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Q0JRZ9

- FCHO2_HUMAN

UniProt

Q0JRZ9 - FCHO2_HUMAN

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
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (12 Dec 2006)
      Previous versions | rss
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    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
    4. protein binding Source: IntAct

    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

    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

    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

    ArrayExpressiQ0JRZ9.
    BgeeiQ0JRZ9.
    CleanExiHS_FCHO2.
    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. 4 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.
    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

    MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS    50
    RSMTKLAKSA SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE 100
    VQKYGEEQVK SHKKTKEEVA GTLEAVQTIQ SITQALQKSK ENYNAKCVEQ 150
    ERLKKEGATQ REIEKAAVKS KKATDTYKLY VEKYALAKAD FEQKMTETAQ 200
    KFQDIEETHL IHIKEIIGSL SNAIKEIHLQ IGQVHEEFIN NMANTTVESL 250
    IQKFAESKGT GKERPGLIEF EECDTASAVE GIKPRKRKTF ALPGIIKKEK 300
    DAESVECPDA DSLNIPDVDE EGYSIKPETN QNDTKENHFY SSSDSDSEDE 350
    EPKKYRIEIK PMHPNNSHHT MASLDELKVS IGNITLSPAI SRHSPVQMNR 400
    NLSNEELTKS KPSAPPNEKG TSDLLAWDPL FGPSLDSSSS SSLTSSSSAR 450
    PTTPLSVGTI VPPPRPASRP KLTSGKLSGI NEIPRPFSPP VTSNTSPPPA 500
    APLARAESSS SISSSASLSA ANTPTVGVSR GPSPVSLGNQ DTLPVAVALT 550
    ESVNAYFKGA DPTKCIVKIT GDMTMSFPSG IIKVFTSNPT PAVLCFRVKN 600
    ISRLEQILPN AQLVFSDPSQ CDSNTKDFWM NMQAVTVYLK KLSEQNPAAS 650
    YYNVDVLKYQ VSSNGIQSTP LNLATYWKCS ASTTDLRVDY KYNPEAMVAP 700
    SVLSNIQVVV PVDGGVTNMQ SLPPAIWNAE QMKAFWKLSS ISEKSENGGS 750
    GSLRAKFDLS EGPSKPTTLA VQFLSEGSTL SGVDFELVGT GYRLSLIKKR 800
    FATGRYLADC 810
    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. 4 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.
    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

    ArrayExpressi Q0JRZ9.
    Bgeei Q0JRZ9.
    CleanExi HS_FCHO2.
    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

    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 1, 2014
    This is version 78 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