENSP00000279550; ENSG00000060138. [P16989-2]
    GeneIDi8531.
    KEGGihsa:8531.
    UCSCiuc001qyt.3. human. [P16989-1]
    uc001qyu.3. human. [P16989-2]

    Polymorphism databases

    DMDMi97536050.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24069 mRNA. Translation: AAA35749.1 . Different initiation.
    L29071
    , L29064 , L29065 , L29066 , L29067 , L29068 , L29069 , L29070 Genomic DNA. Translation: AAA79243.1 .
    X95325 mRNA. Translation: CAA64631.1 .
    X72712 mRNA. Translation: CAA51261.1 .
    AK314846 mRNA. Translation: BAG37363.1 .
    CH471094 Genomic DNA. Translation: EAW96201.1 .
    CH471094 Genomic DNA. Translation: EAW96203.1 .
    BC008801 mRNA. Translation: AAH08801.1 .
    BC015564 mRNA. Translation: AAH15564.1 .
    BC015913 mRNA. Translation: AAH15913.1 .
    BC021926 mRNA. Translation: AAH21926.1 .
    CCDSi CCDS44831.1. [P16989-2 ]
    CCDS8630.1. [P16989-1 ]
    PIRi I53354.
    S69501.
    RefSeqi NP_001138898.1. NM_001145426.1. [P16989-2 ]
    NP_003642.3. NM_003651.4. [P16989-1 ]
    UniGenei Hs.221889.

    3D structure databases

    ProteinModelPortali P16989.
    SMRi P16989. Positions 84-160.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114101. 62 interactions.
    DIPi DIP-42489N.
    IntActi P16989. 27 interactions.
    MINTi MINT-1152000.
    STRINGi 9606.ENSP00000228251.

    PTM databases

    PhosphoSitei P16989.

    Polymorphism databases

    DMDMi 97536050.

    Proteomic databases

    MaxQBi P16989.
    PaxDbi P16989.
    PRIDEi P16989.

    Protocols and materials databases

    DNASUi 8531.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228251 ; ENSP00000228251 ; ENSG00000060138 . [P16989-1 ]
    ENST00000279550 ; ENSP00000279550 ; ENSG00000060138 . [P16989-2 ]
    GeneIDi 8531.
    KEGGi hsa:8531.
    UCSCi uc001qyt.3. human. [P16989-1 ]
    uc001qyu.3. human. [P16989-2 ]

    Organism-specific databases

    CTDi 8531.
    GeneCardsi GC12M010852.
    HGNCi HGNC:2428. YBX3.
    HPAi HPA034838.
    MIMi 603437. gene.
    neXtProti NX_P16989.
    PharmGKBi PA26929.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1278.
    HOGENOMi HOG000116439.
    HOVERGENi HBG008757.
    InParanoidi P16989.
    KOi K06099.
    OMAi LSFNRND.
    OrthoDBi EOG7TBC44.
    PhylomeDBi P16989.
    TreeFami TF317306.

    Miscellaneous databases

    ChiTaRSi CSDA. human.
    GeneWikii CSDA_(gene).
    GenomeRNAii 8531.
    NextBioi 31948.
    PMAP-CutDB P16989.
    PROi P16989.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16989.
    CleanExi HS_CSDA.
    Genevestigatori P16989.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR019844. Cold-shock_CS.
    IPR011129. Cold_shock_prot.
    IPR002059. CSP_DNA-bd.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF00313. CSD. 1 hit.
    [Graphical view ]
    PRINTSi PR00050. COLDSHOCK.
    SMARTi SM00357. CSP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    PROSITEi PS00352. COLD_SHOCK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology."
      Sakura H., Maekawa T., Imamoto F., Yasuda K., Ishii S.
      Gene 73:499-507(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT ALA-75.
    2. "Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domain."
      Kudo S., Mattei M.-G., Fukuda M.
      Eur. J. Biochem. 231:72-82(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANT ALA-75.
      Tissue: Placenta.
    3. "Cold shock domain proteins repress transcription from the GM-CSF promoter."
      Coles L.S., Diamond P., Occhiodoro F., Vadas M.A., Shannon M.F.
      Nucleic Acids Res. 24:2311-2317(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Moschonas N.K.
      Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Blood.
    5. "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).
    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] (ISOFORMS 1 AND 2), VARIANT ALA-75.
      Tissue: Kidney, Lung, Lymph and Muscle.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-203 AND SER-204, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-201; SER-203 AND SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiYBOX3_HUMAN
    AccessioniPrimary (citable) accession number: P16989
    Secondary accession number(s): B2RBW6
    , Q14121, Q969N6, Q96B76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 155 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 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3