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Protein

3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic

Gene

HMGCLL1

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

Functioni

Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis, the products of which support energy production in nonhepatic animal tissues.2 Publications

Catalytic activityi

(S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate.2 Publications

Cofactori

a divalent metal cation1 Publication

Kineticsi

  1. KM=40 µM for (S)-3-hydroxy-3-methylglutaryl-CoA (at pH 9)2 Publications
  2. KM=75 µM for (S)-3-hydroxy-3-methylglutaryl-CoA (at pH 8)2 Publications
  3. KM=28 µM for (S)-3-hydroxy-3-methylglutaryl-CoA2 Publications
  4. KM=49 µM for (S)-3-hydroxy-3-methylglutaryl-CoA (in presence of magnesium)2 Publications
  5. KM=0.18 µM for (S)-3-hydroxy-3-methylglutaryl-CoA (in presence of manganese)2 Publications
  1. Vmax=12 nmol/min/mg enzyme with (S)-3-hydroxy-3-methylglutaryl-CoA as substrate at pH 92 Publications
  2. Vmax=25 nmol/min/mg enzyme with (S)-3-hydroxy-3-methylglutaryl-CoA as substrate at pH 82 Publications

Pathwayi: (S)-3-hydroxy-3-methylglutaryl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Hydroxymethylglutaryl-CoA lyase, mitochondrial (HMGCL), 3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic (HMGCLL1)
This subpathway is part of the pathway (S)-3-hydroxy-3-methylglutaryl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA, the pathway (S)-3-hydroxy-3-methylglutaryl-CoA degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861SubstrateBy similarity
Metal bindingi87 – 871Divalent metal cationBy similarity
Metal bindingi278 – 2781Divalent metal cationBy similarity
Metal bindingi280 – 2801Divalent metal cationBy similarity
Active sitei311 – 3111By similarity
Metal bindingi320 – 3201Divalent metal cationBy similarity

GO - Molecular functioni

  • hydroxymethylglutaryl-CoA lyase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB

GO - Biological processi

  • ketone body biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-77111. Synthesis of Ketone Bodies.
UniPathwayiUPA00896; UER00863.

Chemistry

SwissLipidsiSLP:000001291. [Q8TB92-2]

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic (EC:4.1.3.4)
Alternative name(s):
3-hydroxymethyl-3-methylglutaryl-CoA lyase-like protein 1
Endoplasmic reticulum 3-hydroxymethyl-3-methylglutaryl-CoA lyase
Short name:
er-cHL
Gene namesi
Name:HMGCLL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21359. HMGCLL1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Abolishes myristoylation and induces a subcellular location change. 1 Publication
Mutagenesisi86 – 861R → Q: Abolishes catalytic activity. 1 Publication
Mutagenesisi237 – 2371L → S: Abolishes catalytic activity. 1 Publication
Mutagenesisi278 – 2781H → R: Abolishes catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA134989971.

Polymorphism and mutation databases

BioMutaiHMGCLL1.
DMDMi189028466.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 3703693-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmicPRO_0000334669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiQ8TB92.
PRIDEiQ8TB92.

PTM databases

iPTMnetiQ8TB92.
PhosphoSiteiQ8TB92.

Expressioni

Gene expression databases

BgeeiQ8TB92.
CleanExiHS_HMGCLL1.
ExpressionAtlasiQ8TB92. baseline and differential.
GenevisibleiQ8TB92. HS.

Organism-specific databases

HPAiHPA030223.

Interactioni

Protein-protein interaction databases

BioGridi120006. 2 interactions.
STRINGi9606.ENSP00000381654.

Structurei

3D structure databases

ProteinModelPortaliQ8TB92.
SMRiQ8TB92. Positions 74-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA lyase family.Curated

Phylogenomic databases

eggNOGiKOG2368. Eukaryota.
COG0119. LUCA.
GeneTreeiENSGT00390000017690.
HOGENOMiHOG000219757.
HOVERGENiHBG064656.
InParanoidiQ8TB92.
KOiK01640.
OMAiGMGHRWI.
PhylomeDBiQ8TB92.
TreeFamiTF105363.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR030021. er-cHL.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF33. PTHR10277:SF33. 2 hits.
PfamiPF00682. HMGL-like. 1 hit.
[Graphical view]
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TB92-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQTSLL TNLHCFQPDV
60 70 80 90 100
SGFSVSLAGT VACIHWETSQ LSGLPEFVKI VEVGPRDGLQ NEKVIVPTDI
110 120 130 140 150
KIEFINRLSQ TGLSVIEVTS FVSSRWVPQM ADHTEVMKGI HQYPGVRYPV
160 170 180 190 200
LTPNLQGFHH AVAAGATEIS VFGAASESFS KKNINCSIEE SMGKFEEVVK
210 220 230 240 250
SARHMNIPAR GYVSCALGCP YEGSITPQKV TEVSKRLYGM GCYEISLGDT
260 270 280 290 300
IGVGTPGSMK RMLESVMKEI PPGALAVHCH DTYGQALANI LTALQMGINV
310 320 330 340 350
VDSAVSGLGG CPYAKGASGN VATEDLIYML NGLGLNTGVN LYKVMEAGDF
360 370
ICKAVNKTTN SKVAQASFNA
Length:370
Mass (Da):39,514
Last modified:May 20, 2008 - v3
Checksum:i7DDEE81555E092A1
GO
Isoform 2 (identifier: Q8TB92-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-66: Missing.

Show »
Length:340
Mass (Da):36,328
Checksum:i6F175387821614CC
GO
Isoform 3 (identifier: Q8TB92-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-53: TSLLTNLHCFQPDVSGF → ELQSVMLMLHHGPLRKP
     54-370: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Show »
Length:53
Mass (Da):5,874
Checksum:i16F3265215AF8A2A
GO
Isoform 4 (identifier: Q8TB92-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-66: Missing.
     130-161: Missing.

Note: No experimental confirmation available.
Show »
Length:308
Mass (Da):32,701
Checksum:i49ED9FE7EC8038BB
GO

Sequence cautioni

The sequence BAC87045.1 differs from that shown. Reason: Frameshift at position 253. Curated
The sequence BAG51462.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991D → G in BAH11613 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 6630Missing in isoform 2 and isoform 4. 2 PublicationsVSP_033752Add
BLAST
Alternative sequencei37 – 5317TSLLT…DVSGF → ELQSVMLMLHHGPLRKP in isoform 3. 1 PublicationVSP_038021Add
BLAST
Alternative sequencei54 – 370317Missing in isoform 3. 1 PublicationVSP_038022Add
BLAST
Alternative sequencei130 – 16132Missing in isoform 4. 1 PublicationVSP_044324Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055075 mRNA. Translation: BAG51462.1. Sequence problems.
AK127587 mRNA. Translation: BAC87045.1. Frameshift.
AK293856 mRNA. Translation: BAH11613.1.
AL590290 Genomic DNA. No translation available.
AL590406 Genomic DNA. Translation: CAI40662.1.
CH471081 Genomic DNA. Translation: EAX04442.1.
CH471081 Genomic DNA. Translation: EAX04444.1.
BC024194 mRNA. Translation: AAH24194.2.
CCDSiCCDS43474.1. [Q8TB92-2]
CCDS43475.1. [Q8TB92-1]
CCDS75473.1. [Q8TB92-5]
RefSeqiNP_001035865.1. NM_001042406.1. [Q8TB92-2]
NP_001274670.1. NM_001287741.1. [Q8TB92-5]
NP_001274675.1. NM_001287746.1.
NP_061909.2. NM_019036.2. [Q8TB92-1]
UniGeneiHs.147054.

Genome annotation databases

EnsembliENST00000274901; ENSP00000274901; ENSG00000146151. [Q8TB92-2]
ENST00000308161; ENSP00000309737; ENSG00000146151. [Q8TB92-5]
ENST00000370852; ENSP00000359889; ENSG00000146151. [Q8TB92-4]
ENST00000398661; ENSP00000381654; ENSG00000146151. [Q8TB92-1]
GeneIDi54511.
KEGGihsa:54511.
UCSCiuc003pcn.4. human. [Q8TB92-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055075 mRNA. Translation: BAG51462.1. Sequence problems.
AK127587 mRNA. Translation: BAC87045.1. Frameshift.
AK293856 mRNA. Translation: BAH11613.1.
AL590290 Genomic DNA. No translation available.
AL590406 Genomic DNA. Translation: CAI40662.1.
CH471081 Genomic DNA. Translation: EAX04442.1.
CH471081 Genomic DNA. Translation: EAX04444.1.
BC024194 mRNA. Translation: AAH24194.2.
CCDSiCCDS43474.1. [Q8TB92-2]
CCDS43475.1. [Q8TB92-1]
CCDS75473.1. [Q8TB92-5]
RefSeqiNP_001035865.1. NM_001042406.1. [Q8TB92-2]
NP_001274670.1. NM_001287741.1. [Q8TB92-5]
NP_001274675.1. NM_001287746.1.
NP_061909.2. NM_019036.2. [Q8TB92-1]
UniGeneiHs.147054.

3D structure databases

ProteinModelPortaliQ8TB92.
SMRiQ8TB92. Positions 74-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120006. 2 interactions.
STRINGi9606.ENSP00000381654.

Chemistry

SwissLipidsiSLP:000001291. [Q8TB92-2]

PTM databases

iPTMnetiQ8TB92.
PhosphoSiteiQ8TB92.

Polymorphism and mutation databases

BioMutaiHMGCLL1.
DMDMi189028466.

Proteomic databases

PaxDbiQ8TB92.
PRIDEiQ8TB92.

Protocols and materials databases

DNASUi54511.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274901; ENSP00000274901; ENSG00000146151. [Q8TB92-2]
ENST00000308161; ENSP00000309737; ENSG00000146151. [Q8TB92-5]
ENST00000370852; ENSP00000359889; ENSG00000146151. [Q8TB92-4]
ENST00000398661; ENSP00000381654; ENSG00000146151. [Q8TB92-1]
GeneIDi54511.
KEGGihsa:54511.
UCSCiuc003pcn.4. human. [Q8TB92-1]

Organism-specific databases

CTDi54511.
GeneCardsiHMGCLL1.
HGNCiHGNC:21359. HMGCLL1.
HPAiHPA030223.
neXtProtiNX_Q8TB92.
PharmGKBiPA134989971.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2368. Eukaryota.
COG0119. LUCA.
GeneTreeiENSGT00390000017690.
HOGENOMiHOG000219757.
HOVERGENiHBG064656.
InParanoidiQ8TB92.
KOiK01640.
OMAiGMGHRWI.
PhylomeDBiQ8TB92.
TreeFamiTF105363.

Enzyme and pathway databases

UniPathwayiUPA00896; UER00863.
ReactomeiR-HSA-77111. Synthesis of Ketone Bodies.

Miscellaneous databases

ChiTaRSiHMGCLL1. human.
GenomeRNAii54511.
PROiQ8TB92.

Gene expression databases

BgeeiQ8TB92.
CleanExiHS_HMGCLL1.
ExpressionAtlasiQ8TB92. baseline and differential.
GenevisibleiQ8TB92. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR030021. er-cHL.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF33. PTHR10277:SF33. 2 hits.
PfamiPF00682. HMGL-like. 1 hit.
[Graphical view]
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1; 3 AND 4).
    Tissue: Brain and Cerebellum.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 2).
    Tissue: Brain.
  5. "Identification and characterization of an extramitochondrial human 3-Hydroxy-3-methylglutaryl-CoA lyase."
    Montgomery C., Pei Z., Watkins P.A., Miziorko H.M.
    J. Biol. Chem. 287:33227-33236(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
  6. "Characterization of a novel HMG-CoA Lyase enzyme with a dual location in endoplasmic reticulum and cytosol."
    Arnedo M., Menao S., Puisac B., Teresa-Rodrigo M.E., Gil-Rodriguez M.C., Lopez-Vinas E., Gomez-Puertas P., Casals N., Casale C.H., Hegardt F.G., Pie J.
    J. Lipid Res. 53:2046-2056(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-86; LEU-237 AND HIS-278.

Entry informationi

Entry nameiHMGC2_HUMAN
AccessioniPrimary (citable) accession number: Q8TB92
Secondary accession number(s): B1AQ42
, B3KNV0, B7Z1S7, F8W793, Q6ZSA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 8, 2016
This is version 118 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.