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Q0JRZ9

- FCHO2_HUMAN

UniProt

Q0JRZ9 - FCHO2_HUMAN

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Protein

FCH domain only protein 2

Gene

FCHO2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  2. phosphatidylinositol binding Source: UniProtKB
  3. phosphatidylserine binding Source: UniProtKB

GO - Biological processi

  1. clathrin coat assembly Source: UniProtKB
  2. clathrin-mediated endocytosis Source: UniProtKB
  3. membrane invagination Source: UniProtKB
  4. protein localization to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
FCH domain only protein 2
Gene namesi
Name:FCHO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:25180. FCHO2.

Subcellular locationi

Membraneclathrin-coated pit By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 By similarity.By similarity

GO - Cellular componenti

  1. clathrin-coated vesicle Source: UniProtKB
  2. coated pit Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101F → E: Binds preferentially to larger liposomes. 1 Publication

Organism-specific databases

PharmGKBiPA134911830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 810810FCH domain only protein 2PRO_0000266005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi147 – 147Interchain (with C-273)1 Publication
Disulfide bondi273 – 273Interchain (with C-147)1 Publication
Modified residuei385 – 3851Phosphothreonine1 Publication
Modified residuei387 – 3871Phosphoserine2 Publications
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine3 Publications
Modified residuei488 – 4881Phosphoserine2 Publications
Modified residuei511 – 5111Phosphoserine1 Publication
Modified residuei533 – 5331Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ0JRZ9.
PaxDbiQ0JRZ9.
PRIDEiQ0JRZ9.

PTM databases

PhosphoSiteiQ0JRZ9.

Expressioni

Gene expression databases

BgeeiQ0JRZ9.
CleanExiHS_FCHO2.
ExpressionAtlasiQ0JRZ9. baseline and differential.
GenevestigatoriQ0JRZ9.

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. 7 interactions.
DIPiDIP-29488N.
IntActiQ0JRZ9. 10 interactions.
STRINGi9606.ENSP00000393776.

Structurei

Secondary structure

1
810
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 95
Helixi17 – 6145
Beta strandi67 – 693
Helixi70 – 723
Helixi73 – 11846
Helixi120 – 15637
Helixi160 – 24485
Helixi247 – 25812
Beta strandi261 – 2633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V0OX-ray2.30A/B/C3-274[»]
ProteinModelPortaliQ0JRZ9.
SMRiQ0JRZ9. Positions 3-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0JRZ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8582FCHPROSITE-ProRule annotationAdd
BLAST
Domaini542 – 809268MHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 274272Mediates dimerization and binding to membranes enriched in Pi(4,5)-P2 and induces their tubulationAdd
BLAST
Regioni521 – 810290Mediates interaction with DAB2, EPS15, EPS15R and ITSN1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili87 – 15670Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi434 – 51986Ser-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG324072.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ0JRZ9.
OMAiFNCEGTT.
OrthoDBiEOG712TVK.
PhylomeDBiQ0JRZ9.
TreeFamiTF328986.

Family and domain databases

InterProiIPR001060. 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]
PROSITEiPS50133. FCH. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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 AAH14311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61F → L in AL831971. (PubMed:17974005)Curated
Sequence conflicti286 – 2861K → E in BAG58162. (PubMed:14702039)Curated
Sequence conflicti439 – 4391S → P in BAF84471. (PubMed:14702039)Curated
Sequence conflicti462 – 4621P → Q in AL831971. (PubMed:17974005)Curated
Sequence conflicti617 – 6171D → Y in BAG58162. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti371 – 3711M → V.
Corresponds to variant rs185435 [ dbSNP | Ensembl ].
VAR_029636

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei200 – 23233Missing in isoform 3. 1 PublicationVSP_044812Add
BLAST
Alternative sequencei306 – 37368ECPDA…HTMAS → WSFTVVAQVGMQWRDLGLLH SPPPRFKRFSSYLSLPSSWN YGAHHHIWLIFCIFSRDRVS PYWPGWSRTP in isoform 2. 1 PublicationVSP_021910Add
BLAST
Alternative sequencei374 – 810437Missing in isoform 2. 1 PublicationVSP_021911Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi119369487.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS47230.1. [Q0JRZ9-1 ]
CCDS54868.1. [Q0JRZ9-3 ]
RefSeqi NP_001139504.1. NM_001146032.1. [Q0JRZ9-3 ]
NP_620137.2. NM_138782.2. [Q0JRZ9-1 ]
UniGenei Hs.165762.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V0O X-ray 2.30 A/B/C 3-274 [» ]
ProteinModelPortali Q0JRZ9.
SMRi Q0JRZ9. Positions 3-274.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125437. 7 interactions.
DIPi DIP-29488N.
IntActi Q0JRZ9. 10 interactions.
STRINGi 9606.ENSP00000393776.

PTM databases

PhosphoSitei Q0JRZ9.

Polymorphism databases

DMDMi 119369487.

Proteomic databases

MaxQBi Q0JRZ9.
PaxDbi Q0JRZ9.
PRIDEi Q0JRZ9.

Protocols and materials databases

DNASUi 115548.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000430046 ; ENSP00000393776 ; ENSG00000157107 . [Q0JRZ9-1 ]
ENST00000512348 ; ENSP00000427296 ; ENSG00000157107 . [Q0JRZ9-3 ]
GeneIDi 115548.
KEGGi hsa:115548.
UCSCi uc003kcl.3. human. [Q0JRZ9-1 ]

Organism-specific databases

CTDi 115548.
GeneCardsi GC05P072287.
H-InvDB HIX0004941.
HGNCi HGNC:25180. FCHO2.
HPAi HPA037685.
HPA037686.
MIMi 613438. gene.
neXtProti NX_Q0JRZ9.
PharmGKBi PA134911830.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324072.
GeneTreei ENSGT00510000046419.
HOGENOMi HOG000231544.
HOVERGENi HBG081524.
InParanoidi Q0JRZ9.
OMAi FNCEGTT.
OrthoDBi EOG712TVK.
PhylomeDBi Q0JRZ9.
TreeFami TF328986.

Miscellaneous databases

ChiTaRSi FCHO2. human.
EvolutionaryTracei Q0JRZ9.
GeneWikii FCHO2.
GenomeRNAii 115548.
NextBioi 79607.
PROi Q0JRZ9.
SOURCEi Search...

Gene expression databases

Bgeei Q0JRZ9.
CleanExi HS_FCHO2.
ExpressionAtlasi Q0JRZ9. baseline and differential.
Genevestigatori Q0JRZ9.

Family and domain databases

InterProi IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view ]
Pfami PF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view ]
SMARTi SM00055. FCH. 1 hit.
[Graphical view ]
PROSITEi PS50133. FCH. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain and Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 1 AND 2).
    Tissue: Lung and Urinary bladder.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 AND SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385; SER-387; SER-394; SER-403; SER-488 AND SER-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
    Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
    Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, INTERACTION WITH EPS15; EPS15R; ITSN1 AND ITSN2.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Characterization of the EFC/F-BAR domain protein, FCHO2."
    Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.
    Genes Cells 16:868-878(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS, INTERACTION WITH EPS15 AND AP2A1, SUBCELLULAR LOCATION.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis."
    Mulkearns E.E., Cooper J.A.
    Mol. Biol. Cell 23:1330-1342(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DAB2-MEDIATED ENDOCYTOSIS, INTERACTION WITH DAB2, SUBCELLULAR LOCATION.
  14. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
    Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
    Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPID-BINDING, INTERACTION WITH DAB2; EPS15; EPS15R AND ITSN1.
  15. "Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature."
    Henne W.M., Kent H.M., Ford M.G., Hegde B.G., Daumke O., Butler P.J., Mittal R., Langen R., Evans P.R., McMahon H.T.
    Structure 15:839-852(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-274, FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF PHE-10.

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: October 29, 2014
This is version 79 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

External Data

Dasty 3