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Q8IY81

- SPB1_HUMAN

UniProt

Q8IY81 - SPB1_HUMAN

Protein

pre-rRNA processing protein FTSJ3

Gene

FTSJ3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation.1 PublicationUniRule annotation

    Catalytic activityi

    S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing 2'-O-methylnucleoside.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei58 – 581S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei76 – 761S-adenosyl-L-methionineUniRule annotation
    Binding sitei92 – 921S-adenosyl-L-methionineUniRule annotation
    Binding sitei117 – 1171S-adenosyl-L-methionineUniRule annotation
    Active sitei157 – 1571Proton acceptorUniRule annotation

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. rRNA methyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. enzyme-directed rRNA 2'-O-methylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    pre-rRNA processing protein FTSJ3UniRule annotation (EC:2.1.1.-UniRule annotation)
    Alternative name(s):
    2'-O-ribose RNA methyltransferase SPB1 homologUniRule annotation
    Protein ftsJ homolog 3UniRule annotation
    Putative rRNA methyltransferase 3UniRule annotation
    Gene namesi
    Name:FTSJ3UniRule annotation
    ORF Names:SB92
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17136. FTSJ3.

    Subcellular locationi

    Nucleusnucleolus 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleus Source: HPA
    3. preribosome, small subunit precursor Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28419.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 847847pre-rRNA processing protein FTSJ3PRO_0000155577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei333 – 3331Phosphoserine3 Publications
    Modified residuei335 – 3351Phosphoserine3 Publications
    Modified residuei336 – 3361Phosphoserine4 Publications
    Modified residuei347 – 3471Phosphoserine1 Publication
    Modified residuei356 – 3561Phosphoserine1 Publication
    Modified residuei371 – 3711Phosphothreonine1 Publication
    Modified residuei392 – 3921CitrullineBy similarity
    Modified residuei549 – 5491Phosphoserine1 Publication
    Modified residuei584 – 5841Phosphoserine3 Publications
    Modified residuei644 – 6441Phosphoserine3 Publications
    Modified residuei676 – 6761Phosphoserine1 Publication
    Modified residuei688 – 6881Phosphoserine1 Publication
    Modified residuei783 – 7831CitrullineBy similarity

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ8IY81.
    PaxDbiQ8IY81.
    PRIDEiQ8IY81.

    2D gel databases

    SWISS-2DPAGEQ8IY81.

    PTM databases

    PhosphoSiteiQ8IY81.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IY81.
    BgeeiQ8IY81.
    CleanExiHS_FTSJ3.
    GenevestigatoriQ8IY81.

    Organism-specific databases

    HPAiHPA055544.

    Interactioni

    Subunit structurei

    Interacts with NIP7.1 PublicationUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF2AK2P195252EBI-744088,EBI-640775
    OAS3Q9Y6K52EBI-744088,EBI-6115729

    Protein-protein interaction databases

    BioGridi125581. 55 interactions.
    IntActiQ8IY81. 12 interactions.
    MINTiMINT-1468947.
    STRINGi9606.ENSP00000337518.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IY81.
    SMRiQ8IY81. Positions 23-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili355 – 40753UniRule annotationAdd
    BLAST
    Coiled coili739 – 77739UniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the methyltransferase superfamily. RlmE family. SPB1 subfamily.UniRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0293.
    HOVERGENiHBG075246.
    InParanoidiQ8IY81.
    KOiK14857.
    OMAiDLPEWFV.
    OrthoDBiEOG7WX07S.
    PhylomeDBiQ8IY81.
    TreeFamiTF106102.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_01547. RNA_methyltr_E.
    MF_03163. RNA_methyltr_E_SPB1.
    InterProiIPR015507. rRNA-MeTfrase_E.
    IPR012920. rRNA_MeTfrase_Spb1_C.
    IPR024576. rRNA_MeTfrase_Spb1_DUF3381.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR028589. Spb1.
    [Graphical view]
    PANTHERiPTHR10920. PTHR10920. 1 hit.
    PTHR10920:SF13. PTHR10920:SF13. 1 hit.
    PfamiPF11861. DUF3381. 1 hit.
    PF01728. FtsJ. 1 hit.
    PF07780. Spb1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8IY81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD    50
    LCAAPGGWLQ VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ 100
    ALRKELKTWK VDVVLNDGAP NVGASWVHDA YSQAHLTLMA LRLACDFLAR 150
    GGSFITKVFR SRDYQPLLWI FQQLFRRVQA TKPQASRHES AEIFVVCQGF 200
    LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG YAEGDLTLYH 250
    RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL 300
    GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG 350
    TTKQPSKEEE EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER 400
    VELKMDLPGV SIADEGETGM FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL 450
    PRDDIYVSDV EDDGDDTSLD SDLDPEELAG VRGHQGLRDQ KRMRLTEVQD 500
    DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED DADEALEISQ 550
    AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG 600
    TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE 650
    IVPIEDPAKH RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE 700
    LPEWFVQEEK QHRIRQLPVG KKEVEHYRKR WREINARPIK KVAEAKARKK 750
    RRMLKRLEQT RKKAEAVVNT VDISEREKVA QLRSLYKKAG LGKEKRHVTY 800
    VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ KKKHKRK 847
    Length:847
    Mass (Da):96,558
    Last modified:May 18, 2010 - v2
    Checksum:i06B2F4D28A48026F
    GO

    Sequence cautioni

    The sequence BAA90924.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti278 – 2781E → I in AAL56015. 1 PublicationCurated
    Sequence conflicti278 – 2781E → I in BAA90924. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911Q → E.3 Publications
    Corresponds to variant rs2584625 [ dbSNP | Ensembl ].
    VAR_023284
    Natural varianti424 – 4241S → C.4 Publications
    Corresponds to variant rs2727288 [ dbSNP | Ensembl ].
    VAR_023285

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF327355 mRNA. Translation: AAL56015.1.
    AK000069 mRNA. Translation: BAA90924.1. Different initiation.
    AK315010 mRNA. Translation: BAG37502.1.
    AC015651 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94273.1.
    CH471109 Genomic DNA. Translation: EAW94274.1.
    CH471109 Genomic DNA. Translation: EAW94275.1.
    BC000131 mRNA. Translation: AAH00131.2.
    BC036710 mRNA. Translation: AAH36710.1.
    AL834482 mRNA. Translation: CAD39141.1.
    CCDSiCCDS11644.1.
    RefSeqiNP_060117.3. NM_017647.3.
    UniGeneiHs.463785.

    Genome annotation databases

    EnsembliENST00000427159; ENSP00000396673; ENSG00000108592.
    GeneIDi117246.
    KEGGihsa:117246.
    UCSCiuc002jbz.3. human.

    Polymorphism databases

    DMDMi296452883.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF327355 mRNA. Translation: AAL56015.1 .
    AK000069 mRNA. Translation: BAA90924.1 . Different initiation.
    AK315010 mRNA. Translation: BAG37502.1 .
    AC015651 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94273.1 .
    CH471109 Genomic DNA. Translation: EAW94274.1 .
    CH471109 Genomic DNA. Translation: EAW94275.1 .
    BC000131 mRNA. Translation: AAH00131.2 .
    BC036710 mRNA. Translation: AAH36710.1 .
    AL834482 mRNA. Translation: CAD39141.1 .
    CCDSi CCDS11644.1.
    RefSeqi NP_060117.3. NM_017647.3.
    UniGenei Hs.463785.

    3D structure databases

    ProteinModelPortali Q8IY81.
    SMRi Q8IY81. Positions 23-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125581. 55 interactions.
    IntActi Q8IY81. 12 interactions.
    MINTi MINT-1468947.
    STRINGi 9606.ENSP00000337518.

    PTM databases

    PhosphoSitei Q8IY81.

    Polymorphism databases

    DMDMi 296452883.

    2D gel databases

    SWISS-2DPAGE Q8IY81.

    Proteomic databases

    MaxQBi Q8IY81.
    PaxDbi Q8IY81.
    PRIDEi Q8IY81.

    Protocols and materials databases

    DNASUi 117246.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000427159 ; ENSP00000396673 ; ENSG00000108592 .
    GeneIDi 117246.
    KEGGi hsa:117246.
    UCSCi uc002jbz.3. human.

    Organism-specific databases

    CTDi 117246.
    GeneCardsi GC17M061896.
    HGNCi HGNC:17136. FTSJ3.
    HPAi HPA055544.
    neXtProti NX_Q8IY81.
    PharmGKBi PA28419.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0293.
    HOVERGENi HBG075246.
    InParanoidi Q8IY81.
    KOi K14857.
    OMAi DLPEWFV.
    OrthoDBi EOG7WX07S.
    PhylomeDBi Q8IY81.
    TreeFami TF106102.

    Miscellaneous databases

    ChiTaRSi FTSJ3. human.
    GeneWikii FTSJ3.
    GenomeRNAii 117246.
    NextBioi 80174.
    PROi Q8IY81.

    Gene expression databases

    ArrayExpressi Q8IY81.
    Bgeei Q8IY81.
    CleanExi HS_FTSJ3.
    Genevestigatori Q8IY81.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    HAMAPi MF_01547. RNA_methyltr_E.
    MF_03163. RNA_methyltr_E_SPB1.
    InterProi IPR015507. rRNA-MeTfrase_E.
    IPR012920. rRNA_MeTfrase_Spb1_C.
    IPR024576. rRNA_MeTfrase_Spb1_DUF3381.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR028589. Spb1.
    [Graphical view ]
    PANTHERi PTHR10920. PTHR10920. 1 hit.
    PTHR10920:SF13. PTHR10920:SF13. 1 hit.
    Pfami PF11861. DUF3381. 1 hit.
    PF01728. FtsJ. 1 hit.
    PF07780. Spb1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Zhang W., Li N., Wan T., Chen T., Cao T.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-91 AND CYS-424.
    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], VARIANTS GLU-91 AND CYS-424.
      Tissue: Colon and Placenta.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [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], VARIANTS GLU-91 AND CYS-424.
      Tissue: Placenta and Skin.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-847, VARIANT CYS-424.
      Tissue: Melanoma.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "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.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: 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-333; SER-335; SER-336; SER-356; THR-371; SER-549; SER-584 AND SER-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 SER-336; SER-584; SER-644; SER-676 AND SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The human nucleolar protein FTSJ3 associates with NIP7 and functions in pre-rRNA processing."
      Morello L.G., Coltri P.P., Quaresma A.J., Simabuco F.M., Silva T.C., Singh G., Nickerson J.A., Oliveira C.C., Moore M.J., Zanchin N.I.
      PLoS ONE 6:E29174-E29174(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NIP7, SUBCELLULAR LOCATION.
    18. "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-333; SER-335; SER-336; SER-584 AND SER-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSPB1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IY81
    Secondary accession number(s): B2RCA5
    , D3DU22, Q8N3A3, Q8WXX1, Q9BWM4, Q9NXT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 114 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3