P51114 (FXR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fragile X mental retardation syndrome-related protein 1
Short name=hFXR1p

Gene names

Name:

FXR1

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs By similarity.
Subunit structure	Interacts with FMR1 and FXR2. Interacts with TDRD3, and with CYFIP2 but not with CYFIP1. Ref.7
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Expressed in all tissues examined including heart, brain, kidney and testis. Ref.1
Domain	The tandem Tudor domains preferentially recognize trimethylated histone peptides. Ref.14
Post-translational modification	Arg-445 is dimethylated, probably to asymmetric dimethylarginine.
Sequence similarities	Belongs to the FMR1 family. Contains 2 Agenet-like domains. Contains 2 KH domains.

Ontologies

Keywords
Biological process	Differentiation Myogenesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement PubMed 9642279. Source: ProtInc cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW muscle organ development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translation Inferred from electronic annotation. Source: Compara
Cellular_component	costamere Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay. Source: HPA nucleolus Traceable author statement PubMed 10888599. Source: ProtInc polysome Traceable author statement PubMed 9817930. Source: ProtInc
Molecular_function	G-quadruplex RNA binding Inferred from electronic annotation. Source: Compara RNA binding Traceable author statement Ref.1. Source: ProtInc mRNA 3'-UTR binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Alternative splicing appears to be tissue-specific.

Isoform 1 (identifier: P51114-1)

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.

Isoform 2 (identifier: P51114-2)

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.

Isoform 3 (identifier: P51114-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 621

620

Fragile X mental retardation syndrome-related protein 1

PRO_0000050106

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

442 – 457

16

RNA-binding RGG-box

Compositional bias

50 – 53

4

Poly-Pro

Compositional bias

502 – 510

9

Poly-Arg

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Modified residue

68

1

Phosphotyrosine By similarity

Modified residue

406

1

Phosphoserine Ref.8 Ref.9 Ref.12

Modified residue

409

1

Phosphoserine Ref.8 Ref.9 Ref.12

Modified residue

420

1

Phosphoserine Ref.10 Ref.12

Modified residue

423

1

Phosphoserine Ref.10 Ref.12

Modified residue

485

1

Phosphoserine Ref.12

Modified residue

585

1

Phosphoserine By similarity

Modified residue

587

1

Phosphoserine Ref.9 Ref.12

Modified residue

611

1

Phosphothreonine Ref.12

Natural variations

Alternative sequence

1 – 85

85

Missing in isoform 3.

VSP_019709

Alternative sequence

535 – 539

5

VTVAD → GKRCD in isoform 2.

VSP_019710

Alternative sequence

540 – 621

82

Missing in isoform 2.

VSP_019711

Natural variant

233

1

A → T in a breast cancer sample; somatic mutation. Ref.15

VAR_036050

Natural variant

429

1

D → N. Ref.1
Corresponds to variant rs1051080 [ dbSNP | Ensembl ].

VAR_016077

Natural variant

614

1

A → V.
Corresponds to variant rs11499 [ dbSNP | Ensembl ].

VAR_014890

Experimental info

Sequence conflict

3 – 4

2

EL → DV in AAC50155. Ref.1

Sequence conflict

27

1

S → P in BAF85322. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

621

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Beta strand

15 – 23

9

Beta strand

28 – 34

7

Beta strand

40 – 42

3

Helix

44 – 46

3

Beta strand

64 – 69

6

Beta strand

78 – 88

11

Beta strand

91 – 95

5

Beta strand

104 – 108

5

Helix

109 – 111

3

Beta strand

112 – 114

3

Beta strand

213 – 216

4

Beta strand

218 – 224

7

Helix

227 – 234

8

Helix

239 – 245

7

Beta strand

250 – 256

7

Turn

257 – 260

4

Beta strand

261 – 268

8

Helix

269 – 279

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified May 20, 2008. Version 3. Checksum: 0474A9B593C7C228	FASTA	621	69,721
	10 20 30 40 50 60 MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS 70 80 90 100 110 120 EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT 130 140 150 160 170 180 VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR 190 200 210 220 230 240 VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN 250 260 270 280 290 300 IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE 370 380 390 400 410 420 VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS 430 440 450 460 470 480 DWSLAGEDDR DSRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL 490 500 510 520 530 540 DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY 550 560 570 580 590 600 ISRAESQSRQ RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDD ISKLQRTPGE 610 620 EKINTLKEEN TQEAAVLNGV S
	Isoform 2 (b) (Short) [UniParc]. Checksum: 7D9452D150FC9EE7	FASTA	539	60,792
	10 20 30 40 50 60 MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS 70 80 90 100 110 120 EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT 130 140 150 160 170 180 VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR 190 200 210 220 230 240 VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN 250 260 270 280 290 300 IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN 310 320 330 340 350 360 GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE 370 380 390 400 410 420 VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS 430 440 450 460 470 480 DWSLAGEDDR DSRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL 490 500 510 520 530 DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLGKRCD
	Isoform 3 [UniParc]. Checksum: 4E66F53C3A15BFF8	FASTA	536	59,920
	10 20 30 40 50 60 MMKGEFYVIE YAACDATYNE IVTFERLRPV NQNKTVKKNT FFKCTVDVPE DLREACANEN 70 80 90 100 110 120 AHKDFKKAVG ACRIFYHPET TQLMILSASE ATVKRVNILS DMHLRSIRTK LMLMSRNEEA 130 140 150 160 170 180 TKHLECTKQL AAAFHEEFVV REDLMGLAIG THGSNIQQAR KVPGVTAIEL DEDTGTFRIY 190 200 210 220 230 240 GESADAVKKA RGFLEFVEDF IQVPRNLVGK VIGKNGKVIQ EIVDKSGVVR VRIEGDNENK 250 260 270 280 290 300 LPREDGMVPF VFVGTKESIG NVQVLLEYHI AYLKEVEQLR MERLQIDEQL RQIGSRSYSG 310 320 330 340 350 360 RGRGRRGPNY TSGYGTNSEL SNPSETESER KDELSDWSLA GEDDRDSRHQ RDSRRRPGGR 370 380 390 400 410 420 GRSVSGGRGR GGPRGGKSSI SSVLKDPDSN PYSLLDNTES DQTADTDASE SHHSTNRRRR 430 440 450 460 470 480 SRRRRTDEDA VLMDGMTESD TASVNENGLV TVADYISRAE SQSRQRNLPR ETLAKNKKEM 490 500 510 520 530 AKDVIEEHGP SEKAINGPTS ASGDDISKLQ RTPGEEKINT LKEENTQEAA VLNGVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-409, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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), MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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, MASS SPECTROMETRY.
[13]	"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.
[14]	"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, TUDOR DOMAINS.
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-233.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U25165 mRNA. Translation: AAC50155.1.
AY341428 mRNA. Translation: AAQ20045.1.
AK292633 mRNA. Translation: BAF85322.1.
BC028983 mRNA. Translation: AAH28983.1.

IPI

IPI00016249.
IPI00479630.
IPI00554715.

PIR

S55330.

RefSeq

NP_001013456.1. NM_001013438.2.
NP_001013457.1. NM_001013439.2.
NP_005078.2. NM_005087.3.

UniGene

Hs.478407.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P51114.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51114. 10 interactions.

MINT

MINT-1369113.

STRING

9606.ENSP00000350170.

PTM databases

PhosphoSite

P51114.

Polymorphism databases

DMDM

189047132.

Proteomic databases

PaxDb

P51114.

PRIDE

P51114.

Protocols and materials databases

DNASU

8087.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305586; ENSP00000307633; ENSG00000114416.
ENST00000357559; ENSP00000350170; ENSG00000114416.
ENST00000445140; ENSP00000388828; ENSG00000114416.

GeneID

8087.

KEGG

hsa:8087.

UCSC

uc003fkp.3. human.
uc003fkr.3. human.

Organism-specific databases

CTD

8087.

GeneCards

GC03P180585.

HGNC

HGNC:4023. FXR1.

HPA

HPA018246.

MIM

600819. gene.

neXtProt

NX_P51114.

PharmGKB

PA28439.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG75351.

HOGENOM

HOG000293377.

HOVERGEN

HBG005739.

InParanoid

P51114.

KO

K15516.

OMA

GMVPFTF.

OrthoDB

EOG49KFQB.

PhylomeDB

P51114.

Gene expression databases

ArrayExpress

P51114.

Bgee

P51114.

CleanEx

HS_FXR1.

Genevestigator

P51114.

GermOnline

ENSG00000114416. Homo sapiens.

Family and domain databases

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. 2 hits.
PF00013. KH_1. 2 hits.
[Graphical view]

SMART

SM00322. KH. 2 hits.
[Graphical view]

PROSITE

PS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
PS50304. TUDOR. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FXR1. human.

EvolutionaryTrace

P51114.

GenomeRNAi

8087.

NextBio

30714.

SOURCE

Search...

Entry information

Entry name

FXR1_HUMAN

Accession

Primary (citable) accession number: P51114
Secondary accession number(s): A8K9B8, Q7Z450, Q8N6R8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 132 of the entry and version 3 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.