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Protein

E3 ubiquitin-protein ligase RNF114

Gene

RNF114

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

Functioni

E3 ubiquitin-protein ligase promoting the ubiquitination and degradation of the CDK inhibitor CDKN1A and probably also CDKN1B and CDKN1C. These activities stimulate cell cycle's G1-to-S phase transition and suppress cellular senescence. May play a role in spermatogenesis.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri29 – 6840RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ligase

Keywords - Biological processi

Differentiation, Spermatogenesis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF114 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 114
Zinc finger protein 228
Zinc finger protein 313
Gene namesi
Name:RNF114
Synonyms:ZNF228, ZNF313
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:13094. RNF114.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401502.

Polymorphism and mutation databases

BioMutaiRNF114.
DMDMi20141070.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228E3 ubiquitin-protein ligase RNF114PRO_0000056307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-acetyllysineCombined sources
Modified residuei112 – 1121N6-acetyllysineCombined sources

Post-translational modificationi

Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence of UBE2E1.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiQ9Y508.
MaxQBiQ9Y508.
PaxDbiQ9Y508.
PeptideAtlasiQ9Y508.
PRIDEiQ9Y508.
TopDownProteomicsiQ9Y508-1. [Q9Y508-1]

PTM databases

iPTMnetiQ9Y508.
PhosphoSiteiQ9Y508.

Expressioni

Tissue specificityi

Expressed in numerous tissues, including skin, CD4 lymphocytes and dendritic cells. Highest levels in testis.1 Publication

Gene expression databases

BgeeiQ9Y508.
CleanExiHS_RNF114.
ExpressionAtlasiQ9Y508. baseline and differential.
GenevisibleiQ9Y508. HS.

Organism-specific databases

HPAiHPA021184.

Interactioni

Subunit structurei

Interacts with XAF1, the interaction increases XAF1 stability and proapoptotic effects, and may regulate IFN signaling.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120991. 50 interactions.
IntActiQ9Y508. 26 interactions.
MINTiMINT-1419719.
STRINGi9606.ENSP00000244061.

Structurei

3D structure databases

ProteinModelPortaliQ9Y508.
SMRiQ9Y508. Positions 21-74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri29 – 6840RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IEG7. Eukaryota.
ENOG4111JWC. LUCA.
GeneTreeiENSGT00530000063064.
HOGENOMiHOG000230946.
HOVERGENiHBG074331.
InParanoidiQ9Y508.
KOiK15697.
OMAiIEHIQRR.
OrthoDBiEOG7VDXQ7.
PhylomeDBiQ9Y508.
TreeFamiTF331012.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR008598. Di19_Zn_binding_dom.
IPR027370. Znf-RING_LisH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF05605. zf-Di19. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y508-1) [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
MAAQQRDCGG AAQLAGPAAE ADPLGRFTCP VCLEVYEKPV QVPCGHVFCS
60 70 80 90 100
ACLQECLKPK KPVCGVCRSA LAPGVRAVEL ERQIESTETS CHGCRKNFFL
110 120 130 140 150
SKIRSHVATC SKYQNYIMEG VKATIKDASL QPRNVPNRYT FPCPYCPEKN
160 170 180 190 200
FDQEGLVEHC KLFHSTDTKS VVCPICASMP WGDPNYRSAN FREHIQRRHR
210 220
FSYDTFVDYD VDEEDMMNQV LQRSIIDQ
Length:228
Mass (Da):25,694
Last modified:November 1, 1999 - v1
Checksum:iDF5A962B1EC13A21
GO
Isoform 2 (identifier: Q9Y508-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     173-191: CPICASMPWGDPNYRSANF → SEQSPCLLSVSCYRASITY
     192-228: Missing.

Note: No experimental confirmation available.
Show »
Length:191
Mass (Da):21,004
Checksum:i1F509A3749A2AE10
GO

Sequence cautioni

The sequence CAE45709.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131Q → H in CAE45709 (PubMed:17974005).Curated
Sequence conflicti20 – 201E → K in CAE45709 (PubMed:17974005).Curated
Sequence conflicti34 – 341E → V in CAE45709 (PubMed:17974005).Curated
Sequence conflicti205 – 2051T → A in CAE45709 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei173 – 19119CPICA…RSANF → SEQSPCLLSVSCYRASITY in isoform 2. 1 PublicationVSP_036843Add
BLAST
Alternative sequencei192 – 22837Missing in isoform 2. 1 PublicationVSP_036844Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265215 mRNA. Translation: AAF75763.1.
BX640603 mRNA. Translation: CAE45709.1. Different initiation.
BT006795 mRNA. Translation: AAP35441.1.
AK315638 mRNA. Translation: BAG38006.1.
AK301731 mRNA. Translation: BAG63197.1.
AL031685 Genomic DNA. Translation: CAB46028.1.
CH471077 Genomic DNA. Translation: EAW75641.1.
CH471077 Genomic DNA. Translation: EAW75643.1.
BC013695 mRNA. Translation: AAH13695.1.
BC066919 mRNA. Translation: AAH66919.1.
CCDSiCCDS33482.1. [Q9Y508-1]
RefSeqiNP_061153.1. NM_018683.3. [Q9Y508-1]
UniGeneiHs.144949.

Genome annotation databases

EnsembliENST00000244061; ENSP00000244061; ENSG00000124226. [Q9Y508-1]
GeneIDi55905.
KEGGihsa:55905.
UCSCiuc002xux.4. human. [Q9Y508-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265215 mRNA. Translation: AAF75763.1.
BX640603 mRNA. Translation: CAE45709.1. Different initiation.
BT006795 mRNA. Translation: AAP35441.1.
AK315638 mRNA. Translation: BAG38006.1.
AK301731 mRNA. Translation: BAG63197.1.
AL031685 Genomic DNA. Translation: CAB46028.1.
CH471077 Genomic DNA. Translation: EAW75641.1.
CH471077 Genomic DNA. Translation: EAW75643.1.
BC013695 mRNA. Translation: AAH13695.1.
BC066919 mRNA. Translation: AAH66919.1.
CCDSiCCDS33482.1. [Q9Y508-1]
RefSeqiNP_061153.1. NM_018683.3. [Q9Y508-1]
UniGeneiHs.144949.

3D structure databases

ProteinModelPortaliQ9Y508.
SMRiQ9Y508. Positions 21-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120991. 50 interactions.
IntActiQ9Y508. 26 interactions.
MINTiMINT-1419719.
STRINGi9606.ENSP00000244061.

PTM databases

iPTMnetiQ9Y508.
PhosphoSiteiQ9Y508.

Polymorphism and mutation databases

BioMutaiRNF114.
DMDMi20141070.

Proteomic databases

EPDiQ9Y508.
MaxQBiQ9Y508.
PaxDbiQ9Y508.
PeptideAtlasiQ9Y508.
PRIDEiQ9Y508.
TopDownProteomicsiQ9Y508-1. [Q9Y508-1]

Protocols and materials databases

DNASUi55905.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244061; ENSP00000244061; ENSG00000124226. [Q9Y508-1]
GeneIDi55905.
KEGGihsa:55905.
UCSCiuc002xux.4. human. [Q9Y508-1]

Organism-specific databases

CTDi55905.
GeneCardsiRNF114.
HGNCiHGNC:13094. RNF114.
HPAiHPA021184.
MIMi612451. gene.
neXtProtiNX_Q9Y508.
PharmGKBiPA162401502.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEG7. Eukaryota.
ENOG4111JWC. LUCA.
GeneTreeiENSGT00530000063064.
HOGENOMiHOG000230946.
HOVERGENiHBG074331.
InParanoidiQ9Y508.
KOiK15697.
OMAiIEHIQRR.
OrthoDBiEOG7VDXQ7.
PhylomeDBiQ9Y508.
TreeFamiTF331012.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiRNF114. human.
GenomeRNAii55905.
PROiQ9Y508.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y508.
CleanExiHS_RNF114.
ExpressionAtlasiQ9Y508. baseline and differential.
GenevisibleiQ9Y508. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR008598. Di19_Zn_binding_dom.
IPR027370. Znf-RING_LisH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF05605. zf-Di19. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel human zinc finger protein gene ZNF313."
    Ma Y.-X., Zhang S., Hou Y., Huang X., Wu Q., Sun Y.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:230-237(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Endometrial tumor.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Synovium and Testis.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain and Ovary.
  8. Cited for: TISSUE SPECIFICITY.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "ZNF313 is a novel cell cycle activator with an E3 ligase activity inhibiting cellular senescence by destabilizing p21(WAF1.)."
    Han J., Kim Y.L., Lee K.W., Her N.G., Ha T.K., Yoon S., Jeong S.I., Lee J.H., Kang M.J., Lee M.G., Ryu B.K., Baik J.H., Chi S.G.
    Cell Death Differ. 20:1055-1067(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH XAF1.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRN114_HUMAN
AccessioniPrimary (citable) accession number: Q9Y508
Secondary accession number(s): B2RDQ9
, B4DWY5, E1P627, Q6N0B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 137 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.