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Protein

E3 ubiquitin-protein ligase RNF144A

Gene

Rnf144a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. Mediates the ubiquitination and degradation of the DNA damage kinase PRKDC.By similarity

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 fingeri20 – 7051RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri91 – 15666IBR-typeAdd
BLAST
Zinc fingeri185 – 21430RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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 RNF144A (EC:6.3.2.-)
Alternative name(s):
RING finger protein 144A
UbcM4-interacting protein 4
Ubiquitin-conjugating enzyme 7-interacting protein 4
Gene namesi
Name:Rnf144a
Synonyms:Kiaa0161, Rnf144, Ubce7ip4, Uip4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1344401. Rnf144a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei250 – 27021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292E3 ubiquitin-protein ligase RNF144APRO_0000056299Add
BLAST

Post-translational modificationi

Autoubiquitinated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ925F3.
PRIDEiQ925F3.

Expressioni

Gene expression databases

BgeeiQ925F3.
CleanExiMM_RNF144A.
GenevisibleiQ925F3. MM.

Interactioni

Subunit structurei

Interacts with UBE2L3.1 Publication

Protein-protein interaction databases

BioGridi223824. 1 interaction.
STRINGi10090.ENSMUSP00000020971.

Structurei

3D structure databases

ProteinModelPortaliQ925F3.
SMRiQ925F3. Positions 20-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri20 – 7051RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri91 – 15666IBR-typeAdd
BLAST
Zinc fingeri185 – 21430RING-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000007696.
HOVERGENiHBG052072.
InParanoidiQ925F3.
KOiK11975.
OMAiRWHPGQG.
OrthoDBiEOG77M8PP.
PhylomeDBiQ925F3.
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.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q925F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTARYRPTW DLALDPLVSC KLCLGEYPAE QMTTIAQCQC IFCTLCLKQY
60 70 80 90 100
VELLIKEGLE TAISCPDAAC PKQGHLQENE IECMVAAEIM QRYKKLQFER
110 120 130 140 150
EVLFDPCRTW CPASTCQAVC QLQDIGLQTP QLVQCKACDM EFCSACKARW
160 170 180 190 200
HPGQGCPETM PITFLPGETS SAFKMEEGDA PIKRCPKCRV YIERDEGCAQ
210 220 230 240 250
MMCKNCKHAF CWYCLESLDD DFLLIHYDKG PCRNKLGHSR ASVIWHRTQV
260 270 280 290
VGIFAGFGLL LLVASPFLLL ATPFVLCCKC KCSKGDDDPL PT
Length:292
Mass (Da):32,845
Last modified:December 1, 2001 - v1
Checksum:i5E9A7CBA1521777D
GO

Sequence cautioni

The sequence BAD32182.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF360998 mRNA. Translation: AAK51468.1.
AK038586 mRNA. Translation: BAC30058.1.
AK133544 mRNA. Translation: BAE21715.1.
AK172904 mRNA. Translation: BAD32182.1. Different initiation.
BC030187 mRNA. Translation: AAH30187.1.
CCDSiCCDS36425.1.
RefSeqiNP_001075446.1. NM_001081977.2.
NP_542130.1. NM_080563.4.
XP_006515011.1. XM_006514948.2.
XP_006515012.1. XM_006514949.2.
XP_011242109.1. XM_011243807.1.
UniGeneiMm.214932.
Mm.407984.

Genome annotation databases

EnsembliENSMUST00000020971; ENSMUSP00000020971; ENSMUSG00000020642.
ENSMUST00000062149; ENSMUSP00000056073; ENSMUSG00000020642.
GeneIDi108089.
KEGGimmu:108089.
UCSCiuc007nff.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF360998 mRNA. Translation: AAK51468.1.
AK038586 mRNA. Translation: BAC30058.1.
AK133544 mRNA. Translation: BAE21715.1.
AK172904 mRNA. Translation: BAD32182.1. Different initiation.
BC030187 mRNA. Translation: AAH30187.1.
CCDSiCCDS36425.1.
RefSeqiNP_001075446.1. NM_001081977.2.
NP_542130.1. NM_080563.4.
XP_006515011.1. XM_006514948.2.
XP_006515012.1. XM_006514949.2.
XP_011242109.1. XM_011243807.1.
UniGeneiMm.214932.
Mm.407984.

3D structure databases

ProteinModelPortaliQ925F3.
SMRiQ925F3. Positions 20-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223824. 1 interaction.
STRINGi10090.ENSMUSP00000020971.

Proteomic databases

PaxDbiQ925F3.
PRIDEiQ925F3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020971; ENSMUSP00000020971; ENSMUSG00000020642.
ENSMUST00000062149; ENSMUSP00000056073; ENSMUSG00000020642.
GeneIDi108089.
KEGGimmu:108089.
UCSCiuc007nff.2. mouse.

Organism-specific databases

CTDi9781.
MGIiMGI:1344401. Rnf144a.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000007696.
HOVERGENiHBG052072.
InParanoidiQ925F3.
KOiK11975.
OMAiRWHPGQG.
OrthoDBiEOG77M8PP.
PhylomeDBiQ925F3.
TreeFamiTF324777.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRnf144a. mouse.
PROiQ925F3.
SOURCEiSearch...

Gene expression databases

BgeeiQ925F3.
CleanExiMM_RNF144A.
GenevisibleiQ925F3. MM.

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.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4."
    Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.
    FEBS Lett. 454:257-261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2L3.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hypothalamus and Xiphoid cartilage.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  4. "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].

Entry informationi

Entry nameiR144A_MOUSE
AccessioniPrimary (citable) accession number: Q925F3
Secondary accession number(s): Q3UZZ0, Q6A0B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.