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Q01581

- HMCS1_HUMAN

UniProt

Q01581 - HMCS1_HUMAN

Protein

Hydroxymethylglutaryl-CoA synthase, cytoplasmic

Gene

HMGCS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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

    Pathwayi

    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

    1. drug binding Source: Ensembl
    2. hydroxymethylglutaryl-CoA synthase activity Source: ProtInc
    3. isomerase activity Source: Ensembl
    4. organic acid binding Source: Ensembl

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cellular lipid metabolic process Source: Reactome
    3. cellular response to cholesterol Source: Ensembl
    4. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
    5. cholesterol biosynthetic process Source: Reactome
    6. isoprenoid biosynthetic process Source: InterPro
    7. lipid metabolic process Source: ProtInc
    8. liver development Source: Ensembl
    9. male gonad development Source: Ensembl
    10. response to acid chemical Source: Ensembl
    11. response to drug Source: Ensembl
    12. response to lipoprotein particle Source: Ensembl
    13. response to low light intensity stimulus Source: Ensembl
    14. response to purine-containing compound Source: Ensembl
    15. response to tellurium ion Source: Ensembl
    16. response to vitamin E Source: Ensembl
    17. small molecule metabolic process Source: Reactome

    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: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:5007. HMGCS1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleus Source: HPA
    4. plasma membrane Source: HPA

    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.

    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 – 4951Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ01581.
    PaxDbiQ01581.
    PeptideAtlasiQ01581.
    PRIDEiQ01581.

    PTM databases

    PhosphoSiteiQ01581.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01581.
    BgeeiQ01581.
    CleanExiHS_HMGCS1.
    GenevestigatoriQ01581.

    Organism-specific databases

    HPAiCAB032907.
    HPA036913.
    HPA036914.

    Interactioni

    Protein-protein interaction databases

    BioGridi109400. 10 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 – 258
    Beta strandi28 – 325
    Helixi33 – 408
    Helixi46 – 516
    Beta strandi55 – 573
    Helixi65 – 7915
    Helixi84 – 863
    Beta strandi87 – 937
    Beta strandi100 – 1023
    Helixi104 – 1085
    Helixi109 – 1113
    Turni112 – 1165
    Beta strandi124 – 1274
    Helixi128 – 1303
    Helixi131 – 14313
    Beta strandi152 – 16110
    Helixi169 – 1713
    Beta strandi173 – 18412
    Beta strandi186 – 1894
    Beta strandi195 – 1984
    Beta strandi203 – 2053
    Helixi218 – 24730
    Helixi255 – 2573
    Beta strandi259 – 2635
    Helixi268 – 28518
    Helixi289 – 2913
    Helixi293 – 2953
    Helixi299 – 3013
    Helixi306 – 3083
    Helixi313 – 32210
    Helixi324 – 3307
    Helixi333 – 3353
    Helixi336 – 3416
    Helixi345 – 3473
    Helixi348 – 35912
    Helixi362 – 3654
    Beta strandi369 – 3768
    Turni377 – 3793
    Beta strandi380 – 3889
    Helixi397 – 4037
    Turni404 – 4074
    Helixi408 – 4136
    Beta strandi415 – 4173
    Helixi420 – 43314
    Beta strandi453 – 4586
    Beta strandi464 – 4685

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG    50
    LGQAKMGFCT DREDINSLCM TVVQNLMERN NLSYDCIGRL EVGTETIIDK 100
    SKSVKTNLMQ LFEESGNTDI EGIDTTNACY GGTAAVFNAV NWIESSSWDG 150
    RYALVVAGDI AVYATGNARP TGGVGAVALL IGPNAPLIFE RGLRGTHMQH 200
    AYDFYKPDML SEYPIVDGKL SIQCYLSALD RCYSVYCKKI HAQWQKEGND 250
    KDFTLNDFGF MIFHSPYCKL VQKSLARMLL NDFLNDQNRD KNSIYSGLEA 300
    FGDVKLEDTY FDRDVEKAFM KASSELFSQK TKASLLVSNQ NGNMYTSSVY 350
    GSLASVLAQY SPQQLAGKRI GVFSYGSGLA ATLYSLKVTQ DATPGSALDK 400
    ITASLCDLKS RLDSRTGVAP DVFAENMKLR EDTHHLVNYI PQGSIDSLFE 450
    GTWYLVRVDE KHRRTYARRP TPNDDTLDEG VGLVHSNIAT EHIPSPAKKV 500
    PRLPATAAEP EAAVISNGEH 520
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi1708239.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS34154.1.
    PIRi S27197.
    S45497.
    RefSeqi NP_001091742.1. NM_001098272.2.
    NP_002121.4. NM_002130.7.
    UniGenei Hs.397729.
    Hs.741287.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P8U X-ray 2.00 A/B 16-470 [» ]
    ProteinModelPortali Q01581.
    SMRi Q01581. Positions 16-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109400. 10 interactions.
    IntActi Q01581. 2 interactions.
    STRINGi 9606.ENSP00000322706.

    Chemistry

    GuidetoPHARMACOLOGYi 638.

    PTM databases

    PhosphoSitei Q01581.

    Polymorphism databases

    DMDMi 1708239.

    Proteomic databases

    MaxQBi Q01581.
    PaxDbi Q01581.
    PeptideAtlasi Q01581.
    PRIDEi Q01581.

    Protocols and materials databases

    DNASUi 3157.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325110 ; ENSP00000322706 ; ENSG00000112972 .
    ENST00000433297 ; ENSP00000399402 ; ENSG00000112972 .
    GeneIDi 3157.
    KEGGi hsa:3157.
    UCSCi uc003jnq.5. human.

    Organism-specific databases

    CTDi 3157.
    GeneCardsi GC05M043326.
    HGNCi HGNC:5007. HMGCS1.
    HPAi CAB032907.
    HPA036913.
    HPA036914.
    MIMi 142940. gene.
    neXtProti NX_Q01581.
    PharmGKBi PA29337.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3425.
    HOGENOMi HOG000012351.
    HOVERGENi HBG051912.
    InParanoidi Q01581.
    KOi K01641.
    OMAi RDFTLND.
    OrthoDBi EOG741Z1W.
    PhylomeDBi Q01581.
    TreeFami TF105361.

    Enzyme and pathway databases

    UniPathwayi UPA00058 ; UER00102 .
    BioCyci MetaCyc:ENSG00000112972-MONOMER.
    BRENDAi 2.3.3.10. 2681.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_9405. Cholesterol biosynthesis.

    Miscellaneous databases

    ChiTaRSi HMGCS1. human.
    EvolutionaryTracei Q01581.
    GenomeRNAii 3157.
    NextBioi 12504.
    PROi Q01581.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01581.
    Bgeei Q01581.
    CleanExi HS_HMGCS1.
    Genevestigatori Q01581.

    Family and domain databases

    Gene3Di 3.40.47.10. 1 hit.
    InterProi IPR000590. 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 ]
    Pfami PF08540. HMG_CoA_synt_C. 1 hit.
    PF01154. HMG_CoA_synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 3 hits.
    TIGRFAMsi TIGR01833. HMG-CoA-S_euk. 1 hit.
    PROSITEi PS01226. HMG_COA_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 160 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