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P51114

- FXR1_HUMAN

UniProt

P51114 - FXR1_HUMAN

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Protein

Fragile X mental retardation syndrome-related protein 1

Gene

FXR1

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

Functioni

RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs (By similarity).By similarity

GO - Molecular functioni

  1. G-quadruplex RNA binding Source: Ensembl
  2. mRNA 3'-UTR binding Source: Ensembl
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cell differentiation Source: UniProtKB-KW
  3. muscle organ development Source: UniProtKB-KW
  4. negative regulation of translation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Myogenesis

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fragile X mental retardation syndrome-related protein 1
Short name:
hFXR1p
Gene namesi
Name:FXR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:4023. FXR1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. costamere Source: Ensembl
  2. cytoplasm Source: HPA
  3. membrane Source: UniProtKB
  4. nucleolus Source: ProtInc
  5. polysome Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 621620Fragile X mental retardation syndrome-related protein 1PRO_0000050106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei68 – 681PhosphotyrosineBy similarity
Modified residuei406 – 4061Phosphoserine3 Publications
Modified residuei409 – 4091Phosphoserine3 Publications
Modified residuei420 – 4201Phosphoserine2 Publications
Modified residuei423 – 4231Phosphoserine2 Publications
Modified residuei485 – 4851Phosphoserine1 Publication
Modified residuei587 – 5871Phosphoserine2 Publications
Modified residuei611 – 6111Phosphothreonine1 Publication

Post-translational modificationi

Arg-445 is dimethylated, probably to asymmetric dimethylarginine.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51114.
PaxDbiP51114.
PRIDEiP51114.

PTM databases

PhosphoSiteiP51114.

Expressioni

Tissue specificityi

Expressed in all tissues examined including heart, brain, kidney and testis.1 Publication

Gene expression databases

BgeeiP51114.
CleanExiHS_FXR1.
ExpressionAtlasiP51114. baseline and differential.
GenevestigatoriP51114.

Organism-specific databases

HPAiHPA018246.
HPA055475.

Interactioni

Subunit structurei

Interacts with FMR1 and FXR2. Interacts with TDRD3, and with CYFIP2 but not with CYFIP1.1 Publication

Protein-protein interaction databases

BioGridi113760. 35 interactions.
IntActiP51114. 15 interactions.
MINTiMINT-1369113.
STRINGi9606.ENSP00000350170.

Structurei

Secondary structure

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi15 – 239Combined sources
Beta strandi28 – 347Combined sources
Beta strandi40 – 423Combined sources
Helixi44 – 463Combined sources
Beta strandi64 – 696Combined sources
Beta strandi78 – 8811Combined sources
Beta strandi91 – 955Combined sources
Beta strandi104 – 1085Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi218 – 2247Combined sources
Helixi227 – 2348Combined sources
Helixi239 – 2457Combined sources
Beta strandi250 – 2567Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2688Combined sources
Helixi269 – 27911Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPQNMR-A212-289[»]
3KUFX-ray2.70A2-132[»]
3O8VX-ray2.50A2-132[»]
ProteinModelPortaliP51114.
SMRiP51114. Positions 3-121, 212-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51114.

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
Regioni442 – 45716RNA-binding RGG-boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi50 – 534Poly-Pro
Compositional biasi502 – 5109Poly-Arg

Domaini

The tandem Tudor domains preferentially recognize trimethylated histone peptides.1 Publication

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.
HOGENOMiHOG000293377.
HOVERGENiHBG005739.
InParanoidiP51114.
KOiK15516.
OMAiGMVPFTF.
OrthoDBiEOG7NKKJT.
PhylomeDBiP51114.
TreeFamiTF105427.

Family and domain databases

Gene3Di3.30.1370.10. 2 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. 2 hits.
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 (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Alternative splicing appears to be tissue-specific.

Isoform 1 (identifier: P51114-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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
MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP
60 70 80 90 100
PPPDIKKEIS EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD
110 120 130 140 150
ATYNEIVTFE RLRPVNQNKT VKKNTFFKCT VDVPEDLREA CANENAHKDF
160 170 180 190 200
KKAVGACRIF YHPETTQLMI LSASEATVKR VNILSDMHLR SIRTKLMLMS
210 220 230 240 250
RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN IQQARKVPGV
260 270 280 290 300
TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
310 320 330 340 350
GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL
360 370 380 390 400
LEYHIAYLKE VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG
410 420 430 440 450
TNSELSNPSE TESERKDELS DWSLAGEDDR DSRHQRDSRR RPGGRGRSVS
460 470 480 490 500
GGRGRGGPRG GKSSISSVLK DPDSNPYSLL DNTESDQTAD TDASESHHST
510 520 530 540 550
NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY ISRAESQSRQ
560 570 580 590 600
RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDD ISKLQRTPGE
610 620
EKINTLKEEN TQEAAVLNGV S
Length:621
Mass (Da):69,721
Last modified:May 20, 2008 - v3
Checksum:i0474A9B593C7C228
GO
Isoform 2 (identifier: P51114-2) [UniParc]FASTAAdd to Basket

Also known as: b, Short

The sequence of this isoform differs from the canonical sequence as follows:
     535-539: VTVAD → GKRCD
     540-621: Missing.

Note: Contains a phosphoserine at position 524. Contains a phosphoserine at position 528.

Show »
Length:539
Mass (Da):60,792
Checksum:i7D9452D150FC9EE7
GO
Isoform 3 (identifier: P51114-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Note: No experimental confirmation available.

Show »
Length:536
Mass (Da):59,920
Checksum:i4E66F53C3A15BFF8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42EL → DV in AAC50155. (PubMed:7781595)Curated
Sequence conflicti27 – 271S → P in BAF85322. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331A → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_036050
Natural varianti429 – 4291D → N.1 Publication
Corresponds to variant rs1051080 [ dbSNP | Ensembl ].
VAR_016077
Natural varianti614 – 6141A → V.
Corresponds to variant rs11499 [ dbSNP | Ensembl ].
VAR_014890

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform 3. 1 PublicationVSP_019709Add
BLAST
Alternative sequencei535 – 5395VTVAD → GKRCD in isoform 2. 2 PublicationsVSP_019710
Alternative sequencei540 – 62182Missing in isoform 2. 2 PublicationsVSP_019711Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25165 mRNA. Translation: AAC50155.1.
AY341428 mRNA. Translation: AAQ20045.1.
AK292633 mRNA. Translation: BAF85322.1.
BC028983 mRNA. Translation: AAH28983.1.
CCDSiCCDS3238.1. [P51114-1]
CCDS33894.1. [P51114-3]
CCDS46965.1. [P51114-2]
PIRiS55330.
RefSeqiNP_001013456.1. NM_001013438.2. [P51114-2]
NP_001013457.1. NM_001013439.2. [P51114-3]
NP_005078.2. NM_005087.3. [P51114-1]
UniGeneiHs.478407.

Genome annotation databases

EnsembliENST00000305586; ENSP00000307633; ENSG00000114416. [P51114-3]
ENST00000357559; ENSP00000350170; ENSG00000114416. [P51114-1]
ENST00000445140; ENSP00000388828; ENSG00000114416. [P51114-2]
GeneIDi8087.
KEGGihsa:8087.
UCSCiuc003fkp.3. human. [P51114-1]
uc003fkr.3. human. [P51114-2]

Polymorphism databases

DMDMi189047132.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25165 mRNA. Translation: AAC50155.1 .
AY341428 mRNA. Translation: AAQ20045.1 .
AK292633 mRNA. Translation: BAF85322.1 .
BC028983 mRNA. Translation: AAH28983.1 .
CCDSi CCDS3238.1. [P51114-1 ]
CCDS33894.1. [P51114-3 ]
CCDS46965.1. [P51114-2 ]
PIRi S55330.
RefSeqi NP_001013456.1. NM_001013438.2. [P51114-2 ]
NP_001013457.1. NM_001013439.2. [P51114-3 ]
NP_005078.2. NM_005087.3. [P51114-1 ]
UniGenei Hs.478407.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CPQ NMR - A 212-289 [» ]
3KUF X-ray 2.70 A 2-132 [» ]
3O8V X-ray 2.50 A 2-132 [» ]
ProteinModelPortali P51114.
SMRi P51114. Positions 3-121, 212-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113760. 35 interactions.
IntActi P51114. 15 interactions.
MINTi MINT-1369113.
STRINGi 9606.ENSP00000350170.

PTM databases

PhosphoSitei P51114.

Polymorphism databases

DMDMi 189047132.

Proteomic databases

MaxQBi P51114.
PaxDbi P51114.
PRIDEi P51114.

Protocols and materials databases

DNASUi 8087.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305586 ; ENSP00000307633 ; ENSG00000114416 . [P51114-3 ]
ENST00000357559 ; ENSP00000350170 ; ENSG00000114416 . [P51114-1 ]
ENST00000445140 ; ENSP00000388828 ; ENSG00000114416 . [P51114-2 ]
GeneIDi 8087.
KEGGi hsa:8087.
UCSCi uc003fkp.3. human. [P51114-1 ]
uc003fkr.3. human. [P51114-2 ]

Organism-specific databases

CTDi 8087.
GeneCardsi GC03P180585.
HGNCi HGNC:4023. FXR1.
HPAi HPA018246.
HPA055475.
MIMi 600819. gene.
neXtProti NX_P51114.
PharmGKBi PA28439.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75351.
GeneTreei ENSGT00390000017033.
HOGENOMi HOG000293377.
HOVERGENi HBG005739.
InParanoidi P51114.
KOi K15516.
OMAi GMVPFTF.
OrthoDBi EOG7NKKJT.
PhylomeDBi P51114.
TreeFami TF105427.

Miscellaneous databases

ChiTaRSi FXR1. human.
EvolutionaryTracei P51114.
GeneWikii FXR1.
GenomeRNAii 8087.
NextBioi 30714.
PROi P51114.
SOURCEi Search...

Gene expression databases

Bgeei P51114.
CleanExi HS_FXR1.
ExpressionAtlasi P51114. baseline and differential.
Genevestigatori P51114.

Family and domain databases

Gene3Di 3.30.1370.10. 2 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. 2 hits.
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

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, VARIANT ASN-429, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "Identification of alternatively spliced genes related to spermatogenesis using cDNA microarrays."
    Xu Z.Y., Huang X.Y., Wang H., Xu M., Li J.M., Zhou Z.M., Sha J.H.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Testis.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Thymus.
  4. "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 2).
    Tissue: Cervix.
  5. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-9; 58-70; 246-263 AND 369-376, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: INTERACTION WITH TDRD3.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409 AND SER-587, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-528 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409; SER-420; SER-423; SER-485; SER-587 AND THR-611, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Solution structure of the N-terminal KH domain of human FXR1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 212-289.
  16. "Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2."
    Adams-Cioaba M.A., Guo Y., Bian C., Amaya M.F., Lam R., Wasney G.A., Vedadi M., Xu C., Min J.
    PLoS ONE 5:E13559-E13559(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-132, DOMAINS TUDOR.
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-233.

Entry informationi

Entry nameiFXR1_HUMAN
AccessioniPrimary (citable) accession number: P51114
Secondary accession number(s): A8K9B8, Q7Z450, Q8N6R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 20, 2008
Last modified: October 29, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3