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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. By ubiquitinating CDKN1A/p21 and targeting it for proteasomal degradation, may promote cell proliferation.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri229 – 27042RING-type
Add
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF126 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 126
Gene namesi
Name:RNF126
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:21151. RNF126.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
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 RNF126
PRO_0000056093Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Auto-ubiquitinated.

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

ArrayExpressiQ9BV68.
BgeeiQ9BV68.
CleanExiHS_RNF126.
GenevestigatoriQ9BV68.

Organism-specific databases

HPAiHPA043050.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi120790. 34 interactions.
IntActiQ9BV68. 20 interactions.
MINTiMINT-1032305.
STRINGi9606.ENSP00000292363.

Structurei

3D structure databases

ProteinModelPortaliQ9BV68.
SMRiQ9BV68. Positions 219-288.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5540.
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

MAEASPHPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSTENG    50
SAPSTAPTDQ SRPPLEHVDQ HLFTLPQGYG QFAFGIFDDS FEIPTFPPGA 100
QADDGRDPES RRERDHPSRH RYGARQPRAR LTTRRATGRH EGVPTLEGII 150
QQLVNGIITP ATIPSLGPWG VLHSNPMDYA WGANGLDAII TQLLNQFENT 200
GPPPADKEKI QALPTVPVTE EHVGSGLECP VCKDDYALGE RVRQLPCNHL 250
FHDGCIVPWL EQHDSCPVCR KSLTGQNTAT NPPGLTGVSF SSSSSSSSSS 300
SPSNENATWS PLGRPQPPRP LSNLTL 326
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.
VSP_015693
Alternative sequencei312 – 32615Missing in isoform 2.
VSP_015694Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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. 34 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.
HOGENOMi HOG000116417.
HOVERGENi HBG059832.
InParanoidi Q9BV68.
KOi K11982.
OMAi LEHVDQH.
OrthoDBi EOG7353XB.
PhylomeDBi Q9BV68.
TreeFami TF317985.

Miscellaneous databases

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

Gene expression databases

ArrayExpressi Q9BV68.
Bgeei Q9BV68.
CleanExi HS_RNF126.
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, AUTOUBIQUITINATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-229 AND CYS-232.

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: July 9, 2014
This is version 107 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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