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Q99942 (RNF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RNF5
Synonyms:G16, NG2, RMA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.9 Ref.10 Ref.12 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with PXN. Interacts with Salmonella typhimurium sopA. Interacts with JKAMP. Interacts with TMEM173; the interaction of endogenous proteins is dependent on viral infection. Ref.9 Ref.12 Ref.13

Subcellular location

Membrane; Multi-pass membrane protein. Mitochondrion membrane. Endoplasmic reticulum membrane. Note: Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles. Ref.9 Ref.12

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 180179E3 ubiquitin-protein ligase RNF5
PRO_0000240393

Regions

Transmembrane118 – 13821Helical; Potential
Transmembrane160 – 18021Helical; Potential
Zinc finger27 – 6842RING-type

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.14 Ref.15

Experimental info

Mutagenesis421C → S: Loss of E3 ubiquitin-protein ligase activity. Ref.2
Sequence conflict221G → S in CAB51286. Ref.3
Sequence conflict601E → D in CAB51286. Ref.3
Sequence conflict1171T → A in CAB51286. Ref.3
Sequence conflict1481T → A in CAB51286. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99942 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: E5AFA4DE6DE85942

FASTA18019,881
        10         20         30         40         50         60 
MAAAEEEDGG PEGPNRERGG AGATFECNIC LETAREAVVS VCGHLYCWPC LHQWLETRPE 

        70         80         90        100        110        120 
RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG QRPAPESRGG FQPFGDTGGF 

       130        140        150        160        170        180 
HFSFGVGAFP FGFFTTVFNA HEPFRRGTGV DLGQGHPASS WQDSLFLFLA IFFFFWLLSI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_008844.1. NM_006913.3.
UniGeneHs.731774.

3D structure databases

ProteinModelPortalQ99942.
SMRQ99942. Positions 22-71.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111975. 33 interactions.
DIPDIP-29268N.
IntActQ99942. 22 interactions.
MINTMINT-1032027.
STRING9606.ENSP00000364235.

PTM databases

PhosphoSiteQ99942.

Polymorphism databases

DMDM74762702.

Proteomic databases

PaxDbQ99942.
PRIDEQ99942.

Protocols and materials databases

DNASU6048.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375094; ENSP00000364235; ENSG00000204308.
ENST00000413786; ENSP00000387879; ENSG00000225452.
ENST00000432616; ENSP00000413131; ENSG00000183574.
ENST00000445885; ENSP00000401172; ENSG00000227277.
ENST00000449794; ENSP00000415784; ENSG00000223767.
ENST00000453473; ENSP00000415127; ENSG00000228907.
ENST00000456167; ENSP00000388795; ENSG00000228405.
GeneID6048.
KEGGhsa:6048.
UCSCuc003oaj.4. human.

Organism-specific databases

CTD6048.
GeneCardsGC06P032146.
GC06Pi32157.
GC06Pj32094.
GC06Pl32185.
GC06Pm32222.
GC06Pn32103.
GC06Po32153.
H-InvDBHIX0034363.
HGNCHGNC:10068. RNF5.
HPACAB034107.
HPA052125.
MIM602677. gene.
neXtProtNX_Q99942.
PharmGKBPA34442.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300581.
HOGENOMHOG000238304.
HOVERGENHBG054495.
InParanoidQ99942.
KOK10666.
OMAFQSFGDT.
PhylomeDBQ99942.
TreeFamTF317334.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ99942.
CleanExHS_RNF5.
GenevestigatorQ99942.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRNF5.
GenomeRNAi6048.
NextBio23565.
PROQ99942.
SOURCESearch...

Entry information

Entry nameRNF5_HUMAN
AccessionPrimary (citable) accession number: Q99942
Secondary accession number(s): A2BFI6 expand/collapse secondary AC list , B2R4K3, Q0VDB7, Q9UMQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM