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)

Q06787

- FMR1_HUMAN

UniProt

Q06787 - FMR1_HUMAN

Protein

Fragile X mental retardation protein 1

Gene

FMR1

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 159 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Translation repressor. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression By similarity. RNA-binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C).By similarity

    GO - Molecular functioni

    1. mRNA binding Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. central nervous system development Source: Ensembl
    2. mRNA transport Source: UniProtKB-KW
    3. negative regulation of translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA transport, Transport

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fragile X mental retardation protein 1
    Short name:
    FMRP
    Short name:
    Protein FMR-1
    Gene namesi
    Name:FMR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3775. FMR1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. cytoplasmic stress granule Source: Ensembl
    4. dendritic shaft Source: Ensembl
    5. dendritic spine Source: Ensembl
    6. membrane Source: UniProtKB
    7. mRNA cap binding complex Source: UniProtKB
    8. neuronal ribonucleoprotein granule Source: Ensembl
    9. nucleolus Source: HGNC
    10. nucleoplasm Source: ProtInc
    11. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Fragile X syndrome (FRAX) [MIM:300624]: Common genetic disease (has a prevalence of one in every 2000 children) which is characterized by moderate to severe mental retardation, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most fragile X syndrome patients results from an amplification of a CGG repeat region which is directly in front of the coding region.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti304 – 3041I → N in FRAX; alters protein folding and stability; the protein is able to bind RNA, but has reduced affinity for RNA at high salt concentrations. 1 Publication
    VAR_005234
    Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: In FXTAS, the expanded repeats range in size from 55 to 200 repeats and are referred to as 'premutations'. Full repeat expansions with greater than 200 repeats results in fragile X mental retardation syndrome [MIM:300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Premature ovarian failure 1 (POF1) [MIM:311360]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1262TF → AA: Alters the structural integrity of the N-terminus and leads to aggregation. 1 Publication
    Mutagenesisi500 – 5001S → A: Loss of phosphorylation. 2 Publications
    Mutagenesisi544 – 5441R → K: Reduces arginine methylation by 80%. 2 Publications
    Mutagenesisi546 – 5461R → K: Slightly reduced methylation. 2 Publications

    Keywords - Diseasei

    Disease mutation, Mental retardation, Premature ovarian failure

    Organism-specific databases

    MIMi300623. phenotype.
    300624. phenotype.
    311360. phenotype.
    Orphaneti908. Fragile X syndrome.
    93256. Fragile X-associated tremor/ataxia syndrome.
    619. Primary ovarian failure.
    261483. Xq27.3q28 duplication syndrome.
    PharmGKBiPA28191.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Fragile X mental retardation protein 1PRO_0000050102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei337 – 3371PhosphoserineBy similarity
    Modified residuei370 – 3701Phosphoserine1 Publication
    Modified residuei500 – 5001Phosphoserine1 Publication
    Modified residuei544 – 5441Omega-N-methylated arginine1 Publication

    Post-translational modificationi

    Phosphorylated on several serine residues.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ06787.
    PaxDbiQ06787.
    PRIDEiQ06787.

    PTM databases

    PhosphoSiteiQ06787.

    Expressioni

    Tissue specificityi

    Highest levels found in neurons, brain, testis, placenta and lymphocytes. Also expressed in epithelial tissues and at very low levels in glial cells.2 Publications

    Gene expression databases

    ArrayExpressiQ06787.
    BgeeiQ06787.
    CleanExiHS_FMR1.
    GenevestigatoriQ06787.

    Organism-specific databases

    HPAiCAB012444.
    HPA050118.

    Interactioni

    Subunit structurei

    Component of the CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and FMR1. Interacts with CYFIP1 and CYFIP2. The interaction with brain cytoplasmic RNA 1 (BC1) increases binding affinity for the CYFIP1-EIF4E complex in the brain By similarity. Homooligomer. Found in a RNP granule complex with IGF2BP1. Directly interacts with SMN and TDRD3. Interacts with the SMN core complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Interacts with FXR1, FXR2, IGF2BP1, NUFIP1, NUFIP2, MCRS1 and RANBP9.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CYFIP1Q7L5764EBI-366305,EBI-1048143
    CYFIP2Q96F072EBI-366305,EBI-2433893

    Protein-protein interaction databases

    BioGridi108619. 27 interactions.
    DIPiDIP-29022N.
    DIP-29509N.
    IntActiQ06787. 20 interactions.
    MINTiMINT-108156.
    STRINGi9606.ENSP00000359506.

    Structurei

    Secondary structure

    1
    632
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 2319
    Beta strandi25 – 317
    Beta strandi34 – 363
    Beta strandi40 – 434
    Beta strandi46 – 483
    Beta strandi64 – 674
    Beta strandi80 – 889
    Beta strandi91 – 988
    Beta strandi105 – 1084
    Helixi109 – 1113
    Beta strandi121 – 1233
    Turni124 – 1263
    Beta strandi220 – 2245
    Helixi227 – 2293
    Helixi230 – 2345
    Helixi236 – 2383
    Helixi239 – 2457
    Beta strandi250 – 2567
    Turni257 – 2604
    Beta strandi261 – 2688
    Helixi269 – 27911
    Beta strandi281 – 2899
    Helixi290 – 2923
    Helixi293 – 2975
    Helixi299 – 3013
    Helixi302 – 31110
    Beta strandi314 – 3218
    Beta strandi398 – 4069
    Helixi407 – 42216
    Beta strandi535 – 5384

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BKDNMR-N1-134[»]
    2FMRNMR-A216-280[»]
    2LA5NMR-B527-541[»]
    2QNDX-ray1.90A/B216-425[»]
    DisProtiDP00134.
    ProteinModelPortaliQ06787.
    SMRiQ06787. Positions 1-134, 216-334, 369-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06787.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 5047Agenet-like 1Add
    BLAST
    Domaini63 – 11553Agenet-like 2Add
    BLAST
    Domaini222 – 25130KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini285 – 31430KH 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni419 – 632214Interaction with RANBP9Add
    BLAST
    Regioni534 – 54815RNA-binding RGG-boxAdd
    BLAST

    Domaini

    The tandem Tudor domains preferentially recognize trimethylated histone peptides.By similarity

    Sequence similaritiesi

    Belongs to the FMR1 family.Curated
    Contains 2 Agenet-like domains.Curated
    Contains 2 KH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG75351.
    HOVERGENiHBG005739.
    InParanoidiQ06787.
    KOiK15516.
    OMAiKAWQGMV.
    PhylomeDBiQ06787.
    TreeFamiTF105427.

    Family and domain databases

    Gene3Di3.30.1370.10. 3 hits.
    InterProiIPR008395. Agenet-like_dom.
    IPR022034. Frag_X_MRP_fam.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view]
    PfamiPF05641. Agenet. 1 hit.
    PF12235. FXR1P_C. 1 hit.
    PF00013. KH_1. 2 hits.
    [Graphical view]
    SMARTiSM00322. KH. 2 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 2 hits.
    PROSITEiPS51641. AGENET_LIKE. 2 hits.
    PS50084. KH_TYPE_1. 2 hits.
    [Graphical view]

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Note: At least 12 different isoforms are produced.

    Isoform 6 (identifier: Q06787-1) [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

    MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP    50
    PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 100
    ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 150
    KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 200
    RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 250
    TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 300
    GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 350
    EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 400
    FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 450
    PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS GTNSEASNAS 500
    ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG QGGRGRGGGF 550
    KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS 600
    EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP 632
    Length:632
    Mass (Da):71,174
    Last modified:June 1, 1994 - v1
    Checksum:iF853D6C82E3489B9
    GO
    Isoform 1 (identifier: Q06787-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         376-396: Missing.
         580-596: Missing.

    Show »
    Length:594
    Mass (Da):66,971
    Checksum:iBC65C14768EB268C
    GO
    Isoform 2 (identifier: Q06787-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         491-502: Missing.

    Show »
    Length:620
    Mass (Da):70,025
    Checksum:i8C8BC3876E1D92CA
    GO
    Isoform 3 (identifier: Q06787-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         491-502: Missing.
         580-596: Missing.

    Show »
    Length:603
    Mass (Da):68,030
    Checksum:iB8F3364E88A3489B
    GO
    Isoform 4 (identifier: Q06787-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         491-515: Missing.

    Show »
    Length:607
    Mass (Da):68,455
    Checksum:i561113CBB00CCAD0
    GO
    Isoform 5 (identifier: Q06787-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         491-515: Missing.
         580-596: Missing.

    Show »
    Length:590
    Mass (Da):66,460
    Checksum:i643FA1A3826879A3
    GO
    Isoform 7 (identifier: Q06787-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-596: Missing.

    Show »
    Length:615
    Mass (Da):69,179
    Checksum:iFE061178DA0A7ABB
    GO
    Isoform 8 (identifier: Q06787-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         376-396: Missing.
         491-515: Missing.

    Show »
    Length:586
    Mass (Da):66,246
    Checksum:iB413D4F8FA0D697F
    GO
    Isoform 9 (identifier: Q06787-9) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         376-396: Missing.

    Show »
    Length:611
    Mass (Da):68,966
    Checksum:iE69936008EABA9D6
    GO

    Sequence cautioni

    The sequence AAA52458.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAA62466.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAA62467.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2952Missing in AAA52458. (PubMed:1710175)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381R → Q Rare variant found in a developmentally delayed male; unknown pathological significance. 1 Publication
    VAR_064507
    Natural varianti145 – 1451A → S.
    Corresponds to variant rs29281 [ dbSNP | Ensembl ].
    VAR_029278
    Natural varianti304 – 3041I → N in FRAX; alters protein folding and stability; the protein is able to bind RNA, but has reduced affinity for RNA at high salt concentrations. 1 Publication
    VAR_005234
    Natural varianti546 – 5461R → H.1 Publication
    VAR_005235

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei376 – 39621Missing in isoform 1, isoform 8 and isoform 9. 2 PublicationsVSP_002823Add
    BLAST
    Alternative sequencei491 – 51525Missing in isoform 4, isoform 5 and isoform 8. 1 PublicationVSP_002825Add
    BLAST
    Alternative sequencei491 – 50212Missing in isoform 2 and isoform 3. CuratedVSP_002824Add
    BLAST
    Alternative sequencei580 – 59617Missing in isoform 1, isoform 3, isoform 5 and isoform 7. CuratedVSP_002826Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29074 Genomic DNA. Translation: AAB18828.1.
    L29074 Genomic DNA. Translation: AAB18829.1.
    L29074 Genomic DNA. Translation: AAB18830.1.
    L29074 Genomic DNA. Translation: AAB18831.1.
    L29074 Genomic DNA. Translation: AAB18832.1.
    L29074 Genomic DNA. Translation: AAB18833.1.
    KJ534836 mRNA. Translation: AHW56476.1.
    CH471171 Genomic DNA. Translation: EAW61294.1.
    CH471171 Genomic DNA. Translation: EAW61296.1.
    CH471171 Genomic DNA. Translation: EAW61298.1.
    CH471171 Genomic DNA. Translation: EAW61301.1.
    CH471171 Genomic DNA. Translation: EAW61302.1.
    CH471171 Genomic DNA. Translation: EAW61303.1.
    BC086957 mRNA. Translation: AAH86957.1.
    M67468 mRNA. Translation: AAA52458.1. Different initiation.
    X69962 mRNA. Translation: CAA49586.1.
    S65791 mRNA. Translation: AAB28395.2.
    L19476 Genomic DNA. Translation: AAA62452.2.
    L19477 Genomic DNA. Translation: AAA62453.1.
    L19478 Genomic DNA. Translation: AAA62454.1.
    L19479 Genomic DNA. Translation: AAA62455.1.
    L19480 Genomic DNA. Translation: AAA62456.1.
    L19481 Genomic DNA. Translation: AAA62457.1.
    L19482 Genomic DNA. Translation: AAA62458.1.
    L19483 Genomic DNA. Translation: AAA62459.1.
    L19484 Genomic DNA. Translation: AAA62460.1.
    L19485 Genomic DNA. Translation: AAA62461.1.
    L19486 Genomic DNA. Translation: AAA62462.1.
    L19487 Genomic DNA. Translation: AAA62463.1.
    L19488 Genomic DNA. Translation: AAA62464.1.
    L19489 Genomic DNA. Translation: AAA62465.1.
    L19490 Genomic DNA. Translation: AAA62466.1. Sequence problems.
    L19491 Genomic DNA. Translation: AAA62467.1. Sequence problems.
    L19492 Genomic DNA. Translation: AAA62468.1.
    L19493 Genomic DNA. Translation: AAA62469.1.
    S76590 Genomic DNA. Translation: AAD14228.1.
    CCDSiCCDS14682.1. [Q06787-1]
    PIRiI68614.
    S45243. A40724.
    RefSeqiNP_001172004.1. NM_001185075.1.
    NP_001172005.1. NM_001185076.1.
    NP_001172010.1. NM_001185081.1.
    NP_001172011.1. NM_001185082.1. [Q06787-8]
    NP_002015.1. NM_002024.5. [Q06787-1]
    UniGeneiHs.103183.

    Genome annotation databases

    EnsembliENST00000218200; ENSP00000218200; ENSG00000102081. [Q06787-9]
    ENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
    ENST00000370475; ENSP00000359506; ENSG00000102081. [Q06787-1]
    GeneIDi2332.
    KEGGihsa:2332.
    UCSCiuc004fck.4. human. [Q06787-8]
    uc010nst.3. human. [Q06787-1]

    Polymorphism databases

    DMDMi544328.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29074 Genomic DNA. Translation: AAB18828.1 .
    L29074 Genomic DNA. Translation: AAB18829.1 .
    L29074 Genomic DNA. Translation: AAB18830.1 .
    L29074 Genomic DNA. Translation: AAB18831.1 .
    L29074 Genomic DNA. Translation: AAB18832.1 .
    L29074 Genomic DNA. Translation: AAB18833.1 .
    KJ534836 mRNA. Translation: AHW56476.1 .
    CH471171 Genomic DNA. Translation: EAW61294.1 .
    CH471171 Genomic DNA. Translation: EAW61296.1 .
    CH471171 Genomic DNA. Translation: EAW61298.1 .
    CH471171 Genomic DNA. Translation: EAW61301.1 .
    CH471171 Genomic DNA. Translation: EAW61302.1 .
    CH471171 Genomic DNA. Translation: EAW61303.1 .
    BC086957 mRNA. Translation: AAH86957.1 .
    M67468 mRNA. Translation: AAA52458.1 . Different initiation.
    X69962 mRNA. Translation: CAA49586.1 .
    S65791 mRNA. Translation: AAB28395.2 .
    L19476 Genomic DNA. Translation: AAA62452.2 .
    L19477 Genomic DNA. Translation: AAA62453.1 .
    L19478 Genomic DNA. Translation: AAA62454.1 .
    L19479 Genomic DNA. Translation: AAA62455.1 .
    L19480 Genomic DNA. Translation: AAA62456.1 .
    L19481 Genomic DNA. Translation: AAA62457.1 .
    L19482 Genomic DNA. Translation: AAA62458.1 .
    L19483 Genomic DNA. Translation: AAA62459.1 .
    L19484 Genomic DNA. Translation: AAA62460.1 .
    L19485 Genomic DNA. Translation: AAA62461.1 .
    L19486 Genomic DNA. Translation: AAA62462.1 .
    L19487 Genomic DNA. Translation: AAA62463.1 .
    L19488 Genomic DNA. Translation: AAA62464.1 .
    L19489 Genomic DNA. Translation: AAA62465.1 .
    L19490 Genomic DNA. Translation: AAA62466.1 . Sequence problems.
    L19491 Genomic DNA. Translation: AAA62467.1 . Sequence problems.
    L19492 Genomic DNA. Translation: AAA62468.1 .
    L19493 Genomic DNA. Translation: AAA62469.1 .
    S76590 Genomic DNA. Translation: AAD14228.1 .
    CCDSi CCDS14682.1. [Q06787-1 ]
    PIRi I68614.
    S45243. A40724.
    RefSeqi NP_001172004.1. NM_001185075.1.
    NP_001172005.1. NM_001185076.1.
    NP_001172010.1. NM_001185081.1.
    NP_001172011.1. NM_001185082.1. [Q06787-8 ]
    NP_002015.1. NM_002024.5. [Q06787-1 ]
    UniGenei Hs.103183.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BKD NMR - N 1-134 [» ]
    2FMR NMR - A 216-280 [» ]
    2LA5 NMR - B 527-541 [» ]
    2QND X-ray 1.90 A/B 216-425 [» ]
    DisProti DP00134.
    ProteinModelPortali Q06787.
    SMRi Q06787. Positions 1-134, 216-334, 369-425.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108619. 27 interactions.
    DIPi DIP-29022N.
    DIP-29509N.
    IntActi Q06787. 20 interactions.
    MINTi MINT-108156.
    STRINGi 9606.ENSP00000359506.

    PTM databases

    PhosphoSitei Q06787.

    Polymorphism databases

    DMDMi 544328.

    Proteomic databases

    MaxQBi Q06787.
    PaxDbi Q06787.
    PRIDEi Q06787.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000218200 ; ENSP00000218200 ; ENSG00000102081 . [Q06787-9 ]
    ENST00000370470 ; ENSP00000359501 ; ENSG00000102081 . [Q06787-6 ]
    ENST00000370475 ; ENSP00000359506 ; ENSG00000102081 . [Q06787-1 ]
    GeneIDi 2332.
    KEGGi hsa:2332.
    UCSCi uc004fck.4. human. [Q06787-8 ]
    uc010nst.3. human. [Q06787-1 ]

    Organism-specific databases

    CTDi 2332.
    GeneCardsi GC0XP146993.
    GeneReviewsi FMR1.
    HGNCi HGNC:3775. FMR1.
    HPAi CAB012444.
    HPA050118.
    MIMi 300623. phenotype.
    300624. phenotype.
    309550. gene.
    311360. phenotype.
    neXtProti NX_Q06787.
    Orphaneti 908. Fragile X syndrome.
    93256. Fragile X-associated tremor/ataxia syndrome.
    619. Primary ovarian failure.
    261483. Xq27.3q28 duplication syndrome.
    PharmGKBi PA28191.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75351.
    HOVERGENi HBG005739.
    InParanoidi Q06787.
    KOi K15516.
    OMAi KAWQGMV.
    PhylomeDBi Q06787.
    TreeFami TF105427.

    Miscellaneous databases

    ChiTaRSi FMR1. human.
    EvolutionaryTracei Q06787.
    GeneWikii FMR1.
    GenomeRNAii 2332.
    NextBioi 9465.
    PROi Q06787.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06787.
    Bgeei Q06787.
    CleanExi HS_FMR1.
    Genevestigatori Q06787.

    Family and domain databases

    Gene3Di 3.30.1370.10. 3 hits.
    InterProi IPR008395. Agenet-like_dom.
    IPR022034. Frag_X_MRP_fam.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view ]
    Pfami PF05641. Agenet. 1 hit.
    PF12235. FXR1P_C. 1 hit.
    PF00013. KH_1. 2 hits.
    [Graphical view ]
    SMARTi SM00322. KH. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 2 hits.
    PROSITEi PS51641. AGENET_LIKE. 2 hits.
    PS50084. KH_TYPE_1. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome."
      Verkerk A.J.M.H., Pieretti M., Sutcliffe J.S., Fu Y.H., Kuhl D.P., Pizzuti A., Reiner O., Richards S., Victoria M.F., Zhang F., Eussen B.E., van Ommen G.-J.B., Blonden L.A.J., Riggins G.J., Chastain J.L., Kunst C.B., Galjaard H., Caskey C.T.
      , Nelson D.L., Oostra B.A., Warren S.T.
      Cell 65:905-914(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
      Tissue: Fetal brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY.
      Tissue: Fetal brain and Liver.
    3. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
      Tissue: Fetal brain.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] (ISOFORM 8).
      Tissue: Placenta.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34; 36-139; 141-293; 295-490 AND 492-632.
    8. Erratum
      Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
      Hum. Mol. Genet. 3:684-685(1994) [PubMed] [Europe PMC] [Abstract]
    9. Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 18-34.
    10. "Two new cases of FMR1 deletion associated with mental impairment."
      Hirst M., Grewal P., Flannery A., Slatter R., Maher E., Barton D., Fryns J.-P., Davies K.
      Am. J. Hum. Genet. 56:67-74(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
    11. "The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein."
      Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G.
      Cell 74:291-298(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, INVOLVEMENT IN FRAX.
    12. "Characterization and localization of the FMR-1 gene product associated with fragile X syndrome."
      Verheij C., Bakker C.E., de Graaff E., Keulemans J., Willemsen R., Verkerk A.J.M.H., Galjaard H., Reuser A.J.J., Hoogeveen A.T., Oostra B.A.
      Nature 363:722-724(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation."
      Devys D., Lutz Y., Rouyer N., Bellocq J.-P., Mandel J.-L.
      Nat. Genet. 4:335-340(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN FRAX.
    14. "FMR1 protein: conserved RNP family domains and selective RNA binding."
      Ashley C.T. Jr., Wilkinson K.D., Reines D., Warren S.T.
      Science 262:563-566(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    15. "FXR1, an autosomal homolog of the fragile X mental retardation gene."
      Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L., Dreyfuss G.
      EMBO J. 14:2401-2408(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, SUBCELLULAR LOCATION.
    16. "Studies of FRAXA and FRAXE in women with premature ovarian failure."
      Murray A., Webb J., Grimley S., Conway G., Jacobs P.
      J. Med. Genet. 35:637-640(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN POF1.
    17. "A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein."
      Bardoni B., Schenck A., Mandel J.-L.
      Hum. Mol. Genet. 8:2557-2566(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUFIP1.
    18. "Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties."
      Siomi M.C., Higashijima K., Ishizuka A., Siomi H.
      Mol. Cell. Biol. 22:8438-8447(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-500, MUTAGENESIS OF SER-500.
    19. "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization."
      Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.
      Hum. Mol. Genet. 12:1689-1698(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUFIP2, SUBCELLULAR LOCATION.
    20. "Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs."
      Rackham O., Brown C.M.
      EMBO J. 23:3346-3355(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A RNP GRANULE COMPLEX WITH IGF2BP1, INTERACTION WITH IGF2BP1.
    21. "The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
      Menon R.P., Gibson T.J., Pastore A.
      J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9.
    22. "Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein."
      Dolzhanskaya N., Merz G., Denman R.B.
      Biochemistry 45:10385-10393(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-544, MUTAGENESIS OF ARG-544 AND ARG-546.
    23. "The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons."
      Davidovic L., Bechara E., Gravel M., Jaglin X.H., Tremblay S., Sik A., Bardoni B., Khandjian E.W.
      Hum. Mol. Genet. 15:1525-1538(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCRS1, SUBCELLULAR LOCATION.
    24. "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
      Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
      Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TDRD3.
    25. "In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein."
      Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.
      J. Biol. Chem. 283:5598-5610(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMN AND THE SMN CORE COMPLEX.
    26. "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-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome."
      Musco G., Kharrat A., Stier G., Fraternali F., Gibson T.J., Nilges M., Pastore A.
      Nat. Struct. Biol. 4:712-716(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 216-280.
    30. "The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction."
      Ramos A., Hollingworth D., Adinolfi S., Castets M., Kelly G., Frenkiel T.A., Bardoni B., Pastore A.
      Structure 14:21-31(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-134, MUTAGENESIS OF 125-THR-PHE-126, SUBCELLULAR LOCATION, INTERACTION WITH NUFIP2.
    31. "Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein."
      Valverde R., Pozdnyakova I., Kajander T., Venkatraman J., Regan L.
      Structure 15:1090-1098(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 397-425, CHARACTERIZATION OF VARIANT FRAX ASN-304.
    32. Cited for: VARIANT FRAX ASN-304.
    33. Cited for: CHARACTERIZATION OF FRAX ASN-304.
    34. "Novel point mutation within intron 10 of FMR-1 gene causing fragile X syndrome."
      Wang Y.-C., Lin M.-L., Lin S.J., Li Y.-C., Li S.-Y.
      Hum. Mutat. 10:393-399(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIS-546.
    35. "FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association."
      Feng Y., Absher D., Eberhart D.E., Brown V., Malter H.E., Warren S.T.
      Mol. Cell 1:109-118(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304.
    36. "Intention tremor, parkinsonism, and generalized brain atrophy in male carriers of fragile X."
      Hagerman R.J., Leehey M., Heinrichs W., Tassone F., Wilson R., Hills J., Grigsby J., Gage B., Hagerman P.J.
      Neurology 57:127-130(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN FXTAS.
    37. "Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes."
      Darnell J.C., Fraser C.E., Mostovetsky O., Stefani G., Jones T.A., Eddy S.R., Darnell R.B.
      Genes Dev. 19:903-918(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304.
    38. "Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP."
      Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B., Meister G., Keidel E., Fischer U.
      Hum. Mol. Genet. 17:3236-3246(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304, SUBUNIT, INTERACTION WITH TDRD3.
    39. "Identification of novel FMR1 variants by massively parallel sequencing in developmentally delayed males."
      Collins S.C., Bray S.M., Suhl J.A., Cutler D.J., Coffee B., Zwick M.E., Warren S.T.
      Am. J. Med. Genet. A 152:2512-2520(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLN-138.

    Entry informationi

    Entry nameiFMR1_HUMAN
    AccessioniPrimary (citable) accession number: Q06787
    Secondary accession number(s): A6NNH4
    , D3DWT0, D3DWT1, D3DWT2, G8JL90, Q16578, Q5PQZ6, Q99054
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 159 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

    Miscellaneous

    RNA-binding activity is inhibited by RANBP9.
    The mechanism of the severe phenotype in the Asn-304 patient lies in the sequestration of bound mRNAs in nontranslatable mRNP particles. In the absence of FMRP, these same mRNAs may be partially translated via alternate mRNPs, although perhaps abnormally localized or regulated, resulting in typical fragile X syndrome. Asn-304 mutation maps to a position within the second KH domain of FMRP that is critical for stabilizing sequence-specific RNA-protein interactions. Asn-304 mutation abrogates the association of the FMRP KH 2 domain with its target, kissing complex RNA.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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