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

F-BAR domain only protein 2

Gene

FCHO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.4 Publications

GO - Molecular functioni

GO - Biological processi

  • clathrin coat assembly Source: UniProtKB
  • clathrin-dependent endocytosis Source: UniProtKB
  • membrane invagination Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Enzyme and pathway databases

ReactomeiR-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
F-BAR domain only protein 2
Gene namesi
Name:FCHO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:25180. FCHO2.

Subcellular locationi

GO - Cellular componenti

  • clathrin-coated pit Source: UniProtKB
  • clathrin-coated vesicle Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10F → E: Binds preferentially to larger liposomes. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000157107.
PharmGKBiPA134911830.

Polymorphism and mutation databases

BioMutaiFCHO2.
DMDMi119369487.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002660051 – 810F-BAR domain only protein 2Add BLAST810

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi147Interchain (with C-273)1 Publication
Disulfide bondi273Interchain (with C-147)1 Publication
Modified residuei312PhosphoserineBy similarity1
Modified residuei385PhosphothreonineCombined sources1
Modified residuei387PhosphoserineCombined sources1
Modified residuei394PhosphoserineCombined sources1
Modified residuei403PhosphoserineCombined sources1
Modified residuei488PhosphoserineCombined sources1
Modified residuei493PhosphoserineBy similarity1
Modified residuei496PhosphoserineCombined sources1
Modified residuei508PhosphoserineCombined sources1
Modified residuei510PhosphoserineBy similarity1
Modified residuei511PhosphoserineCombined sources1
Modified residuei533PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated. Mainly undergoes monoubiquitination but also polyubiquitination (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ0JRZ9.
MaxQBiQ0JRZ9.
PaxDbiQ0JRZ9.
PeptideAtlasiQ0JRZ9.
PRIDEiQ0JRZ9.

PTM databases

iPTMnetiQ0JRZ9.
PhosphoSitePlusiQ0JRZ9.

Expressioni

Gene expression databases

BgeeiENSG00000157107.
CleanExiHS_FCHO2.
ExpressionAtlasiQ0JRZ9. baseline and differential.
GenevisibleiQ0JRZ9. HS.

Organism-specific databases

HPAiHPA037685.
HPA037686.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. May form homotetramer. Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit those scaffolding proteins which in turn may interact with the adaptor protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via DPF motifs); mediates LDL receptor/LDLR endocytosis.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab2P980784EBI-2609756,EBI-1391846From a different organism.
EPS15P425663EBI-2609756,EBI-396684

Protein-protein interaction databases

BioGridi125437. 24 interactors.
DIPiDIP-29488N.
IntActiQ0JRZ9. 26 interactors.
STRINGi9606.ENSP00000393776.

Structurei

Secondary structure

1810
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 9Combined sources5
Helixi17 – 61Combined sources45
Beta strandi67 – 69Combined sources3
Helixi70 – 72Combined sources3
Helixi73 – 118Combined sources46
Helixi120 – 156Combined sources37
Helixi160 – 244Combined sources85
Helixi247 – 258Combined sources12
Beta strandi261 – 263Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V0OX-ray2.30A/B/C3-274[»]
ProteinModelPortaliQ0JRZ9.
SMRiQ0JRZ9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0JRZ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 250F-BARPROSITE-ProRule annotationAdd BLAST248
Domaini542 – 809MHDPROSITE-ProRule annotationAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 274Mediates dimerization and binding to membranes enriched in Pi(4,5)-P2 and induces their tubulationAdd BLAST272
Regioni521 – 810Mediates interaction with DAB2, EPS15, EPS15R and ITSN1Add BLAST290

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili87 – 156Sequence analysisAdd BLAST70

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi434 – 519Ser-richAdd BLAST86

Sequence similaritiesi

Belongs to the FCHO family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2398. Eukaryota.
ENOG410Y7RY. LUCA.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ0JRZ9.
KOiK20042.
OMAiSSTKDFW.
OrthoDBiEOG091G0AB1.
PhylomeDBiQ0JRZ9.
TreeFamiTF328986.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS51741. F_BAR. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q0JRZ9-1) [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
MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS
60 70 80 90 100
RSMTKLAKSA SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE
110 120 130 140 150
VQKYGEEQVK SHKKTKEEVA GTLEAVQTIQ SITQALQKSK ENYNAKCVEQ
160 170 180 190 200
ERLKKEGATQ REIEKAAVKS KKATDTYKLY VEKYALAKAD FEQKMTETAQ
210 220 230 240 250
KFQDIEETHL IHIKEIIGSL SNAIKEIHLQ IGQVHEEFIN NMANTTVESL
260 270 280 290 300
IQKFAESKGT GKERPGLIEF EECDTASAVE GIKPRKRKTF ALPGIIKKEK
310 320 330 340 350
DAESVECPDA DSLNIPDVDE EGYSIKPETN QNDTKENHFY SSSDSDSEDE
360 370 380 390 400
EPKKYRIEIK PMHPNNSHHT MASLDELKVS IGNITLSPAI SRHSPVQMNR
410 420 430 440 450
NLSNEELTKS KPSAPPNEKG TSDLLAWDPL FGPSLDSSSS SSLTSSSSAR
460 470 480 490 500
PTTPLSVGTI VPPPRPASRP KLTSGKLSGI NEIPRPFSPP VTSNTSPPPA
510 520 530 540 550
APLARAESSS SISSSASLSA ANTPTVGVSR GPSPVSLGNQ DTLPVAVALT
560 570 580 590 600
ESVNAYFKGA DPTKCIVKIT GDMTMSFPSG IIKVFTSNPT PAVLCFRVKN
610 620 630 640 650
ISRLEQILPN AQLVFSDPSQ CDSNTKDFWM NMQAVTVYLK KLSEQNPAAS
660 670 680 690 700
YYNVDVLKYQ VSSNGIQSTP LNLATYWKCS ASTTDLRVDY KYNPEAMVAP
710 720 730 740 750
SVLSNIQVVV PVDGGVTNMQ SLPPAIWNAE QMKAFWKLSS ISEKSENGGS
760 770 780 790 800
GSLRAKFDLS EGPSKPTTLA VQFLSEGSTL SGVDFELVGT GYRLSLIKKR
810
FATGRYLADC
Length:810
Mass (Da):88,924
Last modified:December 12, 2006 - v2
Checksum:i0FCFBC5D814B5242
GO
Isoform 2 (identifier: Q0JRZ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     306-373: ECPDADSLNI...PNNSHHTMAS → WSFTVVAQVG...PYWPGWSRTP
     374-810: Missing.

Note: No experimental confirmation available.
Show »
Length:375
Mass (Da):43,036
Checksum:i070F5C2EE86C95CF
GO
Isoform 3 (identifier: Q0JRZ9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-232: Missing.

Note: No experimental confirmation available.
Show »
Length:777
Mass (Da):85,146
Checksum:iD316D1D723C3698A
GO

Sequence cautioni

The sequence AAH14311 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6F → L in AL831971 (PubMed:17974005).Curated1
Sequence conflicti286K → E in BAG58162 (PubMed:14702039).Curated1
Sequence conflicti439S → P in BAF84471 (PubMed:14702039).Curated1
Sequence conflicti462P → Q in AL831971 (PubMed:17974005).Curated1
Sequence conflicti617D → Y in BAG58162 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029636371M → V.Corresponds to variant rs185435dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044812200 – 232Missing in isoform 3. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_021910306 – 373ECPDA…HTMAS → WSFTVVAQVGMQWRDLGLLH SPPPRFKRFSSYLSLPSSWN YGAHHHIWLIFCIFSRDRVS PYWPGWSRTP in isoform 2. 1 PublicationAdd BLAST68
Alternative sequenceiVSP_021911374 – 810Missing in isoform 2. 1 PublicationAdd BLAST437

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK291782 mRNA. Translation: BAF84471.1.
AK295141 mRNA. Translation: BAG58162.1.
AL831971 mRNA. No translation available.
AC008972 Genomic DNA. No translation available.
AC020893 Genomic DNA. No translation available.
AC020942 Genomic DNA. No translation available.
BC014311 mRNA. Translation: AAH14311.1. Different initiation.
BC137070 mRNA. Translation: AAI37071.1.
CCDSiCCDS47230.1. [Q0JRZ9-1]
CCDS54868.1. [Q0JRZ9-3]
RefSeqiNP_001139504.1. NM_001146032.1. [Q0JRZ9-3]
NP_620137.2. NM_138782.2. [Q0JRZ9-1]
UniGeneiHs.165762.

Genome annotation databases

EnsembliENST00000430046; ENSP00000393776; ENSG00000157107. [Q0JRZ9-1]
ENST00000512348; ENSP00000427296; ENSG00000157107. [Q0JRZ9-3]
GeneIDi115548.
KEGGihsa:115548.
UCSCiuc003kcl.3. human. [Q0JRZ9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK291782 mRNA. Translation: BAF84471.1.
AK295141 mRNA. Translation: BAG58162.1.
AL831971 mRNA. No translation available.
AC008972 Genomic DNA. No translation available.
AC020893 Genomic DNA. No translation available.
AC020942 Genomic DNA. No translation available.
BC014311 mRNA. Translation: AAH14311.1. Different initiation.
BC137070 mRNA. Translation: AAI37071.1.
CCDSiCCDS47230.1. [Q0JRZ9-1]
CCDS54868.1. [Q0JRZ9-3]
RefSeqiNP_001139504.1. NM_001146032.1. [Q0JRZ9-3]
NP_620137.2. NM_138782.2. [Q0JRZ9-1]
UniGeneiHs.165762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V0OX-ray2.30A/B/C3-274[»]
ProteinModelPortaliQ0JRZ9.
SMRiQ0JRZ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125437. 24 interactors.
DIPiDIP-29488N.
IntActiQ0JRZ9. 26 interactors.
STRINGi9606.ENSP00000393776.

PTM databases

iPTMnetiQ0JRZ9.
PhosphoSitePlusiQ0JRZ9.

Polymorphism and mutation databases

BioMutaiFCHO2.
DMDMi119369487.

Proteomic databases

EPDiQ0JRZ9.
MaxQBiQ0JRZ9.
PaxDbiQ0JRZ9.
PeptideAtlasiQ0JRZ9.
PRIDEiQ0JRZ9.

Protocols and materials databases

DNASUi115548.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000430046; ENSP00000393776; ENSG00000157107. [Q0JRZ9-1]
ENST00000512348; ENSP00000427296; ENSG00000157107. [Q0JRZ9-3]
GeneIDi115548.
KEGGihsa:115548.
UCSCiuc003kcl.3. human. [Q0JRZ9-1]

Organism-specific databases

CTDi115548.
GeneCardsiFCHO2.
H-InvDBHIX0004941.
HGNCiHGNC:25180. FCHO2.
HPAiHPA037685.
HPA037686.
MIMi613438. gene.
neXtProtiNX_Q0JRZ9.
OpenTargetsiENSG00000157107.
PharmGKBiPA134911830.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2398. Eukaryota.
ENOG410Y7RY. LUCA.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ0JRZ9.
KOiK20042.
OMAiSSTKDFW.
OrthoDBiEOG091G0AB1.
PhylomeDBiQ0JRZ9.
TreeFamiTF328986.

Enzyme and pathway databases

ReactomeiR-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

ChiTaRSiFCHO2. human.
EvolutionaryTraceiQ0JRZ9.
GeneWikiiFCHO2.
GenomeRNAii115548.
PROiQ0JRZ9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157107.
CleanExiHS_FCHO2.
ExpressionAtlasiQ0JRZ9. baseline and differential.
GenevisibleiQ0JRZ9. HS.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS51741. F_BAR. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFCHO2_HUMAN
AccessioniPrimary (citable) accession number: Q0JRZ9
Secondary accession number(s): A8K6W7
, B2RNQ9, B4DHK0, E9PG79, Q0JTJ3, Q96CF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 2, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Deforms liposomes into a range of tubule diameters from 20 to 130 nm in vitro.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.