HMG2/YLR450W Protein Information

Standard Name	Hmg2p
Systematic Name	Ylr450wp
ORF Classification	Verified
Description	HMG-CoA reductase; converts HMG-CoA to mevalonate, a rate-limiting step in sterol biosynthesis; one of two isozymes; overproduction induces assembly of peripheral ER membrane arrays and short nuclear-associated membrane stacks; forms foci at the nuclear periphery upon DNA replication stress; HMG2 has a paralog, HMG1, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6)
Name Description	3-Hydroxy-3-MethylGlutaryl-coenzyme a reductase 2

Experimental Data
Molecules/cell	149 7

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,045
Molecular Weight (Da)	115,691
Isoelectric Point (pI)	7.52

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Hmg2p (InterPro)
Transmembrane Domains	There are 7 total predicted transmembrane domains (TMHMM)
Signal Peptide(s)	There are 1 total predicted predicted signal peptide(s) (SignalP)
Physical Interactions	There are 29 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012C9D2 \| P12684 MIPS: YLR450W NCBI: 123338 \| 171688 \| 51013051 \| 6323483 \| 717061 \| NP_013555.1 \| NM_001182338.1 GenBank/EMBL/DDBJ: DAA09750.1 \| AY692800 \| M22255 \| U22382
External Classifications	EC: 1.1.1.34 [Hydroxymethylglutaryl-CoA reductase (NADPH)] TC: 2.A.6.6 [The Eukaryotic (Putative) Sterol Transporter (EST) Family]

Amino Acid Sequence (or in FASTA format)
1 MSLPLKTIVH LVKPFACTAR FSARYPIHVI VVAVLLSAAA YLSVTQSYLN 51 EWKLDSNQYS TYLSIKPDEL FEKCTHYYRS PVSDTWKLLS SKEAADIYTP 101 FHYYLSTISF QSKDNSTTLP SLDDVIYSVD HTRYLLSEEP KIPTELVSEN 151 GTKWRLRNNS NFILDLHNIY RNMVKQFSNK TSEFDQFDLF IILAAYLTLF 201 YTLCCLFNDM RKIGSKFWLS FSALSNSACA LYLSLYTTHS LLKKPASLLS 251 LVIGLPFIVV IIGFKHKVRL AAFSLQKFHR ISIDKKITVS NIIYEAMFQE 301 GAYLIRDYLF YISSFIGCAI YARHLPGLVN FCILSTFMLV FDLLLSATFY 351 SAILSMKLEI NIIHRSTVIR QTLEEDGVVP TTADIIYKDE TASEPHFLRS 401 NVAIILGKAS VIGLLLLINL YVFTDKLNAT ILNTVYFDST IYSLPNFINY 451 KDIGNLSNQV IISVLPKQYY TPLKKYHQIE DSVLLIIDSV SNAIRDQFIS 501 KLLFFAFAVS ISINVYLLNA AKIHTGYMNF QPQSNKIDDL VVQQKSATIE 551 FSETRSMPAS SGLETPVTAK DIIISEEIQN NECVYALSSQ DEPIRPLSNL 601 VELMEKEQLK NMNNTEVSNL VVNGKLPLYS LEKKLEDTTR AVLVRRKALS 651 TLAESPILVS EKLPFRNYDY DRVFGACCEN VIGYMPIPVG VIGPLIIDGT 701 SYHIPMATTE GCLVASAMRG CKAINAGGGA TTVLTKDGMT RGPVVRFPTL 751 IRSGACKIWL DSEEGQNSIK KAFNSTSRFA RLQHIQTCLA GDLLFMRFRT 801 TTGDAMGMNM ISKGVEYSLK QMVEEYGWED MEVVSVSGNY CTDKKPAAIN 851 WIEGRGKSVV AEATIPGDVV KSVLKSDVSA LVELNISKNL VGSAMAGSVG 901 GFNAHAANLV TALFLALGQD PAQNVESSNC ITLMKEVDGD LRISVSMPSI 951 EVGTIGGGTV LEPQGAMLDL LGVRGPHPTE PGANARQLAR IIACAVLAGE 1001 LSLCSALAAG HLVQSHMTHN RKTNKANELP QPSNKGPPCK TSALL*

Amino Acid Sequence (or in FASTA format)

       1  MSLPLKTIVH LVKPFACTAR FSARYPIHVI VVAVLLSAAA YLSVTQSYLN
      51  EWKLDSNQYS TYLSIKPDEL FEKCTHYYRS PVSDTWKLLS SKEAADIYTP
     101  FHYYLSTISF QSKDNSTTLP SLDDVIYSVD HTRYLLSEEP KIPTELVSEN
     151  GTKWRLRNNS NFILDLHNIY RNMVKQFSNK TSEFDQFDLF IILAAYLTLF
     201  YTLCCLFNDM RKIGSKFWLS FSALSNSACA LYLSLYTTHS LLKKPASLLS
     251  LVIGLPFIVV IIGFKHKVRL AAFSLQKFHR ISIDKKITVS NIIYEAMFQE
     301  GAYLIRDYLF YISSFIGCAI YARHLPGLVN FCILSTFMLV FDLLLSATFY
     351  SAILSMKLEI NIIHRSTVIR QTLEEDGVVP TTADIIYKDE TASEPHFLRS
     401  NVAIILGKAS VIGLLLLINL YVFTDKLNAT ILNTVYFDST IYSLPNFINY
     451  KDIGNLSNQV IISVLPKQYY TPLKKYHQIE DSVLLIIDSV SNAIRDQFIS
     501  KLLFFAFAVS ISINVYLLNA AKIHTGYMNF QPQSNKIDDL VVQQKSATIE
     551  FSETRSMPAS SGLETPVTAK DIIISEEIQN NECVYALSSQ DEPIRPLSNL
     601  VELMEKEQLK NMNNTEVSNL VVNGKLPLYS LEKKLEDTTR AVLVRRKALS
     651  TLAESPILVS EKLPFRNYDY DRVFGACCEN VIGYMPIPVG VIGPLIIDGT
     701  SYHIPMATTE GCLVASAMRG CKAINAGGGA TTVLTKDGMT RGPVVRFPTL
     751  IRSGACKIWL DSEEGQNSIK KAFNSTSRFA RLQHIQTCLA GDLLFMRFRT
     801  TTGDAMGMNM ISKGVEYSLK QMVEEYGWED MEVVSVSGNY CTDKKPAAIN
     851  WIEGRGKSVV AEATIPGDVV KSVLKSDVSA LVELNISKNL VGSAMAGSVG
     901  GFNAHAANLV TALFLALGQD PAQNVESSNC ITLMKEVDGD LRISVSMPSI
     951  EVGTIGGGTV LEPQGAMLDL LGVRGPHPTE PGANARQLAR IIACAVLAGE
    1001  LSLCSALAAG HLVQSHMTHN RKTNKANELP QPSNKGPPCK TSALL*

external links for Hmg2p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
YGOB	Complexome	TCDB
YOGY	DIP	YeastRC Structure Prediction (Seattle)
	GeneMANIA

References cited on this page View Complete Literature Guide for Hmg2p

1)	Parks LW, et al. (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
2)	Basson ME, et al. (1986) Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Proc Natl Acad Sci U S A 83(15):5563-7
3)	Wright R, et al. (1988) Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J Cell Biol 107(1):101-14
4)	Koning AJ, et al. (1996) Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations. Mol Biol Cell 7(5):769-89
5)	Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
7)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41