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Protein

F-box/LRR-repeat protein 12

Gene

Fbxl12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia (By similarity).By similarity

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.

GO - Biological processi

  • protein ubiquitination Source: UniProtKB-UniPathway
  • ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box/LRR-repeat protein 12
Alternative name(s):
F-box and leucine-rich repeat protein 12
F-box protein FBL12
Gene namesi
Name:Fbxl12
Synonyms:Fbl12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1354738. Fbxl12.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • ubiquitin ligase complex Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326F-box/LRR-repeat protein 12PRO_0000119858Add
BLAST

Proteomic databases

MaxQBiQ9EPX5.
PaxDbiQ9EPX5.
PRIDEiQ9EPX5.

PTM databases

PhosphoSiteiQ9EPX5.

Expressioni

Gene expression databases

BgeeiQ9EPX5.
CleanExiMM_FBXL12.
ExpressionAtlasiQ9EPX5. baseline and differential.
GenevisibleiQ9EPX5. MM.

Interactioni

Subunit structurei

Interacts with SKP1 and CUL1.By similarity

Protein-protein interaction databases

BioGridi205979. 2 interactions.
MINTiMINT-1340452.
STRINGi10090.ENSMUSP00000083650.

Structurei

3D structure databases

ProteinModelPortaliQ9EPX5.
SMRiQ9EPX5. Positions 7-65, 176-212, 227-259, 280-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4747F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati51 – 7828LRR 1Add
BLAST
Repeati86 – 11126LRR 2Add
BLAST
Repeati113 – 13321LRR 3Add
BLAST
Repeati161 – 18525LRR 4Add
BLAST
Repeati186 – 21126LRR 5Add
BLAST
Repeati212 – 23625LRR 6Add
BLAST
Repeati237 – 26125LRR 7Add
BLAST
Repeati266 – 29126LRR 8Add
BLAST

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 8 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiENOG410IT1J. Eukaryota.
ENOG4111Z4R. LUCA.
GeneTreeiENSGT00390000003354.
HOGENOMiHOG000112675.
HOVERGENiHBG051672.
InParanoidiQ9EPX5.
KOiK10278.
OMAiISMAWLL.
PhylomeDBiQ9EPX5.
TreeFamiTF313434.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR032675. L_dom-like.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLFDLPDL VLLEIFSYLP VRDRIRISRV CHRWKRLVDD RWLWRHVDLT
60 70 80 90 100
LYTMRPKVMW HLLRRYMASR LYSLRMGGYL FSGSQAPQLS PALMRALGQK
110 120 130 140 150
CPNLKRLCLH VADLSMVPIT SLPSTLRTLE LHSCEISMIW LQKEQDPTVL
160 170 180 190 200
PLLECIVLDR VPAFRDEHLQ GLTRFRALRS LVLGGTYRVT ETGLDASLQE
210 220 230 240 250
LSYLQRLEVL GCTLSADSTL LAISRHLRDV RKIRLTVGGL SAQGLVFLEG
260 270 280 290 300
MPVLESLCFQ GPLITPDMPT PTQIVSSCLT MPKLRVLEVQ GLGWEGQEAE
310 320
KILCKGLPHC IVIVRACPKE SMDWWM
Length:326
Mass (Da):37,231
Last modified:March 1, 2001 - v1
Checksum:i5A670BCDBF87CC5B
GO

Sequence cautioni

The sequence AAF09134.1 differs from that shown. Reason: Frameshift at position 309. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176525 mRNA. Translation: AAF09134.1. Frameshift.
AF313405 mRNA. Translation: AAG37272.1.
AK011081 mRNA. Translation: BAB27385.1.
AK029429 mRNA. Translation: BAC26448.1.
AK030910 mRNA. Translation: BAC27180.1.
AK137282 mRNA. Translation: BAE23292.1.
BC005699 mRNA. Translation: AAH05699.1.
BC054471 mRNA. Translation: AAH54471.1.
CCDSiCCDS22880.1.
RefSeqiNP_001002846.1. NM_001002846.2.
NP_001273458.1. NM_001286529.1.
NP_001273459.1. NM_001286530.1.
NP_038939.2. NM_013911.3.
XP_006510460.1. XM_006510397.2.
XP_006510461.1. XM_006510398.2.
XP_006510462.1. XM_006510399.2.
UniGeneiMm.24608.
Mm.390165.
Mm.489685.

Genome annotation databases

EnsembliENSMUST00000086459; ENSMUSP00000083650; ENSMUSG00000066892.
ENSMUST00000148631; ENSMUSP00000119124; ENSMUSG00000066892.
GeneIDi30843.
KEGGimmu:30843.
UCSCiuc009oiz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176525 mRNA. Translation: AAF09134.1. Frameshift.
AF313405 mRNA. Translation: AAG37272.1.
AK011081 mRNA. Translation: BAB27385.1.
AK029429 mRNA. Translation: BAC26448.1.
AK030910 mRNA. Translation: BAC27180.1.
AK137282 mRNA. Translation: BAE23292.1.
BC005699 mRNA. Translation: AAH05699.1.
BC054471 mRNA. Translation: AAH54471.1.
CCDSiCCDS22880.1.
RefSeqiNP_001002846.1. NM_001002846.2.
NP_001273458.1. NM_001286529.1.
NP_001273459.1. NM_001286530.1.
NP_038939.2. NM_013911.3.
XP_006510460.1. XM_006510397.2.
XP_006510461.1. XM_006510398.2.
XP_006510462.1. XM_006510399.2.
UniGeneiMm.24608.
Mm.390165.
Mm.489685.

3D structure databases

ProteinModelPortaliQ9EPX5.
SMRiQ9EPX5. Positions 7-65, 176-212, 227-259, 280-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205979. 2 interactions.
MINTiMINT-1340452.
STRINGi10090.ENSMUSP00000083650.

PTM databases

PhosphoSiteiQ9EPX5.

Proteomic databases

MaxQBiQ9EPX5.
PaxDbiQ9EPX5.
PRIDEiQ9EPX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086459; ENSMUSP00000083650; ENSMUSG00000066892.
ENSMUST00000148631; ENSMUSP00000119124; ENSMUSG00000066892.
GeneIDi30843.
KEGGimmu:30843.
UCSCiuc009oiz.2. mouse.

Organism-specific databases

CTDi54850.
MGIiMGI:1354738. Fbxl12.

Phylogenomic databases

eggNOGiENOG410IT1J. Eukaryota.
ENOG4111Z4R. LUCA.
GeneTreeiENSGT00390000003354.
HOGENOMiHOG000112675.
HOVERGENiHBG051672.
InParanoidiQ9EPX5.
KOiK10278.
OMAiISMAWLL.
PhylomeDBiQ9EPX5.
TreeFamiTF313434.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ9EPX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPX5.
CleanExiMM_FBXL12.
ExpressionAtlasiQ9EPX5. baseline and differential.
GenevisibleiQ9EPX5. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR032675. L_dom-like.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "F-box protein FBL12 containing leucine-rich repeats."
    Ilyin G.P.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic liver, Head and Urinary bladder.
  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].
    Strain: C57BL/6J.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiFXL12_MOUSE
AccessioniPrimary (citable) accession number: Q9EPX5
Secondary accession number(s): Q3UVH7
, Q8CDX0, Q9CY04, Q9QZN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.