Basic Information
Name | Nuclear envelope morphology protein 1 (EC 3.1.3.16) |
Uniprot ID | P38757 |
Systematic gene name | YHR004C |
Standard gene name | NEM1 |
Gene names | NEM1 YHR004C |
Description from SGD | YHR004C NEM1 SGDID:S000001046, Chr VIII from 113094-111754, Genome Release 64-3-1, reverse complement, Verified ORF, "Probable catalytic subunit of Nem1p-Spo7p phosphatase holoenzyme; regulates nuclear growth by controlling phospholipid biosynthesis, required for normal nuclear envelope morphology and sporulation; homolog of the human protein Dullard" |
Protein length | 446 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNALKYFSNH LITTKKQKKI NVEVTKNQDL LGPSKEVSNK YTSHSENDCV
SEVDQQYDHS SSHLKESDQN QERKNSVPKK PKALRSILIE KIASILWALL
LFLPYYLIIK PLMSLWFVFT FPLSVIERRV KHTDKRNRGS NASENELPVS
SSNINDSSEK TNPKNCNLNT IPEAVEDDLN ASDEIILQRD NVKGSLLRAQ
SVKSRPRSYS KSELSLSNHS SSNTVFGTKR MGRFLFPKKL IPKSVLNTQK
KKKLVIDLDE TLIHSASRST THSNSSQGHL VEVKFGLSGI RTLYFIHKRP
YCDLFLTKVS KWYDLIIFTA SMKEYADPVI DWLESSFPSS FSKRYYRSDC
VLRDGVGYIK DLSIVKDSEE NGKGSSSSLD DVIIIDNSPV SYAMNVDNAI
QVEGWISDPT DTDLLNLLPF LEAMRYSTDV RNILALKHGE KAFNIN
SEVDQQYDHS SSHLKESDQN QERKNSVPKK PKALRSILIE KIASILWALL
LFLPYYLIIK PLMSLWFVFT FPLSVIERRV KHTDKRNRGS NASENELPVS
SSNINDSSEK TNPKNCNLNT IPEAVEDDLN ASDEIILQRD NVKGSLLRAQ
SVKSRPRSYS KSELSLSNHS SSNTVFGTKR MGRFLFPKKL IPKSVLNTQK
KKKLVIDLDE TLIHSASRST THSNSSQGHL VEVKFGLSGI RTLYFIHKRP
YCDLFLTKVS KWYDLIIFTA SMKEYADPVI DWLESSFPSS FSKRYYRSDC
VLRDGVGYIK DLSIVKDSEE NGKGSSSSLD DVIIIDNSPV SYAMNVDNAI
QVEGWISDPT DTDLLNLLPF LEAMRYSTDV RNILALKHGE KAFNIN
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[140, 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) |
[140, Phos] | Su, W.M., Han, G.S., Dey, P., Carman, G.M. (2018). Protein kinase A phosphorylates the Nem1-Spo7 protein phosphatase complex that regulates the phosphorylation state of the phosphatidate phosphatase Pah1 in yeast. J Biol Chem 293: 15801-15814. (Publication) (All modifications) |
[195, Phos] | Dubots, E., Cottier, S., Péli-Gulli, M.P., Jaquenoud, M., Bontron, S., Schneiter, R., De Virgilio, C. (2014). TORC1 regulates Pah1 phosphatidate phosphatase activity via the Nem1/Spo7 protein phosphatase complex. PLoS One 9: e104194. (Publication) (All modifications) |
[201, Phos] | Dey, P., Su, W.M., Mirheydari, M., Han, G.S., Carman, G.M. (2019). Protein kinase C mediates the phosphorylation of the Nem1-Spo7 protein phosphatase complex in yeast. J Biol Chem 294: 15997-16009. (Publication) (All modifications) |
[210, 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) |
[210, 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) |
[210, Phos] | Su, W.M., Han, G.S., Dey, P., Carman, G.M. (2018). Protein kinase A phosphorylates the Nem1-Spo7 protein phosphatase complex that regulates the phosphorylation state of the phosphatidate phosphatase Pah1 in yeast. J Biol Chem 293: 15801-15814. (Publication) (All modifications) |
[210, Phos] | Dubots, E., Cottier, S., Péli-Gulli, M.P., Jaquenoud, M., Bontron, S., Schneiter, R., De Virgilio, C. (2014). TORC1 regulates Pah1 phosphatidate phosphatase activity via the Nem1/Spo7 protein phosphatase complex. PLoS One 9: e104194. (Publication) (All modifications) |
[210, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[215, 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) |
[215, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[217, 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) |
[217, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[261, 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) |
[261, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[288, 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) |