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Protein

E3 ubiquitin-protein ligase RNF167

Gene

RNF167

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri230 – 27243RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of cell cycle Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF167 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 167
RING105
Gene namesi
Name:RNF167
ORF Names:LP2254
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:24544. RNF167.

Subcellular locationi

  • Endomembrane system 1 Publication; Single-pass membrane protein 1 Publication

  • Note: Targeted to cytoplasmic membranes.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei174 – 19421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endomembrane system Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2321I → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. 1 Publication
Mutagenesisi260 – 2601W → A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1. 1 Publication

Organism-specific databases

PharmGKBiPA134953711.

Polymorphism and mutation databases

BioMutaiRNF167.
DMDMi74733620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 350326E3 ubiquitin-protein ligase RNF167PRO_0000245593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Auto-ubiquitinated in vitro in the presence of UBE2D1 and UBE2E1.1 Publication

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H6Y7.
MaxQBiQ9H6Y7.
PaxDbiQ9H6Y7.
PeptideAtlasiQ9H6Y7.
PRIDEiQ9H6Y7.

PTM databases

iPTMnetiQ9H6Y7.
PhosphoSiteiQ9H6Y7.
SwissPalmiQ9H6Y7.

Expressioni

Tissue specificityi

Strongly expressed in the kidney and liver (at protein level).1 Publication

Gene expression databases

BgeeiQ9H6Y7.
CleanExiHS_RNF167.
ExpressionAtlasiQ9H6Y7. baseline and differential.
GenevisibleiQ9H6Y7. HS.

Organism-specific databases

HPAiHPA049810.

Interactioni

Subunit structurei

Interacts with SLC22A18.1 Publication

Protein-protein interaction databases

BioGridi117477. 21 interactions.
IntActiQ9H6Y7. 17 interactions.
STRINGi9606.ENSP00000262482.

Structurei

3D structure databases

ProteinModelPortaliQ9H6Y7.
SMRiQ9H6Y7. Positions 230-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 152104PAAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri230 – 27243RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG4628. Eukaryota.
ENOG410Z5DF. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000234362.
HOVERGENiHBG063762.
InParanoidiQ9H6Y7.
KOiK15706.
OMAiCIARRET.
OrthoDBiEOG7NW68S.
PhylomeDBiQ9H6Y7.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_domain.
IPR001841. Znf_RING.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H6Y7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHPAAFPLPV VVAAVLWGAA PTRGLIRATS DHNASMDFAD LPALFGATLS
60 70 80 90 100
QEGLQGFLVE AHPDNACSPI APPPPAPVNG SVFIALLRRF DCNFDLKVLN
110 120 130 140 150
AQKAGYGAAV VHNVNSNELL NMVWNSEEIQ QQIWIPSVFI GERSSEYLRA
160 170 180 190 200
LFVYEKGARV LLVPDNTFPL GYYLIPFTGI VGLLVLAMGA VMIARCIQHR
210 220 230 240 250
KRLQRNRLTK EQLKQIPTHD YQKGDQYDVC AICLDEYEDG DKLRVLPCAH
260 270 280 290 300
AYHSRCVDPW LTQTRKTCPI CKQPVHRGPG DEDQEEETQG QEEGDEGEPR
310 320 330 340 350
DHPASERTPL LGSSPTLPTS FGSLAPAPLV FPGPSTDPPL SPPSSPVILV
Length:350
Mass (Da):38,299
Last modified:March 1, 2001 - v1
Checksum:iD87493CE24C2A418
GO

Sequence cautioni

The sequence AAP34453.1 differs from that shown. Reason: Frameshift at position 65. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241Missing in CAD38958 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211N → K.
Corresponds to variant rs1127356 [ dbSNP | Ensembl ].
VAR_026996

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11060.1.
PIRiT08729.
RefSeqiNP_001307285.1. NM_001320356.1.
NP_001307286.1. NM_001320357.1.
NP_001307287.1. NM_001320358.1.
NP_001307288.1. NM_001320359.1.
NP_001307289.1. NM_001320360.1.
NP_001307290.1. NM_001320361.1.
NP_001307291.1. NM_001320362.1.
NP_001307292.1. NM_001320363.1.
NP_001307293.1. NM_001320364.1.
NP_001307294.1. NM_001320365.1.
NP_056343.1. NM_015528.2.
UniGeneiHs.7158.

Genome annotation databases

EnsembliENST00000262482; ENSP00000262482; ENSG00000108523.
ENST00000571816; ENSP00000459324; ENSG00000108523.
ENST00000572430; ENSP00000458794; ENSG00000108523.
ENST00000575111; ENSP00000460190; ENSG00000108523.
GeneIDi26001.
KEGGihsa:26001.
UCSCiuc002fzs.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11060.1.
PIRiT08729.
RefSeqiNP_001307285.1. NM_001320356.1.
NP_001307286.1. NM_001320357.1.
NP_001307287.1. NM_001320358.1.
NP_001307288.1. NM_001320359.1.
NP_001307289.1. NM_001320360.1.
NP_001307290.1. NM_001320361.1.
NP_001307291.1. NM_001320362.1.
NP_001307292.1. NM_001320363.1.
NP_001307293.1. NM_001320364.1.
NP_001307294.1. NM_001320365.1.
NP_056343.1. NM_015528.2.
UniGeneiHs.7158.

3D structure databases

ProteinModelPortaliQ9H6Y7.
SMRiQ9H6Y7. Positions 230-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117477. 21 interactions.
IntActiQ9H6Y7. 17 interactions.
STRINGi9606.ENSP00000262482.

PTM databases

iPTMnetiQ9H6Y7.
PhosphoSiteiQ9H6Y7.
SwissPalmiQ9H6Y7.

Polymorphism and mutation databases

BioMutaiRNF167.
DMDMi74733620.

Proteomic databases

EPDiQ9H6Y7.
MaxQBiQ9H6Y7.
PaxDbiQ9H6Y7.
PeptideAtlasiQ9H6Y7.
PRIDEiQ9H6Y7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262482; ENSP00000262482; ENSG00000108523.
ENST00000571816; ENSP00000459324; ENSG00000108523.
ENST00000572430; ENSP00000458794; ENSG00000108523.
ENST00000575111; ENSP00000460190; ENSG00000108523.
GeneIDi26001.
KEGGihsa:26001.
UCSCiuc002fzs.4. human.

Organism-specific databases

CTDi26001.
GeneCardsiRNF167.
HGNCiHGNC:24544. RNF167.
HPAiHPA049810.
MIMi610431. gene.
neXtProtiNX_Q9H6Y7.
PharmGKBiPA134953711.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4628. Eukaryota.
ENOG410Z5DF. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000234362.
HOVERGENiHBG063762.
InParanoidiQ9H6Y7.
KOiK15706.
OMAiCIARRET.
OrthoDBiEOG7NW68S.
PhylomeDBiQ9H6Y7.
TreeFamiTF317486.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF167. human.
GenomeRNAii26001.
NextBioi47726.
PROiQ9H6Y7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H6Y7.
CleanExiHS_RNF167.
ExpressionAtlasiQ9H6Y7. baseline and differential.
GenevisibleiQ9H6Y7. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_domain.
IPR001841. Znf_RING.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [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] [Europe PMC] [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. 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: 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SLC22A18, MUTAGENESIS OF ILE-232 AND TRP-260, UBIQUITINATION, TISSUE SPECIFICITY.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRN167_HUMAN
AccessioniPrimary (citable) accession number: Q9H6Y7
Secondary accession number(s): D3DTK8
, Q6XYE0, Q8NDC1, Q9Y3V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.