Basic Information

NameNucleolar complex protein 14 (U three protein 2) (U3 small nucleolar RNA-associated protein 2) (U3 snoRNA-associated protein 2)
Uniprot IDQ99207
Systematic gene nameYDL148C
Standard gene nameNOP14
Gene namesNOP14 UTP2 YDL148C D1566
Description from SGDYDL148C NOP14 SGDID:S000002307, Chr IV from 190586-188154, Genome Release 64-3-1, reverse complement, Verified ORF, "Nucleolar protein; forms a complex with Noc4p that mediates maturation and nuclear export of 40S ribosomal subunits; also present in the small subunit processome complex, which is required for processing of pre-18S rRNA"
Protein length810
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MAGSQLKNLK AALKARGLTG QTNVKSKNKK NSKRQAKEYD REEKKKAIAE
IREEFNPFEI KAARNKRRDG LPSKTADRIA VGKPGISKQI GEEQRKRAFE
ARKMMKNKRG GVIDKRFGER DKLLTEEEKM LERFTRERQS QSKRNANLFN
LEDDEDDGDM FGDGLTHLGQ SLSLEDELAN DEEDFLASKR FNEDDAELQQ
PQRKKTKAEV MKEVIAKSKF YKQERQKAQG IMEDQIDNLD DNFEDVMSEL
MMTQPKKNPM EPKTDLDKEY DIKVKELQLD KRAAPSDRTK TEEEKNAEAE
EKKRELEQQR LDRMNGMIEL EEGEERGVED LDDGFWENEE DYEDDNDGIA
DSDDDIKFED QGRDEGFSQI LKKKNISISC PRTHDALLDQ VKKLDLDDHP
KIVKNIIKAY QPKLAEGNKE KLGKFTAVLL RHIIFLSNQN YLKNVQSFKR
TQNALISILK SLSEKYNREL SEECRDYINE MQARYKKNHF DALSNGDLVF
FSIIGILFST SDQYHLVITP ALILMSQFLE QIKFNSLKRI AFGAVLVRIV
SQYQRISKRY IPEVVYFFQK ILLTFIVEKE NQEKPLDFEN IRLDSYELGL
PLDVDFTKKR STIIPLHTLS TMDTEAHPVD QCVSVLLNVM ESLDATISTV
WKSLPAFNEI ILPIQQLLSA YTSKYSDFEK PRNILNKVEK LTKFTEHIPL
ALQNHKPVSI PTHAPKYEEN FNPDKKSYDP DRTRSEINKM KAQLKKERKF
TMKEIRKDAK FEARQRIEEK NKESSDYHAK MAHIVNTINT EEGAEKNKYE
RERKLRGGKK

Legend

  • X K-acetylation
  • X Phoshorylation
  • X Ubiquitination

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[88, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[352, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[352, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[352, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[352, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[352, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[368, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[368, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[463, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[680, Ubi]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[693, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[716, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[774, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[774, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[775, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[775, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)