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Q3U0V1 (FUBP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Khsrp
Synonyms:Fubp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

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

Sequence similarities

Belongs to the KHSRP family.

Contains 4 KH domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 748747Far upstream element-binding protein 2
PRO_0000298678

Regions

Domain145 – 20965KH 1
Domain234 – 30067KH 2
Domain323 – 38765KH 3
Domain425 – 49268KH 4
Repeat572 – 583121
Repeat618 – 629122
Repeat644 – 655123
Repeat674 – 685124
Region572 – 6851144 X 12 AA imperfect repeats
Compositional bias7 – 6862Gly/Pro-rich
Compositional bias69 – 497429Gly-rich
Compositional bias499 – 613115Ala/Gly/Pro-rich

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue881N6-acetyllysine Ref.6
Modified residue1011Phosphothreonine By similarity
Modified residue1821Phosphoserine Ref.4
Modified residue1851Phosphoserine Ref.4
Modified residue1941Phosphoserine By similarity
Modified residue2751Phosphoserine By similarity
Modified residue4811Phosphoserine By similarity

Experimental info

Sequence conflict3871I → F in BAE33750. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3U0V1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0699217B3E1E54A9

FASTA74876,775
        10         20         30         40         50         60 
MSDYNTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP GGGGASGGPS 

        70         80         90        100        110        120 
QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN TPDFGFGGQK RQLEDGDQPD 

       130        140        150        160        170        180 
SKKLASQGDS IGSQLGPIHP PPRTSMTEEY RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ 

       190        200        210        220        230        240 
ISPDSGGLPE RSVSLTGAPE SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM 

       250        260        270        280        290        300 
IPAGKAGLVI GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV 

       310        320        330        340        350        360 
MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ NDAGVRIQFK 

       370        380        390        400        410        420 
QDDGTGPEKI AHIMGPPDRC EHAARIINDL LQSLRSGPPG PPGAPGMPPG GRGRGRGQGN 

       430        440        450        460        470        480 
WGPPGGEMTF SIPTHKCGLV IGRGGENVKA INQQTGAFVE ISRQLPPNGD PNFKLFVIRG 

       490        500        510        520        530        540 
SPQQIDHAKQ LIEEKIEGPL CPVGPGPGGP GPAGPMGPFN PGPFNQGPPG APPHAGGPPP 

       550        560        570        580        590        600 
HQYPPQGWGN TYPQWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA 

       610        620        630        640        650        660 
APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA 

       670        680        690        700        710        720 
TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPPTQQGQQQ ASGNCHPPPP 

       730        740 
PFSFQPPATV HPALVGSAGN PFPCGVCP 

« Hide

References

[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK156541 mRNA. Translation: BAE33750.1.
CT571247 Genomic DNA. No translation available.
BC064454 mRNA. Translation: AAH64454.1.
BC108414 mRNA. Translation: AAI08415.1.
CCDSCCDS50157.1.
RefSeqNP_034743.3. NM_010613.3.
UniGeneMm.34296.

3D structure databases

ProteinModelPortalQ3U0V1.
SMRQ3U0V1. Positions 131-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200927. 1 interaction.
IntActQ3U0V1. 1 interaction.
STRING10090.ENSMUSP00000007814.

PTM databases

PhosphoSiteQ3U0V1.

Proteomic databases

MaxQBQ3U0V1.
PaxDbQ3U0V1.
PRIDEQ3U0V1.

Protocols and materials databases

DNASU16549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007814; ENSMUSP00000007814; ENSMUSG00000007670.
GeneID16549.
KEGGmmu:16549.
UCSCuc008ddr.2. mouse.

Organism-specific databases

CTD8570.
MGIMGI:1336214. Khsrp.

Phylogenomic databases

eggNOGNOG300923.
GeneTreeENSGT00730000110664.
HOGENOMHOG000231552.
HOVERGENHBG000625.
InParanoidQ3U0V1.
KOK13210.
OMAGPMGPFN.
OrthoDBEOG77Q4WB.
TreeFamTF313654.

Enzyme and pathway databases

ReactomeREACT_217867. Metabolism of RNA.

Gene expression databases

ArrayExpressQ3U0V1.
BgeeQ3U0V1.
CleanExMM_KHSRP.
GenevestigatorQ3U0V1.

Family and domain databases

Gene3D3.30.1370.10. 4 hits.
InterProIPR015096. DUF1897.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamPF09005. DUF1897. 2 hits.
PF00013. KH_1. 4 hits.
[Graphical view]
SMARTSM00322. KH. 4 hits.
[Graphical view]
SUPFAMSSF54791. SSF54791. 4 hits.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50084. KH_TYPE_1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio290019.
PROQ3U0V1.
SOURCESearch...

Entry information

Entry nameFUBP2_MOUSE
AccessionPrimary (citable) accession number: Q3U0V1
Secondary accession number(s): E9QKH3, Q2VPQ6, Q6P2L2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot