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Protein

F-box only protein 11

Gene

FBXO11

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

Functioni

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53.6 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri833 – 90472UBR-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • protein-arginine N-methyltransferase activity Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular protein modification process Source: HGNC
  • peptidyl-arginine N-methylation Source: GOC
  • protein ubiquitination Source: UniProtKB
  • sensory perception of sound Source: Ensembl
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SIGNORiQ86XK2.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 11
Alternative name(s):
Protein arginine N-methyltransferase 9
Vitiligo-associated protein 1
Short name:
VIT-1
Gene namesi
Name:FBXO11
Synonyms:FBX11, PRMT9, VIT1
ORF Names:UG063H01
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:13590. FBXO11.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • cytoplasm Source: HGNC
  • nucleolus Source: HPA
  • nucleus Source: HGNC
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in FBXO11 may be a cause of diffuse large B-cell lymphoma by allowing the accumulation of BCL6, an oncoprotein that has a critical role in lymphomas.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi575 – 5751Q → L: Greatly reduced ability to bind PRDM1 and reduced proteolysis of PRDM1. 1 Publication

Organism-specific databases

Orphaneti3435. Vitiligo.
PharmGKBiPA28031.

Polymorphism and mutation databases

BioMutaiFBXO11.
DMDMi124012093.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 927927F-box only protein 11PRO_0000273574Add
BLAST

Proteomic databases

EPDiQ86XK2.
MaxQBiQ86XK2.
PaxDbiQ86XK2.
PRIDEiQ86XK2.

PTM databases

iPTMnetiQ86XK2.
PhosphoSiteiQ86XK2.

Expressioni

Tissue specificityi

Isoform 5 is expressed in keratinocytes, fibroblasts and melanocytes.1 Publication

Developmental stagei

Protein levels increase during G1 and S phases to decline as cells progress through G2 to enter in G1 phase of the next cell cycle.1 Publication

Gene expression databases

BgeeiQ86XK2.
ExpressionAtlasiQ86XK2. baseline and differential.
GenevisibleiQ86XK2. HS.

Organism-specific databases

HPAiHPA002690.

Interactioni

Subunit structurei

Component of the SCF(FBXO11) complex consisting of CUL1, RBX1, SKP1 and FBXO11. Interacts with p53/TP53, BCL6 and DTL (when not phosphorylated). Interacts with PRMD1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SKP1P632085EBI-1047804,EBI-307486
SNAI1O958636EBI-1047804,EBI-1045459
TP53P046374EBI-1047804,EBI-366083

Protein-protein interaction databases

BioGridi123173. 50 interactions.
DIPiDIP-35680N.
IntActiQ86XK2. 14 interactions.
STRINGi9606.ENSP00000384823.

Structurei

3D structure databases

ProteinModelPortaliQ86XK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 19947F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati395 – 41723PbH1 1Add
BLAST
Repeati418 – 44023PbH1 2Add
BLAST
Repeati441 – 46323PbH1 3Add
BLAST
Repeati464 – 48623PbH1 4Add
BLAST
Repeati487 – 50923PbH1 5Add
BLAST
Repeati510 – 53223PbH1 6Add
BLAST
Repeati533 – 55523PbH1 7Add
BLAST
Repeati556 – 57823PbH1 8Add
BLAST
Repeati579 – 60123PbH1 9Add
BLAST
Repeati602 – 62423PbH1 10Add
BLAST
Repeati625 – 64723PbH1 11Add
BLAST
Repeati648 – 67023PbH1 12Add
BLAST
Repeati671 – 69323PbH1 13Add
BLAST
Repeati694 – 71623PbH1 14Add
BLAST
Repeati717 – 73923PbH1 15Add
BLAST
Repeati740 – 76223PbH1 16Add
BLAST
Repeati763 – 78523PbH1 17Add
BLAST
Repeati786 – 80823PbH1 18Add
BLAST
Repeati809 – 83022PbH1 19Add
BLAST

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 19 PbH1 repeats.Curated
Contains 1 UBR-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri833 – 90472UBR-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1777. Eukaryota.
ENOG410YP8C. LUCA.
GeneTreeiENSGT00530000063425.
HOGENOMiHOG000020584.
HOVERGENiHBG051565.
InParanoidiQ86XK2.
KOiK10297.
OMAiSSRTYVR.
OrthoDBiEOG73803Z.
PhylomeDBiQ86XK2.
TreeFamiTF313602.

Family and domain databases

Gene3Di2.160.20.10. 4 hits.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR001810. F-box_dom.
IPR029799. FBX11/DRE-1.
IPR007742. NosD_dom.
IPR022441. Para_beta_helix_rpt-2.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR003126. Znf_UBR.
[Graphical view]
PANTHERiPTHR22990:SF20. PTHR22990:SF20. 1 hit.
PfamiPF12937. F-box-like. 1 hit.
PF05048. NosD. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00722. CASH. 3 hits.
SM00256. FBOX. 1 hit.
SM00710. PbH1. 19 hits.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 3 hits.
SSF81383. SSF81383. 1 hit.
TIGRFAMsiTIGR03804. para_beta_helix. 4 hits.
PROSITEiPS50181. FBOX. 1 hit.
PS51157. ZF_UBR. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86XK2-1) [UniParc]FASTAAdd to basket

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
MNSVRAANRR PRRVSRPRPV QQQQQQPPQQ PPPQPPQQQP PQQQPPPPPQ
60 70 80 90 100
QQQQQQPPPP PPPPPPLPQE RNNVGERDDD VPADMVAEES GPGAQNSPYQ
110 120 130 140 150
LRRKTLLPKR TACPTKNSME GASTSTTENF GHRAKRARVS GKSQDLSAAP
160 170 180 190 200
AEQYLQEKLP DEVVLKIFSY LLEQDLCRAA CVCKRFSELA NDPILWKRLY
210 220 230 240 250
MEVFEYTRPM MHPEPGKFYQ INPEEYEHPN PWKESFQQLY KGAHVKPGFA
260 270 280 290 300
EHFYSNPARY KGRENMLYYD TIEDALGGVQ EAHFDGLIFV HSGIYTDEWI
310 320 330 340 350
YIESPITMIG AAPGKVADKV IIENTRDSTF VFMEGSEDAY VGYMTIRFNP
360 370 380 390 400
DDKSAQHHNA HHCLEITVNC SPIIDHCIIR STCTVGSAVC VSGQGACPTI
410 420 430 440 450
KHCNISDCEN VGLYITDHAQ GIYEDNEISN NALAGIWVKN HGNPIIRRNH
460 470 480 490 500
IHHGRDVGVF TFDHGMGYFE SCNIHRNRIA GFEVKAYANP TVVRCEIHHG
510 520 530 540 550
QTGGIYVHEK GRGQFIENKI YANNFAGVWI TSNSDPTIRG NSIFNGNQGG
560 570 580 590 600
VYIFGDGRGL IEGNDIYGNA LAGIQIRTNS CPIVRHNKIH DGQHGGIYVH
610 620 630 640 650
EKGQGVIEEN EVYSNTLAGV WVTTGSTPVL RRNRIHSGKQ VGVYFYDNGH
660 670 680 690 700
GVLEDNDIYN HMYSGVQIRT GSNPKIRRNK IWGGQNGGIL VYNSGLGCIE
710 720 730 740 750
DNEIFDNAMA GVWIKTDSNP TLRRNKIHDG RDGGICIFNG GRGLLEENDI
760 770 780 790 800
FRNAQAGVLI STNSHPILRK NRIFDGFAAG IEITNHATAT LEGNQIFNNR
810 820 830 840 850
FGGLFLASGV NVTMKDNKIM NNQDAIEKAV SRGQCLYKIS SYTSYPMHDF
860 870 880 890 900
YRCHTCNTTD RNAICVNCIK KCHQGHDVEF IRHDRFFCDC GAGTLSNPCT
910 920
LAGEPTHDTD TLYDSAPPIE SNTLQHN
Length:927
Mass (Da):103,585
Last modified:January 23, 2007 - v3
Checksum:iCADBD23A6B892A78
GO
Isoform 2 (identifier: Q86XK2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-209: Missing.
     744-770: LLEENDIFRNAQAGVLISTNSHPILRK → IVVNFALVKNPVFHYSSISLMINDIAN
     771-927: Missing.

Show »
Length:561
Mass (Da):62,418
Checksum:i53E2FF0C642059C6
GO
Isoform 6 (identifier: Q86XK2-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Show »
Length:843
Mass (Da):94,056
Checksum:i242712732406F8FA
GO
Isoform 3 (identifier: Q86XK2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
     670-927: Missing.

Note: No experimental confirmation available.
Show »
Length:585
Mass (Da):65,559
Checksum:i319A266C66D541B6
GO
Isoform 4 (identifier: Q86XK2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     197-211: KRLYMEVFEYTRPMM → LGEVAHAYNPSTLGG
     212-927: Missing.

Show »
Length:211
Mass (Da):23,441
Checksum:iEA62852C6C1C91E3
GO
Isoform 5 (identifier: Q86XK2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     885-885: R → RYVAHLLDILPNYFPPHFSNIWVSFCFR

Note: No experimental confirmation available.
Show »
Length:954
Mass (Da):106,864
Checksum:i1F8E7073B253AC2D
GO

Sequence cautioni

The sequence AAF76888.1 differs from that shown.Intron retention.Curated
The sequence AAN76518.1 differs from that shown. Reason: Frameshift at position 141. Curated
The sequence AAY24083.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAB15143.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391L → S in BAB14214 (PubMed:14702039).Curated
Sequence conflicti577 – 5771R → G in AAN76518 (Ref. 2) Curated
Sequence conflicti632 – 6321R → G in BAD97312 (Ref. 3) Curated
Sequence conflicti903 – 9031G → S in AAV87312 (PubMed:17098746).Curated
Sequence conflicti903 – 9031G → S in AAH43258 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261T → S.
Corresponds to variant rs17036993 [ dbSNP | Ensembl ].
VAR_024441
Natural varianti206 – 2061Y → C Found in a patient with lymphoma. 1 Publication
VAR_070073
Natural varianti644 – 6441Y → C Found in a lymphoma cell line; diminishes ubiquitin-mediated degradation of BCL6. 1 Publication
VAR_070074
Natural varianti684 – 6841G → E Found in a patient with lymphoma; strongly diminishes ubiquitin-mediated degradation of BCL6. 1 Publication
VAR_070075
Natural varianti715 – 7151K → N Found in a patient with lymphoma; strongly diminishes ubiquitin-mediated degradation of BCL6. 1 Publication
VAR_070076
Natural varianti715 – 7151K → Q Found in a patient with lymphoma; almost abolishes ubiquitin-mediated degradation of BCL6. 1 Publication
VAR_070077

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 209209Missing in isoform 2. 1 PublicationVSP_022574Add
BLAST
Alternative sequencei1 – 8484Missing in isoform 3 and isoform 6. 4 PublicationsVSP_022573Add
BLAST
Alternative sequencei197 – 21115KRLYM…TRPMM → LGEVAHAYNPSTLGG in isoform 4. 1 PublicationVSP_008860Add
BLAST
Alternative sequencei212 – 927716Missing in isoform 4. 1 PublicationVSP_008861Add
BLAST
Alternative sequencei670 – 927258Missing in isoform 3. 1 PublicationVSP_008862Add
BLAST
Alternative sequencei744 – 77027LLEEN…PILRK → IVVNFALVKNPVFHYSSISL MINDIAN in isoform 2. 1 PublicationVSP_008863Add
BLAST
Alternative sequencei771 – 927157Missing in isoform 2. 1 PublicationVSP_008864Add
BLAST
Alternative sequencei885 – 8851R → RYVAHLLDILPNYFPPHFSN IWVSFCFR in isoform 5. 1 PublicationVSP_008865

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY827075 mRNA. Translation: AAV87312.1.
AF351618 mRNA. Translation: AAN76518.1. Sequence problems.
AK223592 mRNA. Translation: BAD97312.1.
AK022735 mRNA. Translation: BAB14214.1.
AK025477 mRNA. Translation: BAB15143.1. Different initiation.
AK292877 mRNA. Translation: BAF85566.1.
AC006509 Genomic DNA. No translation available.
AC079807 Genomic DNA. Translation: AAY24083.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAX00205.1.
BC012728 mRNA. Translation: AAH12728.2.
BC043258 mRNA. Translation: AAH43258.2.
BC130445 mRNA. Translation: AAI30446.1.
BC136480 mRNA. Translation: AAI36481.1.
AF174599 mRNA. Translation: AAF04520.1.
AF176706 mRNA. Translation: AAF17611.1.
AL117620 mRNA. Translation: CAB56019.1.
AF264714 mRNA. Translation: AAF76888.1. Sequence problems.
CCDSiCCDS1837.1. [Q86XK2-6]
CCDS54357.1. [Q86XK2-1]
PIRiT17329.
RefSeqiNP_001177203.1. NM_001190274.1. [Q86XK2-1]
NP_079409.3. NM_025133.4. [Q86XK2-6]
XP_005264629.1. XM_005264572.3. [Q86XK2-5]
UniGeneiHs.352677.

Genome annotation databases

EnsembliENST00000402508; ENSP00000385398; ENSG00000138081. [Q86XK2-6]
ENST00000403359; ENSP00000384823; ENSG00000138081. [Q86XK2-1]
GeneIDi80204.
KEGGihsa:80204.
UCSCiuc002rwe.3. human. [Q86XK2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY827075 mRNA. Translation: AAV87312.1.
AF351618 mRNA. Translation: AAN76518.1. Sequence problems.
AK223592 mRNA. Translation: BAD97312.1.
AK022735 mRNA. Translation: BAB14214.1.
AK025477 mRNA. Translation: BAB15143.1. Different initiation.
AK292877 mRNA. Translation: BAF85566.1.
AC006509 Genomic DNA. No translation available.
AC079807 Genomic DNA. Translation: AAY24083.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAX00205.1.
BC012728 mRNA. Translation: AAH12728.2.
BC043258 mRNA. Translation: AAH43258.2.
BC130445 mRNA. Translation: AAI30446.1.
BC136480 mRNA. Translation: AAI36481.1.
AF174599 mRNA. Translation: AAF04520.1.
AF176706 mRNA. Translation: AAF17611.1.
AL117620 mRNA. Translation: CAB56019.1.
AF264714 mRNA. Translation: AAF76888.1. Sequence problems.
CCDSiCCDS1837.1. [Q86XK2-6]
CCDS54357.1. [Q86XK2-1]
PIRiT17329.
RefSeqiNP_001177203.1. NM_001190274.1. [Q86XK2-1]
NP_079409.3. NM_025133.4. [Q86XK2-6]
XP_005264629.1. XM_005264572.3. [Q86XK2-5]
UniGeneiHs.352677.

3D structure databases

ProteinModelPortaliQ86XK2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123173. 50 interactions.
DIPiDIP-35680N.
IntActiQ86XK2. 14 interactions.
STRINGi9606.ENSP00000384823.

PTM databases

iPTMnetiQ86XK2.
PhosphoSiteiQ86XK2.

Polymorphism and mutation databases

BioMutaiFBXO11.
DMDMi124012093.

Proteomic databases

EPDiQ86XK2.
MaxQBiQ86XK2.
PaxDbiQ86XK2.
PRIDEiQ86XK2.

Protocols and materials databases

DNASUi80204.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402508; ENSP00000385398; ENSG00000138081. [Q86XK2-6]
ENST00000403359; ENSP00000384823; ENSG00000138081. [Q86XK2-1]
GeneIDi80204.
KEGGihsa:80204.
UCSCiuc002rwe.3. human. [Q86XK2-1]

Organism-specific databases

CTDi80204.
GeneCardsiFBXO11.
H-InvDBHIX0002044.
HGNCiHGNC:13590. FBXO11.
HPAiHPA002690.
MIMi607871. gene.
neXtProtiNX_Q86XK2.
Orphaneti3435. Vitiligo.
PharmGKBiPA28031.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1777. Eukaryota.
ENOG410YP8C. LUCA.
GeneTreeiENSGT00530000063425.
HOGENOMiHOG000020584.
HOVERGENiHBG051565.
InParanoidiQ86XK2.
KOiK10297.
OMAiSSRTYVR.
OrthoDBiEOG73803Z.
PhylomeDBiQ86XK2.
TreeFamiTF313602.

Enzyme and pathway databases

UniPathwayiUPA00143.
SIGNORiQ86XK2.

Miscellaneous databases

ChiTaRSiFBXO11. human.
GeneWikiiFBXO11.
GenomeRNAii80204.
PROiQ86XK2.
SOURCEiSearch...

Gene expression databases

BgeeiQ86XK2.
ExpressionAtlasiQ86XK2. baseline and differential.
GenevisibleiQ86XK2. HS.

Family and domain databases

Gene3Di2.160.20.10. 4 hits.
InterProiIPR006633. Carb-bd_sugar_hydrolysis-dom.
IPR001810. F-box_dom.
IPR029799. FBX11/DRE-1.
IPR007742. NosD_dom.
IPR022441. Para_beta_helix_rpt-2.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR003126. Znf_UBR.
[Graphical view]
PANTHERiPTHR22990:SF20. PTHR22990:SF20. 1 hit.
PfamiPF12937. F-box-like. 1 hit.
PF05048. NosD. 1 hit.
PF02207. zf-UBR. 1 hit.
[Graphical view]
SMARTiSM00722. CASH. 3 hits.
SM00256. FBOX. 1 hit.
SM00710. PbH1. 19 hits.
SM00396. ZnF_UBR1. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 3 hits.
SSF81383. SSF81383. 1 hit.
TIGRFAMsiTIGR03804. para_beta_helix. 4 hits.
PROSITEiPS50181. FBOX. 1 hit.
PS51157. ZF_UBR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity."
    Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W.
    J. Biol. Chem. 282:1797-1804(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53, IDENTIFICATION IN A COMPLEX WITH SKP1; CUL1 AND RBX1.
  2. "Isolation of full-length cDNA clones from human fetal brain cDNA library."
    Mao Y.-M., Xie Y.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Fetal brain.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Kidney.
  4. "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] (ISOFORMS 2 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-927 (ISOFORM 1).
    Tissue: Hepatoma and Teratocarcinoma.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-927 (ISOFORM 1).
    Tissue: Brain, Ovary and Testis.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-212.
  9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-927 (ISOFORM 4).
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 720-927.
    Tissue: Brain.
  11. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 744-927 (ISOFORM 5), TISSUE SPECIFICITY.
  12. "FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues."
    Cook J.R., Lee J.H., Yang Z.H., Krause C.D., Herth N., Hoffmann R., Pestka S.
    Biochem. Biophys. Res. Commun. 342:472-481(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, CAUTION (ISOFORM 2).
  13. "Regulation of TGF-beta signaling, exit from the cell cycle, and cellular migration through cullin cross-regulation: SCF-FBXO11 turns off CRL4-Cdt2."
    Abbas T., Keaton M., Dutta A.
    Cell Cycle 12:2175-2182(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  14. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
    Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
    Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF DTL, INTERACTION WITH DTL.
  15. "Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase."
    Rossi M., Duan S., Jeong Y.T., Horn M., Saraf A., Florens L., Washburn M.P., Antebi A., Pagano M.
    Mol. Cell 49:1159-1166(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF DTL, INTERACTION WITH DTL.
  16. "DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans developmental timing and maturation."
    Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C., Pagano M., Antebi A.
    Dev. Cell 28:697-710(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF PRDM1, INTERACTION WITH PRDM1, MUTAGENESIS OF GLN-575.
  17. "BLMP-1/Blimp-1 regulates the spatiotemporal cell migration pattern in C. elegans."
    Huang T.F., Cho C.Y., Cheng Y.T., Huang J.W., Wu Y.Z., Yeh A.Y., Nishiwaki K., Chang S.C., Wu Y.C.
    PLoS Genet. 10:E1004428-E1004428(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRDM1.
  18. "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas."
    Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.
    Nature 481:90-93(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYS-206; CYS-644; GLU-684; ASN-715 AND GLN-715, CHARACTERIZATION OF VARIANTS CYS-644; GLU-684; ASN-715 AND GLN-715, FUNCTION IN UBIQUITINATION OF BCL6, INTERACTION WITH BCL6, IDENTIFICATION IN THE SCF(FBXO11) COMPLEX, SUBCELLULAR LOCATION, INVOLVEMENT IN LYMPHOMA.

Entry informationi

Entry nameiFBX11_HUMAN
AccessioniPrimary (citable) accession number: Q86XK2
Secondary accession number(s): A1L491
, Q52ZP1, Q53EP7, Q53RT5, Q8IXG3, Q96E90, Q9H6V8, Q9H9L1, Q9NR14, Q9UFK1, Q9UHI1, Q9UKC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 141 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

Caution

Isoform 2: Has been initially named PRMT9 and reported to act as an arginine methyltransferase that can catalyze the formation of omega-N monomethylarginine (MMA) as well as symmetrical and asymmetrical dimethylarginine (sDMA and aDMA), however no further works support these observations (PubMed:16487488). It should not be confused with official PRMT9 (AC Q6P2P2).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.