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Q3U0V1

- FUBP2_MOUSE

UniProt

Q3U0V1 - FUBP2_MOUSE

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Protein
Far upstream element-binding protein 2
Gene
Khsrp, Fubp2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to the dendritic targeting element and may play a role in mRNA trafficking. Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs By similarity.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. mRNA binding Source: MGI

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. mRNA catabolic process Source: MGI
  3. mRNA processing Source: UniProtKB-KW
  4. mRNA transport Source: UniProtKB-KW
  5. regulation of miRNA metabolic process Source: MGI
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_198696. KSRP destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Far upstream element-binding protein 2
Short name:
FUSE-binding protein 2
Alternative name(s):
KH type-splicing regulatory protein
Short name:
KSRP
Gene namesi
Name:Khsrp
Synonyms:Fubp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1336214. Khsrp.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity
Note: A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites By similarity.

GO - Cellular componenti

  1. cytoplasmic stress granule Source: MGI
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 748747Far upstream element-binding protein 2
PRO_0000298678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei88 – 881N6-acetyllysine1 Publication
Modified residuei101 – 1011Phosphothreonine By similarity
Modified residuei182 – 1821Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine By similarity
Modified residuei275 – 2751Phosphoserine By similarity
Modified residuei481 – 4811Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ3U0V1.
PaxDbiQ3U0V1.
PRIDEiQ3U0V1.

PTM databases

PhosphoSiteiQ3U0V1.

Expressioni

Gene expression databases

ArrayExpressiQ3U0V1.
BgeeiQ3U0V1.
CleanExiMM_KHSRP.
GenevestigatoriQ3U0V1.

Interactioni

Subunit structurei

Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRPH1. Interacts with PARN By similarity.

Protein-protein interaction databases

BioGridi200927. 1 interaction.
IntActiQ3U0V1. 1 interaction.
STRINGi10090.ENSMUSP00000007814.

Structurei

3D structure databases

ProteinModelPortaliQ3U0V1.
SMRiQ3U0V1. Positions 131-504.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 20965KH 1
Add
BLAST
Domaini234 – 30067KH 2
Add
BLAST
Domaini323 – 38765KH 3
Add
BLAST
Domaini425 – 49268KH 4
Add
BLAST
Repeati572 – 583121
Add
BLAST
Repeati618 – 629122
Add
BLAST
Repeati644 – 655123
Add
BLAST
Repeati674 – 685124
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni572 – 6851144 X 12 AA imperfect repeats
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 6862Gly/Pro-rich
Add
BLAST
Compositional biasi69 – 497429Gly-rich
Add
BLAST
Compositional biasi499 – 613115Ala/Gly/Pro-rich
Add
BLAST

Sequence similaritiesi

Belongs to the KHSRP family.
Contains 4 KH domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG300923.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ3U0V1.
KOiK13210.
OMAiGPMGPFN.
OrthoDBiEOG77Q4WB.
TreeFamiTF313654.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
InterProiIPR015096. DUF1897.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF09005. DUF1897. 2 hits.
PF00013. KH_1. 4 hits.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50084. KH_TYPE_1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U0V1-1 [UniParc]FASTAAdd to Basket

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MSDYNTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP    50
GGGGASGGPS QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN 100
TPDFGFGGQK RQLEDGDQPD SKKLASQGDS IGSQLGPIHP PPRTSMTEEY 150
RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ ISPDSGGLPE RSVSLTGAPE 200
SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM IPAGKAGLVI 250
GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV 300
MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ 350
NDAGVRIQFK QDDGTGPEKI AHIMGPPDRC EHAARIINDL LQSLRSGPPG 400
PPGAPGMPPG GRGRGRGQGN WGPPGGEMTF SIPTHKCGLV IGRGGENVKA 450
INQQTGAFVE ISRQLPPNGD PNFKLFVIRG SPQQIDHAKQ LIEEKIEGPL 500
CPVGPGPGGP GPAGPMGPFN PGPFNQGPPG APPHAGGPPP HQYPPQGWGN 550
TYPQWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA 600
APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE 650
EYYKKQAQVA TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ 700
PPPTQQGQQQ ASGNCHPPPP PFSFQPPATV HPALVGSAGN PFPCGVCP 748
Length:748
Mass (Da):76,775
Last modified:July 27, 2011 - v2
Checksum:i0699217B3E1E54A9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3871I → F in BAE33750. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK156541 mRNA. Translation: BAE33750.1.
CT571247 Genomic DNA. No translation available.
BC064454 mRNA. Translation: AAH64454.1.
BC108414 mRNA. Translation: AAI08415.1.
CCDSiCCDS50157.1.
RefSeqiNP_034743.3. NM_010613.3.
UniGeneiMm.34296.

Genome annotation databases

EnsembliENSMUST00000007814; ENSMUSP00000007814; ENSMUSG00000007670.
GeneIDi16549.
KEGGimmu:16549.
UCSCiuc008ddr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK156541 mRNA. Translation: BAE33750.1 .
CT571247 Genomic DNA. No translation available.
BC064454 mRNA. Translation: AAH64454.1 .
BC108414 mRNA. Translation: AAI08415.1 .
CCDSi CCDS50157.1.
RefSeqi NP_034743.3. NM_010613.3.
UniGenei Mm.34296.

3D structure databases

ProteinModelPortali Q3U0V1.
SMRi Q3U0V1. Positions 131-504.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200927. 1 interaction.
IntActi Q3U0V1. 1 interaction.
STRINGi 10090.ENSMUSP00000007814.

PTM databases

PhosphoSitei Q3U0V1.

Proteomic databases

MaxQBi Q3U0V1.
PaxDbi Q3U0V1.
PRIDEi Q3U0V1.

Protocols and materials databases

DNASUi 16549.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000007814 ; ENSMUSP00000007814 ; ENSMUSG00000007670 .
GeneIDi 16549.
KEGGi mmu:16549.
UCSCi uc008ddr.2. mouse.

Organism-specific databases

CTDi 8570.
MGIi MGI:1336214. Khsrp.

Phylogenomic databases

eggNOGi NOG300923.
GeneTreei ENSGT00730000110664.
HOGENOMi HOG000231552.
HOVERGENi HBG000625.
InParanoidi Q3U0V1.
KOi K13210.
OMAi GPMGPFN.
OrthoDBi EOG77Q4WB.
TreeFami TF313654.

Enzyme and pathway databases

Reactomei REACT_198696. KSRP destabilizes mRNA.

Miscellaneous databases

NextBioi 290019.
PROi Q3U0V1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q3U0V1.
Bgeei Q3U0V1.
CleanExi MM_KHSRP.
Genevestigatori Q3U0V1.

Family and domain databases

Gene3Di 3.30.1370.10. 4 hits.
InterProi IPR015096. DUF1897.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view ]
Pfami PF09005. DUF1897. 2 hits.
PF00013. KH_1. 4 hits.
[Graphical view ]
SMARTi SM00322. KH. 4 hits.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 4 hits.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50084. KH_TYPE_1. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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: NOD.
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 198-748.
    Strain: C57BL/6.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiFUBP2_MOUSE
AccessioniPrimary (citable) accession number: Q3U0V1
Secondary accession number(s): E9QKH3, Q2VPQ6, Q6P2L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 81 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi