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Q9BV68 (RN126_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase RNF126

EC=6.3.2.-
Alternative name(s):
RING finger protein 126
Gene names
Name:RNF126
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase. By ubiquitinating CDKN1A/p21 and targeting it for proteasomal degradation, may promote cell proliferation. Ref.5

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Highly expressed in liver and testis. Ref.5

Post-translational modification

Auto-ubiquitinated.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BV68-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BV68-2)

The sequence of this isoform differs from the canonical sequence as follows:
     309-311: WSP → SNS
     312-326: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 326325E3 ubiquitin-protein ligase RNF126
PRO_0000056093

Regions

Zinc finger229 – 27042RING-type
Compositional bias289 – 30315Ser-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue51Phosphoserine Ref.4

Natural variations

Alternative sequence309 – 3113WSP → SNS in isoform 2.
VSP_015693
Alternative sequence312 – 32615Missing in isoform 2.
VSP_015694
Natural variant681V → M.
Corresponds to variant rs2285751 [ dbSNP | Ensembl ].
VAR_057217

Experimental info

Mutagenesis2291C → A: Loss of E3 ligase activity; when associated with A-232. Ref.5
Mutagenesis2321C → A: Loss of E3 ligase activity; when associated with A-229. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D422FFB090362F46

FASTA32635,585
        10         20         30         40         50         60 
MAEASPHPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSTENG SAPSTAPTDQ 

        70         80         90        100        110        120 
SRPPLEHVDQ HLFTLPQGYG QFAFGIFDDS FEIPTFPPGA QADDGRDPES RRERDHPSRH 

       130        140        150        160        170        180 
RYGARQPRAR LTTRRATGRH EGVPTLEGII QQLVNGIITP ATIPSLGPWG VLHSNPMDYA 

       190        200        210        220        230        240 
WGANGLDAII TQLLNQFENT GPPPADKEKI QALPTVPVTE EHVGSGLECP VCKDDYALGE 

       250        260        270        280        290        300 
RVRQLPCNHL FHDGCIVPWL EQHDSCPVCR KSLTGQNTAT NPPGLTGVSF SSSSSSSSSS 

       310        320 
SPSNENATWS PLGRPQPPRP LSNLTL 

« Hide

Isoform 2 [UniParc].

Checksum: 0C748E78E6719C3E
Show »

FASTA31133,861

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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] (ISOFORMS 1 AND 2).
Tissue: Brain and Placenta.
[3]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[4]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation."
Zhi X., Zhao D., Wang Z., Zhou Z., Wang C., Chen W., Liu R., Chen C.
Cancer Res. 73:385-394(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-229 AND CYS-232.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000559 mRNA. Translation: BAA91254.1.
BC001442 mRNA. Translation: AAH01442.1.
BC025374 mRNA. Translation: AAH25374.1.
RefSeqNP_919442.1. NM_194460.2.
UniGeneHs.69554.

3D structure databases

ProteinModelPortalQ9BV68.
SMRQ9BV68. Positions 219-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120790. 34 interactions.
IntActQ9BV68. 20 interactions.
MINTMINT-1032305.
STRING9606.ENSP00000292363.

PTM databases

PhosphoSiteQ9BV68.

Polymorphism databases

DMDM74762712.

Proteomic databases

PaxDbQ9BV68.
PRIDEQ9BV68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292363; ENSP00000292363; ENSG00000070423. [Q9BV68-2]
GeneID55658.
KEGGhsa:55658.
UCSCuc010drs.3. human. [Q9BV68-2]

Organism-specific databases

CTD55658.
GeneCardsGC19M000647.
H-InvDBHIX0014558.
HGNCHGNC:21151. RNF126.
HPAHPA043050.
MIM615177. gene.
neXtProtNX_Q9BV68.
PharmGKBPA134876469.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5540.
HOGENOMHOG000116417.
HOVERGENHBG059832.
InParanoidQ9BV68.
KOK11982.
OMAPTDQSRP.
OrthoDBEOG7353XB.
PhylomeDBQ9BV68.
TreeFamTF317985.

Gene expression databases

ArrayExpressQ9BV68.
BgeeQ9BV68.
CleanExHS_RNF126.
GenevestigatorQ9BV68.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNF126. human.
GenomeRNAi55658.
NextBio60383.
PROQ9BV68.
SOURCESearch...

Entry information

Entry nameRN126_HUMAN
AccessionPrimary (citable) accession number: Q9BV68
Secondary accession number(s): Q9NWX1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM