Skip Header

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

Glycine cleavage system H protein, mitochondrial

Gene

GCSH

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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).

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-6783984. Glycine degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H protein, mitochondrial
Alternative name(s):
Lipoic acid-containing protein
Gene namesi
Name:GCSH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 48Mitochondrion3 PublicationsAdd BLAST48
ChainiPRO_000001072249 – 173Glycine cleavage system H protein, mitochondrialAdd BLAST125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei107N6-lipoyllysinePROSITE-ProRule annotation1 Publication1

Proteomic databases

PaxDbiP20821.
PeptideAtlasiP20821.
PRIDEiP20821.

Expressioni

Gene expression databases

BgeeiENSBTAG00000006795.

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

STRINGi9913.ENSBTAP00000008936.

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi57 – 63Combined sources7
Beta strandi66 – 71Combined sources6
Helixi73 – 79Combined sources7
Beta strandi81 – 86Combined sources6
Beta strandi99 – 107Combined sources9
Beta strandi109 – 113Combined sources5
Beta strandi115 – 123Combined sources9
Helixi125 – 127Combined sources3
Helixi133 – 136Combined sources4
Turni138 – 142Combined sources5
Beta strandi145 – 150Combined sources6
Helixi152 – 157Combined sources6
Beta strandi158 – 160Combined sources3
Helixi161 – 172Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KLRX-ray0.88A49-173[»]
3WDNX-ray0.86A49-173[»]
ProteinModelPortaliP20821.
SMRiP20821.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini66 – 148Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST83

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG3373. Eukaryota.
COG0509. LUCA.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
HOVERGENiHBG001129.
InParanoidiP20821.
KOiK02437.
OMAiNTDPYGE.
OrthoDBiEOG091G14BI.
TreeFamiTF300258.

Family and domain databases

CDDicd06848. GCS_H. 1 hit.
HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR033753. GCV_H/Fam206.
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.

P20821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAVRSVR AAVGGLRAIS APSAPCLPRP WGLRAGAVRE LRTGPALLSV
60 70 80 90 100
RKFTEKHEWV TTENGVGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQEEF
110 120 130 140 150
GALESVKAAS ELYSPLSGEV TEINKALAEN PGLVNKSCYE DGWLIKMTFS
160 170
NPSELDELMS EEAYEKYIKS IEE
Length:173
Mass (Da):18,791
Last modified:February 1, 1991 - v1
Checksum:i6FBF64293B465D22
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49S → G AA sequence (PubMed:2553401).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58361 mRNA. Translation: AAA62710.1.
BC120070 mRNA. Translation: AAI20071.1.
PIRiA39214. GCBOH.
RefSeqiNP_777269.1. NM_174844.1.
XP_005218441.1. XM_005218384.2.
UniGeneiBt.4195.

Genome annotation databases

EnsembliENSBTAT00000008936; ENSBTAP00000008936; ENSBTAG00000006795.
GeneIDi317723.
KEGGibta:317723.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58361 mRNA. Translation: AAA62710.1.
BC120070 mRNA. Translation: AAI20071.1.
PIRiA39214. GCBOH.
RefSeqiNP_777269.1. NM_174844.1.
XP_005218441.1. XM_005218384.2.
UniGeneiBt.4195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KLRX-ray0.88A49-173[»]
3WDNX-ray0.86A49-173[»]
ProteinModelPortaliP20821.
SMRiP20821.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008936.

Proteomic databases

PaxDbiP20821.
PeptideAtlasiP20821.
PRIDEiP20821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008936; ENSBTAP00000008936; ENSBTAG00000006795.
GeneIDi317723.
KEGGibta:317723.

Organism-specific databases

CTDi2653.

Phylogenomic databases

eggNOGiKOG3373. Eukaryota.
COG0509. LUCA.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
HOVERGENiHBG001129.
InParanoidiP20821.
KOiK02437.
OMAiNTDPYGE.
OrthoDBiEOG091G14BI.
TreeFamiTF300258.

Enzyme and pathway databases

ReactomeiR-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-6783984. Glycine degradation.

Miscellaneous databases

EvolutionaryTraceiP20821.

Gene expression databases

BgeeiENSBTAG00000006795.

Family and domain databases

CDDicd06848. GCS_H. 1 hit.
HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR033753. GCV_H/Fam206.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiGCSH_BOVIN
AccessioniPrimary (citable) accession number: P20821
Secondary accession number(s): Q0P5G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:3080335 and PubMed:2553401) thought to be a ferredoxin.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.