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Q8JZK9 (HMCS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 85. 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)
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.

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 residue2461N6-acetyllysine By similarity
Modified residue2731N6-acetyllysine By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue4951Phosphoserine By similarity
Modified residue5161Phosphoserine 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: 16141072] [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: 15489334] [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.
XP_001475239.1. XM_001475189.2.
XP_001475257.1. XM_001475207.2.
XP_001475280.1. XM_001475230.2.
XP_003085635.1. XM_003085587.1.
UniGeneMm.61526.

3D structure databases

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

Protein-protein interaction databases

STRINGQ8JZK9.

PTM databases

PhosphoSiteQ8JZK9.

2D gel databases

REPRODUCTION-2DPAGEQ8JZK9.

Proteomic databases

PRIDEQ8JZK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100285; ENSMUSP00000097858; ENSMUSG00000079828.
ENSMUST00000112117; ENSMUSP00000107745; ENSMUSG00000079301.
GeneID100040592.
208715.
KEGGmmu:100040592.
mmu:208715.
UCSCuc007rzv.1. mouse.

Organism-specific databases

CTD3157.
MGIMGI:107592. Hmgcs1.

Phylogenomic databases

HOGENOMHBG578402.
HOVERGENHBG051912.
InParanoidQ8JZK9.
OMADTVNACY.
OrthoDBEOG4F1X30.
PhylomeDBQ8JZK9.

Gene expression databases

ArrayExpressQ8JZK9.
CleanExMM_HMGCS1.
GenevestigatorQ8JZK9.
GermOnlineENSMUSG00000075461. Mus musculus.

Family and domain databases

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]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
KOK01641.
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

NextBio449244.
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: November 16, 2011
This is version 85 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