Reviewed, UniProtKB/Swiss-Prot Q9H6Y7 (RN167_HUMAN)

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.6
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with SLC22A18. Ref.6
Subcellular location	Endomembrane system; Single-pass membrane protein. Note: Targeted to cytoplasmic membranes.
Tissue specificity	Strongly expressed in the kidney and liver (at protein level). Ref.6
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 Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Glycoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCDC59	Q9P031	1	EBI-1055214,EBI-1047110

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	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: dbSNP rs1127356.		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.6
	Mutagenesis	260	1	W → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. Ref.6
	Sequence conflict	224	1	Missing in CAD38958. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H6Y7-1 [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 German cDNA consortium Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases 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]	"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.
[6]	"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
EMBLGenBankDDBJ	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. BC010139 mRNA. Translation: AAH10139.1.
IPI	IPI00023511.
PIR	T08729.
RefSeq	NP_056343.1.
UniGene	Hs.7158
3D structure databases
HSSP	HSSP built from PDB template 1IYM based on UniProtKB Q9LRB7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H6Y7. 3 interactions.
Proteomic databases
PeptideAtlas	Q9H6Y7.
PRIDE	Q9H6Y7.
Genome annotation databases
Ensembl	ENSG00000108523. Homo sapiens. [Contig view]
GeneID	26001.
KEGG	hsa:26001.
Organism-specific databases
GeneCards	GC17P004784.
HGNC	HGNC:24544. RNF167.
MIM	610431. gene.
PharmGKB	PA134953711.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9H6Y7.
HOVERGEN	Q9H6Y7.
OMA	Q9H6Y7. FIGERSA.
Gene expression databases
Bgee	Q9H6Y7.
CleanEx	HS_RNF167.
GermOnline	ENSG00000108523. Homo sapiens.
Family and domain databases
InterPro	IPR003137. PA. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR017907. Znf_RING_CS. [Graphical view]
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 Resources
NextBio	47726.
SOURCE	Search...

Entry information

Entry name

RN167_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)