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Protein

Ganglioside-induced differentiation-associated protein 1

Gene

Gdap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the mitochondrial network by promoting mitochondrial fission.By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ganglioside-induced differentiation-associated protein 1
Short name:
GDAP1
Gene namesi
Name:Gdap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1338002. Gdap1.

Subcellular locationi

  • Mitochondrion outer membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasm 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei292 – 31221HelicalSequence analysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Ganglioside-induced differentiation-associated protein 1PRO_0000186039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki50 – 50Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki172 – 172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki173 – 173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki188 – 188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki190 – 190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei203 – 2031N6-acetyllysine; alternateBy similarity
Cross-linki203 – 203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki206 – 206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki207 – 207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO88741.
PaxDbiO88741.
PRIDEiO88741.

PTM databases

iPTMnetiO88741.
PhosphoSiteiO88741.

Expressioni

Tissue specificityi

Expressed in brain, spinal cord, muscles and intestinal villi. In the central nervous system expressed most prominently in the cortex, cerebellum, thalamus, olfactory bulb, and spinal cord. Expressed also in sciatic nerves and in dorsal root ganglia.1 Publication

Developmental stagei

First expressed at embryonic stage E13. Levels then increase gradually to reach maximum levels at adulthood.

Inductioni

Increased expression during neural differentiation.1 Publication

Gene expression databases

BgeeiO88741.
ExpressionAtlasiO88741. baseline and differential.
GenevisibleiO88741. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiO88741. 2 interactions.
MINTiMINT-4095889.
STRINGi10090.ENSMUSP00000026879.

Structurei

3D structure databases

ProteinModelPortaliO88741.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 10582GST N-terminalAdd
BLAST
Domaini153 – 309157GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni320 – 35839Required for mitochondrial localizationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4420. Eukaryota.
ENOG410YE2J. LUCA.
GeneTreeiENSGT00510000046788.
HOGENOMiHOG000231002.
HOVERGENiHBG051717.
InParanoidiO88741.
OMAiDMKRINI.
OrthoDBiEOG70GMG0.
PhylomeDBiO88741.
TreeFamiTF327072.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O88741-1) [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
MARRQDEARA GVPLRVEGPP DKEVHLILYH WTHSFSSQKV RLVIAEKALK
60 70 80 90 100
CEEHDVSLPL SEHNEPWFMR LNSAGEVPVL VHGENIICEA TQIIDYLEQT
110 120 130 140 150
FLDERTPRLM PDEGSMYYPR VQHYRELLDS LPMDAYTHGC ILHPELTVDS
160 170 180 190 200
MIPAYATTRI RSQIGNTESE LKKLAEENPD LQEAYIAKQK RLKSKLLDHD
210 220 230 240 250
NVKYLKKILD ELEKVLDQVE TELQRRNEET PEEGNQPWLC GESFTLADVS
260 270 280 290 300
LAVTLHRLKF LGFARRNWGH GKRPNLETYY ERVLKRKTFN KVLGHVNNIL
310 320 330 340 350
ISAVLPTAFR VAKKRAPKVL GSTLVVGLLV GMGYFAFMLF RRRLGSMILA

LRPRPNYF
Length:358
Mass (Da):41,311
Last modified:November 1, 1998 - v1
Checksum:i7B533CB34138891F
GO
Isoform 2 (identifier: O88741-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     163-163: Q → M
     164-358: Missing.

Note: No experimental confirmation available.
Show »
Length:163
Mass (Da):18,839
Checksum:i9EB6A9DF30B75DC3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei163 – 1631Q → M in isoform 2. 1 PublicationVSP_008791
Alternative sequencei164 – 358195Missing in isoform 2. 1 PublicationVSP_008792Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17850 mRNA. Translation: CAA76893.1.
AK020988 mRNA. Translation: BAB32270.1.
AK045460 mRNA. Translation: BAC32380.1.
AK049655 mRNA. Translation: BAC33861.1.
AK083814 mRNA. Translation: BAC39027.1.
BC048177 mRNA. Translation: AAH48177.1.
BC051135 mRNA. Translation: AAH51135.1.
CCDSiCCDS14834.1. [O88741-1]
RefSeqiNP_034397.1. NM_010267.3. [O88741-1]
UniGeneiMm.18218.

Genome annotation databases

EnsembliENSMUST00000026879; ENSMUSP00000026879; ENSMUSG00000025777. [O88741-1]
GeneIDi14545.
KEGGimmu:14545.
UCSCiuc007akb.2. mouse. [O88741-2]
uc007akc.2. mouse. [O88741-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17850 mRNA. Translation: CAA76893.1.
AK020988 mRNA. Translation: BAB32270.1.
AK045460 mRNA. Translation: BAC32380.1.
AK049655 mRNA. Translation: BAC33861.1.
AK083814 mRNA. Translation: BAC39027.1.
BC048177 mRNA. Translation: AAH48177.1.
BC051135 mRNA. Translation: AAH51135.1.
CCDSiCCDS14834.1. [O88741-1]
RefSeqiNP_034397.1. NM_010267.3. [O88741-1]
UniGeneiMm.18218.

3D structure databases

ProteinModelPortaliO88741.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88741. 2 interactions.
MINTiMINT-4095889.
STRINGi10090.ENSMUSP00000026879.

PTM databases

iPTMnetiO88741.
PhosphoSiteiO88741.

Proteomic databases

MaxQBiO88741.
PaxDbiO88741.
PRIDEiO88741.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026879; ENSMUSP00000026879; ENSMUSG00000025777. [O88741-1]
GeneIDi14545.
KEGGimmu:14545.
UCSCiuc007akb.2. mouse. [O88741-2]
uc007akc.2. mouse. [O88741-1]

Organism-specific databases

CTDi54332.
MGIiMGI:1338002. Gdap1.

Phylogenomic databases

eggNOGiKOG4420. Eukaryota.
ENOG410YE2J. LUCA.
GeneTreeiENSGT00510000046788.
HOGENOMiHOG000231002.
HOVERGENiHBG051717.
InParanoidiO88741.
OMAiDMKRINI.
OrthoDBiEOG70GMG0.
PhylomeDBiO88741.
TreeFamiTF327072.

Miscellaneous databases

PROiO88741.
SOURCEiSearch...

Gene expression databases

BgeeiO88741.
ExpressionAtlasiO88741. baseline and differential.
GenevisibleiO88741. MM.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of 10 differentially expressed cDNAs in differentiated Neuro2a cells induced through controlled expression of the GD3 synthase gene."
    Liu H., Nakagawa T., Kanematsu T., Uchida T., Tsuji S.
    J. Neurochem. 72:1781-1790(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
    Strain: ICR.
    Tissue: Brain.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain, Spinal cord and Spinal ganglion.
  3. "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 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 162-172; 215-225 AND 292-310, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease."
    Niemann A., Ruegg M., La Padula V., Schenone A., Suter U.
    J. Cell Biol. 170:1067-1078(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiGDAP1_MOUSE
AccessioniPrimary (citable) accession number: O88741
Secondary accession number(s): Q8C7Q5, Q9CTN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

While belonging to the GST superfamily, it lacks glutathione transferase activity.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.