Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99942

- RNF5_HUMAN

UniProt

Q99942 - RNF5_HUMAN

Protein

E3 ubiquitin-protein ligase RNF5

Gene

RNF5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurrs in mitochondria after viral transfection and regulates antiviral responses.5 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri27 – 6842RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB
    4. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cellular protein catabolic process Source: UniProtKB
    2. ER-associated misfolded protein catabolic process Source: UniProtKB
    3. protein K48-linked ubiquitination Source: UniProtKB
    4. protein K63-linked ubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RNF5 (EC:6.3.2.-)
    Alternative name(s):
    Protein G16
    RING finger protein 5
    Ram1 homolog
    Short name:
    HsRma1
    Gene namesi
    Name:RNF5
    Synonyms:G16, NG2, RMA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10068. RNF5.

    Subcellular locationi

    Membrane; Multi-pass membrane protein. Mitochondrion membrane. Endoplasmic reticulum membrane
    Note: Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421C → S: Loss of E3 ubiquitin-protein ligase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 180179E3 ubiquitin-protein ligase RNF5PRO_0000240393Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99942.
    PaxDbiQ99942.
    PRIDEiQ99942.

    PTM databases

    PhosphoSiteiQ99942.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ99942.
    CleanExiHS_RNF5.
    GenevestigatoriQ99942.

    Organism-specific databases

    HPAiCAB034107.
    HPA052125.

    Interactioni

    Subunit structurei

    Interacts with PXN. Interacts with Salmonella typhimurium sopA. Interacts with JKAMP. Interacts with TMEM173; the interaction of endogenous proteins is dependent on viral infection.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFTRP135693EBI-348482,EBI-349854
    PXNP490236EBI-348482,EBI-702209
    UBE2D2P628373EBI-348482,EBI-347677
    UBE2D3P610773EBI-348482,EBI-348268

    Protein-protein interaction databases

    BioGridi111975. 33 interactions.
    DIPiDIP-29268N.
    IntActiQ99942. 22 interactions.
    MINTiMINT-1032027.
    STRINGi9606.ENSP00000364235.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99942.
    SMRiQ99942. Positions 22-71.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei118 – 13821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei160 – 18021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri27 – 6842RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG300581.
    HOGENOMiHOG000238304.
    HOVERGENiHBG054495.
    InParanoidiQ99942.
    KOiK10666.
    OMAiFQSFGDT.
    PhylomeDBiQ99942.
    TreeFamiTF317334.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99942-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAEEEDGG PEGPNRERGG AGATFECNIC LETAREAVVS VCGHLYCWPC    50
    LHQWLETRPE RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG 100
    QRPAPESRGG FQPFGDTGGF HFSFGVGAFP FGFFTTVFNA HEPFRRGTGV 150
    DLGQGHPASS WQDSLFLFLA IFFFFWLLSI 180
    Length:180
    Mass (Da):19,881
    Last modified:May 1, 1997 - v1
    Checksum:iE5AFA4DE6DE85942
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221G → S in CAB51286. 1 PublicationCurated
    Sequence conflicti60 – 601E → D in CAB51286. 1 PublicationCurated
    Sequence conflicti117 – 1171T → A in CAB51286. 1 PublicationCurated
    Sequence conflicti148 – 1481T → A in CAB51286. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB056869 mRNA. Translation: BAB39359.1.
    AJ243936 mRNA. Translation: CAB51286.1.
    AK311859 mRNA. Translation: BAG34800.1.
    BT007105 mRNA. Translation: AAP35769.1.
    U89336 Genomic DNA. Translation: AAB47492.1.
    AL845464 Genomic DNA. Translation: CAI41808.1.
    AL662884 Genomic DNA. Translation: CAI18351.1.
    AL662830 Genomic DNA. Translation: CAI17532.1.
    BX284686 Genomic DNA. Translation: CAM26222.1.
    BX927239 Genomic DNA. Translation: CAQ06594.1.
    CR812478 Genomic DNA. Translation: CAQ10698.1.
    CR933878 Genomic DNA. Translation: CAQ09623.1.
    BC004155 mRNA. Translation: AAH04155.1.
    BC111392 mRNA. Translation: AAI11393.1.
    BC119741 mRNA. Translation: AAI19742.1.
    BC119742 mRNA. Translation: AAI19743.1.
    BC127651 mRNA. Translation: AAI27652.1.
    BC127652 mRNA. Translation: AAI27653.1.
    BC148255 mRNA. Translation: AAI48256.1.
    CCDSiCCDS4745.1.
    RefSeqiNP_008844.1. NM_006913.3.
    UniGeneiHs.731774.

    Genome annotation databases

    EnsembliENST00000375094; ENSP00000364235; ENSG00000204308.
    ENST00000413786; ENSP00000387879; ENSG00000225452.
    ENST00000432616; ENSP00000413131; ENSG00000183574.
    ENST00000445885; ENSP00000401172; ENSG00000227277.
    ENST00000449794; ENSP00000415784; ENSG00000223767.
    ENST00000453473; ENSP00000415127; ENSG00000228907.
    ENST00000456167; ENSP00000388795; ENSG00000228405.
    GeneIDi6048.
    KEGGihsa:6048.
    UCSCiuc003oaj.4. human.

    Polymorphism databases

    DMDMi74762702.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB056869 mRNA. Translation: BAB39359.1 .
    AJ243936 mRNA. Translation: CAB51286.1 .
    AK311859 mRNA. Translation: BAG34800.1 .
    BT007105 mRNA. Translation: AAP35769.1 .
    U89336 Genomic DNA. Translation: AAB47492.1 .
    AL845464 Genomic DNA. Translation: CAI41808.1 .
    AL662884 Genomic DNA. Translation: CAI18351.1 .
    AL662830 Genomic DNA. Translation: CAI17532.1 .
    BX284686 Genomic DNA. Translation: CAM26222.1 .
    BX927239 Genomic DNA. Translation: CAQ06594.1 .
    CR812478 Genomic DNA. Translation: CAQ10698.1 .
    CR933878 Genomic DNA. Translation: CAQ09623.1 .
    BC004155 mRNA. Translation: AAH04155.1 .
    BC111392 mRNA. Translation: AAI11393.1 .
    BC119741 mRNA. Translation: AAI19742.1 .
    BC119742 mRNA. Translation: AAI19743.1 .
    BC127651 mRNA. Translation: AAI27652.1 .
    BC127652 mRNA. Translation: AAI27653.1 .
    BC148255 mRNA. Translation: AAI48256.1 .
    CCDSi CCDS4745.1.
    RefSeqi NP_008844.1. NM_006913.3.
    UniGenei Hs.731774.

    3D structure databases

    ProteinModelPortali Q99942.
    SMRi Q99942. Positions 22-71.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111975. 33 interactions.
    DIPi DIP-29268N.
    IntActi Q99942. 22 interactions.
    MINTi MINT-1032027.
    STRINGi 9606.ENSP00000364235.

    PTM databases

    PhosphoSitei Q99942.

    Polymorphism databases

    DMDMi 74762702.

    Proteomic databases

    MaxQBi Q99942.
    PaxDbi Q99942.
    PRIDEi Q99942.

    Protocols and materials databases

    DNASUi 6048.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375094 ; ENSP00000364235 ; ENSG00000204308 .
    ENST00000413786 ; ENSP00000387879 ; ENSG00000225452 .
    ENST00000432616 ; ENSP00000413131 ; ENSG00000183574 .
    ENST00000445885 ; ENSP00000401172 ; ENSG00000227277 .
    ENST00000449794 ; ENSP00000415784 ; ENSG00000223767 .
    ENST00000453473 ; ENSP00000415127 ; ENSG00000228907 .
    ENST00000456167 ; ENSP00000388795 ; ENSG00000228405 .
    GeneIDi 6048.
    KEGGi hsa:6048.
    UCSCi uc003oaj.4. human.

    Organism-specific databases

    CTDi 6048.
    GeneCardsi GC06P032146.
    GC06Pi32157.
    GC06Pj32094.
    GC06Pl32185.
    GC06Pm32222.
    GC06Pn32103.
    GC06Po32153.
    H-InvDB HIX0034363.
    HGNCi HGNC:10068. RNF5.
    HPAi CAB034107.
    HPA052125.
    MIMi 602677. gene.
    neXtProti NX_Q99942.
    PharmGKBi PA34442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300581.
    HOGENOMi HOG000238304.
    HOVERGENi HBG054495.
    InParanoidi Q99942.
    KOi K10666.
    OMAi FQSFGDT.
    PhylomeDBi Q99942.
    TreeFami TF317334.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GeneWikii RNF5.
    GenomeRNAii 6048.
    NextBioi 23565.
    PROi Q99942.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99942.
    CleanExi HS_RNF5.
    Genevestigatori Q99942.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and mapping of a novel RING-finger gene (RNF5), a human homologue of a putative zinc-finger gene from Caenorhabditis elegans."
      Kyushiki H., Kuga Y., Suzuki M., Takahashi E., Horie M.
      Cytogenet. Cell Genet. 79:114-117(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase."
      Matsuda N., Suzuki T., Tanaka K., Nakano A.
      J. Cell Sci. 114:1949-1957(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-42.
    3. "Characterisation of a novel gene, G16, in the class III region of the human major histocompatibility complex."
      Khanna A., Campbell R.D.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Brain.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Lung.
    9. "RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization."
      Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.
      Mol. Cell. Biol. 23:5331-5345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PXN.
    10. "Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1."
      Zhang Y., Higashide W., Dai S., Sherman D.M., Zhou D.
      J. Biol. Chem. 280:38682-38688(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA."
      Zhong B., Zhang L., Lei C., Li Y., Mao A.P., Yang Y., Wang Y.Y., Zhang X.L., Shu H.B.
      Immunity 30:397-407(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF TMEM173, INTERACTION WITH TMEM173, SUBCELLULAR LOCATION.
    13. "Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP)."
      Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.
      J. Biol. Chem. 284:12099-12109(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF JKAMP, INTERACTION WITH JKAMP.
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRNF5_HUMAN
    AccessioniPrimary (citable) accession number: Q99942
    Secondary accession number(s): A2BFI6
    , B2R4K3, Q0VDB7, Q9UMQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 134 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3