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Q9Y4L5

- RN115_HUMAN

UniProt

Q9Y4L5 - RN115_HUMAN

Protein

E3 ubiquitin-protein ligase RNF115

Gene

RNF115

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Acts as an E2-dependent E3 ubiquitin-protein ligase. May be involved in endocytic trafficking.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri228 – 26942RING-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: InterPro

    GO - Biological processi

    1. protein autoubiquitination 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 RNF115 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 115
    Rabring 7
    Zinc finger protein 364
    Gene namesi
    Name:RNF115
    Synonyms:ZNF364
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18154. RNF115.

    Subcellular locationi

    Cytoplasmcytosol By similarity
    Note: The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261K → R: Loss of autoubiquitination; when associated with R-32. 1 Publication
    Mutagenesisi32 – 321K → R: Loss of autoubiquitination; when associated with R-26. 1 Publication
    Mutagenesisi228 – 2281C → A: Loss of autoubiquitination. 1 Publication
    Mutagenesisi231 – 2311C → A: Loss of autoubiquitination. 1 Publication

    Organism-specific databases

    PharmGKBiPA162401519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 304303E3 ubiquitin-protein ligase RNF115PRO_0000056314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    RING-type zinc finger-dependent and E2-dependent autoubiquitination.2 Publications

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y4L5.
    PaxDbiQ9Y4L5.
    PRIDEiQ9Y4L5.

    PTM databases

    PhosphoSiteiQ9Y4L5.

    Expressioni

    Tissue specificityi

    Expressed at extremely low levels in normal breast, prostate, lung, colon. Higher levels of expression are detected in heart, skeletal muscle, testis as well as in breast and prostate cancer cells.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y4L5.
    BgeeiQ9Y4L5.
    CleanExiHS_RNF115.
    GenevestigatoriQ9Y4L5.

    Organism-specific databases

    HPAiHPA019130.

    Interactioni

    Subunit structurei

    Interacts with RAB7A.1 Publication

    Protein-protein interaction databases

    BioGridi118094. 32 interactions.
    IntActiQ9Y4L5. 8 interactions.
    STRINGi9606.ENSP00000358297.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4L5.
    SMRiQ9Y4L5. Positions 218-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri228 – 26942RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG235630.
    HOGENOMiHOG000116417.
    HOVERGENiHBG059832.
    InParanoidiQ9Y4L5.
    KOiK11982.
    OMAiSTHFAEF.
    OrthoDBiEOG7353XB.
    PhylomeDBiQ9Y4L5.
    TreeFamiTF317985.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Y4L5-1 [UniParc]FASTAAdd to Basket

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    MAEASAAGAD SGAAVAAHRF FCHFCKGEVS PKLPEYICPR CESGFIEEVT    50
    DDSSFLGGGG SRIDNTTTTH FAELWGHLDH TMFFQDFRPF LSSSPLDQDN 100
    RANERGHQTH TDFWGARPPR LPLGRRYRSR GSSRPDRSPA IEGILQHIFA 150
    GFFANSAIPG SPHPFSWSGM LHSNPGDYAW GQTGLDAIVT QLLGQLENTG 200
    PPPADKEKIT SLPTVTVTQE QVDMGLECPV CKEDYTVEEE VRQLPCNHFF 250
    HSSCIVPWLE LHDTCPVCRK SLNGEDSTRQ SQSTEASASN RFSNDSQLHD 300
    RWTF 304
    Length:304
    Mass (Da):33,703
    Last modified:December 7, 2004 - v2
    Checksum:i22F0C8FCC0F55045
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti299 – 2991H → N in CAB45280. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti194 – 1941G → R.
    Corresponds to variant rs11577731 [ dbSNP | Ensembl ].
    VAR_052105

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF542552 mRNA. Translation: AAQ09535.1.
    AF419857 mRNA. Translation: AAP97292.1.
    AK290749 mRNA. Translation: BAF83438.1.
    AL390725, AL160282 Genomic DNA. Translation: CAI13717.1.
    CH471244 Genomic DNA. Translation: EAW71437.1.
    BC054049 mRNA. Translation: AAH54049.1.
    BC064903 mRNA. Translation: AAH64903.1.
    AL079314 mRNA. Translation: CAB45280.1.
    CCDSiCCDS922.1.
    RefSeqiNP_055270.1. NM_014455.3.
    UniGeneiHs.523550.

    Genome annotation databases

    EnsembliENST00000582693; ENSP00000463650; ENSG00000265491.
    GeneIDi27246.
    KEGGihsa:27246.
    UCSCiuc001eoj.3. human.

    Polymorphism databases

    DMDMi56405389.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF542552 mRNA. Translation: AAQ09535.1 .
    AF419857 mRNA. Translation: AAP97292.1 .
    AK290749 mRNA. Translation: BAF83438.1 .
    AL390725 , AL160282 Genomic DNA. Translation: CAI13717.1 .
    CH471244 Genomic DNA. Translation: EAW71437.1 .
    BC054049 mRNA. Translation: AAH54049.1 .
    BC064903 mRNA. Translation: AAH64903.1 .
    AL079314 mRNA. Translation: CAB45280.1 .
    CCDSi CCDS922.1.
    RefSeqi NP_055270.1. NM_014455.3.
    UniGenei Hs.523550.

    3D structure databases

    ProteinModelPortali Q9Y4L5.
    SMRi Q9Y4L5. Positions 218-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118094. 32 interactions.
    IntActi Q9Y4L5. 8 interactions.
    STRINGi 9606.ENSP00000358297.

    PTM databases

    PhosphoSitei Q9Y4L5.

    Polymorphism databases

    DMDMi 56405389.

    Proteomic databases

    MaxQBi Q9Y4L5.
    PaxDbi Q9Y4L5.
    PRIDEi Q9Y4L5.

    Protocols and materials databases

    DNASUi 27246.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000582693 ; ENSP00000463650 ; ENSG00000265491 .
    GeneIDi 27246.
    KEGGi hsa:27246.
    UCSCi uc001eoj.3. human.

    Organism-specific databases

    CTDi 27246.
    GeneCardsi GC01P145611.
    HGNCi HGNC:18154. RNF115.
    HPAi HPA019130.
    neXtProti NX_Q9Y4L5.
    PharmGKBi PA162401519.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235630.
    HOGENOMi HOG000116417.
    HOVERGENi HBG059832.
    InParanoidi Q9Y4L5.
    KOi K11982.
    OMAi STHFAEF.
    OrthoDBi EOG7353XB.
    PhylomeDBi Q9Y4L5.
    TreeFami TF317985.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi RNF115. human.
    GeneWikii ZNF364.
    GenomeRNAii 27246.
    NextBioi 50157.
    PROi Q9Y4L5.

    Gene expression databases

    ArrayExpressi Q9Y4L5.
    Bgeei Q9Y4L5.
    CleanExi HS_RNF115.
    Genevestigatori Q9Y4L5.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of zinc finger protein 364, C3HC4 type (ZNF364), a novel human member of zinc finger protein family."
      Zhang D.L., Cai J.J., Ma D.L.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Guo J.H., She X.Y., Yu L.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Pancreas and Skin.
    7. The European IMAGE consortium
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-304.
      Tissue: Uterus.
    8. "A novel RING-type ubiquitin ligase breast cancer-associated gene 2 correlates with outcome in invasive breast cancer."
      Burger A.M., Gao Y., Amemiya Y., Kahn H.J., Kitching R., Yang Y., Sun P., Narod S.A., Hanna W.M., Seth A.K.
      Cancer Res. 65:10401-10412(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, TISSUE SPECIFICITY.
    9. "Novel RING E3 ubiquitin ligases in breast cancer."
      Burger A., Amemiya Y., Kitching R., Seth A.K.
      Neoplasia 8:689-695(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB7A.
    10. "Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and affects cell migration."
      Amemiya Y., Azmi P., Seth A.
      Mol. Cancer Res. 6:1385-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, MUTAGENESIS OF LYS-26; LYS-32; CYS-228 AND CYS-231.
    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].

    Entry informationi

    Entry nameiRN115_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4L5
    Secondary accession number(s): A8K3Y4, Q5T2V9, Q7Z2J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 107 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3