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Protein

E3 ubiquitin-protein ligase RNF115

Gene

RNF115

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4.1 Publication2 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. ubiquitin protein ligase activity Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  2. protein autoubiquitination Source: UniProtKB
  3. protein K48-linked ubiquitination Source: UniProtKB
  4. protein K63-linked ubiquitination Source: UniProtKB
  5. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
Complete GO annotation...

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 RNF115Curated (EC:6.3.2.-1 Publication)
Alternative name(s):
RING finger protein 115Imported
Rabring 7By similarity
Zinc finger protein 3641 Publication
Gene namesi
Name:RNF115Imported
Synonyms:ZNF3641 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18154. RNF115.

Subcellular locationi

  1. Cytoplasmcytosol By similarity

  2. 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
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiRNF115.
DMDMi56405389.

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

BgeeiQ9Y4L5.
CleanExiHS_RNF115.
GenevestigatoriQ9Y4L5.

Organism-specific databases

HPAiHPA019130.

Interactioni

Subunit structurei

Interacts with RAB7A. Interacts with EGFR and FLT3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZAP2Q150384EBI-2129242,EBI-724310
MDM4O151513EBI-2129242,EBI-398437
UBE2D1P516684EBI-2129242,EBI-743540
UBE2D3P610774EBI-2129242,EBI-348268
UBE2D4Q9Y2X84EBI-2129242,EBI-745527

Protein-protein interaction databases

BioGridi118094. 39 interactions.
IntActiQ9Y4L5. 9 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.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ9Y4L5.
KOiK11982.
OMAiHIFAGFF.
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

« Hide

        10         20         30         40         50
MAEASAAGAD SGAAVAAHRF FCHFCKGEVS PKLPEYICPR CESGFIEEVT
60 70 80 90 100
DDSSFLGGGG SRIDNTTTTH FAELWGHLDH TMFFQDFRPF LSSSPLDQDN
110 120 130 140 150
RANERGHQTH TDFWGARPPR LPLGRRYRSR GSSRPDRSPA IEGILQHIFA
160 170 180 190 200
GFFANSAIPG SPHPFSWSGM LHSNPGDYAW GQTGLDAIVT QLLGQLENTG
210 220 230 240 250
PPPADKEKIT SLPTVTVTQE QVDMGLECPV CKEDYTVEEE VRQLPCNHFF
260 270 280 290 300
HSSCIVPWLE LHDTCPVCRK SLNGEDSTRQ SQSTEASASN RFSNDSQLHD

RWTF
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 (Ref. 7) Curated

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:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS72863.1.
RefSeqiNP_055270.1. NM_014455.3.
UniGeneiHs.523550.

Genome annotation databases

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

Polymorphism and mutation databases

BioMutaiRNF115.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS72863.1.
RefSeqiNP_055270.1. NM_014455.3.
UniGeneiHs.523550.

3D structure databases

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

Protein-protein interaction databases

BioGridi118094. 39 interactions.
IntActiQ9Y4L5. 9 interactions.
STRINGi9606.ENSP00000358297.

PTM databases

PhosphoSiteiQ9Y4L5.

Polymorphism and mutation databases

BioMutaiRNF115.
DMDMi56405389.

Proteomic databases

MaxQBiQ9Y4L5.
PaxDbiQ9Y4L5.
PRIDEiQ9Y4L5.

Protocols and materials databases

DNASUi27246.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi27246.
GeneCardsiGC01P145611.
HGNCiHGNC:18154. RNF115.
HPAiHPA019130.
neXtProtiNX_Q9Y4L5.
PharmGKBiPA162401519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG235630.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ9Y4L5.
KOiK11982.
OMAiHIFAGFF.
OrthoDBiEOG7353XB.
PhylomeDBiQ9Y4L5.
TreeFamiTF317985.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF115. human.
GeneWikiiZNF364.
GenomeRNAii27246.
NextBioi50157.
PROiQ9Y4L5.

Gene expression databases

BgeeiQ9Y4L5.
CleanExiHS_RNF115.
GenevestigatoriQ9Y4L5.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, PATHWAY, CATALYTIC ACTIVITY, 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].
  12. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EGFR AND FLT3.

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: April 29, 2015
This is version 111 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.