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)

Q9UGP4

- LIMD1_HUMAN

UniProt

Q9UGP4 - LIMD1_HUMAN

Protein

LIM domain-containing protein 1

Gene

LIMD1

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 124 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation.5 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transcription corepressor activity Source: UniProtKB
    3. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cell migration Source: UniProtKB
    2. cytoplasmic mRNA processing body assembly Source: MGI
    3. cytoskeleton organization Source: UniProtKB
    4. gene silencing by miRNA Source: MGI
    5. multicellular organismal development Source: ProtInc
    6. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    7. negative regulation of hippo signaling Source: UniProtKB
    8. negative regulation of osteoblast differentiation Source: UniProtKB
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. osteoblast development Source: UniProtKB
    11. phosphorylation Source: UniProtKB
    12. positive regulation of gene silencing by miRNA Source: UniProtKB
    13. regulation of cell shape Source: UniProtKB
    14. regulation of transcription, DNA-templated Source: ProtInc
    15. response to hypoxia Source: UniProtKB
    16. signal transduction Source: ProtInc
    17. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    RNA-mediated gene silencing, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LIM domain-containing protein 1
    Gene namesi
    Name:LIMD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6612. LIMD1.

    Subcellular locationi

    Cytoplasm. Nucleus. CytoplasmP-body. Cell junctionadherens junction. Cell junctionfocal adhesion
    Note: Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions. Down-regulation and/or elimination of its expression from the nucleus of neoplastic cells correlates strongly with poor patient prognosis and aggressive forms of breast carcinoma. Conversely, strong nuclear localization correlates with low-tumor grade and better patient prognosis.

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic mRNA processing body Source: MGI
    4. focal adhesion Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. RISC complex Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA30385.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 676676LIM domain-containing protein 1PRO_0000075801Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei272 – 2721Phosphoserine3 Publications
    Modified residuei277 – 2771Phosphoserine3 Publications
    Modified residuei304 – 3041Phosphoserine2 Publications
    Modified residuei421 – 4211Phosphoserine3 Publications
    Modified residuei424 – 4241Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated during mitosis.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UGP4.
    PaxDbiQ9UGP4.
    PRIDEiQ9UGP4.

    PTM databases

    PhosphoSiteiQ9UGP4.

    Expressioni

    Tissue specificityi

    Expressed in normal and breast cancer tissues (at protein level). Ubiquitous.2 Publications

    Inductioni

    Down-regulated in lung cancer.1 Publication

    Gene expression databases

    ArrayExpressiQ9UGP4.
    BgeeiQ9UGP4.
    CleanExiHS_LIMD1.
    GenevestigatoriQ9UGP4.

    Interactioni

    Subunit structurei

    Interacts (via LIM domains) with TRAF6. Found in a complex with TRAF6, PRKCZ and SQSTM1. Interacts (via LIM domains) SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain) By similarity. Interacts with SQSTM1 and RB1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, EGLN1/PHD2, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM zinc-binding 2) with isoform 1 and isoform 3 of VHL. Interacts (via LIM domains) with SNAI1 (via SNAG domain).By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORFQ9Q2G45EBI-2652871,EBI-6248094From a different organism.

    Protein-protein interaction databases

    BioGridi114475. 25 interactions.
    IntActiQ9UGP4. 8 interactions.
    MINTiMINT-1193166.
    STRINGi9606.ENSP00000273317.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UGP4.
    SMRiQ9UGP4. Positions 470-658.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini470 – 53162LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini535 – 59561LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini595 – 66470LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 13481Mediates nuclear exportAdd
    BLAST
    Regioni186 – 26075Interaction with EGLN1/PHD2Add
    BLAST
    Regioni404 – 44239Interaction with RB1Add
    BLAST
    Regioni472 – 676205Necessary for nuclear localizationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the zyxin/ajuba family.Curated
    Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG331290.
    HOGENOMiHOG000072700.
    HOVERGENiHBG052327.
    InParanoidiQ9UGP4.
    KOiK16682.
    OMAiSLASPKW.
    PhylomeDBiQ9UGP4.
    TreeFamiTF320310.

    Family and domain databases

    Gene3Di2.10.110.10. 3 hits.
    InterProiIPR028734. LIMD1.
    IPR001781. Znf_LIM.
    [Graphical view]
    PANTHERiPTHR24219:SF3. PTHR24219:SF3. 1 hit.
    PfamiPF00412. LIM. 3 hits.
    [Graphical view]
    SMARTiSM00132. LIM. 3 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UGP4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKYDDLGLE ASKFIEDLNM YEASKDGLFR VDKGAGNNPE FEETRRVFAT    50
    KMAKIHLQQQ QQQLLQEETL PRGSRGPVNG GGRLGPQARW EVVGSKLTVD 100
    GAAKPPLAAS TGAPGAVTTL AAGQPPYPPQ EQRSRPYLHG TRHGSQDCGS 150
    RESLATSEMS AFHQPGPCED PSCLTHGDYY DNLSLASPKW GDKPGVSPSI 200
    GLSVGSGWPS SPGSDPPLPK PCGDHPLNHR QLSLSSSRSS EGSLGGQNSG 250
    IGGRSSEKPT GLWSTASSQR VSPGLPSPNL ENGAPAVGPV QPRTPSVSAP 300
    LALSCPRQGG LPRSNSGLGG EVSGVMSKPN VDPQPWFQDG PKSYLSSSAP 350
    SSSPAGLDGS QQGAVPGLGP KPGCTDLGTG PKLSPTSLVH PVMSTLPELS 400
    CKEGPLGWSS DGSLGSVLLD SPSSPRVRLP CQPLVPGPEL RPSAAELKLE 450
    ALTQRLEREM DAHPKADYFG ACVKCSKGVF GAGQACQAMG NLYHDTCFTC 500
    AACSRKLRGK AFYFVNGKVF CEEDFLYSGF QQSADRCFLC GHLIMDMILQ 550
    ALGKSYHPGC FRCVICNECL DGVPFTVDSE NKIYCVRDYH KVLAPKCAAC 600
    GLPILPPEGS DETIRVVSMD RDYHVECYHC EDCGLELNDE DGHRCYPLED 650
    HLFCHSCHVK RLEKRPSSTA LHQHHF 676
    Length:676
    Mass (Da):72,190
    Last modified:May 1, 2000 - v1
    Checksum:i085DF06F047B49E6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361G → D.
    Corresponds to variant rs2578662 [ dbSNP | Ensembl ].
    VAR_050147
    Natural varianti415 – 4151G → R.
    Corresponds to variant rs3733113 [ dbSNP | Ensembl ].
    VAR_021993

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132408 mRNA. Translation: CAB63652.1.
    AJ312686 Genomic DNA. Translation: CAC35917.1.
    AJ297357 Genomic DNA. Translation: CAB95944.1.
    BC117236 mRNA. Translation: AAI17237.1.
    BC117238 mRNA. Translation: AAI17239.1.
    CCDSiCCDS2729.1.
    RefSeqiNP_055055.1. NM_014240.2.
    UniGeneiHs.193370.
    Hs.621057.

    Genome annotation databases

    EnsembliENST00000273317; ENSP00000273317; ENSG00000144791.
    GeneIDi8994.
    KEGGihsa:8994.
    UCSCiuc003coq.3. human.

    Polymorphism databases

    DMDMi47605932.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132408 mRNA. Translation: CAB63652.1 .
    AJ312686 Genomic DNA. Translation: CAC35917.1 .
    AJ297357 Genomic DNA. Translation: CAB95944.1 .
    BC117236 mRNA. Translation: AAI17237.1 .
    BC117238 mRNA. Translation: AAI17239.1 .
    CCDSi CCDS2729.1.
    RefSeqi NP_055055.1. NM_014240.2.
    UniGenei Hs.193370.
    Hs.621057.

    3D structure databases

    ProteinModelPortali Q9UGP4.
    SMRi Q9UGP4. Positions 470-658.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114475. 25 interactions.
    IntActi Q9UGP4. 8 interactions.
    MINTi MINT-1193166.
    STRINGi 9606.ENSP00000273317.

    PTM databases

    PhosphoSitei Q9UGP4.

    Polymorphism databases

    DMDMi 47605932.

    Proteomic databases

    MaxQBi Q9UGP4.
    PaxDbi Q9UGP4.
    PRIDEi Q9UGP4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273317 ; ENSP00000273317 ; ENSG00000144791 .
    GeneIDi 8994.
    KEGGi hsa:8994.
    UCSCi uc003coq.3. human.

    Organism-specific databases

    CTDi 8994.
    GeneCardsi GC03P045611.
    HGNCi HGNC:6612. LIMD1.
    MIMi 604543. gene.
    neXtProti NX_Q9UGP4.
    PharmGKBi PA30385.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331290.
    HOGENOMi HOG000072700.
    HOVERGENi HBG052327.
    InParanoidi Q9UGP4.
    KOi K16682.
    OMAi SLASPKW.
    PhylomeDBi Q9UGP4.
    TreeFami TF320310.

    Miscellaneous databases

    ChiTaRSi LIMD1. human.
    GeneWikii LIMD1.
    GenomeRNAii 8994.
    NextBioi 33727.
    PROi Q9UGP4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UGP4.
    Bgeei Q9UGP4.
    CleanExi HS_LIMD1.
    Genevestigatori Q9UGP4.

    Family and domain databases

    Gene3Di 2.10.110.10. 3 hits.
    InterProi IPR028734. LIMD1.
    IPR001781. Znf_LIM.
    [Graphical view ]
    PANTHERi PTHR24219:SF3. PTHR24219:SF3. 1 hit.
    Pfami PF00412. LIM. 3 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 3 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel gene containing LIM domains (LIMD1) is located within the common eliminated region 1 (C3CER1) in 3p21.3."
      Kiss H., Kedra D., Yang Y., Kost-Alimova M., Kiss C., O'Brien K.P., Fransson I., Klein G., Imreh S., Dumanski J.P.
      Hum. Genet. 105:552-559(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "The LZTFL1 gene is a part of a transcriptional map covering 250 kb within the common eliminated region 1 (C3CER1) in 3p21.3."
      Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G., Imreh S., Dumanski J.P.
      Genomics 73:10-19(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [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].
      Tissue: Brain.
    4. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    5. "LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at chromosome 3p21.3, binds pRB and represses E2F-driven transcription."
      Sharp T.V., Munoz F., Bourboulia D., Presneau N., Darai E., Wang H.-W., Cannon M., Butcher D.N., Nicholson A.G., Klein G., Imreh S., Boshoff C.
      Proc. Natl. Acad. Sci. U.S.A. 101:16531-16536(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RB1, SUBCELLULAR LOCATION, INDUCTION.
    6. "The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex."
      Feng Y., Longmore G.D.
      Mol. Cell. Biol. 25:4010-4022(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1.
    7. "Cell cycle regulated phosphorylation of LIMD1 in cell lines and expression in human breast cancers."
      Huggins C.J., Andrulis I.L.
      Cancer Lett. 267:55-66(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    8. "Ajuba LIM proteins are snail/slug corepressors required for neural crest development in Xenopus."
      Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L., Longmore G.D.
      Dev. Cell 14:424-436(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAI1.
    9. "Differential subcellular localisation of the tumour suppressor protein LIMD1 in breast cancer correlates with patient survival."
      Spendlove I., Al-Attar A., Watherstone O., Webb T.M., Ellis I.O., Longmore G.D., Sharp T.V.
      Int. J. Cancer 123:2247-2253(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-421 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Ajuba LIM proteins are negative regulators of the Hippo signaling pathway."
      Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B., Longmore G.D.
      Curr. Biol. 20:657-662(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2.
    14. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E; AGO1; AGO2; DCP2 AND DDX6.
    15. "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-272; SER-277 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
      Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
      BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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].
    19. Cited for: FUNCTION, INTERACTION WITH EGLN1/PHD2; EGLN2/PHD1; EGLN3/PHD3 AND VHL, IDENTIFICATION IN A COMPLEX WITH CUL2; EGLN1/PHD2; VHL AND TCEB2.

    Entry informationi

    Entry nameiLIMD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UGP4
    Secondary accession number(s): Q17RQ1, Q9BQQ9, Q9NQ47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 124 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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