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Q92945 (FUBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
p75
Gene names
Name:KHSRP
Synonyms:FUBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length711 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 By similarity. 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. Ref.1 Ref.5 Ref.8

Subunit structure

Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRPH1. Interacts with PARN. Ref.8 Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites By similarity. Ref.24

Tissue specificity

Detected in neural and non-neural cell lines.

Domain

KH domains KH 3 and KH 4 behave as independent binding modules and can interact with different regions of the AU-rich RNA targets of degradation.

Post-translational modification

Phosphorylation at Ser-193 leads to the unfolding of the unstable KH domain 1, creating a site for 14-3-3 YWHAZ binding, which promotes nuclear localization and impairs the RNA degradation function.

Sequence similarities

Belongs to the KHSRP family.

Contains 4 KH domains.

Sequence caution

The sequence AAC50892.1 differs from that shown. Reason: Frameshift at positions 304, 309, 466 and 473.

The sequence AAH85004.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
mRNA transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandDNA-binding
RNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement PubMed 10911989. Source: UniProtKB

RNA splicing, via transesterification reactions

Traceable author statement PubMed 10911989. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.1. Source: ProtInc

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic stress granule

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 711710Far upstream element-binding protein 2
PRO_0000050137

Regions

Domain144 – 20865KH 1
Domain233 – 29967KH 2
Domain322 – 38665KH 3
Domain424 – 49168KH 4
Repeat571 – 582121
Repeat617 – 628122
Repeat643 – 654123
Repeat673 – 684124
Region571 – 6841144 X 12 AA imperfect repeats
Compositional bias7 – 6761Gly/Pro-rich
Compositional bias68 – 496429Gly-rich
Compositional bias498 – 612115Ala/Gly/Pro-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.15 Ref.21 Ref.22
Modified residue871N6-acetyllysine By similarity
Modified residue1001Phosphothreonine Ref.14
Modified residue1811Phosphoserine Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20
Modified residue1841Phosphoserine By similarity
Modified residue1931Phosphoserine Ref.24
Modified residue2741Phosphoserine Ref.14 Ref.20
Modified residue4801Phosphoserine Ref.10 Ref.18 Ref.20

Experimental info

Sequence conflict461G → C in AAB53222. Ref.1
Sequence conflict461G → C in AAD29861. Ref.4
Sequence conflict961V → G in AAC50892. Ref.5
Sequence conflict406 – 4072MP → I in AAC50892. Ref.5
Sequence conflict4221Missing in AAC50892. Ref.5
Sequence conflict487 – 4882AK → CR in AAC50892. Ref.5
Sequence conflict694 – 6963GPG → VP in AAC50892. Ref.5

Secondary structure

...................................................................... 711
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92945 [UniParc].

Last modified November 30, 2010. Version 4.
Checksum: AB0B7C0B5B938114

FASTA71173,115
        10         20         30         40         50         60 
MSDYSTGGPP PGPPPPAGGG GGAGGAGGGP PPGPPGAGDR GGGGPGGGGP GGGSAGGPSQ 

        70         80         90        100        110        120 
PPGGGGPGIR KDAFADAVQR ARQIAAKIGG DAATTVNNST PDFGFGGQKR QLEDGDQPES 

       130        140        150        160        170        180 
KKLASQGDSI SSQLGPIHPP PRTSMTEEYR VPDGMVGLII GRGGEQINKI QQDSGCKVQI 

       190        200        210        220        230        240 
SPDSGGLPER SVSLTGAPES VQKAKMMLDD IVSRGRGGPP GQFHDNANGG QNGTVQEIMI 

       250        260        270        280        290        300 
PAGKAGLVIG KGGETIKQLQ ERAGVKMILI QDGSQNTNVD KPLRIIGDPY KVQQACEMVM 

       310        320        330        340        350        360 
DILRERDQGG FGDRNEYGSR IGGGIDVPVP RHSVGVVIGR SGEMIKKIQN DAGVRIQFKQ 

       370        380        390        400        410        420 
DDGTGPEKIA HIMGPPDRCE HAARIINDLL QSLRSGPPGP PGGPGMPPGG RGRGRGQGNW 

       430        440        450        460        470        480 
GPPGGEMTFS IPTHKCGLVI GRGGENVKAI NQQTGAFVEI SRQLPPNGDP NFKLFIIRGS 

       490        500        510        520        530        540 
PQQIDHAKQL IEEKIEGPLC PVGPGPGGPG PAGPMGPFNP GPFNQGPPGA PPHAGGPPPH 

       550        560        570        580        590        600 
QYPPQGWGNT YPQWQPPAPH DPSKAAAAAA DPNAAWAAYY SHYYQQPPGP VPGPAPAPAA 

       610        620        630        640        650        660 
PPAQGEPPQP PPTGQSDYTK AWEEYYKKIG QQPQQPGAPP QQDYTKAWEE YYKKQAQVAT 

       670        680        690        700        710 
GGGPGAPPGS QPDYSAAWAE YYRQQAAYYG QTPGPGGPQP PPTQQGQQQA Q 

« Hide

References

« Hide 'large scale' references
[1]"A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer."
Min H., Turck C.W., Nikolic J.M., Black D.L.
Genes Dev. 11:1023-1036(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-85; 123-128; 267-281; 283-291; 348-359; 474-488; 489-494; 621-627; 629-646 AND 647-653, FUNCTION.
Tissue: Neuroblastoma and Retinoblastoma.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Ovary.
[4]"Mapping of the KHSRP gene to a region of conserved synteny on human chromosome 19p13.3 and mouse chromosome 17."
Ring H.Z., Vameghi-Meyers V., Nikolic J.M., Min H., Black D.L., Francke U.
Genomics 56:350-352(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115 AND 573-711.
[5]"The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators."
Davis-Smyth T., Duncan R.C., Zheng T., Michelotti G., Levens D.
J. Biol. Chem. 271:31679-31687(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-711, FUNCTION.
Tissue: B-cell lymphoma and Skeletal muscle.
[6]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 151-162; 321-331 AND 385-394, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-566.
Tissue: Brain.
[8]"Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein."
Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L.
Mol. Cell. Biol. 20:7463-7479(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTBP1; PTBP2 AND HNRPH1.
[9]"A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery."
Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M., Chen C.-Y.
Mol. Cell 14:571-583(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARN.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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 kidney.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-181 AND SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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 SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-181 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-181; SER-274 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation."
Garcia-Mayoral M.F., Hollingworth D., Masino L., Diaz-Moreno I., Kelly G., Gherzi R., Chou C.F., Chen C.Y., Ramos A.
Structure 15:485-498(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 218-418 AND 423-525.
[24]"Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding."
Diaz-Moreno I., Hollingworth D., Frenkiel T.A., Kelly G., Martin S., Howell S., Garcia-Mayoral M., Gherzi R., Briata P., Ramos A.
Nat. Struct. Mol. Biol. 16:238-246(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 130-218 AND 221-305, PHOSPHORYLATION AT SER-193, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94832 mRNA. Translation: AAB53222.1.
AC011491 Genomic DNA. No translation available.
AC011539 Genomic DNA. No translation available.
BC085004 mRNA. Translation: AAH85004.1. Sequence problems.
AF093747, AF093745 Genomic DNA. Translation: AAD29861.1.
AF093748 Genomic DNA. Translation: AAD29862.1.
U69126 mRNA. Translation: AAC50892.1. Frameshift.
AB209662 mRNA. Translation: BAD92899.1.
CCDSCCDS45936.1.
RefSeqNP_003676.2. NM_003685.2.
UniGeneHs.727344.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HH2NMR-A424-525[»]
2HH3NMR-A318-418[»]
2JVZNMR-A233-396[»]
2OPUNMR-A130-218[»]
2OPVNMR-A221-305[»]
4B8TNMR-A317-418[»]
ProteinModelPortalQ92945.
SMRQ92945. Positions 130-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114139. 47 interactions.
DIPDIP-48484N.
IntActQ92945. 14 interactions.
MINTMINT-2813544.
STRING9606.ENSP00000381216.

Chemistry

ChEMBLCHEMBL1795105.

PTM databases

PhosphoSiteQ92945.

Polymorphism databases

DMDM313104306.

2D gel databases

REPRODUCTION-2DPAGEQ92945.

Proteomic databases

MaxQBQ92945.
PaxDbQ92945.
PRIDEQ92945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398148; ENSP00000381216; ENSG00000088247.
GeneID8570.
KEGGhsa:8570.
UCSCuc002mer.4. human.

Organism-specific databases

CTD8570.
GeneCardsGC19M006413.
H-InvDBHIX0040083.
HGNCHGNC:6316. KHSRP.
HPAHPA034739.
HPA056518.
MIM603445. gene.
neXtProtNX_Q92945.
PharmGKBPA30097.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300923.
HOGENOMHOG000231552.
HOVERGENHBG000625.
InParanoidQ92945.
KOK13210.
OMAGPMGPFN.
OrthoDBEOG77Q4WB.
PhylomeDBQ92945.
TreeFamTF313654.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ92945.
BgeeQ92945.
CleanExHS_KHSRP.
GenevestigatorQ92945.

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.
PROSITEPS50084. KH_TYPE_1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKHSRP. human.
EvolutionaryTraceQ92945.
GeneWikiKHSRP.
GenomeRNAi8570.
NextBio32149.
PMAP-CutDBQ92945.
PROQ92945.
SOURCESearch...

Entry information

Entry nameFUBP2_HUMAN
AccessionPrimary (citable) accession number: Q92945
Secondary accession number(s): O00301 expand/collapse secondary AC list , Q59EZ9, Q5U4P6, Q9UNT5, Q9UQH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM