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Q8WZ73

- RFFL_HUMAN

UniProt

Q8WZ73 - RFFL_HUMAN

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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

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. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. 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 SFN. 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 kinase binding Source: UniProtKB
  5. ubiquitin protein ligase activity Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

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

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 rififylinCurated (EC:6.3.2.-1 Publication)
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:RFFLImported
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. endosome membrane Source: UniProtKB
  3. membrane Source: UniProtKB
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiQ8WZ73.
CleanExiHS_RFFL.
ExpressionAtlasiQ8WZ73. baseline and differential.
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; the interaction stabilizes MDM2.5 Publications

Protein-protein interaction databases

BioGridi125593. 23 interactions.
IntActiQ8WZ73. 2 interactions.
STRINGi9606.ENSP00000326170.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 the ubiquitination of target proteins.1 Publication
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.
GeneTreeiENSGT00390000012719.
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

        10         20         30         40         50
MWATCCNWFC LDGQPEEVPP PQGARMQAYS NPGYSSFPSP TGLEPSCKSC
60 70 80 90 100
GAHFANTARK QTCLDCKKNF CMTCSSQVGN GPRLCLLCQR FRATAFQREE
110 120 130 140 150
LMKMKVKDLR DYLSLHDIST EMCREKEELV LLVLGQQPVI SQEDRTRAST
160 170 180 190 200
LSPDFPEQQA FLTQPHSSMV PPTSPNLPSS SAQATSVPPA QVQENQQANG
210 220 230 240 250
HVSQDQEEPV YLESVARVPA EDETQSIDSE DSFVPGRRAS LSDLTDLEDI
260 270 280 290 300
EGLTVRQLKE ILARNFVNYK GCCEKWELME RVTRLYKDQK GLQHLVSGAE
310 320 330 340 350
DQNGGAVPSG LEENLCKICM DSPIDCVLLE CGHMVTCTKC GKRMNECPIC
360
RQYVIRAVHV FRS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 23 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.
GeneTreei ENSGT00390000012719.
HOGENOMi HOG000068080.
HOVERGENi HBG055079.
InParanoidi Q8WZ73.
OMAi HQQANGH.
OrthoDBi EOG70GMFS.
PhylomeDBi Q8WZ73.
TreeFami TF325195.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

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

Gene expression databases

Bgeei Q8WZ73.
CleanExi HS_RFFL.
ExpressionAtlasi Q8WZ73. baseline and differential.
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

« Hide 'large scale' publications
  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, PATHWAY.
  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, DOMAIN.
  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: November 26, 2014
This is version 120 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