Q06787 (FMR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fragile X mental retardation protein 1
Short name=FMRP
Short name=Protein FMR-1

Gene names

Name:

FMR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	632 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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).
Subunit structure	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. Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.30 Ref.38
Subcellular location	Cytoplasm. Nucleus › nucleolus Ref.12 Ref.13 Ref.15 Ref.19 Ref.23 Ref.30.
Tissue specificity	Highest levels found in neurons, brain, testis, placenta and lymphocytes. Also expressed in epithelial tissues and at very low levels in glial cells. Ref.2 Ref.13
Domain	The tandem Tudor domains preferentially recognize trimethylated histone peptides By similarity.
Post-translational modification	Phosphorylated on several serine residues By similarity. Ref.18
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.13 Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16
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.
Sequence similarities	Belongs to the FMR1 family. Contains 2 Agenet-like domains. Contains 2 KH domains.
Sequence caution	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.

Ontologies

Keywords
Biological process	mRNA transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation Premature ovarian failure
Domain	Repeat
Ligand	RNA-binding
Molecular function	Repressor
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	central nervous system development Inferred from electronic annotation. Source: Ensembl mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translational initiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Traceable author statement Ref.30. Source: HGNC cytoplasmic stress granule Inferred from electronic annotation. Source: Ensembl dendritic shaft Inferred from electronic annotation. Source: Ensembl dendritic spine Inferred from electronic annotation. Source: Ensembl mRNA cap binding complex Inferred from sequence or structural similarity. Source: UniProtKB neuronal ribonucleoprotein granule Inferred from electronic annotation. Source: Ensembl nucleolus Traceable author statement Ref.30. Source: HGNC nucleoplasm Traceable author statement PubMed 10888599. Source: ProtInc synapse Inferred from electronic annotation. Source: Ensembl
Molecular_function	RNA binding Traceable author statement PubMed 8156595. Source: ProtInc mRNA binding Traceable author statement Ref.14. Source: ProtInc poly(A) RNA binding Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYFIP1	Q7L576	4	EBI-366305,EBI-1048143
CYFIP2	Q96F07	2	EBI-366305,EBI-2433893

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: At least 12 different isoforms are produced.

Isoform 6 (identifier: Q06787-1)

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.

Isoform 1 (identifier: Q06787-2)

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

Isoform 2 (identifier: Q06787-3)

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

Isoform 3 (identifier: Q06787-4)

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

Isoform 4 (identifier: Q06787-5)

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

Isoform 5 (identifier: Q06787-6)

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

Isoform 7 (identifier: Q06787-7)

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

Isoform 8 (identifier: Q06787-8)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 632

632

Fragile X mental retardation protein 1

PRO_0000050102

Regions

Domain

4 – 50

47

Agenet-like 1

Domain

63 – 115

53

Agenet-like 2

Domain

222 – 251

30

KH 1

Domain

285 – 314

30

KH 2

Region

419 – 632

214

Interaction with RANBP9

Region

534 – 548

15

RNA-binding RGG-box

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.28

Modified residue

337

1

Phosphoserine By similarity

Modified residue

370

1

Phosphoserine Ref.26

Modified residue

500

1

Phosphoserine Ref.18

Modified residue

544

1

Omega-N-methylated arginine Ref.22

Natural variations

Alternative sequence

376 – 396

21

Missing in isoform 1 and isoform 8.

VSP_002823

Alternative sequence

491 – 515

25

Missing in isoform 4, isoform 5 and isoform 8.

VSP_002825

Alternative sequence

491 – 502

12

Missing in isoform 2 and isoform 3.

VSP_002824

Alternative sequence

580 – 596

17

Missing in isoform 1, isoform 3, isoform 5 and isoform 7.

VSP_002826

Natural variant

138

1

R → Q Rare variant found in a developmentally delayed male; unknown pathological significance. Ref.39

VAR_064507

Natural variant

145

1

A → S.
Corresponds to variant rs29281 [ dbSNP | Ensembl ].

VAR_029278

Natural variant

304

1

I → 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. Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38

VAR_005234

Natural variant

546

1

R → H. Ref.34

VAR_005235

Experimental info

Mutagenesis

125 – 126

2

TF → AA: Alters the structural integrity of the N-terminus and leads to aggregation. Ref.30

Mutagenesis

500

1

S → A: Loss of phosphorylation. Ref.18 Ref.30

Mutagenesis

544

1

R → K: Reduces arginine methylation by 80%. Ref.22 Ref.30

Mutagenesis

546

1

R → K: Slightly reduced methylation. Ref.22 Ref.30

Sequence conflict

294 – 295

2

Missing in AAA52458. Ref.1

Secondary structure

1

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632

Helix Strand Turn

Details...

Beta strand

5 – 23

19

Beta strand

25 – 31

7

Beta strand

34 – 36

3

Beta strand

40 – 43

4

Beta strand

46 – 48

3

Beta strand

64 – 67

4

Beta strand

80 – 88

9

Beta strand

91 – 98

8

Beta strand

105 – 108

4

Helix

109 – 111

3

Beta strand

121 – 123

3

Turn

124 – 126

3

Beta strand

220 – 224

5

Helix

227 – 229

3

Helix

230 – 234

5

Helix

236 – 238

3

Helix

239 – 245

7

Beta strand

250 – 256

7

Turn

257 – 260

4

Beta strand

261 – 268

8

Helix

269 – 279

11

Beta strand

281 – 289

9

Helix

290 – 292

3

Helix

293 – 297

5

Helix

299 – 301

3

Helix

302 – 311

10

Beta strand

314 – 321

8

Beta strand

398 – 406

9

Helix

407 – 422

16

Beta strand

535 – 538

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 6 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: F853D6C82E3489B9	FASTA	632	71,174
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 430 440 450 460 470 480 LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 490 500 510 520 530 540 HGRRGPGYTS GTNSEASNAS ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG 550 560 570 580 590 600 QGGRGRGGGF KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS 610 620 630 EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP
	Isoform 1 [UniParc]. Checksum: BC65C14768EB268C	FASTA	594	66,971
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL 430 440 450 460 470 480 RQIGASSRPP PNRTDKEKSY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSG TNSEASNASE 490 500 510 520 530 540 TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRGGGGRGQ GGRGRGGGFK GNDDHSRTDN 550 560 570 580 590 RPRNPREAKG RTTDGSLQNT SSEGSRLRTG KDRNQKKEKP DSVDGQQPLV NGVP
	Isoform 2 [UniParc]. Checksum: 8C8BC3876E1D92CA	FASTA	620	70,025
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 430 440 450 460 470 480 LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 490 500 510 520 530 540 HGRRGPGYTS ESDHRDELSD WSLAPTEEER ESFLRRGDGR RRGGGGRGQG GRGRGGGFKG 550 560 570 580 590 600 NDDHSRTDNR PRNPREAKGR TTDGSLQIRV DCNNERSVHT KTLQNTSSEG SRLRTGKDRN 610 620 QKKEKPDSVD GQQPLVNGVP
	Isoform 3 [UniParc]. Checksum: B8F3364E88A3489B	FASTA	603	68,030
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 430 440 450 460 470 480 LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 490 500 510 520 530 540 HGRRGPGYTS ESDHRDELSD WSLAPTEEER ESFLRRGDGR RRGGGGRGQG GRGRGGGFKG 550 560 570 580 590 600 NDDHSRTDNR PRNPREAKGR TTDGSLQNTS SEGSRLRTGK DRNQKKEKPD SVDGQQPLVN GVP
	Isoform 4 [UniParc]. Checksum: 561113CBB00CCAD0	FASTA	607	68,455
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 430 440 450 460 470 480 LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 490 500 510 520 530 540 HGRRGPGYTS APTEEERESF LRRGDGRRRG GGGRGQGGRG RGGGFKGNDD HSRTDNRPRN 550 560 570 580 590 600 PREAKGRTTD GSLQIRVDCN NERSVHTKTL QNTSSEGSRL RTGKDRNQKK EKPDSVDGQQ PLVNGVP
	Isoform 5 [UniParc]. Checksum: 643FA1A3826879A3	FASTA	590	66,460
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 430 440 450 460 470 480 LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 490 500 510 520 530 540 HGRRGPGYTS APTEEERESF LRRGDGRRRG GGGRGQGGRG RGGGFKGNDD HSRTDNRPRN 550 560 570 580 590 PREAKGRTTD GSLQNTSSEG SRLRTGKDRN QKKEKPDSVD GQQPLVNGVP
	Isoform 7 [UniParc]. Checksum: FE061178DA0A7ABB	FASTA	615	69,179
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 430 440 450 460 470 480 LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 490 500 510 520 530 540 HGRRGPGYTS GTNSEASNAS ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG 550 560 570 580 590 600 QGGRGRGGGF KGNDDHSRTD NRPRNPREAK GRTTDGSLQN TSSEGSRLRT GKDRNQKKEK 610 PDSVDGQQPL VNGVP
	Isoform 8 [UniParc]. Checksum: B413D4F8FA0D697F	FASTA	586	66,246
	10 20 30 40 50 60 MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 70 80 90 100 110 120 ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 130 140 150 160 170 180 ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 190 200 210 220 230 240 AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 250 260 270 280 290 300 IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 370 380 390 400 410 420 NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL 430 440 450 460 470 480 RQIGASSRPP PNRTDKEKSY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSA PTEEERESFL 490 500 510 520 530 540 RRGDGRRRGG GGRGQGGRGR GGGFKGNDDH SRTDNRPRNP REAKGRTTDG SLQIRVDCNN 550 560 570 580 ERSVHTKTLQ NTSSEGSRLR TGKDRNQKKE KPDSVDGQQP LVNGVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Alternative splicing in the fragile X gene FMR1." Verkerk A.J.M.H., de Graaff E., de Boulle K., Eichler E.E., Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J., Nelson D.L., Oostra B.A. Hum. Mol. Genet. 2:399-404(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY. Tissue: Fetal brain and Liver.
[3]	Erratum Verkerk A.J.H.M., de Graaff E., de Boulle K., Eichler E.E., Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J., Nelson D.L., Oostra B.A. Hum. Mol. Genet. 2:1348-1348(1993) [PubMed] [Europe PMC] [Abstract]
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Fine structure of the human FMR1 gene." Eichler E.E., Richards S., Gibbs R.A., Nelson D.L. Hum. Mol. Genet. 2:1147-1153(1993) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] 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]	"A point mutation in the FMR-1 gene associated with fragile X mental retardation." de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J., van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J. Nat. Genet. 3:31-35(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FRAX ASN-304.
[33]	"Characterization of FMR1 proteins isolated from different tissues." Verheij C., de Graaff E., Bakker C.E., Willemsen R., Willems P.J., Meijer N., Galjaard H., Reuser A.J.J., Oostra B.A., Hoogeveen A.T. Hum. Mol. Genet. 4:895-901(1995) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L29074 Genomic DNA. Translation: AAB18828.1.
L29074 Genomic DNA. Translation: AAB18829.1.
L29074 Genomic DNA. Translation: AAB18830.1.
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.
L29074 Genomic DNA. Translation: AAB18831.1.
L29074 Genomic DNA. Translation: AAB18832.1.
L29074 Genomic DNA. Translation: AAB18833.1.
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.

PIR

I68614.
A40724. S45243.

RefSeq

NP_001172004.1. NM_001185075.1.
NP_001172005.1. NM_001185076.1.
NP_001172010.1. NM_001185081.1.
NP_001172011.1. NM_001185082.1.
NP_002015.1. NM_002024.5.

UniGene

Hs.103183.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00134.

ProteinModelPortal

Q06787.

SMR

Q06787. Positions 1-134, 216-425.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

108619. 25 interactions.

DIP

DIP-29022N.
DIP-29509N.

IntAct

Q06787. 20 interactions.

MINT

MINT-108156.

STRING

9606.ENSP00000359506.

PTM databases

PhosphoSite

Q06787.

Polymorphism databases

DMDM

544328.

Proteomic databases

PaxDb

Q06787.

PRIDE

Q06787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
ENST00000370475; ENSP00000359506; ENSG00000102081. [Q06787-1]
ENST00000599497; ENSP00000472650; ENSG00000268103. [Q06787-6]
ENST00000602057; ENSP00000472931; ENSG00000268103. [Q06787-1]

GeneID

2332.

KEGG

hsa:2332.

UCSC

uc004fck.4. human. [Q06787-8]
uc010nst.3. human. [Q06787-1]

Organism-specific databases

CTD

2332.

GeneCards

GC0XP146993.

HGNC

HGNC:3775. FMR1.

HPA

CAB012444.
HPA050118.

MIM

300623. phenotype.
300624. phenotype.
309550. gene.
311360. phenotype.

neXtProt

NX_Q06787.

Orphanet

908. Fragile X syndrome.
93256. Fragile X-associated tremor/ataxia syndrome.
619. Primary ovarian failure.
261483. Xq27.3q28 duplication syndrome.

PharmGKB

PA28191.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG75351.

HOVERGEN

HBG005739.

InParanoid

Q06787.

KO

K15516.

OMA

KAWQGMV.

PhylomeDB

Q06787.

TreeFam

TF105427.

Gene expression databases

ArrayExpress

Q06787.

Bgee

Q06787.

CleanEx

HS_FMR1.

Genevestigator

Q06787.

Family and domain databases

Gene3D

3.30.1370.10. 3 hits.

InterPro

IPR008395. Agenet-like_dom.
IPR022034. Frag_X_MRP_fam.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]

Pfam

PF05641. Agenet. 1 hit.
PF12235. FXR1P_C. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]

SMART

SM00322. KH. 2 hits.
[Graphical view]

SUPFAM

SSF54791. SSF54791. 2 hits.

PROSITE

PS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FMR1. human.

EvolutionaryTrace

Q06787.

GeneWiki

FMR1.

GenomeRNAi

2332.

NextBio

9465.

PRO

Q06787.

SOURCE

Search...

Entry information

Entry name

FMR1_HUMAN

Accession

Primary (citable) accession number: Q06787
Secondary accession number(s): A6NNH4 , D3DWT0, D3DWT1, D3DWT2, Q16578, Q5PQZ6, Q99054

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 16, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.