Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23434 (GCSH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine cleavage system H protein, mitochondrial
Alternative name(s):
Lipoic acid-containing protein
Gene names
Name:GCSH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST). HAMAP-Rule MF_00272

Cofactor

Binds 1 lipoyl cofactor covalently.

Subunit structure

Interacts with GLDC By similarity. The glycine cleavage system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH). HAMAP-Rule MF_00272

Subcellular location

Mitochondrion HAMAP-Rule MF_00272.

Involvement in disease

Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the GcvH family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Mitochondrion HAMAP-Rule MF_00272
Chain49 – 173125Glycine cleavage system H protein, mitochondrial HAMAP-Rule MF_00272
PRO_0000010723

Amino acid modifications

Modified residue1071N6-lipoyllysine HAMAP-Rule MF_00272

Natural variations

Natural variant211S → L. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs8052579 [ dbSNP | Ensembl ].
VAR_018846
Natural variant731N → S. Ref.3
Corresponds to variant rs8177877 [ dbSNP | Ensembl ].
VAR_018847

Sequences

Sequence LengthMass (Da)Tools
P23434 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 3CC5D09D59C1243D

FASTA17318,885
        10         20         30         40         50         60 
MALRVVRSVR ALLCTLRAVP SPAAPCPPRP WQLGVGAVRT LRTGPALLSV RKFTEKHEWV 

        70         80         90        100        110        120 
TTENGIGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQDEF GALESVKAAS ELYSPLSGEV 

       130        140        150        160        170 
TEINEALAEN PGLVNKSCYE DGWLIKMTLS NPSELDELMS EEAYEKYIKS IEE 

« Hide

References

« Hide 'large scale' references
[1]"The glycine cleavage system: structure of a cDNA encoding human H-protein, and partial characterization of its gene in patients with hyperglycinemias."
Koyata H., Hiraga K.
Am. J. Hum. Genet. 48:351-361(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-21.
[2]"The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning."
Fujiwara K., Okamura-Ikeda K., Hayasaka K., Motokawa Y.
Biochem. Biophys. Res. Commun. 176:711-716(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-21.
[3]NIEHS SNPs program
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-21 AND SER-73.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT LEU-21.
Tissue: Placenta and Skeletal muscle.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00723 mRNA. Translation: BAA00625.1.
M69175 mRNA. Translation: AAA36011.1.
AY310735 Genomic DNA. Translation: AAP50260.1.
AC092718 Genomic DNA. No translation available.
BC000790 mRNA. Translation: AAH00790.1.
BC020922 mRNA. Translation: AAH20922.1.
PIRGCHUH. A36662.
RefSeqNP_004474.2. NM_004483.4.
UniGeneHs.546256.

3D structure databases

ProteinModelPortalP23434.
SMRP23434. Positions 49-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108923. 3 interactions.
IntActP23434. 3 interactions.
MINTMINT-1391441.
STRING9606.ENSP00000319531.

Chemistry

DrugBankDB00145. Glycine.

PTM databases

PhosphoSiteP23434.

Polymorphism databases

DMDM311033385.

Proteomic databases

PaxDbP23434.
PRIDEP23434.

Protocols and materials databases

DNASU2653.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315467; ENSP00000319531; ENSG00000140905.
GeneID2653.
KEGGhsa:2653.
UCSCuc002fgd.3. human.

Organism-specific databases

CTD2653.
GeneCardsGC16M081115.
H-InvDBHIX0013270.
HIX0028692.
HGNCHGNC:4208. GCSH.
HPAHPA041368.
MIM238330. gene.
605899. phenotype.
neXtProtNX_P23434.
Orphanet289863. Atypical glycine encephalopathy.
289860. Infantile glycine encephalopathy.
289857. Neonatal glycine encephalopathy.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0509.
HOGENOMHOG000239392.
HOVERGENHBG001129.
InParanoidP23434.
KOK02437.
OMAWLFRIKA.
OrthoDBEOG7RNK1M.
PhylomeDBP23434.
TreeFamTF300258.

Enzyme and pathway databases

SABIO-RKP23434.

Gene expression databases

BgeeP23434.
CleanExHS_GCSH.
GenevestigatorP23434.

Family and domain databases

HAMAPMF_00272. GcvH.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR11715. PTHR11715. 1 hit.
PfamPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR00527. gcvH. 1 hit.
PROSITEPS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGCSH.
GenomeRNAi2653.
NextBio10484.
PROP23434.
SOURCESearch...

Entry information

Entry nameGCSH_HUMAN
AccessionPrimary (citable) accession number: P23434
Secondary accession number(s): Q9H1E9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM