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Q9P0V3

- SH3B4_HUMAN

UniProt

Q9P0V3 - SH3B4_HUMAN

Protein

SH3 domain-binding protein 4

Gene

SH3BP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin-mediated endocytosis. Alternatively, may acts as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy.2 Publications

    GO - Molecular functioni

    1. GDP-dissociation inhibitor activity Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. Ras GTPase binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to amino acid stimulus Source: UniProtKB
    2. endocytosis Source: UniProtKB-KW
    3. negative regulation of cell growth Source: UniProtKB
    4. negative regulation of cell proliferation Source: UniProtKB
    5. negative regulation of GTPase activity Source: UniProtKB
    6. negative regulation of TOR signaling Source: UniProtKB
    7. positive regulation of autophagy Source: UniProtKB
    8. protein localization to lysosome Source: UniProtKB
    9. regulation of catalytic activity Source: UniProtKB

    Keywords - Biological processi

    Endocytosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SH3 domain-binding protein 4
    Alternative name(s):
    EH-binding protein 10
    Transferrin receptor-trafficking protein
    Gene namesi
    Name:SH3BP4
    Synonyms:BOG25, EHB10, TTP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10826. SH3BP4.

    Subcellular locationi

    Membraneclathrin-coated pit. Cytoplasmic vesicleclathrin-coated vesicle. Nucleus Curated
    Note: Specifically associated with transferrin receptor-containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus.

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB-SubCell
    2. coated pit Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Coated pit, Cytoplasmic vesicle, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921W → A: Loss of function. Loss of targeting to the clathrin-coated pits and vesicles. Loss of interaction with DNM2, RRAGB and RRAGC. No effect on localization to the plasma membrane. 2 Publications

    Organism-specific databases

    PharmGKBiPA35734.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 963963SH3 domain-binding protein 4PRO_0000274574Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphoserine2 Publications
    Modified residuei246 – 2461Phosphoserine2 Publications
    Modified residuei637 – 6371Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated upon EGF stimulation. Phosphorylation prevents interaction with DNM2.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P0V3.
    PaxDbiQ9P0V3.
    PRIDEiQ9P0V3.

    PTM databases

    PhosphoSiteiQ9P0V3.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested with higher expression in pancreas. Expressed by retinal pigment epithelial cells (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9P0V3.
    BgeeiQ9P0V3.
    CleanExiHS_SH3BP4.
    GenevestigatoriQ9P0V3.

    Organism-specific databases

    HPAiHPA037533.

    Interactioni

    Subunit structurei

    Homodimer or homooligomer. Interacts with DNM2, EPS15, clathrin, the adapter protein complex 2/AP-2 and TFRC. Interacts with the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD; the interaction is most probably direct, preferentially occurs with their inactive GDP-bound form and is negatively regulated by amino acids.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1049513,EBI-1049513
    CIZ1Q9ULV32EBI-1049513,EBI-2652948
    DNM2P505703EBI-1049513,EBI-346547
    Dnm2P390525EBI-1049513,EBI-349613From a different organism.
    PLEKHA1Q9HB212EBI-1049513,EBI-2652984
    TFRCP027866EBI-1049513,EBI-355727

    Protein-protein interaction databases

    BioGridi117194. 31 interactions.
    IntActiQ9P0V3. 29 interactions.
    MINTiMINT-1649163.
    STRINGi9606.ENSP00000340237.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P0V3.
    SMRiQ9P0V3. Positions 61-112.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 11460SH3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SH3 domain mediates localization to the clathrin-coated pits and vesicles. The SH3 domain mediates interaction with DNM2 and the cytoplasmic part of TFRC with a lower affinity. The SH3 domain also mediates interaction with RRAGB, RRAGC and is required for the negative regulation of mTORC1.

    Sequence similaritiesi

    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG46295.
    HOGENOMiHOG000015297.
    HOVERGENiHBG057439.
    InParanoidiQ9P0V3.
    OMAiFFCRAEL.
    OrthoDBiEOG7GJ6C4.
    PhylomeDBiQ9P0V3.
    TreeFamiTF105572.

    Family and domain databases

    InterProiIPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR000906. ZU5.
    [Graphical view]
    PfamiPF07653. SH3_2. 1 hit.
    PF14604. SH3_9. 1 hit.
    PF00791. ZU5. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P0V3-1) [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

    MAAQRIRAAN SNGLPRCKSE GTLIDLSEGF SETSFNDIKV PSPSALLVDN    50
    PTPFGNAKEV IAIKDYCPTN FTTLKFSKGD HLYVLDTSGG EWWYAHNTTE 100
    MGYIPSSYVQ PLNYRNSTLS DSGMIDNLPD SPDEVAKELE LLGGWTDDKK 150
    VPGRMYSNNP FWNGVQTNPF LNGNVPVMPS LDELNPKSTV DLLLFDAGTS 200
    SFTESSSATT NSTGNIFDEL PVTNGLHAEP PVRRDNPFFR SKRSYSLSEL 250
    SVLQAKSDAP TSSSFFTGLK SPAPEQFQSR EDFRTAWLNH RKLARSCHDL 300
    DLLGQSPGWG QTQAVETNIV CKLDSSGGAV QLPDTSISIH VPEGHVAPGE 350
    TQQISMKALL DPPLELNSDR SCSISPVLEV KLSNLEVKTS IILEMKVSAE 400
    IKNDLFSKST VGLQCLRSDS KEGPYVSVPL NCSCGDTVQA QLHNLEPCMY 450
    VAVVAHGPSI LYPSTVWDFI NKKVTVGLYG PKHIHPSFKT VVTIFGHDCA 500
    PKTLLVSEVT RQAPNPAPVA LQLWGKHQFV LSRPQDLKVC MFSNMTNYEV 550
    KASEQAKVVR GFQLKLGKVS RLIFPITSQN PNELSDFTLR VQVKDDQEAI 600
    LTQFCVQTPQ PPPKSAIKPS GQRRFLKKNE VGKIILSPFA TTTKYPTFQD 650
    RPVSSLKFGK LLKTVVRQNK NHYLLEYKKG DGIALLSEER VRLRGQLWTK 700
    EWYIGYYQGR VGLVHTKNVL VVGRARPSLC SGPELSTSVL LEQILRPCKF 750
    LTYIYASVRT LLMENISSWR SFADALGYVN LPLTFFCRAE LDSEPERVAS 800
    VLEKLKEDCN NTENKERKSF QKELVMALLK MDCQGLVVRL IQDFVLLTTA 850
    VEVAQRWREL AEKLAKVSKQ QMDAYESPHR DRNGVVDSEA MWKPAYDFLL 900
    TWSHQIGDSY RDVIQELHLG LDKMKNPITK RWKHLTGTLI LVNSLDVLRA 950
    AAFSPADQDD FVI 963
    Length:963
    Mass (Da):107,496
    Last modified:October 1, 2000 - v1
    Checksum:i7F98200AC420F3D5
    GO
    Isoform 2 (identifier: Q9P0V3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         515-925: Missing.

    Note: No experimental confirmation available. Dubious isoform produced through aberrant splice sites.

    Show »
    Length:552
    Mass (Da):60,337
    Checksum:i1C9C5ABE339BFD7D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti235 – 2351D → N in ABB18377. (PubMed:16325581)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551M → T.1 Publication
    Corresponds to variant rs3731644 [ dbSNP | Ensembl ].
    VAR_030330
    Natural varianti197 – 1971A → T.1 Publication
    Corresponds to variant rs3731646 [ dbSNP | Ensembl ].
    VAR_030331

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei515 – 925411Missing in isoform 2. 1 PublicationVSP_022823Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF147747 mRNA. Translation: AAF33022.1.
    DQ232895 mRNA. Translation: ABB18377.1.
    AC010148 Genomic DNA. Translation: AAY14916.1.
    AC114814 Genomic DNA. Translation: AAY24025.1.
    BC057396 mRNA. Translation: AAH57396.1.
    AF015043 mRNA. Translation: AAD01551.1.
    CCDSiCCDS2513.1. [Q9P0V3-1]
    RefSeqiNP_055336.1. NM_014521.2. [Q9P0V3-1]
    UniGeneiHs.516777.

    Genome annotation databases

    EnsembliENST00000344528; ENSP00000340237; ENSG00000130147. [Q9P0V3-1]
    ENST00000392011; ENSP00000375867; ENSG00000130147. [Q9P0V3-1]
    ENST00000409212; ENSP00000386862; ENSG00000130147. [Q9P0V3-1]
    GeneIDi23677.
    KEGGihsa:23677.
    UCSCiuc002vvp.3. human. [Q9P0V3-1]

    Polymorphism databases

    DMDMi74753102.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF147747 mRNA. Translation: AAF33022.1 .
    DQ232895 mRNA. Translation: ABB18377.1 .
    AC010148 Genomic DNA. Translation: AAY14916.1 .
    AC114814 Genomic DNA. Translation: AAY24025.1 .
    BC057396 mRNA. Translation: AAH57396.1 .
    AF015043 mRNA. Translation: AAD01551.1 .
    CCDSi CCDS2513.1. [Q9P0V3-1 ]
    RefSeqi NP_055336.1. NM_014521.2. [Q9P0V3-1 ]
    UniGenei Hs.516777.

    3D structure databases

    ProteinModelPortali Q9P0V3.
    SMRi Q9P0V3. Positions 61-112.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117194. 31 interactions.
    IntActi Q9P0V3. 29 interactions.
    MINTi MINT-1649163.
    STRINGi 9606.ENSP00000340237.

    PTM databases

    PhosphoSitei Q9P0V3.

    Polymorphism databases

    DMDMi 74753102.

    Proteomic databases

    MaxQBi Q9P0V3.
    PaxDbi Q9P0V3.
    PRIDEi Q9P0V3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344528 ; ENSP00000340237 ; ENSG00000130147 . [Q9P0V3-1 ]
    ENST00000392011 ; ENSP00000375867 ; ENSG00000130147 . [Q9P0V3-1 ]
    ENST00000409212 ; ENSP00000386862 ; ENSG00000130147 . [Q9P0V3-1 ]
    GeneIDi 23677.
    KEGGi hsa:23677.
    UCSCi uc002vvp.3. human. [Q9P0V3-1 ]

    Organism-specific databases

    CTDi 23677.
    GeneCardsi GC02P235876.
    HGNCi HGNC:10826. SH3BP4.
    HPAi HPA037533.
    MIMi 605611. gene.
    neXtProti NX_Q9P0V3.
    PharmGKBi PA35734.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46295.
    HOGENOMi HOG000015297.
    HOVERGENi HBG057439.
    InParanoidi Q9P0V3.
    OMAi FFCRAEL.
    OrthoDBi EOG7GJ6C4.
    PhylomeDBi Q9P0V3.
    TreeFami TF105572.

    Miscellaneous databases

    ChiTaRSi SH3BP4. human.
    GeneWikii SH3BP4.
    GenomeRNAii 23677.
    NextBioi 46541.
    PROi Q9P0V3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0V3.
    Bgeei Q9P0V3.
    CleanExi HS_SH3BP4.
    Genevestigatori Q9P0V3.

    Family and domain databases

    InterProi IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR000906. ZU5.
    [Graphical view ]
    Pfami PF07653. SH3_2. 1 hit.
    PF14604. SH3_9. 1 hit.
    PF00791. ZU5. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, chromosomal localization, and characterization of cDNA from a novel gene, SH3BP4, expressed by human corneal fibroblasts."
      Dunlevy J.R., Berryhill B.L., Vergnes J.-P., SundarRaj N., Hassell J.R.
      Genomics 62:519-524(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Corneal fibroblast.
    2. "TTP specifically regulates the internalization of the transferrin receptor."
      Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P.
      Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN ENDOCYTOSIS, INTERACTION WITH AP-2; CLATHRIN; DNM2; EPS15 AND TFRC, OLIGOMERIZATION, PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-92, VARIANTS THR-155 AND THR-197.
      Tissue: Placenta.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORM 1).
      Tissue: Eye.
    5. "Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module."
      Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E., Minenkova O., Cesareni G., Pelicci P.G., Di Fiore P.P.
      Genes Dev. 11:2239-2249(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-963 (ISOFORM 2), INTERACTION WITH EPS15.
      Tissue: Fibroblast.
    6. "Nuclear and plasma membrane localization of SH3BP4 in retinal pigment epithelial cells."
      Khanobdee K., Kolberg J.B., Dunlevy J.R.
      Mol. Vis. 10:933-942(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "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.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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 SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 signaling."
      Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J., Kim D.H.
      Mol. Cell 46:833-846(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MTORC1 SIGNALING, INTERACTION WITH RRAGA; RRAGB; RRAGC AND RRAGD, MUTAGENESIS OF TRP-92.

    Entry informationi

    Entry nameiSH3B4_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0V3
    Secondary accession number(s): O95082
    , Q309A3, Q53QD0, Q53TD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 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

    Overexpression or depletion of SH3BP4 result in a specific decrease of the transferrin receptor endocytosis that can be rescued by DNM2 overexpression.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3