P51116 (FXR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fragile X mental retardation syndrome-related protein 2

Gene names

Name:	FXR2
Synonyms:	FMR1L2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA-binding protein.
Subunit structure	Interacts with FMR1 and FXR1. Interacts with CYFIP2 but not with CYFIP1. Interacts with TDRD3. Ref.9
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FMR1 family. Contains 2 KH domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytosolic large ribosomal subunit Traceable author statement. Source: ProtInc
Molecular function	RNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARL6IP1	Q15041	3	EBI-740459,EBI-714543
LCMT1	Q9UIC8	2	EBI-740459,EBI-747632
LDOC1	O95751	3	EBI-740459,EBI-740738
MBIP	Q9NS73	3	EBI-740459,EBI-741953
MEAF6	Q9HAF1	3	EBI-740459,EBI-399266
NT5C2	P49902	3	EBI-740459,EBI-742084
PAICS	P22234	3	EBI-740459,EBI-712261
RABAC1	Q9UI14	3	EBI-740459,EBI-712367

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 673

673

Fragile X mental retardation syndrome-related protein 2

PRO_0000050110

Regions

Domain

232 – 261

30

KH 1

Domain

295 – 324

30

KH 2

Compositional bias

414 – 418

5

Poly-Ser

Compositional bias

544 – 552

9

Poly-Arg

Compositional bias

584 – 594

11

Poly-Arg

Amino acid modifications

Modified residue

411

1

Phosphothreonine Ref.12

Modified residue

453

1

Phosphoserine Ref.10

Modified residue

455

1

Phosphothreonine Ref.10

Modified residue

519

1

Phosphotyrosine Ref.7

Modified residue

525

1

Phosphoserine Ref.12

Modified residue

533

1

Phosphoserine Ref.12

Modified residue

566

1

Phosphoserine Ref.12

Modified residue

598

1

Phosphothreonine Ref.10 Ref.12 Ref.13 Ref.14

Modified residue

601

1

Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

603

1

Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Natural variations

Natural variant

591

1

R → P.
Corresponds to variant rs36013555 [ dbSNP | Ensembl ].

VAR_055979

Experimental info

Sequence conflict

625 – 626

2

RP → SA in AAC50292. Ref.1

Secondary structure

1

.

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673

Helix Strand Turn

Details...

Beta strand

30 – 33

4

Beta strand

35 – 40

6

Beta strand

50 – 53

4

Beta strand

74 – 77

4

Beta strand

90 – 97

8

Beta strand

102 – 106

5

Beta strand

115 – 117

3

Helix

119 – 121

3

Beta strand

122 – 124

3

Sequences

	Sequence		Length	Mass (Da)
	P51116 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: B8A498C3F634D41F	FASTA	673	74,223
	10 20 30 40 50 60 MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER QIPFGDVRLP 70 80 90 100 110 120 PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD FYVIEYAACD ATYNEIVTLE 130 140 150 160 170 180 RLRPVNPNPL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF LNITNSELFI 190 200 210 220 230 240 LSTTEAPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM 250 260 270 280 290 300 GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR 310 320 330 340 350 360 NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT RENISNAQAL 370 380 390 400 410 420 LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG SGGSDKAGYS TDESSSSSLH 430 440 450 460 470 480 ATRTYGGSYG GRGRGRRTGG PAYGPSSDVS TASETESEKR EEPNRAGPGD RDPPTRGEES 490 500 510 520 530 540 RRRPTGGRGR GPPPAPRPTS RYNSSSISSV LKDPDSNPYS LLDTSEPEPP VDSEPGEPPP 550 560 570 580 590 600 ASARRRRSRR RRTDEDRTVM DGGLESDGPN MTENGLEDES RPQRRNRSRR RRNRGNRTDG 610 620 630 640 650 660 SISGDRQPVT VADYISRAES QSRQRPPLER TKPSEDSLSG QKGDSVSKLP KGPSENGELS 670 APLELGSMVN GVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2." Zhang Y., O'Connor J.P., Siomi M.C., Srinivasan S., Dutra A., Nussbaum R.L., Dreyfuss G. EMBO J. 14:5358-5366(1995) [PubMed: 7489725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[4]	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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and PNS.
[6]	"The rat androgen-binding protein (ABP/SHBG) gene contains triplet repeats similar to unstable triplets: evidence that the ABP/SHBG and the fragile X-related 2 genes overlap." Joseph D.R. Steroids 63:2-4(1998) [PubMed: 9437788] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
[7]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, MASS SPECTROMETRY.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-603, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 18664458] [Abstract] Cited for: INTERACTION WITH TDRD3.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; THR-455; THR-598; SER-601 AND SER-603, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-603, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-525; SER-533; SER-566; THR-598; SER-601 AND SER-603, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598; SER-601 AND SER-603, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598; SER-601 AND SER-603, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31501 mRNA. Translation: AAC50292.1.
BT009817 mRNA. Translation: AAP88819.1.
AK313836 mRNA. Translation: BAG36569.1.
CH471108 Genomic DNA. Translation: EAW90154.1.
CH471108 Genomic DNA. Translation: EAW90155.1.
BC067272 mRNA. Translation: AAH67272.1.
BC020090 mRNA. Translation: AAH20090.1.
AF044263 Genomic DNA. Translation: AAC03357.1.

IPI

IPI00016250.

PIR

S60173.

RefSeq

NP_004851.2. NM_004860.3.

UniGene

Hs.52788.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3H8Z	X-ray	1.92	A	13-136	[»]

ProteinModelPortal

P51116.

SMR

P51116. Positions 13-131, 222-396.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51116. 62 interactions.

MINT

MINT-108243.

STRING

P51116.

PTM databases

PhosphoSite

P51116.

Polymorphism databases

DMDM

90177782.

Proteomic databases

PRIDE

P51116.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250113; ENSP00000250113; ENSG00000129245.

GeneID

9513.

KEGG

hsa:9513.

Organism-specific databases

CTD

9513.

GeneCards

GC17M007494.

H-InvDB

HIX0013506.

HGNC

HGNC:4024. FXR2.

HPA

CAB011205.
HPA022997.

MIM

605339. gene.

neXtProt

NX_P51116.

PharmGKB

PA28440.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13982.

HOGENOM

HBG717761.

HOVERGEN

HBG005739.

InParanoid

P51116.

OMA

DPPTRGE.

OrthoDB

EOG45HRX4.

PhylomeDB

P51116.

Gene expression databases

ArrayExpress

P51116.

Bgee

P51116.

CleanEx

HS_FXR2.

Genevestigator

P51116.

GermOnline

ENSG00000129245. Homo sapiens.

Family and domain databases

InterPro

IPR008395. Agenet.
IPR022034. Frag_X_MRP_fam.
IPR004087. KH.
IPR004088. KH_type_1.
IPR018111. KH_type_1_subgr.
[Graphical view]

KO

K15516.

Pfam

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

SMART

SM00322. KH. 2 hits.
[Graphical view]

PROSITE

PS50084. KH_TYPE_1. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

35646.

SOURCE

Search...

Entry information

Entry name

FXR2_HUMAN

Accession

Primary (citable) accession number: P51116
Secondary accession number(s): B2R9M2, D3DTQ1, Q8WUM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 7, 2006
Last modified:	January 25, 2012
This is version 106 of the entry and version 2 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.