Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q99942 (RNF5_HUMAN)

Last modified June 16, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    E3 ubiquitin-protein ligase RNF5
    EC=6.3.2.-
Alternative name(s):
    RING finger protein 5
      Short name=HsRma1
    Protein G16
Gene names
Name: RNF5
Synonyms: G16, NG2, RMA1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Ref.2 Ref.9 Ref.10

Subunit structure

Interacts with PXN. Interacts with Salmonella typhimurium sopA. Interacts with JAMP By similarity.

Subcellular location

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

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentMembrane
   DomainTransmembrane
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Gene Ontology (GO)
   Biological processmodification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.1 Ref.9

Inferred from physical interaction. Source: IntAct

zinc ion binding Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 180180E3 ubiquitin-protein ligase RNF5
PRO_0000240393

Regions

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

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
Q99942-1 [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: 9533025] [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: 11329381] [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: 14702039] [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: 14656967] [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: 14574404] [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: 15489334] [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: 12861019] [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: 16176924] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00012608.
RefSeqNP_008844.1.
UniGeneHs.534342

3D structure databases

HSSPHSSP built from PDB template 1FBV based on UniProtKB P22681.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99942. 11 interactions.

Proteomic databases

PRIDEQ99942.

Genome annotation databases

EnsemblENSG00000183574. Homo sapiens. [Contig view]
ENSG00000204308. Homo sapiens. [Contig view]
ENSG00000206254. Homo sapiens. [Contig view]
GeneID6048.
KEGGhsa:6048.

Organism-specific databases

GeneCardsGC06P032254.
HGNCHGNC:10068. RNF5.
MIM602677. gene.
PharmGKBPA34442.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ99942.
HOVERGENQ99942.
OMAQ99942. FQSFGDT.

Gene expression databases

BgeeQ99942.
CleanExHS_RNF5.
GermOnlineENSG00000204308. Homo sapiens.

Family and domain databases

InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio23565.
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: June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents