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Reviewed, UniProtKB/Swiss-Prot Q96EQ8 (RN125_HUMAN)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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 names
Name: RNF125
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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. Ref.4

Pathway

Protein modification; protein ubiquitination.

Tissue specificity

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. Ref.4 Ref.3

Sequence similarities

Contains 1 RING-type zinc finger.

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Ontologies

Keywords
   Biological processImmune response
Ubl conjugation pathway
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMLipoprotein
Myristate
Gene Ontology (GO)
   Biological processimmune response

Inferred from electronic annotation. Source: UniProtKB-KW

modification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 232231E3 ubiquitin-protein ligase RNF125
PRO_0000056090

Regions

Zinc finger37 – 7640RING-type

Amino acid modifications

Lipidation21N-myristoyl glycine Probable

Experimental info

Mutagenesis21G → A: Abolishes ability to regulate T-cell activation but not E3 ligase activity in vitro. Ref.4
Mutagenesis371C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-41. Ref.4
Mutagenesis401C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-38. Ref.4
Mutagenesis541H → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-58. Ref.4
Mutagenesis571C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-55. Ref.4
Mutagenesis721C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-76. Ref.4
Mutagenesis751C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-73. Ref.4
Sequence conflict105 – 1084TLVC → IVLY in AAH12021. Ref.2
Sequence conflict1871S → N in BAA91182. Ref.1
Sequence conflict2321T → A in AAH12021. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q96EQ8-1 [UniParc].

Last modified April 3, 2007. Version 4.
Checksum: E3D93D546AD99D81

FASTA23226,454
        10         20         30         40         50         60 
MGSVLSTDSG KSAPASATAR ALERRRDPEL PVTSFDCAVC LEVLHQPVRT RCGHVFCRSC 

        70         80         90        100        110        120 
IATSLKNNKW TCPYCRAYLP SEGVPATDVA KRMKSEYKNC AECDTLVCLS EMRAHIRTCQ 

       130        140        150        160        170        180 
KYIDKYGPLQ ELEETAARCV CPFCQRELYE DSLLDHCITH HRSERRPVFC PLCRLIPDEN 

       190        200        210        220        230 
PSSFSGSLIR HLQVSHTLFY DDFIDFNIIE EALIRRVLDR SLLEYVNHSN TT

« Hide

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References

« Hide 'large scale' references
[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. 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: 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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"Systematic identification of regulatory proteins critical for T-cell activation."
Chu P., Pardo J., Zhao H., Li C.C., Pali E., Shen M.M., Qu K., Yu S.X., Huang B.C.B., Yu P., Masuda E.S., Molineaux S.M., Kolbinger F., Aversa G., de Vries J., Payan D.G., Liao X.C.
J. Biol. 2:21.1-21.16(2003) [PubMed: 12974981] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
[4]"A novel E3 ubiquitin ligase TRAC-1 positively regulates T cell activation."
Zhao H., Li C.C., Pardo J., Chu P.C., Liao C.X., Huang J., Dong J.G., Zhou X., Huang Q., Huang B.C.B., Bennett M.K., Molineaux S.M., Lu H., Daniel-Issakani S., Payan D.G., Masuda E.S.
J. Immunol. 174:5288-5297(2005) [PubMed: 15843525] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-2; CYS-37; CYS-40; HIS-54; CYS-57; CYS-72 AND CYS-75.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK000463 mRNA. Translation: BAA91182.1.
BC012021 mRNA. Translation: AAH12021.1.
IPIIPI00410652.
RefSeqNP_060301.2.
UniGeneHs.633703

3D structure databases

HSSPHSSP built from PDB template 1RMD based on UniProtKB P15919.
ModBaseSearch...

Proteomic databases

PRIDEQ96EQ8.

Genome annotation databases

EnsemblENSG00000101695. Homo sapiens. [Contig view]
GeneID54941.
KEGGhsa:54941.

Organism-specific databases

GeneCardsGC18P027852.
H-InvDBHIX0014384.
HGNCHGNC:21150. RNF125.
MIM610432. gene.
PharmGKBPA134950383.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ96EQ8.
HOVERGENQ96EQ8.
OMAQ96EQ8. RAYLPSE.

Gene expression databases

ArrayExpressQ96EQ8.
BgeeQ96EQ8.
CleanExHS_RNF125.
GermOnlineENSG00000101695. Homo sapiens.

Family and domain databases

InterProIPR015880. Znf_C2H2-like.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio58082.
SOURCESearch...

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Entry information

Entry nameRN125_HUMAN
AccessionPrimary (citable) accession number: Q96EQ8
Secondary accession number(s): Q9NX39
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: April 3, 2007
Last modified: June 16, 2009
This is version 64 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents