Q9H6Y7 (RN167_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF167
EC=6.3.2.-

Alternative name(s):
RING finger protein 167
RING105

Gene names

Name:	RNF167
ORF Names:	LP2254

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	350 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	May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition. Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with SLC22A18. Ref.7
Subcellular location	Endomembrane system; Single-pass membrane protein. Note: Targeted to cytoplasmic membranes. Ref.7
Tissue specificity	Strongly expressed in the kidney and liver (at protein level). Ref.7
Post-translational modification	Auto-ubiquitinated in vitro in the presence of UBE2D1 and UBE2E1.
Sequence similarities	Contains 1 PA (protease associated) domain. Contains 1 RING-type zinc finger.
Sequence caution	The sequence AAP34453.1 differs from that shown. Reason: Frameshift at position 65.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Glycoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of cell cycle Inferred from mutant phenotype Ref.7. Source: UniProtKB protein polyubiquitination Inferred from direct assay Ref.7. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction Ref.7. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.7. 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
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 350	326	E3 ubiquitin-protein ligase RNF167		PRO_0000245593
Regions
	Transmembrane	174 – 194	21	Helical; Potential
	Domain	49 – 152	104	PA
	Zinc finger	230 – 272	43	RING-type; atypical
Amino acid modifications
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	121	1	N → K. Corresponds to variant rs1127356 [ dbSNP | Ensembl ].		VAR_026996
Experimental info
	Mutagenesis	232	1	I → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. Ref.7
	Mutagenesis	260	1	W → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. Ref.7
	Sequence conflict	224	1	Missing in CAD38958. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H6Y7 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: D87493CE24C2A418	FASTA	350	38,299
	10 20 30 40 50 60 MHPAAFPLPV VVAAVLWGAA PTRGLIRATS DHNASMDFAD LPALFGATLS QEGLQGFLVE 70 80 90 100 110 120 AHPDNACSPI APPPPAPVNG SVFIALLRRF DCNFDLKVLN AQKAGYGAAV VHNVNSNELL 130 140 150 160 170 180 NMVWNSEEIQ QQIWIPSVFI GERSSEYLRA LFVYEKGARV LLVPDNTFPL GYYLIPFTGI 190 200 210 220 230 240 VGLLVLAMGA VMIARCIQHR KRLQRNRLTK EQLKQIPTHD YQKGDQYDVC AICLDEYEDG 250 260 270 280 290 300 DKLRVLPCAH AYHSRCVDPW LTQTRKTCPI CKQPVHRGPG DEDQEEETQG QEEGDEGEPR 310 320 330 340 350 DHPASERTPL LGSSPTLPTS FGSLAPAPLV FPGPSTDPPL SPPSSPVILV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal kidney.
[2]	"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: Colon.
[3]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed: 15498874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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 (SEP-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Tumor suppressor candidate TSSC5 is regulated by UbcH6 and a novel ubiquitin ligase RING105." Yamada H.Y., Gorbsky G.J. Oncogene 25:1330-1339(2006) [PubMed: 16314844] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SLC22A18, MUTAGENESIS OF ILE-232 AND TRP-260, UBIQUITINATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL050060 mRNA. Translation: CAB43253.1. AL834284 mRNA. Translation: CAD38958.1. AK025329 mRNA. Translation: BAB15113.1. AY203930 mRNA. Translation: AAP34453.1. Frameshift. CR457340 mRNA. Translation: CAG33621.1. CH471108 Genomic DNA. Translation: EAW90385.1. CH471108 Genomic DNA. Translation: EAW90387.1. CH471108 Genomic DNA. Translation: EAW90388.1. BC010139 mRNA. Translation: AAH10139.1.
IPI	IPI00023511.
PIR	T08729.
RefSeq	NP_056343.1. NM_015528.1.
UniGene	Hs.7158.
3D structure databases
ProteinModelPortal	Q9H6Y7.
SMR	Q9H6Y7. Positions 78-151, 225-276.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H6Y7. 9 interactions.
STRING	Q9H6Y7.
Polymorphism databases
DMDM	74733620.
Proteomic databases
PeptideAtlas	Q9H6Y7.
PRIDE	Q9H6Y7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262482; ENSP00000262482; ENSG00000108523. ENST00000381350; ENSP00000370754; ENSG00000108523.
GeneID	26001.
KEGG	hsa:26001.
UCSC	uc002fzq.1. human.
Organism-specific databases
CTD	26001.
GeneCards	GC17P004784.
H-InvDB	HIX0013455.
HGNC	HGNC:24544. RNF167.
MIM	610431. gene.
neXtProt	NX_Q9H6Y7.
PharmGKB	PA134953711.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18497.
GeneTree	ENSGT00600000084260.
HOGENOM	HBG748141.
HOVERGEN	HBG063762.
InParanoid	Q9H6Y7.
OMA	MLFEDLP.
OrthoDB	EOG4QJRP0.
PhylomeDB	Q9H6Y7.
Gene expression databases
ArrayExpress	Q9H6Y7.
Bgee	Q9H6Y7.
CleanEx	HS_RNF167.
Genevestigator	Q9H6Y7.
GermOnline	ENSG00000108523. Homo sapiens.
Family and domain databases
InterPro	IPR003137. Protease-assoc_domain. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
Pfam	PF02225. PA. 1 hit. PF00097. zf-C3HC4. 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
NextBio	47726.
SOURCE	Search...

Entry information

Entry name

RN167_HUMAN

Accession

Primary (citable) accession number: Q9H6Y7
Secondary accession number(s): D3DTK8 , Q6XYE0, Q8NDC1, Q9Y3V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	March 1, 2001
Last modified:	December 14, 2011
This is version 87 of the entry and version 1 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.