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Q9BV68

- RN126_HUMAN

UniProt

Q9BV68 - RN126_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF126

Gene

RNF126

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

Functioni

E3 ubiquitin-protein ligase that regulates several biological processes through ubiquitination of various target proteins. Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. Through their polyubiquitination, may play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4. May also be part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. May provide the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the mislocalized proteins and their targeting to the proteasome (PubMed:24981174). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (PubMed:24275455). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (PubMed:23026136). May monoubiquitinate AICDA (PubMed:23277564).By similarity3 Publications1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri229 – 27042RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin protein ligase activity Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. protein K48-linked ubiquitination Source: UniProtKB
  4. protein K63-linked ubiquitination Source: UniProtKB
  5. protein monoubiquitination Source: UniProtKB
  6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. regulation of cell proliferation Source: UniProtKB
  8. regulation of protein localization Source: UniProtKB
  9. retrograde transport, endosome to Golgi Source: UniProtKB
  10. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway 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 RNF126Curated (EC:6.3.2.-2 Publications)
Alternative name(s):
RING finger protein 126Imported
Gene namesi
Name:RNF126Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:21151. RNF126.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi229 – 2291C → A: Loss of E3 ligase activity; when associated with A-232. 1 Publication
Mutagenesisi232 – 2321C → A: Loss of E3 ligase activity; when associated with A-229. 1 Publication

Organism-specific databases

PharmGKBiPA134876469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 326325E3 ubiquitin-protein ligase RNF126PRO_0000056093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated. May undergo autoubiquitination.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9BV68.
PaxDbiQ9BV68.
PRIDEiQ9BV68.

PTM databases

PhosphoSiteiQ9BV68.

Expressioni

Tissue specificityi

Highly expressed in liver and testis.1 Publication

Gene expression databases

BgeeiQ9BV68.
CleanExiHS_RNF126.
ExpressionAtlasiQ9BV68. baseline and differential.
GenevestigatoriQ9BV68.

Organism-specific databases

HPAiHPA043050.

Interactioni

Subunit structurei

Interacts with CCDC50, EGFR, FLT3 and SCAMP3. Interacts with BAG6 (via ubiquitin-like domain); required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol. Interacts with CDKN1A. Interacts with AICDA.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2D1P516683EBI-357322,EBI-743540
UBE2D3P610773EBI-357322,EBI-348268
UBE2D4Q9Y2X83EBI-357322,EBI-745527

Protein-protein interaction databases

BioGridi120790. 52 interactions.
IntActiQ9BV68. 20 interactions.
MINTiMINT-1032305.
STRINGi9606.ENSP00000292363.

Structurei

3D structure databases

ProteinModelPortaliQ9BV68.
SMRiQ9BV68. Positions 219-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 10096Required for interaction with BAG61 PublicationAdd
BLAST
Regioni200 – 304105Sufficient for interaction with AICDA1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi289 – 30315Ser-richAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri229 – 27042RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5540.
GeneTreeiENSGT00530000062967.
HOGENOMiHOG000116417.
HOVERGENiHBG059832.
InParanoidiQ9BV68.
KOiK11982.
OMAiLEHVDQH.
OrthoDBiEOG7353XB.
PhylomeDBiQ9BV68.
TreeFamiTF317985.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BV68-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAEASPHPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSTENG
60 70 80 90 100
SAPSTAPTDQ SRPPLEHVDQ HLFTLPQGYG QFAFGIFDDS FEIPTFPPGA
110 120 130 140 150
QADDGRDPES RRERDHPSRH RYGARQPRAR LTTRRATGRH EGVPTLEGII
160 170 180 190 200
QQLVNGIITP ATIPSLGPWG VLHSNPMDYA WGANGLDAII TQLLNQFENT
210 220 230 240 250
GPPPADKEKI QALPTVPVTE EHVGSGLECP VCKDDYALGE RVRQLPCNHL
260 270 280 290 300
FHDGCIVPWL EQHDSCPVCR KSLTGQNTAT NPPGLTGVSF SSSSSSSSSS
310 320
SPSNENATWS PLGRPQPPRP LSNLTL
Length:326
Mass (Da):35,585
Last modified:June 1, 2001 - v1
Checksum:iD422FFB090362F46
GO
Isoform 2 (identifier: Q9BV68-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:311
Mass (Da):33,861
Checksum:i0C748E78E6719C3E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681V → M.
Corresponds to variant rs2285751 [ dbSNP | Ensembl ].
VAR_057217

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei309 – 3113WSP → SNS in isoform 2. 2 PublicationsVSP_015693
Alternative sequencei312 – 32615Missing in isoform 2. 2 PublicationsVSP_015694Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000559 mRNA. Translation: BAA91254.1.
BC001442 mRNA. Translation: AAH01442.1.
BC025374 mRNA. Translation: AAH25374.1.
CCDSiCCDS12039.1. [Q9BV68-2]
RefSeqiNP_919442.1. NM_194460.2. [Q9BV68-2]
UniGeneiHs.69554.

Genome annotation databases

EnsembliENST00000292363; ENSP00000292363; ENSG00000070423. [Q9BV68-2]
GeneIDi55658.
KEGGihsa:55658.
UCSCiuc010drs.3. human. [Q9BV68-2]

Polymorphism databases

DMDMi74762712.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000559 mRNA. Translation: BAA91254.1 .
BC001442 mRNA. Translation: AAH01442.1 .
BC025374 mRNA. Translation: AAH25374.1 .
CCDSi CCDS12039.1. [Q9BV68-2 ]
RefSeqi NP_919442.1. NM_194460.2. [Q9BV68-2 ]
UniGenei Hs.69554.

3D structure databases

ProteinModelPortali Q9BV68.
SMRi Q9BV68. Positions 219-288.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120790. 52 interactions.
IntActi Q9BV68. 20 interactions.
MINTi MINT-1032305.
STRINGi 9606.ENSP00000292363.

PTM databases

PhosphoSitei Q9BV68.

Polymorphism databases

DMDMi 74762712.

Proteomic databases

MaxQBi Q9BV68.
PaxDbi Q9BV68.
PRIDEi Q9BV68.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000292363 ; ENSP00000292363 ; ENSG00000070423 . [Q9BV68-2 ]
GeneIDi 55658.
KEGGi hsa:55658.
UCSCi uc010drs.3. human. [Q9BV68-2 ]

Organism-specific databases

CTDi 55658.
GeneCardsi GC19M000647.
H-InvDB HIX0014558.
HGNCi HGNC:21151. RNF126.
HPAi HPA043050.
MIMi 615177. gene.
neXtProti NX_Q9BV68.
PharmGKBi PA134876469.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5540.
GeneTreei ENSGT00530000062967.
HOGENOMi HOG000116417.
HOVERGENi HBG059832.
InParanoidi Q9BV68.
KOi K11982.
OMAi LEHVDQH.
OrthoDBi EOG7353XB.
PhylomeDBi Q9BV68.
TreeFami TF317985.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi RNF126. human.
GenomeRNAii 55658.
NextBioi 60383.
PROi Q9BV68.
SOURCEi Search...

Gene expression databases

Bgeei Q9BV68.
CleanExi HS_RNF126.
ExpressionAtlasi Q9BV68. baseline and differential.
Genevestigatori Q9BV68.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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] (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, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CDKN1A, SUBCELLULAR LOCATION, UBIQUITINATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-229 AND CYS-232.
  6. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCDC50; EGFR; FLT3 AND SCAMP3.
  7. "Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase."
    Delker R.K., Zhou Y., Strikoudis A., Stebbins C.E., Papavasiliou F.N.
    Proc. Natl. Acad. Sci. U.S.A. 110:1029-1034(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AICDA.
  8. "The ubiquitin ligase RNF126 regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor."
    Smith C.J., McGlade C.J.
    Exp. Cell Res. 320:219-232(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6."
    Rodrigo-Brenni M.C., Gutierrez E., Hegde R.S.
    Mol. Cell 55:227-237(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH BAG6.

Entry informationi

Entry nameiRN126_HUMAN
AccessioniPrimary (citable) accession number: Q9BV68
Secondary accession number(s): Q9NWX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 109 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 19
    Human chromosome 19: 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

External Data

Dasty 3