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Protein

Hydroxymethylglutaryl-CoA synthase, cytoplasmic

Gene

HMGCS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathway: (R)-mevalonate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Hydroxymethylglutaryl-CoA synthase, cytoplasmic (HMGCS1), Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMGCS2)
  3. 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl coenzyme A reductase
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Proton donor/acceptorPROSITE-ProRule annotation
Active sitei129 – 1291Acyl-thioester intermediate
Active sitei264 – 2641Proton donor/acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  • drug binding Source: Ensembl
  • hydroxymethylglutaryl-CoA synthase activity Source: ProtInc
  • isomerase activity Source: Ensembl
  • organic acid binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000112972-MONOMER.
BRENDAi2.3.3.10. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
UniPathwayiUPA00058; UER00102.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylglutaryl-CoA synthase, cytoplasmic (EC:2.3.3.10)
Short name:
HMG-CoA synthase
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene namesi
Name:HMGCS1
Synonyms:HMGCS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:5007. HMGCS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291C → A or S: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA29337.

Polymorphism and mutation databases

BioMutaiHMGCS1.
DMDMi1708239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Hydroxymethylglutaryl-CoA synthase, cytoplasmicPRO_0000213747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei273 – 2731N6-acetyllysine1 Publication
Modified residuei476 – 4761Phosphothreonine1 Publication
Modified residuei495 – 4951Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ01581.
PaxDbiQ01581.
PeptideAtlasiQ01581.
PRIDEiQ01581.

PTM databases

PhosphoSiteiQ01581.

Expressioni

Gene expression databases

BgeeiQ01581.
CleanExiHS_HMGCS1.
ExpressionAtlasiQ01581. baseline and differential.
GenevisibleiQ01581. HS.

Organism-specific databases

HPAiCAB032907.
HPA036913.
HPA036914.

Interactioni

Protein-protein interaction databases

BioGridi109400. 19 interactions.
IntActiQ01581. 2 interactions.
STRINGi9606.ENSP00000322706.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 258Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 408Combined sources
Helixi46 – 516Combined sources
Beta strandi55 – 573Combined sources
Helixi65 – 7915Combined sources
Helixi84 – 863Combined sources
Beta strandi87 – 937Combined sources
Beta strandi100 – 1023Combined sources
Helixi104 – 1085Combined sources
Helixi109 – 1113Combined sources
Turni112 – 1165Combined sources
Beta strandi124 – 1274Combined sources
Helixi128 – 1303Combined sources
Helixi131 – 14313Combined sources
Beta strandi152 – 16110Combined sources
Helixi169 – 1713Combined sources
Beta strandi173 – 18412Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi203 – 2053Combined sources
Helixi218 – 24730Combined sources
Helixi255 – 2573Combined sources
Beta strandi259 – 2635Combined sources
Helixi268 – 28518Combined sources
Helixi289 – 2913Combined sources
Helixi293 – 2953Combined sources
Helixi299 – 3013Combined sources
Helixi306 – 3083Combined sources
Helixi313 – 32210Combined sources
Helixi324 – 3307Combined sources
Helixi333 – 3353Combined sources
Helixi336 – 3416Combined sources
Helixi345 – 3473Combined sources
Helixi348 – 35912Combined sources
Helixi362 – 3654Combined sources
Beta strandi369 – 3768Combined sources
Turni377 – 3793Combined sources
Beta strandi380 – 3889Combined sources
Helixi397 – 4037Combined sources
Turni404 – 4074Combined sources
Helixi408 – 4136Combined sources
Beta strandi415 – 4173Combined sources
Helixi420 – 43314Combined sources
Beta strandi453 – 4586Combined sources
Beta strandi464 – 4685Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P8UX-ray2.00A/B16-470[»]
ProteinModelPortaliQ01581.
SMRiQ01581. Positions 16-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01581.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA synthase family.Curated

Phylogenomic databases

eggNOGiCOG3425.
GeneTreeiENSGT00390000006096.
HOGENOMiHOG000012351.
HOVERGENiHBG051912.
InParanoidiQ01581.
KOiK01641.
OMAiRDFTLND.
OrthoDBiEOG741Z1W.
PhylomeDBiQ01581.
TreeFamiTF105361.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEiPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01581-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG
60 70 80 90 100
LGQAKMGFCT DREDINSLCM TVVQNLMERN NLSYDCIGRL EVGTETIIDK
110 120 130 140 150
SKSVKTNLMQ LFEESGNTDI EGIDTTNACY GGTAAVFNAV NWIESSSWDG
160 170 180 190 200
RYALVVAGDI AVYATGNARP TGGVGAVALL IGPNAPLIFE RGLRGTHMQH
210 220 230 240 250
AYDFYKPDML SEYPIVDGKL SIQCYLSALD RCYSVYCKKI HAQWQKEGND
260 270 280 290 300
KDFTLNDFGF MIFHSPYCKL VQKSLARMLL NDFLNDQNRD KNSIYSGLEA
310 320 330 340 350
FGDVKLEDTY FDRDVEKAFM KASSELFSQK TKASLLVSNQ NGNMYTSSVY
360 370 380 390 400
GSLASVLAQY SPQQLAGKRI GVFSYGSGLA ATLYSLKVTQ DATPGSALDK
410 420 430 440 450
ITASLCDLKS RLDSRTGVAP DVFAENMKLR EDTHHLVNYI PQGSIDSLFE
460 470 480 490 500
GTWYLVRVDE KHRRTYARRP TPNDDTLDEG VGLVHSNIAT EHIPSPAKKV
510 520
PRLPATAAEP EAAVISNGEH
Length:520
Mass (Da):57,294
Last modified:October 1, 1996 - v2
Checksum:iC669212BF86CFF9B
GO

Sequence cautioni

The sequence AAH00297.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481G → A in CAA47061 (PubMed:1358203).Curated
Sequence conflicti251 – 2511K → N in CAA47061 (PubMed:1358203).Curated
Sequence conflicti299 – 2991E → K in CAA47061 (PubMed:1358203).Curated
Sequence conflicti364 – 3641Q → H in CAA47061 (PubMed:1358203).Curated
Sequence conflicti420 – 4201P → Q in CAA47061 (PubMed:1358203).Curated
Sequence conflicti519 – 5202EH → VW in CAA47061 (PubMed:1358203).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66435 mRNA. Translation: CAA47061.1.
L25798 mRNA. Translation: AAA62411.1.
BT007302 mRNA. Translation: AAP35966.1.
AK315593 mRNA. Translation: BAG37965.1.
CH471119 Genomic DNA. Translation: EAW56054.1.
BC000297 mRNA. Translation: AAH00297.2. Different initiation.
CCDSiCCDS34154.1.
PIRiS27197.
S45497.
RefSeqiNP_001091742.1. NM_001098272.2.
NP_002121.4. NM_002130.7.
UniGeneiHs.397729.
Hs.741287.

Genome annotation databases

EnsembliENST00000325110; ENSP00000322706; ENSG00000112972.
ENST00000433297; ENSP00000399402; ENSG00000112972.
GeneIDi3157.
KEGGihsa:3157.
UCSCiuc003jnq.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66435 mRNA. Translation: CAA47061.1.
L25798 mRNA. Translation: AAA62411.1.
BT007302 mRNA. Translation: AAP35966.1.
AK315593 mRNA. Translation: BAG37965.1.
CH471119 Genomic DNA. Translation: EAW56054.1.
BC000297 mRNA. Translation: AAH00297.2. Different initiation.
CCDSiCCDS34154.1.
PIRiS27197.
S45497.
RefSeqiNP_001091742.1. NM_001098272.2.
NP_002121.4. NM_002130.7.
UniGeneiHs.397729.
Hs.741287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P8UX-ray2.00A/B16-470[»]
ProteinModelPortaliQ01581.
SMRiQ01581. Positions 16-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109400. 19 interactions.
IntActiQ01581. 2 interactions.
STRINGi9606.ENSP00000322706.

Chemistry

GuidetoPHARMACOLOGYi638.

PTM databases

PhosphoSiteiQ01581.

Polymorphism and mutation databases

BioMutaiHMGCS1.
DMDMi1708239.

Proteomic databases

MaxQBiQ01581.
PaxDbiQ01581.
PeptideAtlasiQ01581.
PRIDEiQ01581.

Protocols and materials databases

DNASUi3157.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325110; ENSP00000322706; ENSG00000112972.
ENST00000433297; ENSP00000399402; ENSG00000112972.
GeneIDi3157.
KEGGihsa:3157.
UCSCiuc003jnq.5. human.

Organism-specific databases

CTDi3157.
GeneCardsiGC05M043326.
HGNCiHGNC:5007. HMGCS1.
HPAiCAB032907.
HPA036913.
HPA036914.
MIMi142940. gene.
neXtProtiNX_Q01581.
PharmGKBiPA29337.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3425.
GeneTreeiENSGT00390000006096.
HOGENOMiHOG000012351.
HOVERGENiHBG051912.
InParanoidiQ01581.
KOiK01641.
OMAiRDFTLND.
OrthoDBiEOG741Z1W.
PhylomeDBiQ01581.
TreeFamiTF105361.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00102.
BioCyciMetaCyc:ENSG00000112972-MONOMER.
BRENDAi2.3.3.10. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSiHMGCS1. human.
EvolutionaryTraceiQ01581.
GenomeRNAii3157.
NextBioi12504.
PROiQ01581.
SOURCEiSearch...

Gene expression databases

BgeeiQ01581.
CleanExiHS_HMGCS1.
ExpressionAtlasiQ01581. baseline and differential.
GenevisibleiQ01581. HS.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEiPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amplification and direct sequencing of a cDNA encoding human cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase."
    Russ A.P., Ruzicka V., Maerz W., Appelhans H., Gross W.
    Biochim. Biophys. Acta 1132:329-331(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  2. "Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes."
    Rokosz L.L., Boulton D.A., Butkiewicz E.A., Sanyal G., Cueto M.A., Lachance P.A., Hermes J.D.
    Arch. Biochem. Biophys. 312:1-13(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MUTAGENESIS.
    Tissue: Fetal adrenal gland.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Lung.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-476 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHMCS1_HUMAN
AccessioniPrimary (citable) accession number: Q01581
Secondary accession number(s): B2RDL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.