Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23434

- GCSH_HUMAN

UniProt

P23434 - GCSH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glycine cleavage system H protein, mitochondrial

Gene

GCSH

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

Functioni

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).

Cofactori

Binds 1 lipoyl cofactor covalently.

GO - Molecular functioni

  1. aminomethyltransferase activity Source: ProtInc

GO - Biological processi

  1. glycine catabolic process Source: ProtInc
  2. glycine decarboxylation via glycine cleavage system Source: Ensembl
  3. methylation Source: GOC
Complete GO annotation...

Enzyme and pathway databases

SABIO-RKP23434.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H protein, mitochondrial
Alternative name(s):
Lipoic acid-containing protein
Gene namesi
Name:GCSH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4208. GCSH.

Subcellular locationi

GO - Cellular componenti

  1. glycine cleavage complex Source: ProtInc
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

MIMi605899. phenotype.
Orphaneti289863. Atypical glycine encephalopathy.
289860. Infantile glycine encephalopathy.
289857. Neonatal glycine encephalopathy.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848MitochondrionAdd
BLAST
Chaini49 – 173125Glycine cleavage system H protein, mitochondrialPRO_0000010723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071N6-lipoyllysine1 Publication

Proteomic databases

MaxQBiP23434.
PaxDbiP23434.
PRIDEiP23434.

PTM databases

PhosphoSiteiP23434.

Expressioni

Gene expression databases

BgeeiP23434.
CleanExiHS_GCSH.
ExpressionAtlasiP23434. baseline.
GenevestigatoriP23434.

Organism-specific databases

HPAiHPA041368.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi108923. 3 interactions.
IntActiP23434. 3 interactions.
MINTiMINT-1391441.
STRINGi9606.ENSP00000319531.

Structurei

3D structure databases

ProteinModelPortaliP23434.
SMRiP23434. Positions 49-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvH family.Curated
Contains 1 lipoyl-binding domain.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0509.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
HOVERGENiHBG001129.
InParanoidiP23434.
KOiK02437.
OMAiTQDHEWL.
OrthoDBiEOG7RNK1M.
PhylomeDBiP23434.
TreeFamiTF300258.

Family and domain databases

HAMAPiMF_00272. GcvH.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR11715. PTHR11715. 1 hit.
PfamiPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR00527. gcvH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23434-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALRVVRSVR ALLCTLRAVP SPAAPCPPRP WQLGVGAVRT LRTGPALLSV
60 70 80 90 100
RKFTEKHEWV TTENGIGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQDEF
110 120 130 140 150
GALESVKAAS ELYSPLSGEV TEINEALAEN PGLVNKSCYE DGWLIKMTLS
160 170
NPSELDELMS EEAYEKYIKS IEE
Length:173
Mass (Da):18,885
Last modified:November 2, 2010 - v2
Checksum:i3CC5D09D59C1243D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211S → L.4 Publications
Corresponds to variant rs8052579 [ dbSNP | Ensembl ].
VAR_018846
Natural varianti73 – 731N → S.1 Publication
Corresponds to variant rs8177877 [ dbSNP | Ensembl ].
VAR_018847

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10933.1.
PIRiA36662. GCHUH.
RefSeqiNP_004474.2. NM_004483.4.
UniGeneiHs.546256.

Genome annotation databases

EnsembliENST00000315467; ENSP00000319531; ENSG00000140905.
GeneIDi2653.
KEGGihsa:2653.
UCSCiuc002fgd.3. human.

Polymorphism databases

DMDMi311033385.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10933.1.
PIRi A36662. GCHUH.
RefSeqi NP_004474.2. NM_004483.4.
UniGenei Hs.546256.

3D structure databases

ProteinModelPortali P23434.
SMRi P23434. Positions 49-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108923. 3 interactions.
IntActi P23434. 3 interactions.
MINTi MINT-1391441.
STRINGi 9606.ENSP00000319531.

Chemistry

DrugBanki DB00145. Glycine.

PTM databases

PhosphoSitei P23434.

Polymorphism databases

DMDMi 311033385.

Proteomic databases

MaxQBi P23434.
PaxDbi P23434.
PRIDEi P23434.

Protocols and materials databases

DNASUi 2653.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315467 ; ENSP00000319531 ; ENSG00000140905 .
GeneIDi 2653.
KEGGi hsa:2653.
UCSCi uc002fgd.3. human.

Organism-specific databases

CTDi 2653.
GeneCardsi GC16M081115.
GeneReviewsi GCSH.
H-InvDB HIX0013270.
HIX0028692.
HGNCi HGNC:4208. GCSH.
HPAi HPA041368.
MIMi 238330. gene.
605899. phenotype.
neXtProti NX_P23434.
Orphaneti 289863. Atypical glycine encephalopathy.
289860. Infantile glycine encephalopathy.
289857. Neonatal glycine encephalopathy.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0509.
GeneTreei ENSGT00390000011666.
HOGENOMi HOG000239392.
HOVERGENi HBG001129.
InParanoidi P23434.
KOi K02437.
OMAi TQDHEWL.
OrthoDBi EOG7RNK1M.
PhylomeDBi P23434.
TreeFami TF300258.

Enzyme and pathway databases

SABIO-RK P23434.

Miscellaneous databases

GeneWikii GCSH.
GenomeRNAii 2653.
NextBioi 10484.
PROi P23434.
SOURCEi Search...

Gene expression databases

Bgeei P23434.
CleanExi HS_GCSH.
ExpressionAtlasi P23434. baseline.
Genevestigatori P23434.

Family and domain databases

HAMAPi MF_00272. GcvH.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view ]
PANTHERi PTHR11715. PTHR11715. 1 hit.
Pfami PF01597. GCV_H. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR00527. gcvH. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, LIPOYLATION AT LYS-107.
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGCSH_HUMAN
AccessioniPrimary (citable) accession number: P23434
Secondary accession number(s): Q9H1E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 156 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3