Q96EQ8 (RN125_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

RNF125

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	232 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	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.3 Ref.4
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity Ubl conjugation pathway
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	innate immune response Traceable author statement. Source: Reactome negative regulation of type I interferon production Traceable author statement. Source: Reactome
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 232	231	E3 ubiquitin-protein ligase RNF125		PRO_0000056090
Regions
	Zinc finger	37 – 76	40	RING-type
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine Probable
Experimental info
	Mutagenesis	2	1	G → A: Abolishes ability to regulate T-cell activation but not E3 ligase activity in vitro. Ref.4
	Mutagenesis	37	1	C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-41. Ref.4
	Mutagenesis	40	1	C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-38. Ref.4
	Mutagenesis	54	1	H → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-58. Ref.4
	Mutagenesis	57	1	C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-55. Ref.4
	Mutagenesis	72	1	C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-76. Ref.4
	Mutagenesis	75	1	C → A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-73. Ref.4
	Sequence conflict	105 – 108	4	TLVC → IVLY in AAH12021. Ref.2
	Sequence conflict	187	1	S → N in BAA91182. Ref.1
	Sequence conflict	232	1	T → A in AAH12021. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q96EQ8 [UniParc]. Last modified April 3, 2007. Version 4. Checksum: E3D93D546AD99D81	FASTA	232	26,454
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK000463 mRNA. Translation: BAA91182.1. BC012021 mRNA. Translation: AAH12021.1.
IPI	IPI00410652.
RefSeq	NP_060301.2. NM_017831.3.
UniGene	Hs.633703.
3D structure databases
ProteinModelPortal	Q96EQ8.
SMR	Q96EQ8. Positions 29-174.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96EQ8. 13 interactions.
STRING	Q96EQ8.
Polymorphism databases
DMDM	143811449.
Proteomic databases
PRIDE	Q96EQ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217740; ENSP00000217740; ENSG00000101695.
GeneID	54941.
KEGG	hsa:54941.
UCSC	uc002kxf.1. human.
Organism-specific databases
CTD	54941.
GeneCards	GC18P029598.
H-InvDB	HIX0014384.
HGNC	HGNC:21150. RNF125.
HPA	HPA041514.
MIM	610432. gene.
neXtProt	NX_Q96EQ8.
PharmGKB	PA134950383.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14432.
GeneTree	ENSGT00530000063064.
HOGENOM	HBG125695.
HOVERGEN	HBG098958.
InParanoid	Q96EQ8.
OMA	HIRTCEK.
OrthoDB	EOG4SJ5FM.
PhylomeDB	Q96EQ8.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q96EQ8.
Bgee	Q96EQ8.
CleanEx	HS_RNF125.
Genevestigator	Q96EQ8.
GermOnline	ENSG00000101695. Homo sapiens.
Family and domain databases
InterPro	IPR015880. Znf_C2H2-like. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KO	K12170.
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. SM00355. ZnF_C2H2. 2 hits. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	58082.
SOURCE	Search...

Entry information

Entry name

RN125_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 89 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.