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

Chorion-specific transcription factor GCMa

Gene

Gcm1

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

Functioni

Transcription factor that is necessary for placental development.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761Zinc 1
Metal bindingi82 – 821Zinc 2
Metal bindingi86 – 861Zinc 2
Metal bindingi113 – 1131Zinc 2
Metal bindingi116 – 1161Zinc 2
Metal bindingi125 – 1251Zinc 1
Metal bindingi152 – 1521Zinc 1
Metal bindingi154 – 1541Zinc 1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi14 – 169156GCMPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • astrocyte fate commitment Source: MGI
  • branching involved in labyrinthine layer morphogenesis Source: MGI
  • cell differentiation involved in embryonic placenta development Source: MGI
  • positive regulation of syncytium formation by plasma membrane fusion Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Chorion-specific transcription factor GCMa
Alternative name(s):
GCM motif protein 1
Short name:
mGCM1
Short name:
mGCMa
Glial cells missing homolog 1
Gene namesi
Name:Gcm1
Synonyms:Gcma
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:108045. Gcm1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nucleus Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631N → A: No effect on DNA binding. 1 Publication
Mutagenesisi63 – 631N → Q: Slight decrease of DNA binding. 1 Publication
Mutagenesisi65 – 651N → A: Strong decrease of DNA binding. 1 Publication
Mutagenesisi65 – 651N → D: Loss of DNA binding. 1 Publication
Mutagenesisi74 – 741K → A, L or M: Loss of DNA binding. 1 Publication
Mutagenesisi76 – 761C → A: Loss of transcription activation. 1 Publication
Mutagenesisi82 – 821C → A: Loss of transcription activation. 1 Publication
Mutagenesisi113 – 1131C → A: Loss of transcription activation. 1 Publication
Mutagenesisi125 – 1251C → A: Loss of transcription activation. 1 Publication
Mutagenesisi152 – 1521H → A: Loss of transcription activation. 1 Publication
Mutagenesisi154 – 1541H → A: Loss of transcription activation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Chorion-specific transcription factor GCMaPRO_0000126648Add
BLAST

Post-translational modificationi

Polyubiquitinated in the presence of UBE2D2 and FBXW2 (in vitro).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiP70348.
PRIDEiP70348.

PTM databases

iPTMnetiP70348.
PhosphoSiteiP70348.

Expressioni

Tissue specificityi

Placenta specific.1 Publication

Gene expression databases

BgeeiP70348.
CleanExiMM_GCM1.
ExpressionAtlasiP70348. baseline and differential.
GenevisibleiP70348. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024104.

Structurei

Secondary structure

1
436
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 534Combined sources
Beta strandi61 – 644Combined sources
Beta strandi72 – 765Combined sources
Beta strandi79 – 824Combined sources
Beta strandi89 – 913Combined sources
Helixi102 – 1109Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 1499Combined sources
Helixi160 – 1678Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ODHX-ray2.85A1-174[»]
ProteinModelPortaliP70348.
SMRiP70348. Positions 14-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70348.

Family & Domainsi

Sequence similaritiesi

Contains 1 GCM DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IKM6. Eukaryota.
ENOG4110IIJ. LUCA.
HOGENOMiHOG000112700.
HOVERGENiHBG039460.
InParanoidiP70348.
OMAiWDFDEEM.
OrthoDBiEOG7M3J08.
PhylomeDBiP70348.
TreeFamiTF324146.

Family and domain databases

InterProiIPR003902. Tscrpt_reg_GCM.
[Graphical view]
PfamiPF03615. GCM. 1 hit.
[Graphical view]
ProDomiPD014393. GCM_motif. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF90073. SSF90073. 1 hit.
PROSITEiPS50807. GCM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70348-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELDDFDPED KEILSWDIND VKLPQNVKTT DWFQEWPDSY VKHIYSSDDR
60 70 80 90 100
NAQRHLSSWA MRNTNNHNSR ILKKSCLGVV VCSRDCSTEE GRKIYLRPAI
110 120 130 140 150
CDKARQKQQR KSCPNCNGPL KLIPCRGHGG FPVTNFWRHD GRFIFFQSKG
160 170 180 190 200
EHDHPRPETK LEAEARRAMK KVHMASASNS LRMKGRPAAK ALPAEIPSQG
210 220 230 240 250
SLPLTWSFQE GVQLPGTYST PLIANAPQQN SLNDCLSFPK SYDLGGSTEL
260 270 280 290 300
EDPTSTLDSM KFYERCKFSS SRIYGSEEQF QPPVPGTYGD YEDLQTWNKN
310 320 330 340 350
VALGRNPSDD IYYPAYPLPV ASWPYDYFPS QNSLEHLPQQ VPSEPPAAQP
360 370 380 390 400
GCHPLWSNPG GEPYEEKVSV DLSSYVPSLT YHPPQQDPFL LTYGSPTQQQ
410 420 430
HALPGKSNRW DFDEEMACMG LDHFNNEMLL NFCSLR
Length:436
Mass (Da):49,589
Last modified:February 1, 1997 - v1
Checksum:i99F4E441800582DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111G → S in BAA13650 (PubMed:8962155).Curated
Sequence conflicti230 – 2301N → K in BAA13650 (PubMed:8962155).Curated
Sequence conflicti241 – 2411S → N in BAA13650 (PubMed:8962155).Curated
Sequence conflicti413 – 4131D → E in BAA13650 (PubMed:8962155).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59876 mRNA. Translation: AAC52822.1.
D88612 mRNA. Translation: BAA13650.1.
BC066866 mRNA. Translation: AAH66866.1.
CCDSiCCDS23356.1.
PIRiS74257.
RefSeqiNP_032129.2. NM_008103.3.
UniGeneiMm.1400.

Genome annotation databases

EnsembliENSMUST00000024104; ENSMUSP00000024104; ENSMUSG00000023333.
GeneIDi14531.
KEGGimmu:14531.
UCSCiuc009qto.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59876 mRNA. Translation: AAC52822.1.
D88612 mRNA. Translation: BAA13650.1.
BC066866 mRNA. Translation: AAH66866.1.
CCDSiCCDS23356.1.
PIRiS74257.
RefSeqiNP_032129.2. NM_008103.3.
UniGeneiMm.1400.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ODHX-ray2.85A1-174[»]
ProteinModelPortaliP70348.
SMRiP70348. Positions 14-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024104.

PTM databases

iPTMnetiP70348.
PhosphoSiteiP70348.

Proteomic databases

PaxDbiP70348.
PRIDEiP70348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024104; ENSMUSP00000024104; ENSMUSG00000023333.
GeneIDi14531.
KEGGimmu:14531.
UCSCiuc009qto.1. mouse.

Organism-specific databases

CTDi8521.
MGIiMGI:108045. Gcm1.

Phylogenomic databases

eggNOGiENOG410IKM6. Eukaryota.
ENOG4110IIJ. LUCA.
HOGENOMiHOG000112700.
HOVERGENiHBG039460.
InParanoidiP70348.
OMAiWDFDEEM.
OrthoDBiEOG7M3J08.
PhylomeDBiP70348.
TreeFamiTF324146.

Miscellaneous databases

EvolutionaryTraceiP70348.
NextBioi286180.
PROiP70348.
SOURCEiSearch...

Gene expression databases

BgeeiP70348.
CleanExiMM_GCM1.
ExpressionAtlasiP70348. baseline and differential.
GenevisibleiP70348. MM.

Family and domain databases

InterProiIPR003902. Tscrpt_reg_GCM.
[Graphical view]
PfamiPF03615. GCM. 1 hit.
[Graphical view]
ProDomiPD014393. GCM_motif. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF90073. SSF90073. 1 hit.
PROSITEiPS50807. GCM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gcm1, a mammalian homolog of Drosophila glial cells missing."
    Altshuller Y., Copeland N.G., Gilbert D.J., Jenkins N.A., Frohman M.A.
    FEBS Lett. 393:201-204(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Placenta.
  2. "The gcm-motif: a novel DNA binding motif conserved in Drosophila and mammals."
    Akiyama Y., Hosoya T., Poole A.M., Hotta Y.
    Proc. Natl. Acad. Sci. U.S.A. 93:14912-14916(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Placenta.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition."
    Cohen S.X., Moulin M., Hashemolhosseini S., Kilian K., Wegner M., Mueller C.W.
    EMBO J. 22:1835-1845(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-174 IN COMPLEX WITH DNA AND ZINC IONS, MUTAGENESIS OF ASN-63; ASN-65; LYS-74; CYS-76; CYS-82; CYS-113; CYS-125; HIS-152 AND HIS-154.

Entry informationi

Entry nameiGCM1_MOUSE
AccessioniPrimary (citable) accession number: P70348
Secondary accession number(s): O09103
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 120 of the entry and version 1 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.