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Protein

Fragile X mental retardation syndrome-related protein 2

Gene

FXR2

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

Functioni

RNA-binding protein.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • mRNA binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc

GO - Biological processi

  • negative regulation of translation Source: GO_Central
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fragile X mental retardation syndrome-related protein 2
Gene namesi
Name:FXR2
Synonyms:FMR1L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:4024. FXR2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: CACAO
  • cytosolic large ribosomal subunit Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: GO_Central
  • polysome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28440.

Polymorphism and mutation databases

BioMutaiFXR2.
DMDMi90177782.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Fragile X mental retardation syndrome-related protein 2PRO_0000050110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei533 – 5331Phosphoserine1 Publication
Modified residuei566 – 5661Phosphoserine2 Publications
Modified residuei598 – 5981Phosphothreonine4 Publications
Modified residuei601 – 6011Phosphoserine3 Publications
Modified residuei603 – 6031Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP51116.
PaxDbiP51116.
PRIDEiP51116.

PTM databases

PhosphoSiteiP51116.

Expressioni

Gene expression databases

BgeeiP51116.
CleanExiHS_FXR2.
ExpressionAtlasiP51116. baseline.
GenevisibleiP51116. HS.

Organism-specific databases

HPAiCAB011205.
HPA022997.

Interactioni

Subunit structurei

Interacts with FMR1 and FXR1. Interacts with CYFIP2 but not with CYFIP1. Interacts with TDRD3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-740459,EBI-740459
AP1M1Q9BXS54EBI-740459,EBI-541426
ARL6IP1Q150413EBI-740459,EBI-714543
BAZ2BQ9UIF8-23EBI-740459,EBI-10321972
BYSLQ138955EBI-740459,EBI-358049
C10orf62Q5T6814EBI-740459,EBI-744052
CAMK2DQ135573EBI-740459,EBI-351018
CDKL3Q8IVW43EBI-740459,EBI-3919850
CEP44Q9C0F13EBI-740459,EBI-744115
CEP55D3DR373EBI-740459,EBI-10173536
FAM90A1Q86YD73EBI-740459,EBI-6658203
FMR1Q06787-83EBI-740459,EBI-10224470
HMBOX1Q6NT763EBI-740459,EBI-2549423
HMBOX1Q6NT76-23EBI-740459,EBI-10212206
LASP1Q148473EBI-740459,EBI-742828
LCMT1Q9UIC82EBI-740459,EBI-747632
LCP2Q130943EBI-740459,EBI-346946
LDOC1O957513EBI-740459,EBI-740738
MBIPQ9NS733EBI-740459,EBI-741953
MEAF6Q9HAF13EBI-740459,EBI-399266
MFAP1P550813EBI-740459,EBI-1048159
MIA3Q5JRA6-23EBI-740459,EBI-10244342
MMTAG2Q9BU763EBI-740459,EBI-742459
MORF4L1Q9UBU83EBI-740459,EBI-399246
MRPL43Q8N9833EBI-740459,EBI-1043145
NIF3L1Q9GZT83EBI-740459,EBI-740897
NT5C2P499023EBI-740459,EBI-742084
PAF1Q8N7H54EBI-740459,EBI-2607770
PAICSP222343EBI-740459,EBI-712261
PCBD1P614574EBI-740459,EBI-740475
PIM1P113093EBI-740459,EBI-696621
POM121Q96HA14EBI-740459,EBI-739990
PRAM1Q96QH23EBI-740459,EBI-2860740
RABAC1Q9UI143EBI-740459,EBI-712367
SCELO951713EBI-740459,EBI-7543896
SRPK2P783623EBI-740459,EBI-593303
SYT6Q5T7P8-23EBI-740459,EBI-10246152
SYTL4Q96C243EBI-740459,EBI-747142
TBC1D22BQ9NU193EBI-740459,EBI-8787464
YES1P079473EBI-740459,EBI-515331
ZBTB22O152093EBI-740459,EBI-723574
ZMAT2Q96NC03EBI-740459,EBI-2682299

Protein-protein interaction databases

BioGridi114890. 119 interactions.
IntActiP51116. 97 interactions.
MINTiMINT-108243.
STRINGi9606.ENSP00000250113.

Structurei

Secondary structure

1
673
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 195Combined sources
Beta strandi25 – 339Combined sources
Beta strandi35 – 428Combined sources
Beta strandi50 – 534Combined sources
Helixi54 – 563Combined sources
Beta strandi74 – 796Combined sources
Beta strandi88 – 9811Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi115 – 1173Combined sources
Helixi119 – 1213Combined sources
Beta strandi122 – 1243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H8ZX-ray1.92A13-136[»]
ProteinModelPortaliP51116.
SMRiP51116. Positions 13-212, 222-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51116.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 6047Agenet-like 1Add
BLAST
Domaini73 – 12553Agenet-like 2Add
BLAST
Domaini232 – 26130KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini295 – 32430KH 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi414 – 4185Poly-Ser
Compositional biasi544 – 5529Poly-Arg
Compositional biasi584 – 59411Poly-ArgAdd
BLAST

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.
InParanoidiP51116.
KOiK15516.
OMAiFRSIRTK.
OrthoDBiEOG7NKKJT.
PhylomeDBiP51116.
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. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER
60 70 80 90 100
QIPFGDVRLP PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD
110 120 130 140 150
FYVIEYAACD ATYNEIVTLE RLRPVNPNPL ATKGSFFKVT MAVPEDLREA
160 170 180 190 200
CSNENVHKEF KKALGANCIF LNITNSELFI LSTTEAPVKR ASLLGDMHFR
210 220 230 240 250
SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM GLAIGTHGAN
260 270 280 290 300
IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR
310 320 330 340 350
NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT
360 370 380 390 400
RENISNAQAL LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG
410 420 430 440 450
SGGSDKAGYS TDESSSSSLH ATRTYGGSYG GRGRGRRTGG PAYGPSSDVS
460 470 480 490 500
TASETESEKR EEPNRAGPGD RDPPTRGEES RRRPTGGRGR GPPPAPRPTS
510 520 530 540 550
RYNSSSISSV LKDPDSNPYS LLDTSEPEPP VDSEPGEPPP ASARRRRSRR
560 570 580 590 600
RRTDEDRTVM DGGLESDGPN MTENGLEDES RPQRRNRSRR RRNRGNRTDG
610 620 630 640 650
SISGDRQPVT VADYISRAES QSRQRPPLER TKPSEDSLSG QKGDSVSKLP
660 670
KGPSENGELS APLELGSMVN GVS
Length:673
Mass (Da):74,223
Last modified:March 7, 2006 - v2
Checksum:iB8A498C3F634D41F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti625 – 6262RP → SA in AAC50292 (PubMed:7489725).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti252 – 2521Q → H.1 Publication
Corresponds to variant rs17854734 [ dbSNP | Ensembl ].
VAR_067039
Natural varianti591 – 5911R → P.
Corresponds to variant rs36013555 [ dbSNP | Ensembl ].
VAR_055979

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC020090 mRNA. Translation: AAH20090.1.
BC051907 mRNA. Translation: AAH51907.1.
BC067272 mRNA. Translation: AAH67272.1.
AF044263 Genomic DNA. Translation: AAC03357.1.
CCDSiCCDS45604.1.
PIRiS60173.
RefSeqiNP_004851.2. NM_004860.3.
UniGeneiHs.52788.

Genome annotation databases

EnsembliENST00000250113; ENSP00000250113; ENSG00000129245.
GeneIDi9513.
KEGGihsa:9513.
UCSCiuc002gia.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC020090 mRNA. Translation: AAH20090.1.
BC051907 mRNA. Translation: AAH51907.1.
BC067272 mRNA. Translation: AAH67272.1.
AF044263 Genomic DNA. Translation: AAC03357.1.
CCDSiCCDS45604.1.
PIRiS60173.
RefSeqiNP_004851.2. NM_004860.3.
UniGeneiHs.52788.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H8ZX-ray1.92A13-136[»]
ProteinModelPortaliP51116.
SMRiP51116. Positions 13-212, 222-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114890. 119 interactions.
IntActiP51116. 97 interactions.
MINTiMINT-108243.
STRINGi9606.ENSP00000250113.

PTM databases

PhosphoSiteiP51116.

Polymorphism and mutation databases

BioMutaiFXR2.
DMDMi90177782.

Proteomic databases

MaxQBiP51116.
PaxDbiP51116.
PRIDEiP51116.

Protocols and materials databases

DNASUi9513.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250113; ENSP00000250113; ENSG00000129245.
GeneIDi9513.
KEGGihsa:9513.
UCSCiuc002gia.2. human.

Organism-specific databases

CTDi9513.
GeneCardsiGC17M007494.
HGNCiHGNC:4024. FXR2.
HPAiCAB011205.
HPA022997.
MIMi605339. gene.
neXtProtiNX_P51116.
PharmGKBiPA28440.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG75351.
GeneTreeiENSGT00390000017033.
HOGENOMiHOG000293377.
HOVERGENiHBG005739.
InParanoidiP51116.
KOiK15516.
OMAiFRSIRTK.
OrthoDBiEOG7NKKJT.
PhylomeDBiP51116.
TreeFamiTF105427.

Miscellaneous databases

ChiTaRSiFXR2. human.
EvolutionaryTraceiP51116.
GeneWikiiFXR2.
GenomeRNAii9513.
NextBioi35646.
PROiP51116.
SOURCEiSearch...

Gene expression databases

BgeeiP51116.
CleanExiHS_FXR2.
ExpressionAtlasiP51116. baseline.
GenevisibleiP51116. HS.

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. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  4. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-252.
    Tissue: Lymph, PNS and Skin.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-533; SER-566; THR-598; SER-601 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598; SER-601 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-566 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598 AND SER-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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 (1.92 ANGSTROMS) OF 13-136, DOMAINS TUDOR.

Entry informationi

Entry nameiFXR2_HUMAN
AccessioniPrimary (citable) accession number: P51116
Secondary accession number(s): B2R9M2
, D3DTQ1, Q86V09, Q8WUM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 7, 2006
Last modified: June 24, 2015
This is version 140 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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