Reviewed, UniProtKB/Swiss-Prot Q99942 (RNF5_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.9
Subcellular location	Membrane; Multi-pass membrane protein Potential. Note: Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles. Ref.9
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Membrane
Domain	Transmembrane Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ligase 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT5	O95870	1	EBI-348482,EBI-348517
CFTR	P13569	1	EBI-348482,EBI-349854
FHOD1	Q9Y613	1	EBI-348482,EBI-348433
PXN	P49023	3	EBI-348482,EBI-702209
UBE2D2	P62837	2	EBI-348482,EBI-347677
UBE2D3	P61077	2	EBI-348482,EBI-348268
UBE2E1	P51965	1	EBI-348482,EBI-348546
UBE2E3	Q969T4	1	EBI-348482,EBI-348496

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 180	179	E3 ubiquitin-protein ligase RNF5		PRO_0000240393
Regions
	Transmembrane	118 – 138	21	Potential
	Transmembrane	160 – 180	21	Potential
	Zinc finger	27 – 68	42	RING-type
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.11
Experimental info
	Mutagenesis	42	1	C → S: Loss of E3 ubiquitin-protein ligase activity. Ref.2
	Sequence conflict	22	1	G → S in CAB51286. Ref.3
	Sequence conflict	60	1	E → D in CAB51286. Ref.3
	Sequence conflict	117	1	T → A in CAB51286. Ref.3
	Sequence conflict	148	1	T → A in CAB51286. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q99942-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: E5AFA4DE6DE85942	FASTA	180	19,881
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
+	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.
IPI	IPI00012608.
RefSeq	NP_008844.1.
UniGene	Hs.718462
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29268N.
IntAct	Q99942. 18 interactions.
STRING	Q99942.
Proteomic databases
PRIDE	Q99942.
Genome annotation databases
Ensembl	ENST00000375094; ENSP00000364235; ENSG00000204308; Homo sapiens. [Genome view] ENST00000413786; ENSP00000387879; ENSG00000225452; Homo sapiens. [Genome view] ENST00000432616; ENSP00000413131; ENSG00000183574; Homo sapiens. [Genome view] ENST00000445885; ENSP00000401172; ENSG00000227277; Homo sapiens. [Genome view] ENST00000449794; ENSP00000415784; ENSG00000223767; Homo sapiens. [Genome view] ENST00000453473; ENSP00000415127; ENSG00000228907; Homo sapiens. [Genome view] ENST00000456167; ENSP00000388795; ENSG00000228405; Homo sapiens. [Genome view]
GeneID	6048.
KEGG	hsa:6048.
UCSC	uc003oaj.2. human.
Organism-specific databases
CTD	6048.
GeneCards	GC06P032254.
HGNC	HGNC:10068. RNF5.
MIM	602677. gene.
PharmGKB	PA34442.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG21064.
HOVERGEN	Q99942.
InParanoid	Q99942.
OMA	FQSFGDT.
PhylomeDB	Q99942.
Gene expression databases
CleanEx	HS_RNF5.
Genevestigator	Q99942.
GermOnline	ENSG00000204308. Homo sapiens.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	23565.
SOURCE	Search...

Entry information

Entry name

RNF5_HUMAN

Accession

Primary (citable) accession number: Q99942
Secondary accession number(s): A2BFI6 , B2R4K3, Q0VDB7, Q9UMQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	May 1, 1997
Last modified:	January 19, 2010
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.