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Protein

E3 ubiquitin-protein ligase RNF144B

Gene

RNF144B

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

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.2 Publications

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 fingeri30 – 8051RING-type 1; atypicalAdd
BLAST
Zinc fingeri101 – 16666IBR-typeAdd
BLAST
Zinc fingeri193 – 22230RING-type 2; degenerateAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, 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 RNF144B (EC:6.3.2.-)
Alternative name(s):
IBR domain-containing protein 2
RING finger protein 144B
p53-inducible RING finger protein
Gene namesi
Name:RNF144B
Synonyms:IBRDC2, P53RFP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21578. RNF144B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei258 – 27821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial membrane Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401565.

Polymorphism and mutation databases

BioMutaiRNF144B.
DMDMi57012811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303E3 ubiquitin-protein ligase RNF144BPRO_0000055911Add
BLAST

Post-translational modificationi

Auto-ubiquitinated.

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ7Z419.
PRIDEiQ7Z419.

Expressioni

Tissue specificityi

Broadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis.2 Publications

Gene expression databases

BgeeiQ7Z419.
CleanExiHS_RNF144B.
GenevisibleiQ7Z419. HS.

Organism-specific databases

HPAiCAB046013.
HPA054127.

Interactioni

Subunit structurei

Interacts with UBE2L3, UBE2L6 and LCMT2, as well as with BAX.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BAXQ078125EBI-2129982,EBI-516580
UBE2L6O149334EBI-2129982,EBI-2129974

GO - Molecular functioni

Protein-protein interaction databases

BioGridi129106. 16 interactions.
DIPiDIP-43771N.
IntActiQ7Z419. 9 interactions.
MINTiMINT-1771863.
STRINGi9606.ENSP00000259939.

Structurei

3D structure databases

ProteinModelPortaliQ7Z419.
SMRiQ7Z419. Positions 28-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme (By similarity). The transmembrane domain is essential for translocation to the mitochondria upon induction of apoptosis.By similarity

Sequence similaritiesi

Belongs to the RBR family. RNF144 subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri30 – 8051RING-type 1; atypicalAdd
BLAST
Zinc fingeri101 – 16666IBR-typeAdd
BLAST
Zinc fingeri193 – 22230RING-type 2; degenerateAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000007696.
HOVERGENiHBG052072.
InParanoidiQ7Z419.
KOiK11975.
OMAiCRIYIER.
OrthoDBiEOG77M8PP.
PhylomeDBiQ7Z419.
TreeFamiTF324777.

Family and domain databases

InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 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: Q7Z419-1) [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
MGSAGRLHYL AMTAENPTPG DLAPAPLITC KLCLCEQSLD KMTTLQECQC
60 70 80 90 100
IFCTACLKQY MQLAIREGCG SPITCPDMVC LNHGTLQEAE IACLVPVDQF
110 120 130 140 150
QLYQRLKFER EVHLDPYRTW CPVADCQTVC PVASSDPGQP VLVECPSCHL
160 170 180 190 200
KFCSCCKDAW HAEVSCRDSQ PIVLPTEHRA LFGTDAEAPI KQCPVCRVYI
210 220 230 240 250
ERNEGCAQMM CKNCKHTFCW YCLQNLDNDI FLRHYDKGPC RNKLGHSRAS
260 270 280 290 300
VMWNRTQVVG ILVGLGIIAL VTSPLLLLAS PCIICCVCKS CRGKKKKHDP

STT
Length:303
Mass (Da):33,697
Last modified:October 1, 2003 - v1
Checksum:i9FD505CDFB70B6A5
GO
Isoform 2 (identifier: Q7Z419-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MGSAGRLHYLAMTAENPTPGD → MLWITMPHPAHLGLFIAVTLS
     22-110: Missing.

Note: No experimental confirmation available.
Show »
Length:214
Mass (Da):23,856
Checksum:i79776522FF903E30
GO

Sequence cautioni

The sequence CAD38622.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621L → P in CAD38622 (PubMed:17974005).Curated
Sequence conflicti275 – 2751Missing in AAH63311 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MGSAG…PTPGD → MLWITMPHPAHLGLFIAVTL S in isoform 2. 1 PublicationVSP_055853Add
BLAST
Alternative sequencei22 – 11089Missing in isoform 2. 1 PublicationVSP_055854Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076367 mRNA. Translation: BAC02434.1.
AK096832 mRNA. Translation: BAG53370.1.
AK302935 mRNA. Translation: BAG64094.1.
AL832329 mRNA. Translation: CAD38622.1. Different initiation.
AL138725 Genomic DNA. Translation: CAI15148.2.
CH471087 Genomic DNA. Translation: EAW55407.1.
BC063311 mRNA. Translation: AAH63311.1.
CCDSiCCDS34345.1. [Q7Z419-1]
RefSeqiNP_877434.2. NM_182757.3. [Q7Z419-1]
XP_005249041.1. XM_005248984.3. [Q7Z419-1]
UniGeneiHs.148741.

Genome annotation databases

EnsembliENST00000259939; ENSP00000259939; ENSG00000137393. [Q7Z419-1]
GeneIDi255488.
KEGGihsa:255488.
UCSCiuc003ncs.3. human. [Q7Z419-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076367 mRNA. Translation: BAC02434.1.
AK096832 mRNA. Translation: BAG53370.1.
AK302935 mRNA. Translation: BAG64094.1.
AL832329 mRNA. Translation: CAD38622.1. Different initiation.
AL138725 Genomic DNA. Translation: CAI15148.2.
CH471087 Genomic DNA. Translation: EAW55407.1.
BC063311 mRNA. Translation: AAH63311.1.
CCDSiCCDS34345.1. [Q7Z419-1]
RefSeqiNP_877434.2. NM_182757.3. [Q7Z419-1]
XP_005249041.1. XM_005248984.3. [Q7Z419-1]
UniGeneiHs.148741.

3D structure databases

ProteinModelPortaliQ7Z419.
SMRiQ7Z419. Positions 28-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129106. 16 interactions.
DIPiDIP-43771N.
IntActiQ7Z419. 9 interactions.
MINTiMINT-1771863.
STRINGi9606.ENSP00000259939.

Polymorphism and mutation databases

BioMutaiRNF144B.
DMDMi57012811.

Proteomic databases

PaxDbiQ7Z419.
PRIDEiQ7Z419.

Protocols and materials databases

DNASUi255488.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259939; ENSP00000259939; ENSG00000137393. [Q7Z419-1]
GeneIDi255488.
KEGGihsa:255488.
UCSCiuc003ncs.3. human. [Q7Z419-1]

Organism-specific databases

CTDi255488.
GeneCardsiRNF144B.
HGNCiHGNC:21578. RNF144B.
HPAiCAB046013.
HPA054127.
neXtProtiNX_Q7Z419.
PharmGKBiPA162401565.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000007696.
HOVERGENiHBG052072.
InParanoidiQ7Z419.
KOiK11975.
OMAiCRIYIER.
OrthoDBiEOG77M8PP.
PhylomeDBiQ7Z419.
TreeFamiTF324777.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiRNF144B. human.
GenomeRNAii255488.
PROiQ7Z419.

Gene expression databases

BgeeiQ7Z419.
CleanExiHS_RNF144B.
GenevisibleiQ7Z419. HS.

Family and domain databases

InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1."
    Ng C.-C., Arakawa H., Fukuda S., Kondoh H., Nakamura Y.
    Oncogene 22:4449-4458(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH LCMT2.
  2. "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: Prostate and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Placenta.
  7. "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis."
    Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.
    FEBS Lett. 580:940-947(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH UBE2L3 AND UBE2L6.
  8. "IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation."
    Benard G., Neutzner A., Peng G., Wang C., Livak F., Youle R.J., Karbowski M.
    EMBO J. 29:1458-1471(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH BAX.

Entry informationi

Entry nameiR144B_HUMAN
AccessioniPrimary (citable) accession number: Q7Z419
Secondary accession number(s): B3KUA8
, B4DZI2, Q5TB85, Q6P4Q0, Q8N3R7, Q9BX38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 1, 2003
Last modified: June 8, 2016
This is version 116 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

Caution

Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.