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Protein

Far upstream element-binding protein 3

Gene

FUBP3

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

Functioni

May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression.

GO - Molecular functioni

GO - Biological processi

  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • transcription, DNA-templated Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Far upstream element-binding protein 3
Short name:
FUSE-binding protein 3
Gene namesi
Name:FUBP3
Synonyms:FBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:4005. FUBP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28421.

Polymorphism and mutation databases

BioMutaiFUBP3.
DMDMi37078499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 572571Far upstream element-binding protein 3PRO_0000050140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei76 – 761PhosphothreonineCombined sources
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei539 – 5391PhosphoserineCombined sources
Modified residuei569 – 5691PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96I24.
MaxQBiQ96I24.
PaxDbiQ96I24.
PRIDEiQ96I24.

2D gel databases

REPRODUCTION-2DPAGEIPI00377261.

PTM databases

iPTMnetiQ96I24.
PhosphoSiteiQ96I24.
SwissPalmiQ96I24.

Expressioni

Tissue specificityi

Detected in a number of cell lines.

Gene expression databases

BgeeiQ96I24.
CleanExiHS_FUBP3.
ExpressionAtlasiQ96I24. baseline and differential.
GenevisibleiQ96I24. HS.

Organism-specific databases

HPAiHPA047658.
HPA058392.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
QKIQ96PU84EBI-954200,EBI-945792

Protein-protein interaction databases

BioGridi114451. 54 interactions.
DIPiDIP-50124N.
IntActiQ96I24. 27 interactions.
MINTiMINT-4095364.
STRINGi9606.ENSP00000318177.

Structurei

3D structure databases

ProteinModelPortaliQ96I24.
SMRiQ96I24. Positions 74-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 14165KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 22867KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini253 – 31765KH 3PROSITE-ProRule annotationAdd
BLAST
Domaini354 – 42168KH 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1676. Eukaryota.
ENOG410XZYE. LUCA.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ96I24.
KOiK13210.
OMAiATPHQNT.
OrthoDBiEOG77Q4WB.
PhylomeDBiQ96I24.
TreeFamiTF313654.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF00013. 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: Q96I24-1) [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
MAELVQGQSA PVGMKAEGFV DALHRVRQIA AKIDSIPHLN NSTPLVDPSV
60 70 80 90 100
YGYGVQKRPL DDGVGNQLGA LVHQRTVITE EFKVPDKMVG FIIGRGGEQI
110 120 130 140 150
SRIQAESGCK IQIASESSGI PERPCVLTGT PESIEQAKRL LGQIVDRCRN
160 170 180 190 200
GPGFHNDIDS NSTIQEILIP ASKVGLVIGR GGETIKQLQE RTGVKMVMIQ
210 220 230 240 250
DGPLPTGADK PLRITGDAFK VQQAREMVLE IIREKDQADF RGVRGDFNSR
260 270 280 290 300
MGGGSIEVSV PRFAVGIVIG RNGEMIKKIQ NDAGVRIQFK PDDGISPERA
310 320 330 340 350
AQVMGPPDRC QHAAHIISEL ILTAQERDGF GGLAAARGRG RGRGDWSVGA
360 370 380 390 400
PGGVQEITYT VPADKCGLVI GKGGENIKSI NQQSGAHVEL QRNPPPNSDP
410 420 430 440 450
NLRRFTIRGV PQQIEVARQL IDEKVGGTNL GAPGAFGQSP FSQPPAPPHQ
460 470 480 490 500
NTFPPRSSGC FPNMAAKVNG NPHSTPVSGP PAFLTQGWGS TYQAWQQPTQ
510 520 530 540 550
QVPSQQSQPQ SSQPNYSKAW EDYYKKQSHA ASAAPQASSP PDYTMAWAEY
560 570
YRQQVAFYGQ TLGQAQAHSQ EQ
Length:572
Mass (Da):61,640
Last modified:September 26, 2003 - v2
Checksum:iF1BE223542BC197D
GO
Isoform 2 (identifier: Q96I24-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: MAELVQGQSAPVGMKAEGFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGV → MPPI
     298-548: Missing.

Note: No experimental confirmation available.
Show »
Length:261
Mass (Da):28,492
Checksum:i6D70D9731D957E6D
GO

Sequence cautioni

The sequence AAC50893.1 differs from that shown. Reason: Frameshift at position 18. Curated
The sequence AAH01325.1 differs from that shown. Reason: Frameshift at position 527. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721V → D in AAC50893 (PubMed:8940189).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6464MAELV…LDDGV → MPPI in isoform 2. 1 PublicationVSP_008323Add
BLAST
Alternative sequencei298 – 548251Missing in isoform 2. 1 PublicationVSP_008324Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69127 mRNA. Translation: AAC50893.1. Frameshift.
AK295155 mRNA. Translation: BAG58170.1.
AL353695, AL359092 Genomic DNA. Translation: CAH70960.1.
AL353695, AL359092 Genomic DNA. Translation: CAH70961.1.
AL359092, AL353695 Genomic DNA. Translation: CAM45743.1.
AL359092, AL353695 Genomic DNA. Translation: CAM45745.1.
CH471090 Genomic DNA. Translation: EAW87937.1.
BC001325 mRNA. Translation: AAH01325.1. Frameshift.
BC007874 mRNA. Translation: AAH07874.1.
BC137338 mRNA. Translation: AAI37339.1.
BC137340 mRNA. Translation: AAI37341.1.
CCDSiCCDS43893.1. [Q96I24-1]
RefSeqiNP_003925.1. NM_003934.1. [Q96I24-1]
UniGeneiHs.673029.
Hs.740088.
Hs.98751.

Genome annotation databases

EnsembliENST00000319725; ENSP00000318177; ENSG00000107164. [Q96I24-1]
GeneIDi8939.
KEGGihsa:8939.
UCSCiuc004bzr.2. human. [Q96I24-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69127 mRNA. Translation: AAC50893.1. Frameshift.
AK295155 mRNA. Translation: BAG58170.1.
AL353695, AL359092 Genomic DNA. Translation: CAH70960.1.
AL353695, AL359092 Genomic DNA. Translation: CAH70961.1.
AL359092, AL353695 Genomic DNA. Translation: CAM45743.1.
AL359092, AL353695 Genomic DNA. Translation: CAM45745.1.
CH471090 Genomic DNA. Translation: EAW87937.1.
BC001325 mRNA. Translation: AAH01325.1. Frameshift.
BC007874 mRNA. Translation: AAH07874.1.
BC137338 mRNA. Translation: AAI37339.1.
BC137340 mRNA. Translation: AAI37341.1.
CCDSiCCDS43893.1. [Q96I24-1]
RefSeqiNP_003925.1. NM_003934.1. [Q96I24-1]
UniGeneiHs.673029.
Hs.740088.
Hs.98751.

3D structure databases

ProteinModelPortaliQ96I24.
SMRiQ96I24. Positions 74-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114451. 54 interactions.
DIPiDIP-50124N.
IntActiQ96I24. 27 interactions.
MINTiMINT-4095364.
STRINGi9606.ENSP00000318177.

PTM databases

iPTMnetiQ96I24.
PhosphoSiteiQ96I24.
SwissPalmiQ96I24.

Polymorphism and mutation databases

BioMutaiFUBP3.
DMDMi37078499.

2D gel databases

REPRODUCTION-2DPAGEIPI00377261.

Proteomic databases

EPDiQ96I24.
MaxQBiQ96I24.
PaxDbiQ96I24.
PRIDEiQ96I24.

Protocols and materials databases

DNASUi8939.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319725; ENSP00000318177; ENSG00000107164. [Q96I24-1]
GeneIDi8939.
KEGGihsa:8939.
UCSCiuc004bzr.2. human. [Q96I24-1]

Organism-specific databases

CTDi8939.
GeneCardsiFUBP3.
HGNCiHGNC:4005. FUBP3.
HPAiHPA047658.
HPA058392.
MIMi603536. gene.
neXtProtiNX_Q96I24.
PharmGKBiPA28421.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1676. Eukaryota.
ENOG410XZYE. LUCA.
GeneTreeiENSGT00730000110664.
HOGENOMiHOG000231552.
HOVERGENiHBG000625.
InParanoidiQ96I24.
KOiK13210.
OMAiATPHQNT.
OrthoDBiEOG77Q4WB.
PhylomeDBiQ96I24.
TreeFamiTF313654.

Miscellaneous databases

ChiTaRSiFUBP3. human.
GenomeRNAii8939.
NextBioi33614.
PROiQ96I24.
SOURCEiSearch...

Gene expression databases

BgeeiQ96I24.
CleanExiHS_FUBP3.
ExpressionAtlasiQ96I24. baseline and differential.
GenevisibleiQ96I24. HS.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF00013. 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. "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] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Cervix and Placenta.
  6. Cited for: PROTEIN SEQUENCE OF 2-15; 88-95; 226-233; 251-271; 287-299; 328-337; 393-403 AND 409-418, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma and Ovarian carcinoma.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 226-233 AND 263-271, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-76; SER-296; SER-539 AND SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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 ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFUBP3_HUMAN
AccessioniPrimary (citable) accession number: Q96I24
Secondary accession number(s): A3KFK8
, A3KFL0, Q92946, Q9BVB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: May 11, 2016
This is version 145 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.