Q9Y4L5 (RN115_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RNF115
Synonyms:	ZNF364

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as an E2-dependent E3 ubiquitin-protein ligase. May be involved in endocytic trafficking. Ref.8 Ref.10
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with RAB7A. Ref.9
Subcellular location	Cytoplasm › cytosol By similarity. Note: The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes By similarity.
Tissue specificity	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. Ref.8
Post-translational modification	RING-type zinc finger-dependent and E2-dependent autoubiquitination.
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein autoubiquitination Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.10. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	E3 ubiquitin-protein ligase RNF115		PRO_0000056314
Regions
	Zinc finger	228 – 269	42	RING-type
Natural variations
	Natural variant	194	1	G → R. Corresponds to variant rs11577731 [ dbSNP | Ensembl ].		VAR_052105
Experimental info
	Mutagenesis	26	1	K → R: Loss of autoubiquitination; when associated with R-32. Ref.10
	Mutagenesis	32	1	K → R: Loss of autoubiquitination; when associated with R-26. Ref.10
	Mutagenesis	228	1	C → A: Loss of autoubiquitination. Ref.10
	Mutagenesis	231	1	C → A: Loss of autoubiquitination. Ref.10
	Sequence conflict	299	1	H → N in CAB45280. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q9Y4L5 [UniParc]. Last modified December 7, 2004. Version 2. Checksum: 22F0C8FCC0F55045	FASTA	304	33,703
	10 20 30 40 50 60 MAEASAAGAD SGAAVAAHRF FCHFCKGEVS PKLPEYICPR CESGFIEEVT DDSSFLGGGG 70 80 90 100 110 120 SRIDNTTTTH FAELWGHLDH TMFFQDFRPF LSSSPLDQDN RANERGHQTH TDFWGARPPR 130 140 150 160 170 180 LPLGRRYRSR GSSRPDRSPA IEGILQHIFA GFFANSAIPG SPHPFSWSGM LHSNPGDYAW 190 200 210 220 230 240 GQTGLDAIVT QLLGQLENTG PPPADKEKIT SLPTVTVTQE QVDMGLECPV CKEDYTVEEE 250 260 270 280 290 300 VRQLPCNHFF HSSCIVPWLE LHDTCPVCRK SLNGEDSTRQ SQSTEASASN RFSNDSQLHD RWTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00337608.
RefSeq	NP_055270.1. NM_014455.2. XP_003960213.1. XM_003960164.1.
UniGene	Hs.523550.
3D structure databases
ProteinModelPortal	Q9Y4L5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y4L5. 7 interactions.
STRING	9606.ENSP00000358297.
PTM databases
PhosphoSite	Q9Y4L5.
Polymorphism databases
DMDM	56405389.
Proteomic databases
PaxDb	Q9Y4L5.
PRIDE	Q9Y4L5.
Protocols and materials databases
DNASU	27246.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369291; ENSP00000358297; ENSG00000121848.
GeneID	101060478. 27246.
KEGG	hsa:101060478. hsa:27246.
UCSC	uc001eoj.3. human.
Organism-specific databases
CTD	27246.
GeneCards	GC01P145611.
HGNC	HGNC:18154. RNF115.
HPA	HPA019130.
neXtProt	NX_Q9Y4L5.
PharmGKB	PA162401519.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG235630.
HOGENOM	HOG000116417.
HOVERGEN	HBG059832.
InParanoid	Q9Y4L5.
KO	K11982.
OMA	STHFAEF.
OrthoDB	EOG4VX262.
PhylomeDB	Q9Y4L5.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9Y4L5.
Bgee	Q9Y4L5.
CleanEx	HS_RNF115.
Genevestigator	Q9Y4L5.
GermOnline	ENSG00000121848. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF13639. zf-RING_2. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RNF115. human.
NextBio	50157.

Entry information

Entry name

RN115_HUMAN

Accession

Primary (citable) accession number: Q9Y4L5
Secondary accession number(s): A8K3Y4, Q5T2V9, Q7Z2J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	December 7, 2004
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.