Basic Information
Name | Myosin-4 (SWI5-dependent HO expression protein 1) |
Uniprot ID | P32492 |
Systematic gene name | YAL029C |
Standard gene name | MYO4 |
Gene names | MYO4 SHE1 YAL029C FUN22 |
Description from SGD | YAL029C MYO4 SGDID:S000000027, Chr I from 92270-87855, Genome Release 64-3-1, reverse complement, Verified ORF, "Type V myosin motor involved in actin-based transport of cargos; required for mRNA transport, including ASH1 mRNA, and facilitating the growth and movement of ER tubules into the growing bud along with She3p; MYO4 has a paralog, MYO2, that arose from the whole genome duplication" |
Protein length | 1471 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSFEVGTKCW YPHKEQGWIG GEVTKNDFFE GTFHLELKLE DGETVSIETN
SFENDDDHPT LPVLRNPPIL ESTDDLTTLS YLNEPAVLHA IKKRYMNGQI
YTYSGIVLIA ANPFDKVDHL YSREMIQNYS SKRKDELEPH LFAIAEEAYR
FMVHEKANQT VVVSGESGAG KTVSAKYIMR YFASVQESNN REGEVEMSQI
ESQILATNPI MEAFGNAKTT RNDNSSRFGK YLQILFDENT TIRGSKIRTY
LLEKSRLVYQ PETERNYHIF YQILEGLPEP VKQELHLSSP KDYHYTNQGG
QPNIAGIDEA REYKITTDAL SLVGINHETQ LGIFKILAGL LHIGNIEMKM
TRNDASLSSE EQNLQIACEL LGIDPFNFAK WIVKKQIVTR SEKIVTNLNY
NQALIARDSV AKFIYSTLFD WLVDNINKTL YDPELDQQDH VFSFIGILDI
YGFEHFEKNS FEQFCINYAN EKLQQEFNQH VFKLEQEEYV KEEIEWSFIE
FSDNQPCIDL IENKLGILSL LDEESRLPSG SDESWASKLY SAFNKPPSNE
VFSKPRFGQT KFIVSHYAVD VEYEVEGFIE KNRDSVSLGH LDVFKATTNP
IFKQILDNRE LRSDDAPEEQ NTEKKIMIPA RLSQKKPTLG SMFKKSLGEL
MAIINSTNVH YIRCIKPNSE KKPWEFDNLM VLSQLRACGV LETIRISCAG
FPSRWTFDEF VQRYFLLTDY SLWSGILYNP DLPKEAIVNF CQSILDATIS
DSAKYQIGNT KIFFKAGMLA FLEKLRTNKM NEICIIIQKK IRARYYRLQY
LQTMESIKKC QSQIRSLLVR TRVDHELKTR AAILLQTNIR ALWKREYYRA
AIGQIIKLQC TCKRKLILDS VNRKFMLMAA VIIQSYIRSY GHKTDYRTLK
RSSILVQSAM RMQLARRRYI VLQKEVEERN IRASYGIGLL EEAIEFKNSF
ILNLEMLNDS YTRLTQLLQG DLSNIPSKQR QEYETIVNGY NDKISKLKTL
QVEIMNTLNK KNALKERKKK QSSLIQSHMQ SLAAIKGNKP SRLSDEVKSM
KQELAFIENV IAQDFTTTYS ANKNDKVKGL GIAGQQVKPK LVNVIRRESG
NPDLLELLMD LNCYTLEVTE GYLKKVNVTE VNGDNVLGPI HVITTVVSSL
VRNGLLIQSS KFISKVLLTV ESIVMSLPKD ETMLGGIFWL SNLSRLPAFA
ANQKTLYEAN GGDEKDKLTL IYLNDLENET LKVFDKIYST WLVKFMKHAS
AHIEIFDMVL NEKLFKNSGD EKFAKLFTFL NEFDAVLCKF QVVDSMHTKI
FNDTLKYLNV MLFNDLITKC PALNWKYGYE VDRNIERLVS WFEPRIEDVR
PNLIQIIQAV KILQLKISNL NEFKLLFDFW YALNPAQIQA ILLKYKPANK
GEAGVPNEIL NYLANVIKRE NLSLPGKMEI MLSAQFDSAK NHLRYDTSAI
TQNSNTEGLA TVSKIIKLDR K
SFENDDDHPT LPVLRNPPIL ESTDDLTTLS YLNEPAVLHA IKKRYMNGQI
YTYSGIVLIA ANPFDKVDHL YSREMIQNYS SKRKDELEPH LFAIAEEAYR
FMVHEKANQT VVVSGESGAG KTVSAKYIMR YFASVQESNN REGEVEMSQI
ESQILATNPI MEAFGNAKTT RNDNSSRFGK YLQILFDENT TIRGSKIRTY
LLEKSRLVYQ PETERNYHIF YQILEGLPEP VKQELHLSSP KDYHYTNQGG
QPNIAGIDEA REYKITTDAL SLVGINHETQ LGIFKILAGL LHIGNIEMKM
TRNDASLSSE EQNLQIACEL LGIDPFNFAK WIVKKQIVTR SEKIVTNLNY
NQALIARDSV AKFIYSTLFD WLVDNINKTL YDPELDQQDH VFSFIGILDI
YGFEHFEKNS FEQFCINYAN EKLQQEFNQH VFKLEQEEYV KEEIEWSFIE
FSDNQPCIDL IENKLGILSL LDEESRLPSG SDESWASKLY SAFNKPPSNE
VFSKPRFGQT KFIVSHYAVD VEYEVEGFIE KNRDSVSLGH LDVFKATTNP
IFKQILDNRE LRSDDAPEEQ NTEKKIMIPA RLSQKKPTLG SMFKKSLGEL
MAIINSTNVH YIRCIKPNSE KKPWEFDNLM VLSQLRACGV LETIRISCAG
FPSRWTFDEF VQRYFLLTDY SLWSGILYNP DLPKEAIVNF CQSILDATIS
DSAKYQIGNT KIFFKAGMLA FLEKLRTNKM NEICIIIQKK IRARYYRLQY
LQTMESIKKC QSQIRSLLVR TRVDHELKTR AAILLQTNIR ALWKREYYRA
AIGQIIKLQC TCKRKLILDS VNRKFMLMAA VIIQSYIRSY GHKTDYRTLK
RSSILVQSAM RMQLARRRYI VLQKEVEERN IRASYGIGLL EEAIEFKNSF
ILNLEMLNDS YTRLTQLLQG DLSNIPSKQR QEYETIVNGY NDKISKLKTL
QVEIMNTLNK KNALKERKKK QSSLIQSHMQ SLAAIKGNKP SRLSDEVKSM
KQELAFIENV IAQDFTTTYS ANKNDKVKGL GIAGQQVKPK LVNVIRRESG
NPDLLELLMD LNCYTLEVTE GYLKKVNVTE VNGDNVLGPI HVITTVVSSL
VRNGLLIQSS KFISKVLLTV ESIVMSLPKD ETMLGGIFWL SNLSRLPAFA
ANQKTLYEAN GGDEKDKLTL IYLNDLENET LKVFDKIYST WLVKFMKHAS
AHIEIFDMVL NEKLFKNSGD EKFAKLFTFL NEFDAVLCKF QVVDSMHTKI
FNDTLKYLNV MLFNDLITKC PALNWKYGYE VDRNIERLVS WFEPRIEDVR
PNLIQIIQAV KILQLKISNL NEFKLLFDFW YALNPAQIQA ILLKYKPANK
GEAGVPNEIL NYLANVIKRE NLSLPGKMEI MLSAQFDSAK NHLRYDTSAI
TQNSNTEGLA TVSKIIKLDR K
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
[585, 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) |
[585, 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) |
[585, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[587, 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) |
[934, 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) |
[965, 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) |
[965, 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) |
[965, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1041, 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) |
[1041, 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) |
[1041, 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) |
[1041, 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) |
[1041, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1044, 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) |
[1044, 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) |
[1044, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |