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Q92945

- FUBP2_HUMAN

UniProt

Q92945 - FUBP2_HUMAN

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Protein

Far upstream element-binding protein 2

Gene

KHSRP

Organism
Homo sapiens (Human)
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 (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.By similarity3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. mRNA binding Source: Ensembl
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA catabolic process Source: Ensembl
  3. mRNA metabolic process Source: Reactome
  4. mRNA processing Source: ProtInc
  5. mRNA transport Source: UniProtKB-KW
  6. regulation of miRNA metabolic process Source: Ensembl
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. RNA metabolic process Source: Reactome
  9. RNA splicing Source: UniProtKB
  10. RNA splicing, via transesterification reactions Source: UniProtKB
  11. 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_18355. ATF4 activates genes.
REACT_25042. 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
p75
Gene namesi
Name:KHSRP
Synonyms:FUBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:6316. KHSRP.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
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: Ensembl
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30097.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 711710Far upstream element-binding protein 2PRO_0000050137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei87 – 871N6-acetyllysineBy similarity
Modified residuei100 – 1001Phosphothreonine1 Publication
Modified residuei181 – 1811Phosphoserine7 Publications
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei274 – 2741Phosphoserine2 Publications
Modified residuei480 – 4801Phosphoserine3 Publications

Post-translational modificationi

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.9 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92945.
PaxDbiQ92945.
PRIDEiQ92945.

2D gel databases

REPRODUCTION-2DPAGEQ92945.

PTM databases

PhosphoSiteiQ92945.

Miscellaneous databases

PMAP-CutDBQ92945.

Expressioni

Tissue specificityi

Detected in neural and non-neural cell lines.

Gene expression databases

BgeeiQ92945.
CleanExiHS_KHSRP.
ExpressionAtlasiQ92945. baseline and differential.
GenevestigatoriQ92945.

Organism-specific databases

HPAiHPA034739.
HPA056518.

Interactioni

Subunit structurei

Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRPH1. Interacts with PARN.2 Publications

Protein-protein interaction databases

BioGridi114139. 51 interactions.
DIPiDIP-48484N.
IntActiQ92945. 16 interactions.
MINTiMINT-2813544.
STRINGi9606.ENSP00000381216.

Structurei

Secondary structure

1
711
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi132 – 1343Combined sources
Helixi141 – 1444Combined sources
Beta strandi146 – 1516Combined sources
Helixi153 – 1597Combined sources
Turni161 – 1633Combined sources
Helixi165 – 17410Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi188 – 1947Combined sources
Helixi198 – 21619Combined sources
Beta strandi234 – 2407Combined sources
Turni242 – 2443Combined sources
Turni245 – 2495Combined sources
Turni251 – 2533Combined sources
Helixi254 – 2618Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi281 – 2877Combined sources
Helixi289 – 30214Combined sources
Beta strandi306 – 3083Combined sources
Turni317 – 3193Combined sources
Beta strandi325 – 3306Combined sources
Turni331 – 3333Combined sources
Helixi334 – 3385Combined sources
Beta strandi340 – 3423Combined sources
Helixi343 – 35210Combined sources
Beta strandi355 – 3584Combined sources
Beta strandi363 – 37513Combined sources
Helixi376 – 39318Combined sources
Beta strandi400 – 4056Combined sources
Turni413 – 4153Combined sources
Beta strandi427 – 4326Combined sources
Helixi433 – 4353Combined sources
Turni436 – 4383Combined sources
Turni441 – 4444Combined sources
Helixi446 – 4538Combined sources
Beta strandi454 – 4607Combined sources
Beta strandi472 – 4798Combined sources
Helixi481 – 49414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HH2NMR-A424-525[»]
2HH3NMR-A318-418[»]
2JVZNMR-A233-396[»]
2OPUNMR-A130-218[»]
2OPVNMR-A221-305[»]
4B8TNMR-A317-418[»]
ProteinModelPortaliQ92945.
SMRiQ92945. Positions 130-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92945.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini144 – 20865KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini233 – 29967KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini322 – 38665KH 3PROSITE-ProRule annotationAdd
BLAST
Domaini424 – 49168KH 4PROSITE-ProRule annotationAdd
BLAST
Repeati571 – 582121Add
BLAST
Repeati617 – 628122Add
BLAST
Repeati643 – 654123Add
BLAST
Repeati673 – 684124Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni571 – 6841144 X 12 AA imperfect repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 6761Gly/Pro-richAdd
BLAST
Compositional biasi68 – 496429Gly-richAdd
BLAST
Compositional biasi498 – 612115Ala/Gly/Pro-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the KHSRP family.Curated
Contains 4 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG300923.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ92945.
KOiK13210.
OMAiGPMGPFN.
OrthoDBiEOG77Q4WB.
PhylomeDBiQ92945.
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.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92945-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDYSTGGPP PGPPPPAGGG GGAGGAGGGP PPGPPGAGDR GGGGPGGGGP
60 70 80 90 100
GGGSAGGPSQ PPGGGGPGIR KDAFADAVQR ARQIAAKIGG DAATTVNNST
110 120 130 140 150
PDFGFGGQKR QLEDGDQPES KKLASQGDSI SSQLGPIHPP PRTSMTEEYR
160 170 180 190 200
VPDGMVGLII GRGGEQINKI QQDSGCKVQI SPDSGGLPER SVSLTGAPES
210 220 230 240 250
VQKAKMMLDD IVSRGRGGPP GQFHDNANGG QNGTVQEIMI PAGKAGLVIG
260 270 280 290 300
KGGETIKQLQ ERAGVKMILI QDGSQNTNVD KPLRIIGDPY KVQQACEMVM
310 320 330 340 350
DILRERDQGG FGDRNEYGSR IGGGIDVPVP RHSVGVVIGR SGEMIKKIQN
360 370 380 390 400
DAGVRIQFKQ DDGTGPEKIA HIMGPPDRCE HAARIINDLL QSLRSGPPGP
410 420 430 440 450
PGGPGMPPGG RGRGRGQGNW GPPGGEMTFS IPTHKCGLVI GRGGENVKAI
460 470 480 490 500
NQQTGAFVEI SRQLPPNGDP NFKLFIIRGS PQQIDHAKQL IEEKIEGPLC
510 520 530 540 550
PVGPGPGGPG PAGPMGPFNP GPFNQGPPGA PPHAGGPPPH QYPPQGWGNT
560 570 580 590 600
YPQWQPPAPH DPSKAAAAAA DPNAAWAAYY SHYYQQPPGP VPGPAPAPAA
610 620 630 640 650
PPAQGEPPQP PPTGQSDYTK AWEEYYKKIG QQPQQPGAPP QQDYTKAWEE
660 670 680 690 700
YYKKQAQVAT GGGPGAPPGS QPDYSAAWAE YYRQQAAYYG QTPGPGGPQP
710
PPTQQGQQQA Q
Length:711
Mass (Da):73,115
Last modified:November 30, 2010 - v4
Checksum:iAB0B7C0B5B938114
GO

Sequence cautioni

The sequence AAC50892.1 differs from that shown. Reason: Frameshift at positions 304, 309, 466 and 473. Curated
The sequence AAH85004.1 differs from that shown. Reason: Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461G → C in AAB53222. (PubMed:9136930)Curated
Sequence conflicti46 – 461G → C in AAD29861. (PubMed:10087204)Curated
Sequence conflicti96 – 961V → G in AAC50892. (PubMed:8940189)Curated
Sequence conflicti406 – 4072MP → I in AAC50892. (PubMed:8940189)Curated
Sequence conflicti422 – 4221Missing in AAC50892. (PubMed:8940189)Curated
Sequence conflicti487 – 4882AK → CR in AAC50892. (PubMed:8940189)Curated
Sequence conflicti694 – 6963GPG → VP in AAC50892. (PubMed:8940189)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45936.1.
RefSeqiNP_003676.2. NM_003685.2.
UniGeneiHs.727344.

Genome annotation databases

EnsembliENST00000398148; ENSP00000381216; ENSG00000088247.
GeneIDi8570.
KEGGihsa:8570.
UCSCiuc002mer.4. human.

Polymorphism databases

DMDMi313104306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS45936.1.
RefSeqi NP_003676.2. NM_003685.2.
UniGenei Hs.727344.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HH2 NMR - A 424-525 [» ]
2HH3 NMR - A 318-418 [» ]
2JVZ NMR - A 233-396 [» ]
2OPU NMR - A 130-218 [» ]
2OPV NMR - A 221-305 [» ]
4B8T NMR - A 317-418 [» ]
ProteinModelPortali Q92945.
SMRi Q92945. Positions 130-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114139. 51 interactions.
DIPi DIP-48484N.
IntActi Q92945. 16 interactions.
MINTi MINT-2813544.
STRINGi 9606.ENSP00000381216.

Chemistry

ChEMBLi CHEMBL1795105.

PTM databases

PhosphoSitei Q92945.

Polymorphism databases

DMDMi 313104306.

2D gel databases

REPRODUCTION-2DPAGE Q92945.

Proteomic databases

MaxQBi Q92945.
PaxDbi Q92945.
PRIDEi Q92945.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398148 ; ENSP00000381216 ; ENSG00000088247 .
GeneIDi 8570.
KEGGi hsa:8570.
UCSCi uc002mer.4. human.

Organism-specific databases

CTDi 8570.
GeneCardsi GC19M006413.
H-InvDB HIX0040083.
HGNCi HGNC:6316. KHSRP.
HPAi HPA034739.
HPA056518.
MIMi 603445. gene.
neXtProti NX_Q92945.
PharmGKBi PA30097.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300923.
GeneTreei ENSGT00730000110664.
HOGENOMi HOG000231552.
HOVERGENi HBG000625.
InParanoidi Q92945.
KOi K13210.
OMAi GPMGPFN.
OrthoDBi EOG77Q4WB.
PhylomeDBi Q92945.
TreeFami TF313654.

Enzyme and pathway databases

Reactomei REACT_18355. ATF4 activates genes.
REACT_25042. KSRP destabilizes mRNA.

Miscellaneous databases

ChiTaRSi KHSRP. human.
EvolutionaryTracei Q92945.
GeneWikii KHSRP.
GenomeRNAii 8570.
NextBioi 32149.
PMAP-CutDB Q92945.
PROi Q92945.
SOURCEi Search...

Gene expression databases

Bgeei Q92945.
CleanExi HS_KHSRP.
ExpressionAtlasi Q92945. baseline and differential.
Genevestigatori Q92945.

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 PS50084. KH_TYPE_1. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiFUBP2_HUMAN
AccessioniPrimary (citable) accession number: Q92945
Secondary accession number(s): O00301
, Q59EZ9, Q5U4P6, Q9UNT5, Q9UQH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 142 of the entry and version 4 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3