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Protein

Fragile X mental retardation protein 1

Gene

FMR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • mRNA binding Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3775. FMR1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytoplasmic stress granule Source: Ensembl
  • dendrite Source: Ensembl
  • membrane Source: UniProtKB
  • mRNA cap binding complex Source: UniProtKB
  • nucleolus Source: HGNC
  • nucleoplasm Source: ProtInc
  • nucleus Source: GO_Central
  • polysome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Fragile X syndrome (FRAX)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionCommon 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.

See also OMIM:300624
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. 5 Publications
VAR_005234
Fragile X tremor/ataxia syndrome (FXTAS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionIn 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.

See also OMIM:300623
Premature ovarian failure 1 (POF1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:311360

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. 1 Publication
Mutagenesisi544 – 5441R → K: Reduces arginine methylation by 80%. 1 Publication
Mutagenesisi546 – 5461R → K: Slightly reduced methylation. 1 Publication

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.

Polymorphism and mutation databases

BioMutaiFMR1.
DMDMi544328.

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 – 5001Phosphoserine2 Publications
Modified residuei544 – 5441Omega-N-methylarginine1 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

BgeeiQ06787.
CleanExiHS_FMR1.
ExpressionAtlasiQ06787. baseline and differential.
GenevisibleiQ06787. HS.

Organism-specific databases

HPAiCAB012444.
HPA050118.
HPA056084.

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
FSD2A1L4K13EBI-10224470,EBI-5661036
FXR2P511163EBI-10224470,EBI-740459

Protein-protein interaction databases

BioGridi108619. 32 interactions.
DIPiDIP-29022N.
DIP-29509N.
IntActiQ06787. 22 interactions.
MINTiMINT-108156.
STRINGi9606.ENSP00000359506.

Structurei

Secondary structure

1
632
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi15 – 239Combined sources
Beta strandi25 – 328Combined sources
Helixi33 – 353Combined sources
Beta strandi40 – 434Combined sources
Helixi44 – 463Combined sources
Beta strandi64 – 696Combined sources
Beta strandi71 – 755Combined sources
Beta strandi78 – 8811Combined sources
Beta strandi91 – 977Combined sources
Helixi100 – 1034Combined sources
Beta strandi104 – 1085Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1143Combined sources
Turni123 – 1253Combined sources
Beta strandi127 – 1326Combined sources
Turni135 – 1384Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 1474Combined sources
Helixi148 – 1547Combined sources
Beta strandi157 – 1626Combined sources
Turni163 – 1664Combined sources
Beta strandi167 – 1737Combined sources
Helixi177 – 19822Combined sources
Beta strandi220 – 2245Combined sources
Helixi227 – 2293Combined sources
Helixi230 – 2345Combined sources
Helixi236 – 2383Combined sources
Helixi239 – 2457Combined sources
Beta strandi250 – 2567Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2688Combined sources
Helixi269 – 27911Combined sources
Beta strandi281 – 2899Combined sources
Helixi290 – 2923Combined sources
Helixi293 – 2975Combined sources
Helixi299 – 3013Combined sources
Helixi302 – 31110Combined sources
Beta strandi314 – 3218Combined sources
Beta strandi398 – 4069Combined sources
Helixi407 – 42216Combined sources
Beta strandi535 – 5384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKDNMR-N1-134[»]
2FMRNMR-A216-280[»]
2LA5NMR-B527-541[»]
2QNDX-ray1.90A/B216-425[»]
4OVAX-ray3.00A/B/C/D1-209[»]
4QVZX-ray3.20A/B1-213[»]
4QW2X-ray2.99A/B1-213[»]
DisProtiDP00134.
ProteinModelPortaliQ06787.
SMRiQ06787. Positions 3-202, 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.
GeneTreeiENSGT00390000017033.
HOVERGENiHBG005739.
InParanoidiQ06787.
KOiK15516.
OMAiSRVGPNA.
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. AlignAdd to basket

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

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP
60 70 80 90 100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD
110 120 130 140 150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF
160 170 180 190 200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM
210 220 230 240 250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV
260 270 280 290 300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
310 320 330 340 350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP
360 370 380 390 400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP
410 420 430 440 450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP
460 470 480 490 500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS GTNSEASNAS
510 520 530 540 550
ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG QGGRGRGGGF
560 570 580 590 600
KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS
610 620 630
EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP
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.Curated
The sequence AAA62466.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAA62467.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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. 5 Publications
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:
EMBLi
GenBanki
DDBJi
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]
CCDS55519.1. [Q06787-9]
CCDS76039.1. [Q06787-8]
PIRiI68614.
S45243. A40724.
RefSeqiNP_001172004.1. NM_001185075.1.
NP_001172005.1. NM_001185076.1. [Q06787-9]
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.
ENST00000440235; ENSP00000413764; ENSG00000102081. [Q06787-8]
GeneIDi2332.
KEGGihsa:2332.
UCSCiuc004fck.4. human. [Q06787-8]
uc010nst.3. human. [Q06787-1]
uc022cge.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS55519.1. [Q06787-9]
CCDS76039.1. [Q06787-8]
PIRiI68614.
S45243. A40724.
RefSeqiNP_001172004.1. NM_001185075.1.
NP_001172005.1. NM_001185076.1. [Q06787-9]
NP_001172010.1. NM_001185081.1.
NP_001172011.1. NM_001185082.1. [Q06787-8]
NP_002015.1. NM_002024.5. [Q06787-1]
UniGeneiHs.103183.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKDNMR-N1-134[»]
2FMRNMR-A216-280[»]
2LA5NMR-B527-541[»]
2QNDX-ray1.90A/B216-425[»]
4OVAX-ray3.00A/B/C/D1-209[»]
4QVZX-ray3.20A/B1-213[»]
4QW2X-ray2.99A/B1-213[»]
DisProtiDP00134.
ProteinModelPortaliQ06787.
SMRiQ06787. Positions 3-202, 216-334, 369-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108619. 32 interactions.
DIPiDIP-29022N.
DIP-29509N.
IntActiQ06787. 22 interactions.
MINTiMINT-108156.
STRINGi9606.ENSP00000359506.

PTM databases

PhosphoSiteiQ06787.

Polymorphism and mutation databases

BioMutaiFMR1.
DMDMi544328.

Proteomic databases

MaxQBiQ06787.
PaxDbiQ06787.
PRIDEiQ06787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000218200; ENSP00000218200; ENSG00000102081. [Q06787-9]
ENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
ENST00000370475; ENSP00000359506; ENSG00000102081.
ENST00000440235; ENSP00000413764; ENSG00000102081. [Q06787-8]
GeneIDi2332.
KEGGihsa:2332.
UCSCiuc004fck.4. human. [Q06787-8]
uc010nst.3. human. [Q06787-1]
uc022cge.1. human.

Organism-specific databases

CTDi2332.
GeneCardsiGC0XP146993.
GeneReviewsiFMR1.
HGNCiHGNC:3775. FMR1.
HPAiCAB012444.
HPA050118.
HPA056084.
MIMi300623. phenotype.
300624. phenotype.
309550. gene.
311360. phenotype.
neXtProtiNX_Q06787.
Orphaneti908. Fragile X syndrome.
93256. Fragile X-associated tremor/ataxia syndrome.
619. Primary ovarian failure.
261483. Xq27.3q28 duplication syndrome.
PharmGKBiPA28191.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG75351.
GeneTreeiENSGT00390000017033.
HOVERGENiHBG005739.
InParanoidiQ06787.
KOiK15516.
OMAiSRVGPNA.
PhylomeDBiQ06787.
TreeFamiTF105427.

Miscellaneous databases

ChiTaRSiFMR1. human.
EvolutionaryTraceiQ06787.
GeneWikiiFMR1.
GenomeRNAii2332.
NextBioi9465.
PROiQ06787.
SOURCEiSearch...

Gene expression databases

BgeeiQ06787.
CleanExiHS_FMR1.
ExpressionAtlasiQ06787. baseline and differential.
GenevisibleiQ06787. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  30. "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.
  31. "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.
  32. "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.
  33. Cited for: VARIANT FRAX ASN-304.
  34. Cited for: CHARACTERIZATION OF FRAX ASN-304.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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.
  40. "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: July 22, 2015
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.