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Reviewed, UniProtKB/Swiss-Prot Q9H6Y7 (RN167_HUMAN)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 RNF167
    EC=6.3.2.-
Alternative name(s):
    RING finger protein 167
    RING105
Gene names
Name: RNF167
ORF Names: LP2254
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processUbl conjugation pathway
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMGlycoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological processmodification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionligase 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

CCDC59Q9P0311EBI-1055214,EBI-1047110

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 350326E3 ubiquitin-protein ligase RNF167
PRO_0000245593

Regions

Transmembrane174 – 19421 Potential
Domain49 – 152104PA
Zinc finger230 – 27243RING-type; atypical

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential

Natural variations

Natural variant1211N → K: dbSNP rs1127356.
VAR_026996

Experimental info

Mutagenesis2321I → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. Ref.6
Mutagenesis2601W → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. Ref.6
Sequence conflict2241Missing in CAD38958. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9H6Y7-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D87493CE24C2A418

FASTA35038,299
        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 

« Hide

References

« Hide '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. 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: 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. expand/collapse author list , 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

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.
IPIIPI00023511.
PIRT08729.
RefSeqNP_056343.1.
UniGeneHs.7158

3D structure databases

HSSPHSSP built from PDB template 1IYM based on UniProtKB Q9LRB7.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9H6Y7. 3 interactions.

Proteomic databases

PeptideAtlasQ9H6Y7.
PRIDEQ9H6Y7.

Genome annotation databases

EnsemblENSG00000108523. Homo sapiens. [Contig view]
GeneID26001.
KEGGhsa:26001.

Organism-specific databases

GeneCardsGC17P004784.
HGNCHGNC:24544. RNF167.
MIM610431. gene.
PharmGKBPA134953711.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9H6Y7.
HOVERGENQ9H6Y7.
OMAQ9H6Y7. FIGERSA.

Gene expression databases

BgeeQ9H6Y7.
CleanExHS_RNF167.
GermOnlineENSG00000108523. Homo sapiens.

Family and domain databases

InterProIPR003137. PA.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF02225. PA. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio47726.
SOURCESearch...

Entry information

Entry nameRN167_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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