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Protein

Glycine cleavage system H protein, mitochondrial

Gene

Gcsh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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) (By similarity).By similarity

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915383. Gcsh.

Subcellular locationi

GO - Cellular componenti

  • glycine cleavage complex Source: InterPro
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545MitochondrionBy similarityAdd
BLAST
Chaini46 – 170125Glycine cleavage system H protein, mitochondrialPRO_0000010724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

EPDiQ91WK5.
PaxDbiQ91WK5.
PRIDEiQ91WK5.

PTM databases

iPTMnetiQ91WK5.
PhosphoSiteiQ91WK5.

Expressioni

Gene expression databases

GenevisibleiQ91WK5. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ91WK5. 2 interactions.
MINTiMINT-4125893.
STRINGi10090.ENSMUSP00000037131.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 503Combined sources
Beta strandi54 – 607Combined sources
Beta strandi63 – 686Combined sources
Helixi70 – 767Combined sources
Beta strandi78 – 836Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi115 – 1206Combined sources
Turni124 – 1263Combined sources
Helixi130 – 1334Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi142 – 1454Combined sources
Helixi151 – 1533Combined sources
Beta strandi155 – 1573Combined sources
Helixi158 – 1669Combined sources
Turni167 – 1693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EDGNMR-A48-170[»]
ProteinModelPortaliQ91WK5.
SMRiQ91WK5. Positions 41-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91WK5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 14583Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ91WK5.
KOiK02437.
OMAiNTDPYGE.
OrthoDBiEOG7RNK1M.
TreeFamiTF300258.

Family and domain databases

HAMAPiMF_00272. GcvH.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
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.

Q91WK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQVSRSLR VVAYSLRTAL TFCSPRPCVP SAAAVRSLRT GSALLSVRKF
60 70 80 90 100
TEKHEWITTE EGIGTVGISN FAQEALGDVV YCSLPEVGTK LKKQEEFGAL
110 120 130 140 150
ESVKAASELY SPLSGEVTEV NEALAENPGL VNKSCYEDGW LIKMTLSDPS
160 170
EMDELMSEEA YEKYVKSIEE
Length:170
Mass (Da):18,637
Last modified:October 3, 2012 - v2
Checksum:iC0464972C79C00EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211T → A in AAH14745 (PubMed:15489334).Curated
Sequence conflicti152 – 1521M → L in AAH14745 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003788 mRNA. Translation: BAB22996.2.
AK019983 mRNA. Translation: BAB31951.1.
AK050373 mRNA. Translation: BAC34217.1.
AC162858 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11574.1.
BC014745 mRNA. Translation: AAH14745.1.
CCDSiCCDS22696.1.
RefSeqiNP_080848.1. NM_026572.3.
UniGeneiMm.258462.

Genome annotation databases

EnsembliENSMUST00000040484; ENSMUSP00000037131; ENSMUSG00000034424.
GeneIDi68133.
KEGGimmu:68133.
UCSCiuc009not.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003788 mRNA. Translation: BAB22996.2.
AK019983 mRNA. Translation: BAB31951.1.
AK050373 mRNA. Translation: BAC34217.1.
AC162858 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11574.1.
BC014745 mRNA. Translation: AAH14745.1.
CCDSiCCDS22696.1.
RefSeqiNP_080848.1. NM_026572.3.
UniGeneiMm.258462.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EDGNMR-A48-170[»]
ProteinModelPortaliQ91WK5.
SMRiQ91WK5. Positions 41-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91WK5. 2 interactions.
MINTiMINT-4125893.
STRINGi10090.ENSMUSP00000037131.

PTM databases

iPTMnetiQ91WK5.
PhosphoSiteiQ91WK5.

Proteomic databases

EPDiQ91WK5.
PaxDbiQ91WK5.
PRIDEiQ91WK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040484; ENSMUSP00000037131; ENSMUSG00000034424.
GeneIDi68133.
KEGGimmu:68133.
UCSCiuc009not.1. mouse.

Organism-specific databases

CTDi2653.
MGIiMGI:1915383. Gcsh.

Phylogenomic databases

eggNOGiKOG3373. Eukaryota.
COG0509. LUCA.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
HOVERGENiHBG001129.
InParanoidiQ91WK5.
KOiK02437.
OMAiNTDPYGE.
OrthoDBiEOG7RNK1M.
TreeFamiTF300258.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ91WK5.
NextBioi326496.
PROiQ91WK5.
SOURCEiSearch...

Gene expression databases

GenevisibleiQ91WK5. MM.

Family and domain databases

HAMAPiMF_00272. GcvH.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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].
    Strain: FVB/N.
    Tissue: Kidney.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Testis.
  6. "Solution structure of the GCV_H domain from mouse glycine."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 41-170.

Entry informationi

Entry nameiGCSH_MOUSE
AccessioniPrimary (citable) accession number: Q91WK5
Secondary accession number(s): Q9CY75, Q9D197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 3, 2012
Last modified: March 16, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.