P36016

Name	Heat shock protein 70 homolog LHS1 (EC 3.6.1.-)
Uniprot ID	P36016
Systematic gene name	YKL073W
Standard gene name	LHS1
Gene names	LHS1 YKL073W YKL355
Description from SGD	YKL073W LHS1 SGDID:S000001556, Chr XI from 296430-299075, Genome Release 64-3-1, Verified ORF, "Molecular chaperone of the endoplasmic reticulum lumen; involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway"
Protein length	881
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MRNVLRLLFL TAFVAIGSLA AVLGVDYGQQ NIKAIVVSPQ APLELVLTPE
AKRKEISGLS IKRLPGYGKD DPNGIERIYG SAVGSLATRF PQNTLLHLKP
LLGKSLEDET TVTLYSKQHP GLEMVSTNRS TIAFLVDNVE YPLEELVAMN
VQEIANRANS LLKDRDARTE DFVNKMSFTI PDFFDQHQRK ALLDASSITT
GIEETYLVSE GMSVAVNFVL KQRQFPPGEQ QHYIVYDMGS GSIKASMFSI
LQPEDTTQPV TIEFEGYGYN PHLGGAKFTM DIGSLIENKF LETHPAIRTD
ELHANPKALA KINQAAEKAK LILSANSEAS INIESLINDI DFRTSITRQE
FEEFIADSLL DIVKPINDAV TKQFGGYGTN LPEINGVILA GGSSRIPIVQ
DQLIKLVSEE KVLRNVNADE SAVNGVVMRG IKLSNSFKTK PLNVVDRSVN
TYSFKLSNES ELYDVFTRGS AYPNKTSILT NTTDSIPNNF TIDLFENGKL
FETITVNSGA IKNSYSSDKC SSGVAYNITF DLSSDRLFSI QEVNCICQSE
NDIGNSKQIK NKGSRLAFTS EDVEIKRLSP SERSRLHEHI KLLDKQDKER
FQFQENLNVL ESNLYDARNL LMDDEVMQNG PKSQVEELSE MVKVYLDWLE
DASFDTDPED IVSRIREIGI LKKKIELYMD SAKEPLNSQQ FKGMLEEGHK
LLQAIETHKN TVEEFLSQFE TEFADTIDNV REEFKKIKQP AYVSKALSTW
EETLTSFKNS ISEIEKFLAK NLFGEDLREH LFEIKLQFDM YRTKLEEKLR
LIKSGDESRL NEIKKLHLRN FRLQKRKEEK LKRKLEQEKS RNNNETESTV
INSADDKTTI VNDKTTESNP SSEEDILHDE L

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[60, 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)
[60, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[128, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[233, 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)
[233, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[240, 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)
[240, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[458, Glyc]	Poljak, K.,  Selevsek, N.,  Ngwa, E.,  Grossmann, J.,  Losfeld, M.E.,  Aebi, M. (2018). Quantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae. Mol Cell Proteomics 17: 18-30. (Publication) (All modifications)
[458, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[481, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[527, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[844, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[846, 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)
[846, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[871, 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)
[871, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[872, 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)
[872, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)