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Protein

Far upstream element-binding protein 1

Gene

FUBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription.1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • single-stranded DNA binding Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

  • positive regulation of gene expression Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Far upstream element-binding protein 1
Short name:
FBP
Short name:
FUSE-binding protein 1
Alternative name(s):
DNA helicase V
Short name:
hDH V
Gene namesi
Name:FUBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4004. FUBP1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28420.

Polymorphism and mutation databases

BioMutaiFUBP1.
DMDMi116241370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 644643Far upstream element-binding protein 1PRO_0000050135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei153 – 1531PhosphothreonineCombined sources
Modified residuei630 – 6301PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated. This targets the protein for proteasome-mediated degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96AE4.
MaxQBiQ96AE4.
PaxDbiQ96AE4.
PRIDEiQ96AE4.
TopDownProteomicsiQ96AE4-1. [Q96AE4-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00375441.

PTM databases

iPTMnetiQ96AE4.
PhosphoSiteiQ96AE4.
SwissPalmiQ96AE4.

Expressioni

Gene expression databases

BgeeiQ96AE4.
CleanExiHS_FUBP1.
ExpressionAtlasiQ96AE4. baseline and differential.
GenevisibleiQ96AE4. HS.

Organism-specific databases

HPAiHPA006149.

Interactioni

Subunit structurei

Found in a complex with PUF60 and far upstream element (FUSE) DNA segment. Interacts with PUF60 and JTV1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131554EBI-711404,EBI-745226
USP22Q9UPT93EBI-711404,EBI-723510

Protein-protein interaction databases

BioGridi114399. 99 interactions.
DIPiDIP-47273N.
IntActiQ96AE4. 33 interactions.
MINTiMINT-1374324.
STRINGi9606.ENSP00000359804.

Structurei

Secondary structure

1
644
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4415Combined sources
Beta strandi101 – 1088Combined sources
Helixi109 – 1113Combined sources
Helixi112 – 1165Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 13010Combined sources
Beta strandi133 – 1364Combined sources
Beta strandi144 – 1529Combined sources
Helixi154 – 16815Combined sources
Beta strandi278 – 2836Combined sources
Helixi284 – 2918Combined sources
Helixi293 – 2953Combined sources
Helixi296 – 30510Combined sources
Beta strandi308 – 3125Combined sources
Beta strandi319 – 3279Combined sources
Helixi329 – 34618Combined sources
Beta strandi378 – 3847Combined sources
Turni385 – 3873Combined sources
Helixi388 – 3925Combined sources
Helixi394 – 3963Combined sources
Helixi397 – 40610Combined sources
Beta strandi409 – 4135Combined sources
Turni417 – 4193Combined sources
Beta strandi424 – 4307Combined sources
Helixi433 – 44614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J4WNMR-A278-447[»]
2KXHNMR-B27-52[»]
4LIJX-ray1.80A/B/C86-175[»]
ProteinModelPortaliQ96AE4.
SMRiQ96AE4. Positions 22-52, 98-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96AE4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 16465KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini185 – 25167KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 33965KH 3PROSITE-ProRule annotationAdd
BLAST
Domaini376 – 44368KH 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 2614Gly-richAdd
BLAST
Compositional biasi349 – 39648Gly-richAdd
BLAST
Compositional biasi450 – 560111Pro-richAdd
BLAST

Sequence similaritiesi

Contains 4 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1676. Eukaryota.
ENOG410XZYE. LUCA.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ96AE4.
KOiK13210.
OrthoDBiEOG77Q4WB.
PhylomeDBiQ96AE4.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96AE4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADYSTVPPP SSGSAGGGGG GGGGGGVNDA FKDALQRARQ IAAKIGGDAG
60 70 80 90 100
TSLNSNDYGY GGQKRPLEDG DQPDAKKVAP QNDSFGTQLP PMHQQQSRSV
110 120 130 140 150
MTEEYKVPDG MVGFIIGRGG EQISRIQQES GCKIQIAPDS GGLPERSCML
160 170 180 190 200
TGTPESVQSA KRLLDQIVEK GRPAPGFHHG DGPGNAVQEI MIPASKAGLV
210 220 230 240 250
IGKGGETIKQ LQERAGVKMV MIQDGPQNTG ADKPLRITGD PYKVQQAKEM
260 270 280 290 300
VLELIRDQGG FREVRNEYGS RIGGNEGIDV PIPRFAVGIV IGRNGEMIKK
310 320 330 340 350
IQNDAGVRIQ FKPDDGTTPE RIAQITGPPD RCQHAAEIIT DLLRSVQAGN
360 370 380 390 400
PGGPGPGGRG RGRGQGNWNM GPPGGLQEFN FIVPTGKTGL IIGKGGETIK
410 420 430 440 450
SISQQSGARI ELQRNPPPNA DPNMKLFTIR GTPQQIDYAR QLIEEKIGGP
460 470 480 490 500
VNPLGPPVPH GPHGVPGPHG PPGPPGPGTP MGPYNPAPYN PGPPGPAPHG
510 520 530 540 550
PPAPYAPQGW GNAYPHWQQQ APPDPAKAGT DPNSAAWAAY YAHYYQQQAQ
560 570 580 590 600
PPPAAPAGAP TTTQTNGQGD QQNPAPAGQV DYTKAWEEYY KKMGQAVPAP
610 620 630 640
TGAPPGGQPD YSAAWAEYYR QQAAYYAQTS PQGMPQHPPA PQGQ
Length:644
Mass (Da):67,560
Last modified:October 17, 2006 - v3
Checksum:i1FD422EA2FC49531
GO
Isoform 2 (identifier: Q96AE4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-97: Missing.
     643-644: GQ → CRFDPASIELAL

Note: No experimental confirmation available.
Show »
Length:653
Mass (Da):68,605
Checksum:i52CB50319085539A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti399 – 3991I → K.
Corresponds to variant rs12748509 [ dbSNP | Ensembl ].
VAR_049679

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei97 – 971Missing in isoform 2. 1 PublicationVSP_021107
Alternative sequencei643 – 6442GQ → CRFDPASIELAL in isoform 2. 1 PublicationVSP_008321

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05040 mRNA. Translation: AAA17976.2.
AC096948 Genomic DNA. No translation available.
BC017247 mRNA. Translation: AAH17247.1.
CCDSiCCDS683.1. [Q96AE4-1]
PIRiA53184.
RefSeqiNP_001290362.1. NM_001303433.1.
NP_003893.2. NM_003902.4. [Q96AE4-1]
UniGeneiHs.567380.
Hs.707742.

Genome annotation databases

EnsembliENST00000294623; ENSP00000294623; ENSG00000162613. [Q96AE4-2]
ENST00000370768; ENSP00000359804; ENSG00000162613. [Q96AE4-1]
GeneIDi8880.
KEGGihsa:8880.
UCSCiuc001dii.4. human. [Q96AE4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05040 mRNA. Translation: AAA17976.2.
AC096948 Genomic DNA. No translation available.
BC017247 mRNA. Translation: AAH17247.1.
CCDSiCCDS683.1. [Q96AE4-1]
PIRiA53184.
RefSeqiNP_001290362.1. NM_001303433.1.
NP_003893.2. NM_003902.4. [Q96AE4-1]
UniGeneiHs.567380.
Hs.707742.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J4WNMR-A278-447[»]
2KXHNMR-B27-52[»]
4LIJX-ray1.80A/B/C86-175[»]
ProteinModelPortaliQ96AE4.
SMRiQ96AE4. Positions 22-52, 98-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114399. 99 interactions.
DIPiDIP-47273N.
IntActiQ96AE4. 33 interactions.
MINTiMINT-1374324.
STRINGi9606.ENSP00000359804.

PTM databases

iPTMnetiQ96AE4.
PhosphoSiteiQ96AE4.
SwissPalmiQ96AE4.

Polymorphism and mutation databases

BioMutaiFUBP1.
DMDMi116241370.

2D gel databases

REPRODUCTION-2DPAGEIPI00375441.

Proteomic databases

EPDiQ96AE4.
MaxQBiQ96AE4.
PaxDbiQ96AE4.
PRIDEiQ96AE4.
TopDownProteomicsiQ96AE4-1. [Q96AE4-1]

Protocols and materials databases

DNASUi8880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294623; ENSP00000294623; ENSG00000162613. [Q96AE4-2]
ENST00000370768; ENSP00000359804; ENSG00000162613. [Q96AE4-1]
GeneIDi8880.
KEGGihsa:8880.
UCSCiuc001dii.4. human. [Q96AE4-1]

Organism-specific databases

CTDi8880.
GeneCardsiFUBP1.
HGNCiHGNC:4004. FUBP1.
HPAiHPA006149.
MIMi603444. gene.
neXtProtiNX_Q96AE4.
PharmGKBiPA28420.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1676. Eukaryota.
ENOG410XZYE. LUCA.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ96AE4.
KOiK13210.
OrthoDBiEOG77Q4WB.
PhylomeDBiQ96AE4.
TreeFamiTF313654.

Miscellaneous databases

ChiTaRSiFUBP1. human.
EvolutionaryTraceiQ96AE4.
GeneWikiiFar_upstream_element-binding_protein_1.
GenomeRNAii8880.
NextBioi33343.
PROiQ96AE4.
SOURCEiSearch...

Gene expression databases

BgeeiQ96AE4.
CleanExiHS_FUBP1.
ExpressionAtlasiQ96AE4. baseline and differential.
GenevisibleiQ96AE4. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif."
    Duncan R., Bazar L., Michelotti G., Tomonaga T., Krutzsch H., Avigan M., Levens D.
    Genes Dev. 8:465-480(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 192-194; 204-207; 273-280; 285-291; 301-315; 322-329; 395-398; 410-412; 431-439 AND 441-444, FUNCTION.
    Tissue: Leukemia.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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] (ISOFORM 2).
    Tissue: Brain.
  4. "Identification of human DNA helicase V with the far upstream element-binding protein."
    Vindigni A., Ochem A., Triolo G., Falaschi A.
    Nucleic Acids Res. 29:1061-1067(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 45-64; 134-146; 272-284; 309-322; 380-387; 415-425 AND 431-440.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 107-118; 134-146; 163-170; 249-256; 272-293 AND 332-344, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  6. "Large-scale proteomic analysis of the human spliceosome."
    Rappsilber J., Ryder U., Lamond A.I., Mann M.
    Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "The FBP interacting repressor targets TFIIH to inhibit activated transcription."
    Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
    Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH PUF60 AND FUSE DNA, INTERACTION WITH PUF60.
  8. "Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation."
    Kim M.J., Park B.-J., Kang Y.-S., Kim H.J., Park J.-H., Kang J.W., Lee S.W., Han J.M., Lee H.-W., Kim S.
    Nat. Genet. 34:330-336(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JTV1, UBIQUITINATION, PROTEASOME-MEDIATED DEGRADATION.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND SER-630, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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 ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-630, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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 THR-153 AND SER-630, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-140 AND SER-630, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Structure and dynamics of KH domains from FBP bound to single-stranded DNA."
    Braddock D.T., Louis J.M., Baber J.L., Levens D., Clore G.M.
    Nature 415:1051-1056(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 278-447 IN COMPLEX WITH SINGLE-STRANDED FUSE DNA.

Entry informationi

Entry nameiFUBP1_HUMAN
AccessioniPrimary (citable) accession number: Q96AE4
Secondary accession number(s): Q12828
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 17, 2006
Last modified: May 11, 2016
This is version 155 of the entry and version 3 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.