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Protein

FYVE, RhoGEF and PH domain-containing protein 2

Gene

Fgd2

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

Functioni

Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Activates JNK1 via CDC42 but not RAC1. Binds to phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri458 – 518FYVE-typePROSITE-ProRule annotationAdd BLAST61

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol phosphate binding Source: MGI
  • Rho guanyl-nucleotide exchange factor activity Source: MGI

GO - Biological processi

  • positive regulation of JUN kinase activity Source: MGI
  • regulation of Rho protein signal transduction Source: InterPro

Keywordsi

Molecular functionGuanine-nucleotide releasing factor
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-193648 NRAGE signals death through JNK
R-MMU-194840 Rho GTPase cycle
R-MMU-416482 G alpha (12/13) signalling events

Names & Taxonomyi

Protein namesi
Recommended name:
FYVE, RhoGEF and PH domain-containing protein 2
Gene namesi
Name:Fgd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1347084 Fgd2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi287S → A: No effect on early endosome localization and reduced JNK1 activation; when associated with A-288. 1 Publication1
Mutagenesisi288N → A: No effect on early endosome localization and reduced JNK1 activation; when associated with A-287. 1 Publication1
Mutagenesisi454Q → K: Loss of early endosome localization; when associated with T-455. 1 Publication1
Mutagenesisi455W → T: Loss of early endosome localization; when associated with K-454. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000809431 – 655FYVE, RhoGEF and PH domain-containing protein 2Add BLAST655

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineCombined sources1
Modified residuei39PhosphoserineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei644PhosphothreonineCombined sources1
Modified residuei654PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BY35
PaxDbiQ8BY35
PeptideAtlasiQ8BY35
PRIDEiQ8BY35

PTM databases

iPTMnetiQ8BY35
PhosphoSitePlusiQ8BY35

Expressioni

Tissue specificityi

Lymph node, spleen, B-lymphocytes and macrophages (at protein level). Expressed at high levels in lymph node, spleen, B-lymphocytes and bone marrow macrophages. Expressed at lower levels in mature bone marrow dendritic cells. In both immature and mature B-cells, expression is down-regulated by prior B-cell receptor signaling. Expression remains high in resting B and memory cells but declines upon differentiation into plasma cells.2 Publications

Gene expression databases

BgeeiENSMUSG00000024013
CleanExiMM_FGD2
ExpressionAtlasiQ8BY35 baseline and differential
GenevisibleiQ8BY35 MM

Interactioni

GO - Molecular functioni

  • Rho guanyl-nucleotide exchange factor activity Source: MGI

Protein-protein interaction databases

BioGridi204940, 1 interactor
STRINGi10090.ENSMUSP00000024810

Structurei

3D structure databases

ProteinModelPortaliQ8BY35
SMRiQ8BY35
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini102 – 290DHPROSITE-ProRule annotationAdd BLAST189
Domaini319 – 418PH 1PROSITE-ProRule annotationAdd BLAST100
Domaini544 – 641PH 2PROSITE-ProRule annotationAdd BLAST98

Domaini

The FYVE-type zinc-finger is necessary for early endosome localization. Recruitment to endosomal membranes via this domain requires the presence of phosphatidylinositol 3-phosphate or other phosphatidylinositides.1 Publication
The PH domain is necessary for localization to the ruffle membrane. Recruitment to ruffle membrane occurs through binding of phosphoinositides by the PH domain. This domain also contributes to the lipid-binding properties of the protein.1 Publication
The DH domain is necessary for its ability to activate JNK1 via CDC42.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri458 – 518FYVE-typePROSITE-ProRule annotationAdd BLAST61

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4424 Eukaryota
ENOG410XRXV LUCA
GeneTreeiENSGT00890000139342
HOGENOMiHOG000220866
HOVERGENiHBG007506
InParanoidiQ8BY35
KOiK05721
OMAiDPMERYL
OrthoDBiEOG091G03FU
PhylomeDBiQ8BY35
TreeFamiTF316247

Family and domain databases

CDDicd13386 PH1_FGD2, 1 hit
cd13236 PH2_FGD1-4, 1 hit
cd00160 RhoGEF, 1 hit
Gene3Di1.20.900.10, 1 hit
2.30.29.30, 2 hits
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR035941 FGD1-4_PH2
IPR037797 FGD2_PH1
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000306 Znf_FYVE
IPR017455 Znf_FYVE-rel
IPR011011 Znf_FYVE_PHD
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF01363 FYVE, 1 hit
PF00169 PH, 2 hits
PF00621 RhoGEF, 1 hit
SMARTiView protein in SMART
SM00064 FYVE, 1 hit
SM00233 PH, 2 hits
SM00325 RhoGEF, 1 hit
SUPFAMiSSF48065 SSF48065, 1 hit
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50010 DH_2, 1 hit
PS50003 PH_DOMAIN, 2 hits
PS50178 ZF_FYVE, 1 hit

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8BY35-1) [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
MERACEKQDS VCNLVAVFEN NRTPGEAPGS HSLEDQPHSP EHQLSLSPEP
60 70 80 90 100
WEAPPVKEAL KSEFRPVSRT YLSSLKNKLS SGAWRRSCQP GVSPGPETQE
110 120 130 140 150
PEEKRVVREL LETEQAYVAR LHLLDQVFFQ ELLREAGRSK AFPEDVVKLI
160 170 180 190 200
FSNISSIYRF HAQFFLPELQ RRVDDWAATP RIGDVIQKLA PFLKMYSEYV
210 220 230 240 250
KNFERAAELL ATWMDKSQPF QEVVTRIQCS EASSSLTLQH HMLEPVQRIP
260 270 280 290 300
RYELLLKEYV QKLPAQAPDL EDAQRALDMI FSAAQHSNAA IAEMERLQGL
310 320 330 340 350
WDVYQRLGLE DDIVDPSNTL LREGPVLKIS FRRSDPMERY LVLFNNMLLY
360 370 380 390 400
CVPRVLQVGA QFQVRTRIDV AGMKVRELTD AEFPHSFLVS GKQRTLELQA
410 420 430 440 450
RSRDEMVSWM QACQAAIDQV EKRSETFKAA VQGPQGDTQE PKPQVEELGL
460 470 480 490 500
RAPQWVRDKM VTMCMRCQEP FNALTRRRHH CRACGYVVCA KCSDYRAELK
510 520 530 540 550
YDSNRPNRVC LTCYTFLTGN VLPQGKEDKR RGILEKEASA APEQSLVCSF
560 570 580 590 600
LQLIGDKCSR SLPRSWCVIP RDDPLVLYVY AAPQDTKAHT SIPLLGYQVI
610 620 630 640 650
SGPQGDPRVF QLQQSGQQYT FKAESVELQG RWVTAIKRAA SGRTPEGPDE

EDVSD
Length:655
Mass (Da):74,634
Last modified:March 1, 2003 - v1
Checksum:iF5272F107A29BDBE
GO
Isoform 2 (identifier: Q8BY35-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.

Note: No experimental confirmation available.
Show »
Length:461
Mass (Da):52,531
Checksum:iEFAFDF5AE884928C
GO

Sequence cautioni

The sequence AAC35430 differs from that shown. Reason: Frameshift at position 606.Curated
The sequence AAP45200 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39S → I in ABC70180 (PubMed:10458911).Curated1
Sequence conflicti39S → I in AAC35430 (Ref. 2) Curated1
Sequence conflicti543E → D in ABC70180 (PubMed:10458911).Curated1
Sequence conflicti560 – 561RS → ST in BAE33605 (PubMed:16141072).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0130731 – 194Missing in isoform 2. 1 PublicationAdd BLAST194

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017368 mRNA Translation: AAC35430.1 Frameshift.
DQ344523 mRNA Translation: ABC70180.1
AK042260 mRNA Translation: BAC31206.1
AK156151 mRNA Translation: BAE33605.1
AY301264 Genomic DNA Translation: AAP45199.1
AY301264 Genomic DNA Translation: AAP45200.1 Sequence problems.
BC021845 mRNA Translation: AAH21845.1
CCDSiCCDS37537.1 [Q8BY35-1]
RefSeqiNP_001153010.1, NM_001159538.1
NP_038738.2, NM_013710.4 [Q8BY35-1]
XP_006524363.1, XM_006524300.3 [Q8BY35-2]
XP_011244775.1, XM_011246473.2 [Q8BY35-2]
UniGeneiMm.279187

Genome annotation databases

EnsembliENSMUST00000024810; ENSMUSP00000024810; ENSMUSG00000024013 [Q8BY35-1]
GeneIDi26382
KEGGimmu:26382
UCSCiuc008bsx.2 mouse [Q8BY35-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiFGD2_MOUSE
AccessioniPrimary (citable) accession number: Q8BY35
Secondary accession number(s): O88841
, Q2L9D2, Q3U195, Q7TSE3, Q8VDH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: March 28, 2018
This is version 124 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health