Basic Information
Name | Endoplasmic reticulum membrane protein 65 (65 kDa endoplasmic reticulum membrane protein) |
Uniprot ID | P40085 |
Systematic gene name | YER140W |
Standard gene name | EMP65 |
Gene names | EMP65 YER140W |
Description from SGD | YER140W EMP65 SGDID:S000000942, Chr V from 451565-453235, Genome Release 64-3-1, Verified ORF, "Integral membrane protein of the ER; forms an ER-membrane associated protein complex with Slp1p; identified along with SLP1 in a screen for mutants defective in the unfolded protein response (UPR); proposed to function in the folding of integral membrane proteins; interacts genetically with MPS3; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies" |
Protein length | 556 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MQHKDTAVAK DTAKKRLLRR NSAPSAIHII SRLDKKWSFL WNTIDRHNIV
EEQDESSAAK SEEEHEDDYE LEQLLNMIRI PMFLEKFMLF ALLTSLDCFL
YYFTVLPIRL IKGYVKQFKS YRQHYRLQQR SGHKNKIPFR YRITSREYKE
RCMIFIIVIS SILLSKLDTS KLYHRIKRQS TMKLYMLFSV LEMADKMLAS
LGQSLLTVML SRKNSERILL HKCLLVSMSL TYVTIHGYVL VYQAISLNIA
VNSYSNALLT LLLSMQFAEI KSSVLKKFDK EGFFQITIAD VVERFKLTLL
LSITGLRNLQ SWSSSLSNTS INFWSPRSTL SIVINILCGP MVSVVGSEVL
VDWAKHAYIT KFNRIRPQIY DKFYYIIYKD YSTRTHKLED RLGLPLPAFV
VLFIVMVRPT LFKSSEPSYL PSLFRILFMG ASVFLLALLA KFTLDLILIK
WSKRIEQRFR DQAFNTVVTE EEYVPGLLSG GMGKVDVSTR IALHSDYNKE
NRIETESVSP MRKRKTTLTA ECTPPSLNDI RRQKDSKNPR SLENVARYKM
VSKRIW
EEQDESSAAK SEEEHEDDYE LEQLLNMIRI PMFLEKFMLF ALLTSLDCFL
YYFTVLPIRL IKGYVKQFKS YRQHYRLQQR SGHKNKIPFR YRITSREYKE
RCMIFIIVIS SILLSKLDTS KLYHRIKRQS TMKLYMLFSV LEMADKMLAS
LGQSLLTVML SRKNSERILL HKCLLVSMSL TYVTIHGYVL VYQAISLNIA
VNSYSNALLT LLLSMQFAEI KSSVLKKFDK EGFFQITIAD VVERFKLTLL
LSITGLRNLQ SWSSSLSNTS INFWSPRSTL SIVINILCGP MVSVVGSEVL
VDWAKHAYIT KFNRIRPQIY DKFYYIIYKD YSTRTHKLED RLGLPLPAFV
VLFIVMVRPT LFKSSEPSYL PSLFRILFMG ASVFLLALLA KFTLDLILIK
WSKRIEQRFR DQAFNTVVTE EEYVPGLLSG GMGKVDVSTR IALHSDYNKE
NRIETESVSP MRKRKTTLTA ECTPPSLNDI RRQKDSKNPR SLENVARYKM
VSKRIW
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
[22, 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) |
[22, 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) |
[22, 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) |
[22, 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) |
[22, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[22, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[22, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[22, Phos] | 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) |
[22, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[180, 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) |
[180, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[181, 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) |
[181, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[189, 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) |
[189, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[495, 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) |
[509, 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) |