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Q8WZ73

- RFFL_HUMAN

UniProt

Q8WZ73 - RFFL_HUMAN

Protein

E3 ubiquitin-protein ligase rififylin

Gene

RFFL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Also ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate apoptosis downstream of death domain receptors. Also negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SNF. May also play a role in endocytic recycling.5 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 9656FYVE-typeAdd
    BLAST
    Zinc fingeri316 – 35136RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. p53 binding Source: UniProtKB
    3. protease binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: UniProtKB
    6. ubiquitin protein ligase binding Source: UniProtKB
    7. ubiquitin-protein transferase activity Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. intracellular protein transport Source: Ensembl
    2. negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: UniProtKB
    3. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
    4. negative regulation of signal transduction by p53 class mediator Source: UniProtKB
    5. negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    6. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    7. protein K48-linked ubiquitination Source: UniProtKB
    8. regulation of fibroblast migration Source: UniProtKB
    9. regulation of TOR signaling Source: UniProtKB
    10. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase rififylin (EC:6.3.2.-)
    Alternative name(s):
    Caspase regulator CARP2
    Caspases-8 and -10-associated RING finger protein 2
    Short name:
    CARP-2
    FYVE-RING finger protein Sakura
    Short name:
    Fring
    RING finger and FYVE-like domain-containing protein 1
    RING finger protein 189
    RING finger protein 34-like
    Gene namesi
    Name:RFFL
    Synonyms:RNF189, RNF34L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:24821. RFFL.

    Subcellular locationi

    Cytoplasmcytosol. Cell membrane; Peripheral membrane protein. Recycling endosome membrane By similarity; Peripheral membrane protein By similarity
    Note: The FYVE-type zinc finger may mediate phosphatidylinositol phosphate-binding and control subcellular localization.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: Ensembl
    3. cytosol Source: UniProtKB-SubCell
    4. endosome membrane Source: UniProtKB
    5. membrane Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. recycling endosome membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi333 – 3331H → A: Loss of E3 ubiquitin protein ligase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671086.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 363363E3 ubiquitin-protein ligase rififylinPRO_0000056025Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei226 – 2261Phosphoserine1 Publication
    Modified residuei229 – 2291Phosphoserine1 Publication

    Post-translational modificationi

    Autoubiquitinated.By similarity
    Palmitoylated.By similarity
    Undergoes caspase-mediated cleavage upon death-receptor activation, by TNFSF10 for instance. May be mediated by the caspases CASP8 and CASP10 in a negative feedback loop.

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8WZ73.
    PaxDbiQ8WZ73.
    PRIDEiQ8WZ73.

    PTM databases

    PhosphoSiteiQ8WZ73.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.1 Publication

    Inductioni

    Down-regulated upon DNA damage.1 Publication

    Gene expression databases

    ArrayExpressiQ8WZ73.
    BgeeiQ8WZ73.
    CleanExiHS_RFFL.
    GenevestigatoriQ8WZ73.

    Organism-specific databases

    HPAiCAB008096.
    HPA017910.
    HPA019492.

    Interactioni

    Subunit structurei

    Interacts with CASP8 and CASP10. Interacts with RIPK1 (via protein kinase domain); involved in RIPK1 ubiquitination. Interacts with PRR5L. Interacts (via RING-type zinc finger) with p53/TP53; involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc finger) with MDM2.5 Publications

    Protein-protein interaction databases

    BioGridi125593. 17 interactions.
    IntActiQ8WZ73. 2 interactions.
    STRINGi9606.ENSP00000326170.

    Structurei

    Secondary structure

    1
    363
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni48 – 503
    Helixi57 – 593
    Turni64 – 663
    Helixi72 – 743
    Helixi86 – 938
    Turni94 – 963
    Helixi98 – 1025
    Helixi106 – 11510
    Helixi126 – 13510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y02X-ray1.80A26-145[»]
    ProteinModelPortaliQ8WZ73.
    SMRiQ8WZ73. Positions 45-139, 275-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WZ73.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 12020SAP 1Add
    BLAST
    Domaini250 – 26415SAP 2Add
    BLAST

    Domaini

    The RING-type zinc finger is required for target protein ubiquitination.
    The FYVE-type zinc finger domain is required for localization to the recycling endosome membranes and the function in endocytic recycling.By similarity

    Sequence similaritiesi

    Contains 1 FYVE-type zinc finger.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 2 SAP domains.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 9656FYVE-typeAdd
    BLAST
    Zinc fingeri316 – 35136RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG121302.
    HOGENOMiHOG000068080.
    HOVERGENiHBG055079.
    InParanoidiQ8WZ73.
    OMAiHQQANGH.
    OrthoDBiEOG70GMFS.
    PhylomeDBiQ8WZ73.
    TreeFamiTF325195.

    Family and domain databases

    Gene3Di3.30.40.10. 2 hits.
    InterProiIPR011011. Znf_FYVE_PHD.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WZ73-1) [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

    MWATCCNWFC LDGQPEEVPP PQGARMQAYS NPGYSSFPSP TGLEPSCKSC    50
    GAHFANTARK QTCLDCKKNF CMTCSSQVGN GPRLCLLCQR FRATAFQREE 100
    LMKMKVKDLR DYLSLHDIST EMCREKEELV LLVLGQQPVI SQEDRTRAST 150
    LSPDFPEQQA FLTQPHSSMV PPTSPNLPSS SAQATSVPPA QVQENQQANG 200
    HVSQDQEEPV YLESVARVPA EDETQSIDSE DSFVPGRRAS LSDLTDLEDI 250
    EGLTVRQLKE ILARNFVNYK GCCEKWELME RVTRLYKDQK GLQHLVSGAE 300
    DQNGGAVPSG LEENLCKICM DSPIDCVLLE CGHMVTCTKC GKRMNECPIC 350
    RQYVIRAVHV FRS 363
    Length:363
    Mass (Da):40,514
    Last modified:March 1, 2002 - v1
    Checksum:i9456ED5A0503AFFB
    GO
    Isoform 2 (identifier: Q8WZ73-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         296-303: Missing.

    Show »
    Length:355
    Mass (Da):39,713
    Checksum:i0F22B82AD059DE03
    GO
    Isoform 3 (identifier: Q8WZ73-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         197-224: Missing.
         296-303: Missing.

    Show »
    Length:327
    Mass (Da):36,633
    Checksum:i34CE0CD40417BE8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271E → G in AAH28424. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei197 – 22428Missing in isoform 3. 1 PublicationVSP_015751Add
    BLAST
    Alternative sequencei296 – 3038Missing in isoform 2 and isoform 3. 2 PublicationsVSP_015752

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF434816 mRNA. Translation: AAL30771.1.
    AY098935 mRNA. Translation: AAM29181.1.
    AK093112 mRNA. Translation: BAC04059.1.
    CR933651 mRNA. Translation: CAI45952.1.
    CH471147 Genomic DNA. Translation: EAW80172.1.
    CH471147 Genomic DNA. Translation: EAW80173.1.
    CH471147 Genomic DNA. Translation: EAW80176.1.
    CH471147 Genomic DNA. Translation: EAW80177.1.
    CH471147 Genomic DNA. Translation: EAW80178.1.
    BC015681 mRNA. Translation: AAH15681.2.
    BC028424 mRNA. Translation: AAH28424.1.
    CCDSiCCDS11286.1. [Q8WZ73-1]
    RefSeqiNP_001017368.1. NM_001017368.1. [Q8WZ73-1]
    UniGeneiHs.13680.

    Genome annotation databases

    EnsembliENST00000315249; ENSP00000326170; ENSG00000092871. [Q8WZ73-1]
    ENST00000394597; ENSP00000378096; ENSG00000092871. [Q8WZ73-1]
    ENST00000413582; ENSP00000408513; ENSG00000092871. [Q8WZ73-2]
    ENST00000415395; ENSP00000412322; ENSG00000092871. [Q8WZ73-1]
    ENST00000447669; ENSP00000389832; ENSG00000092871. [Q8WZ73-1]
    ENST00000584655; ENSP00000463035; ENSG00000092871. [Q8WZ73-3]
    GeneIDi117584.
    KEGGihsa:117584.
    UCSCiuc002him.1. human. [Q8WZ73-2]
    uc002hin.1. human. [Q8WZ73-1]
    uc002hip.2. human. [Q8WZ73-3]

    Polymorphism databases

    DMDMi74760639.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF434816 mRNA. Translation: AAL30771.1 .
    AY098935 mRNA. Translation: AAM29181.1 .
    AK093112 mRNA. Translation: BAC04059.1 .
    CR933651 mRNA. Translation: CAI45952.1 .
    CH471147 Genomic DNA. Translation: EAW80172.1 .
    CH471147 Genomic DNA. Translation: EAW80173.1 .
    CH471147 Genomic DNA. Translation: EAW80176.1 .
    CH471147 Genomic DNA. Translation: EAW80177.1 .
    CH471147 Genomic DNA. Translation: EAW80178.1 .
    BC015681 mRNA. Translation: AAH15681.2 .
    BC028424 mRNA. Translation: AAH28424.1 .
    CCDSi CCDS11286.1. [Q8WZ73-1 ]
    RefSeqi NP_001017368.1. NM_001017368.1. [Q8WZ73-1 ]
    UniGenei Hs.13680.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y02 X-ray 1.80 A 26-145 [» ]
    ProteinModelPortali Q8WZ73.
    SMRi Q8WZ73. Positions 45-139, 275-361.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125593. 17 interactions.
    IntActi Q8WZ73. 2 interactions.
    STRINGi 9606.ENSP00000326170.

    PTM databases

    PhosphoSitei Q8WZ73.

    Polymorphism databases

    DMDMi 74760639.

    Proteomic databases

    MaxQBi Q8WZ73.
    PaxDbi Q8WZ73.
    PRIDEi Q8WZ73.

    Protocols and materials databases

    DNASUi 117584.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315249 ; ENSP00000326170 ; ENSG00000092871 . [Q8WZ73-1 ]
    ENST00000394597 ; ENSP00000378096 ; ENSG00000092871 . [Q8WZ73-1 ]
    ENST00000413582 ; ENSP00000408513 ; ENSG00000092871 . [Q8WZ73-2 ]
    ENST00000415395 ; ENSP00000412322 ; ENSG00000092871 . [Q8WZ73-1 ]
    ENST00000447669 ; ENSP00000389832 ; ENSG00000092871 . [Q8WZ73-1 ]
    ENST00000584655 ; ENSP00000463035 ; ENSG00000092871 . [Q8WZ73-3 ]
    GeneIDi 117584.
    KEGGi hsa:117584.
    UCSCi uc002him.1. human. [Q8WZ73-2 ]
    uc002hin.1. human. [Q8WZ73-1 ]
    uc002hip.2. human. [Q8WZ73-3 ]

    Organism-specific databases

    CTDi 117584.
    GeneCardsi GC17M033333.
    HGNCi HGNC:24821. RFFL.
    HPAi CAB008096.
    HPA017910.
    HPA019492.
    MIMi 609735. gene.
    neXtProti NX_Q8WZ73.
    PharmGKBi PA142671086.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG121302.
    HOGENOMi HOG000068080.
    HOVERGENi HBG055079.
    InParanoidi Q8WZ73.
    OMAi HQQANGH.
    OrthoDBi EOG70GMFS.
    PhylomeDBi Q8WZ73.
    TreeFami TF325195.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q8WZ73.
    GeneWikii RFFL.
    GenomeRNAii 117584.
    NextBioi 80230.
    PROi Q8WZ73.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WZ73.
    Bgeei Q8WZ73.
    CleanExi HS_RFFL.
    Genevestigatori Q8WZ73.

    Family and domain databases

    Gene3Di 3.30.40.10. 2 hits.
    InterProi IPR011011. Znf_FYVE_PHD.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Fring, a protein with a modified FYVE domain and a ring domain."
      Hong W.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Kanbe D., Araki K., Nawa H.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "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] (ISOFORM 1).
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis carcinoma.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3).
      Tissue: Testis.
    7. "Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth."
      McDonald E.R. III, El-Deiry W.S.
      Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH CASP8 AND CASP10, MUTAGENESIS OF HIS-333, PROTEOLYTIC DEGRADATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation."
      Yang W., Rozan L.M., McDonald E.R. III, Navaraj A., Liu J.J., Matthew E.M., Wang W., Dicker D.T., El-Deiry W.S.
      J. Biol. Chem. 282:3273-3281(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN P53/TP53 UBIQUITINATION, INTERACTION WITH P53/TP53.
    9. "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2."
      Yang W., Dicker D.T., Chen J., El-Deiry W.S.
      Cell Cycle 7:670-682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF SFN, INTERACTION WITH MDM2 AND P53/TP53, INDUCTION.
    10. "CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation."
      Liao W., Xiao Q., Tchikov V., Fujita K., Yang W., Wincovitch S., Garfield S., Conze D., El-Deiry W.S., Schuetze S., Srinivasula S.M.
      Curr. Biol. 18:641-649(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TNF SIGNALING, INTERACTION WITH RIPK1, SUBCELLULAR LOCATION.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
      Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
      Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF PRR5L, INTERACTION WITH PRR5L AND THE MTORC2 COMPLEX.
    13. "Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2."
      Tibbetts M.D., Shiozaki E.N., Gu L., McDonald E.R. III, El-Deiry W.S., Shi Y.
      Structure 12:2257-2263(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 26-145.

    Entry informationi

    Entry nameiRFFL_HUMAN
    AccessioniPrimary (citable) accession number: Q8WZ73
    Secondary accession number(s): E1P633
    , Q8NHW0, Q8TBY7, Q96BE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 118 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3