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Protein

E3 ubiquitin-protein ligase Praja-1

Gene

Pja1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome. May be involved in protein sorting.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri530 – 57142RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Praja-1 (EC:6.3.2.-)
Short name:
Praja1
Gene namesi
Name:Pja1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1101765. Pja1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi533 – 5331C → A: No effect on MAGED1 binding. Decrease in ubiquitination of MAGED1. No inhibition of DLX5-dependent transcriptional activity. 1 Publication
Mutagenesisi553 – 5531H → S: Loss of ubiquitination activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 578578E3 ubiquitin-protein ligase Praja-1PRO_0000056000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311PhosphothreonineCombined sources
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei319 – 3191PhosphoserineCombined sources

Post-translational modificationi

Substrate for E2-dependent ubiquitination.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO55176.
PRIDEiO55176.

PTM databases

iPTMnetiO55176.
PhosphoSiteiO55176.

Expressioni

Tissue specificityi

Expressed in brain, liver, kidney. Highest levels in brain where it is found in many regions including cortical and subcortical areas and in neurons of the amygdala. Weak expression also found in testis. Also expressed in developing embryo.

Inductioni

By fear memory. Differential induction of isoforms.

Gene expression databases

BgeeiO55176.
CleanExiMM_PJA1.
ExpressionAtlasiO55176. baseline and differential.
GenevisibleiO55176. MM.

Interactioni

Subunit structurei

Binds ubiquitin-conjugating enzymes (E2s). Binds, in vitro and in vivo, the MAGE conserved domain of MAGED1. Binds weakly Necdin, in vitro. Interacts with UBE2D2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Maged1Q9QYH62EBI-1801670,EBI-1801274

Protein-protein interaction databases

BioGridi202189. 1 interaction.
IntActiO55176. 3 interactions.
STRINGi10090.ENSMUSP00000109420.

Structurei

3D structure databases

ProteinModelPortaliO55176.
SMRiO55176. Positions 499-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi230 – 2367Poly-Asp
Compositional biasi292 – 2954Poly-Arg

Domaini

The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri530 – 57142RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
HOGENOMiHOG000230900.
HOVERGENiHBG003815.
InParanoidiO55176.
KOiK10633.
OMAiYSRYPPR.
OrthoDBiEOG7TJ3HJ.
PhylomeDBiO55176.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031227. PJA1.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR15710:SF2. PTHR15710:SF2. 1 hit.
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Alternative splicing appears to be tissue-specific.

Isoform 1 (identifier: O55176-3) [UniParc]FASTAAdd to basket

Also known as: Praja1a

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
MSHQERIASQ RRTTAEVPMH RSTANQSKRS RSPFASTRRR WDDSESSGAS
60 70 80 90 100
LAVESEDYSR YPPREYRASG SRRGLAYGHI DTVVARDSEE EGAGPVDRLP
110 120 130 140 150
VRGKAGKFKD DPEKGARSSR FTSVNHDAKE ECGKVESPPA ARCSARRAEL
160 170 180 190 200
SKQNGSSASQ ISSAEGRAAA KGNNSLERER QNLPARPSRA PVSICGGGEN
210 220 230 240 250
TPKSAEEPVV RPKVRNVATP NCMKPKVFFD TDDDDDVPHS TSRWRDAADA
260 270 280 290 300
EEAHAEGLAR RGRGEAASSS EPRYAEDQDA RSEQAKADKV PRRRRTMADP
310 320 330 340 350
DFWAYTDDYY RYYEEDSDSD KEWMAALRRK YRSREQPQSS SGESWELLPG
360 370 380 390 400
KEELERQQAG AGSLASAGSN GSGYPEEVQD PSLQEEEQAS LEEGEIPWLR
410 420 430 440 450
YNENESSSEG DNESTHELIQ PGMFMLDGNN NLEDDSSVSE DLEVDWSLFD
460 470 480 490 500
GFADGLGVAE AISYVDPQFL TYMALEERLA QAMETALAHL ESLAVDVEVA
510 520 530 540 550
NPPASKESID ALPEILVTED HGAVGQEMCC PICCSEYVKG EVATELPCHH
560 570
YFHKPCVSIW LQKSGTCPVC RCMFPPPL
Length:578
Mass (Da):63,906
Last modified:December 12, 2006 - v3
Checksum:i11B2D3C1F8982143
GO
Isoform 2 (identifier: O55176-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     60-243: Missing.

Show »
Length:394
Mass (Da):44,066
Checksum:iE7079C43B283ABA4
GO
Isoform 3 (identifier: O55176-4) [UniParc]FASTAAdd to basket

Also known as: Praja1c

The sequence of this isoform differs from the canonical sequence as follows:
     197-411: Missing.

Show »
Length:363
Mass (Da):39,676
Checksum:i8CFD7C8983F5B90A
GO
Isoform 4 (identifier: O55176-5) [UniParc]FASTAAdd to basket

Also known as: Praja1d

The sequence of this isoform differs from the canonical sequence as follows:
     185-187: ARP → PLF
     188-578: Missing.

Show »
Length:187
Mass (Da):20,548
Checksum:i54FFD305EA13E2FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361D → DD in AAK15764 (PubMed:11533224).Curated
Sequence conflicti515 – 5151I → M in BAB23982 (PubMed:16141072).Curated
Sequence conflicti523 – 5231A → T in AAK15764 (PubMed:11533224).Curated
Sequence conflicti523 – 5231A → T in AAK15765 (PubMed:11533224).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei60 – 243184Missing in isoform 2. 1 PublicationVSP_007519Add
BLAST
Alternative sequencei185 – 1873ARP → PLF in isoform 4. 1 PublicationVSP_022011
Alternative sequencei188 – 578391Missing in isoform 4. 1 PublicationVSP_007520Add
BLAST
Alternative sequencei197 – 411215Missing in isoform 3. 1 PublicationVSP_007521Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06944 mRNA. Translation: AAC00205.2.
AF335250 mRNA. Translation: AAK15764.2.
AF335251 mRNA. Translation: AAK15765.2.
AF335252 mRNA. Translation: AAK15766.1.
AK005373 mRNA. Translation: BAB23982.1.
BC037616 mRNA. Translation: AAH37616.1.
CCDSiCCDS41070.1. [O55176-3]
RefSeqiNP_001076579.1. NM_001083110.2. [O55176-3]
NP_032879.2. NM_008853.3.
XP_011245847.1. XM_011247545.1. [O55176-3]
UniGeneiMm.8211.

Genome annotation databases

EnsembliENSMUST00000036354; ENSMUSP00000109420; ENSMUSG00000034403. [O55176-3]
ENSMUST00000113792; ENSMUSP00000109423; ENSMUSG00000034403. [O55176-3]
ENSMUST00000167246; ENSMUSP00000132393; ENSMUSG00000034403. [O55176-3]
GeneIDi18744.
KEGGimmu:18744.
UCSCiuc009tvl.1. mouse. [O55176-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06944 mRNA. Translation: AAC00205.2.
AF335250 mRNA. Translation: AAK15764.2.
AF335251 mRNA. Translation: AAK15765.2.
AF335252 mRNA. Translation: AAK15766.1.
AK005373 mRNA. Translation: BAB23982.1.
BC037616 mRNA. Translation: AAH37616.1.
CCDSiCCDS41070.1. [O55176-3]
RefSeqiNP_001076579.1. NM_001083110.2. [O55176-3]
NP_032879.2. NM_008853.3.
XP_011245847.1. XM_011247545.1. [O55176-3]
UniGeneiMm.8211.

3D structure databases

ProteinModelPortaliO55176.
SMRiO55176. Positions 499-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202189. 1 interaction.
IntActiO55176. 3 interactions.
STRINGi10090.ENSMUSP00000109420.

PTM databases

iPTMnetiO55176.
PhosphoSiteiO55176.

Proteomic databases

PaxDbiO55176.
PRIDEiO55176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036354; ENSMUSP00000109420; ENSMUSG00000034403. [O55176-3]
ENSMUST00000113792; ENSMUSP00000109423; ENSMUSG00000034403. [O55176-3]
ENSMUST00000167246; ENSMUSP00000132393; ENSMUSG00000034403. [O55176-3]
GeneIDi18744.
KEGGimmu:18744.
UCSCiuc009tvl.1. mouse. [O55176-3]

Organism-specific databases

CTDi64219.
MGIiMGI:1101765. Pja1.

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
HOGENOMiHOG000230900.
HOVERGENiHBG003815.
InParanoidiO55176.
KOiK10633.
OMAiYSRYPPR.
OrthoDBiEOG7TJ3HJ.
PhylomeDBiO55176.

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPja1. mouse.
NextBioi294897.
PROiO55176.
SOURCEiSearch...

Gene expression databases

BgeeiO55176.
CleanExiMM_PJA1.
ExpressionAtlasiO55176. baseline and differential.
GenevisibleiO55176. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031227. PJA1.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR15710:SF2. PTHR15710:SF2. 1 hit.
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Praja1, a novel gene encoding a RING-H2 motif in mouse development."
    Mishra L., Tully R.E., Monga S.P.S., Yu P., Cai T., Makalowski W., Mezey E., Pavan W.J., Mishra B.
    Oncogene 15:2361-2368(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. Mishra L.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Identification of genes expressed in the amygdala during the formation of fear memory."
    Stork O., Stork S., Pape H.-C., Obata K.
    Learn. Memory 8:209-219(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Amygdala.
  4. Stork O., Stork S.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS (ISOFORMS 1 AND 3).
  5. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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: Eye.
  7. "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination."
    Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A UBIQUITATION LIGASE, MUTAGENESIS OF HIS-553.
  8. "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
    Yu P., Chen Y., Tagle D.A., Cai T.
    Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBE2D2.
  9. "A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1."
    Sasaki A., Masuda Y., Iwai K., Ikeda K., Watanabe K.
    J. Biol. Chem. 277:22541-22546(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGED1, MUTAGENESIS OF CYS-533.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231; SER-317 AND SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Spleen and Testis.

Entry informationi

Entry nameiPJA1_MOUSE
AccessioniPrimary (citable) accession number: O55176
Secondary accession number(s): Q8CFU2
, Q99MJ1, Q99MJ2, Q99MJ3, Q9DB04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: December 12, 2006
Last modified: March 16, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.