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Protein

E3 ubiquitin-protein ligase RNF125

Gene

RNF125

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

Functioni

E3 ubiquitin-protein ligase that acts as a positive regulator of T-cell activation. E3 ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins.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 fingeri37 – 7640RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri100 – 11920C2HC-type1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Adaptive immunity, Immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF125 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 125
T-cell RING activation protein 1
Short name:
TRAC-1
Gene namesi
Name:RNF125
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:21150. RNF125.

Subcellular locationi

  • Golgi apparatus membrane 1 Publication; Lipid-anchor 1 Publication

  • Note: Shows a reticular staining pattern within the cell and is probably expressed at other intracellular membranes in addition to the Golgi membrane. Not detected at the plasma membrane.1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Tenorio syndrome (TNORS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by overgrowth, macrocephaly, and intellectual disability. Some patients may have mild hydrocephaly, hypoglycemia, and inflammatory diseases resembling Sjogren syndrome.
See also OMIM:616260
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121M → I in TNORS. 1 Publication
VAR_073353
Natural varianti163 – 1631S → L in TNORS. 1 Publication
VAR_073354
Natural varianti174 – 1741R → C in TNORS. 1 Publication
VAR_073355

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Abolishes ability to regulate T-cell activation but not E3 ligase activity in vitro. Also abolishes myristoylation and membrane localization. 2 Publications
Mutagenesisi37 – 371C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-40. 2 Publications
Mutagenesisi40 – 401C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-37. 2 Publications
Mutagenesisi54 – 541H → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-58. 1 Publication
Mutagenesisi57 – 571C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-55. 1 Publication
Mutagenesisi72 – 721C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-76. 1 Publication
Mutagenesisi75 – 751C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-73. 1 Publication
Mutagenesisi217 – 2171V → P: Reduced ubiquitination and reduced binding to ubiquitinated proteins; when associated with Q-221. 1 Publication
Mutagenesisi221 – 2211S → Q: Reduced ubiquitination and reduced binding to ubiquitinated proteins; when associated with P-217. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi616260. phenotype.
PharmGKBiPA134950383.

Polymorphism and mutation databases

BioMutaiRNF125.
DMDMi143811449.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 232231E3 ubiquitin-protein ligase RNF125PRO_0000056090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication

Post-translational modificationi

Autoubiquitinated, leading to its subsequent proteasomal degradation.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Ubl conjugation

Proteomic databases

PaxDbiQ96EQ8.
PRIDEiQ96EQ8.

PTM databases

iPTMnetiQ96EQ8.
PhosphoSiteiQ96EQ8.

Expressioni

Tissue specificityi

Predominantly expressed in lymphoid tissues, including bone marrow, spleen and thymus. Also weakly expressed in other tissues. Predominant in the CD4+ and CD8+ T-cells, suggesting that it is preferentially confined to T-cells.2 Publications

Gene expression databases

BgeeiQ96EQ8.
CleanExiHS_RNF125.
ExpressionAtlasiQ96EQ8. baseline and differential.
GenevisibleiQ96EQ8. HS.

Organism-specific databases

HPAiHPA041514.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120281. 20 interactions.
DIPiDIP-52778N.
IntActiQ96EQ8. 19 interactions.
STRINGi9606.ENSP00000217740.

Structurei

3D structure databases

ProteinModelPortaliQ96EQ8.
SMRiQ96EQ8. Positions 27-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 22415Required for interaction with ubiquitin and for autoubiquitination1 PublicationAdd
BLAST

Sequence similaritiesi

Contains 1 C2HC-type zinc finger.1 Publication
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 7640RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri100 – 11920C2HC-type1 PublicationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IJHI. Eukaryota.
ENOG410YBNH. LUCA.
GeneTreeiENSGT00530000063064.
HOGENOMiHOG000230946.
HOVERGENiHBG098958.
InParanoidiQ96EQ8.
KOiK12170.
OMAiVTSFDCS.
OrthoDBiEOG7SFHXF.
PhylomeDBiQ96EQ8.
TreeFamiTF331012.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR008598. Di19_Zn_binding_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF05605. zf-Di19. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q96EQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSVLSTDSG KSAPASATAR ALERRRDPEL PVTSFDCAVC LEVLHQPVRT
60 70 80 90 100
RCGHVFCRSC IATSLKNNKW TCPYCRAYLP SEGVPATDVA KRMKSEYKNC
110 120 130 140 150
AECDTLVCLS EMRAHIRTCQ KYIDKYGPLQ ELEETAARCV CPFCQRELYE
160 170 180 190 200
DSLLDHCITH HRSERRPVFC PLCRLIPDEN PSSFSGSLIR HLQVSHTLFY
210 220 230
DDFIDFNIIE EALIRRVLDR SLLEYVNHSN TT
Length:232
Mass (Da):26,454
Last modified:April 3, 2007 - v4
Checksum:iE3D93D546AD99D81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1084TLVC → IVLY in AAH12021 (PubMed:15489334).Curated
Sequence conflicti187 – 1871S → N in BAA91182 (PubMed:14702039).Curated
Sequence conflicti232 – 2321T → A in AAH12021 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121M → I in TNORS. 1 Publication
VAR_073353
Natural varianti163 – 1631S → L in TNORS. 1 Publication
VAR_073354
Natural varianti174 – 1741R → C in TNORS. 1 Publication
VAR_073355

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000463 mRNA. Translation: BAA91182.1.
BC012021 mRNA. Translation: AAH12021.1.
CCDSiCCDS11902.1.
RefSeqiNP_060301.2. NM_017831.3.
UniGeneiHs.633703.

Genome annotation databases

EnsembliENST00000217740; ENSP00000217740; ENSG00000101695.
GeneIDi54941.
KEGGihsa:54941.
UCSCiuc002kxf.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000463 mRNA. Translation: BAA91182.1.
BC012021 mRNA. Translation: AAH12021.1.
CCDSiCCDS11902.1.
RefSeqiNP_060301.2. NM_017831.3.
UniGeneiHs.633703.

3D structure databases

ProteinModelPortaliQ96EQ8.
SMRiQ96EQ8. Positions 27-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120281. 20 interactions.
DIPiDIP-52778N.
IntActiQ96EQ8. 19 interactions.
STRINGi9606.ENSP00000217740.

PTM databases

iPTMnetiQ96EQ8.
PhosphoSiteiQ96EQ8.

Polymorphism and mutation databases

BioMutaiRNF125.
DMDMi143811449.

Proteomic databases

PaxDbiQ96EQ8.
PRIDEiQ96EQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217740; ENSP00000217740; ENSG00000101695.
GeneIDi54941.
KEGGihsa:54941.
UCSCiuc002kxf.2. human.

Organism-specific databases

CTDi54941.
GeneCardsiRNF125.
H-InvDBHIX0014384.
HGNCiHGNC:21150. RNF125.
HPAiHPA041514.
MIMi610432. gene.
616260. phenotype.
neXtProtiNX_Q96EQ8.
PharmGKBiPA134950383.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJHI. Eukaryota.
ENOG410YBNH. LUCA.
GeneTreeiENSGT00530000063064.
HOGENOMiHOG000230946.
HOVERGENiHBG098958.
InParanoidiQ96EQ8.
KOiK12170.
OMAiVTSFDCS.
OrthoDBiEOG7SFHXF.
PhylomeDBiQ96EQ8.
TreeFamiTF331012.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

GeneWikiiRNF125.
GenomeRNAii54941.
PROiQ96EQ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ96EQ8.
CleanExiHS_RNF125.
ExpressionAtlasiQ96EQ8. baseline and differential.
GenevisibleiQ96EQ8. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR008598. Di19_Zn_binding_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF05605. zf-Di19. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Carcinoma.
  2. "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: Testis.
  3. Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
  4. Cited for: FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-2; CYS-37; CYS-40; HIS-54; CYS-57; CYS-72 AND CYS-75.
  5. "T-cell regulator RNF125/TRAC-1 belongs to a novel family of ubiquitin ligases with zinc fingers and a ubiquitin-binding domain."
    Giannini A.L., Gao Y., Bijlmakers M.J.
    Biochem. J. 410:101-111(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, AUTOUBIQUITINATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; CYS-37; CYS-40; VAL-217 AND SER-221.
  6. Cited for: INVOLVEMENT IN TNORS, VARIANTS TNORS ILE-112; LEU-163 AND CYS-174.

Entry informationi

Entry nameiRN125_HUMAN
AccessioniPrimary (citable) accession number: Q96EQ8
Secondary accession number(s): Q9NX39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: April 3, 2007
Last modified: June 8, 2016
This is version 129 of the entry and version 4 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 18
    Human chromosome 18: 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.