Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8JZK9 (HMCS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxymethylglutaryl-CoA synthase, cytoplasmic
Short name=HMG-CoA synthase
EC=2.3.3.10
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene names
Name:Hmgcs1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase By similarity.

Catalytic activity

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the HMG-CoA synthase family.

Ontologies

Keywords
   Biological processCholesterol biosynthesis
Cholesterol metabolism
Lipid biosynthesis
Lipid metabolism
Steroid biosynthesis
Steroid metabolism
Sterol biosynthesis
Sterol metabolism
   Cellular componentCytoplasm
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from electronic annotation. Source: Compara

cellular response to cholesterol

Inferred from electronic annotation. Source: Compara

cellular response to follicle-stimulating hormone stimulus

Inferred from electronic annotation. Source: Compara

cholesterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

isoprenoid biosynthetic process

Inferred from electronic annotation. Source: InterPro

liver development

Inferred from electronic annotation. Source: Compara

male gonad development

Inferred from electronic annotation. Source: Compara

response to acid

Inferred from electronic annotation. Source: Compara

response to drug

Inferred from electronic annotation. Source: Compara

response to lipoprotein particle stimulus

Inferred from electronic annotation. Source: Compara

response to low light intensity stimulus

Inferred from electronic annotation. Source: Compara

response to purine-containing compound

Inferred from electronic annotation. Source: Compara

response to tellurium ion

Inferred from electronic annotation. Source: Compara

response to vitamin E

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: Compara

plasma membrane

Inferred from electronic annotation. Source: Compara

   Molecular_functiondrug binding

Inferred from electronic annotation. Source: Compara

hydroxymethylglutaryl-CoA synthase activity

Inferred from electronic annotation. Source: EC

isomerase activity

Inferred from electronic annotation. Source: Compara

organic acid binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Hydroxymethylglutaryl-CoA synthase, cytoplasmic
PRO_0000213748

Sites

Active site1291 Potential

Amino acid modifications

Modified residue41Phosphoserine By similarity
Modified residue461N6-acetyllysine By similarity
Modified residue2731N6-acetyllysine By similarity
Modified residue4951Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8JZK9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E28F8772CF64D85C

FASTA52057,569
        10         20         30         40         50         60 
MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG LGQARMGFCT 

        70         80         90        100        110        120 
DREDINSLCL TVVQKLMERH SLSYDCIGRL EVGTETIIDK SKSVKSNLMQ LFEESGNTDI 

       130        140        150        160        170        180 
EGIDTTNACY GGTAAVFNAV NWVESSSWDG RYALVVAGDI AIYATGNARP TGGVGAVALL 

       190        200        210        220        230        240 
IGPNAPLIFD RGLRGTHMQH AYDFYKPDML SEYPVVDGKL SIQCYLSALD RCYSVYRKKI 

       250        260        270        280        290        300 
RAQWQKEGKD KDFTLNDFGF MIFHSPYCKL VQKSLARMFL NDFLNDQNRD KNSIYSGLEA 

       310        320        330        340        350        360 
FGDVKLEDTY FDRDVEKAFM KASSELFNQK TKASLLVSNQ NGNMYTSSVY GSLASVLAQY 

       370        380        390        400        410        420 
SPQQLAGKRV GVFSYGSGLA ATLYSLKVTQ DATPGSALDK ITASLCDLKS RLDSRTCVAP 

       430        440        450        460        470        480 
DVFAENMKLR EDTHHLANYI PQCSIDSLFE GTWYLVRVDE KHRRTYARRP FTNDHSLDEG 

       490        500        510        520 
MGLVHSNTAT EHIPSPAKKV PRLPATSAES ESAVISNGEH

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Muellerian duct and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N and FVB/N-3.
Tissue: Eye and Mammary tumor.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 47-75; 90-100; 220-231; 278-289; 292-313; 322-330; 370-409; 416-428 AND 469-498, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC023851 mRNA. Translation: AAH23851.1.
BC029693 mRNA. Translation: AAH29693.1.
BC034317 mRNA. Translation: AAH34317.1.
AK031297 mRNA. Translation: BAC27338.1.
AK044835 mRNA. Translation: BAC32112.1.
AK045094 mRNA. Translation: BAC32218.1.
AK135551 mRNA. Translation: BAE22579.1.
IPIIPI00331707.
RefSeqNP_666054.2. NM_145942.4.
UniGeneMm.61526.

3D structure databases

ProteinModelPortalQ8JZK9.
SMRQ8JZK9. Positions 16-470.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000097858.

PTM databases

PhosphoSiteQ8JZK9.

2D gel databases

REPRODUCTION-2DPAGEQ8JZK9.

Proteomic databases

PaxDbQ8JZK9.
PRIDEQ8JZK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000179869; ENSMUSP00000136944; ENSMUSG00000093930.
GeneID208715.
KEGGmmu:208715.
UCSCuc007rzv.1. mouse.

Organism-specific databases

CTD3157.
MGIMGI:107592. Hmgcs1.

Phylogenomic databases

eggNOGCOG3425.
GeneTreeENSGT00390000006096.
HOGENOMHOG000012351.
HOVERGENHBG051912.
InParanoidQ8JZK9.
KOK01641.
OMARDFTLND.
OrthoDBEOG4F1X30.

Enzyme and pathway databases

UniPathwayUPA00058; UER00102.

Gene expression databases

BgeeQ8JZK9.
CleanExMM_HMGCS1.
GenevestigatorQ8JZK9.
GermOnlineENSMUSG00000075461. Mus musculus.

Family and domain databases

Gene3D3.40.47.10. 1 hit.
InterProIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372391.
SOURCESearch...

Entry information

Entry nameHMCS1_MOUSE
AccessionPrimary (citable) accession number: Q8JZK9
Secondary accession number(s): Q3UXI4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 1, 2002
Last modified: April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents