PJA1
E3 ubiquitin-protein ligase Praja-1
Also known as: FLJ11830, PJA1_HUMAN, PRAJA1, RNF70
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q8NG27
- Gene
- PJA1
- Ensembl
- ENSG00000181191
- Chromosome
- X
- Canonical length
- 643 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nucleoli
OverviewNCBI Gene
This gene encodes an enzyme that has E2-dependent E3 ubiquitin-protein ligase activity. This enzyme belongs to a class of ubiquitin ligases that include a RING finger motif, and it can interact with the E2 ubiquitin-conjugating enzyme UbcH5B. This gene is located in an area of chromosome X where several X-linked cognitive disability disorders have been associated, and it has also been found as part of a contiguous gene deletion associated with craniofrontonasal syndrome, though a direct link to any disorder has yet to be demonstrated. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2010]
Canonical amino-acid sequenceUniProt
643 residues, UniProt reviewed canonical sequence.
>Q8NG27|PJA1
1 MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT NSEVPMHRSA
61 PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSRYP PREYRASGSR RGMAYGHIDS
121 YGADDSEEEG AGPVERPPVR GKTGKFKDDK LYDPEKGARS LAGPPPHFSS FSRDVREERD
181 KLDPVPAARC SASRADFLPQ SSVASQSSSE GKLATKGDSS ERERREQNLP ARPSRAPVSI
241 CGGGENTSKS AEEPVVRPKI RNLASPNCVK PKIFFDTDDD DDMPHSTSRW RDTANDNEGH
301 SDGLARRGRG ESSSGYPEPK YPEDKREARS DQVKPEKVPR RRRTMADPDF WTHSDDYYKY
361 CDEDSDSDKE WIAALRRKYR SREQTLSSSG ESWETLPGKE EREPPQAKVS ASTGTSPGPG
421 ASASAGAGAG ASAGSNGSNY LEEVREPSLQ EEQASLEEGE IPWLQYHEND SSSEGDNDSG
481 HELMQPGVFM LDGNNNLEDD SSVSEDLEVD WSLFDGFADG LGVAEAISYV DPQFLTYMAL
541 EERLAQAMET ALAHLESLAV DVEVANPPAS KESIDALPEI LVTEDHGAVG QEMCCPICCS
601 EYVKGEVATE LPCHHYFHKP CVSIWLQKSG TCPVCRCMFP PPLLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PJA1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.66
- Highest tissue expression
- 151 nTPM
Expression across tissuesHPA
Tissue
- epididymis: 151 nTPM
- basal ganglia: 63 nTPM
- hypothalamus: 49 nTPM
- cerebral cortex: 48 nTPM
- amygdala: 43 nTPM
- hippocampal formation: 38 nTPM
Single-cell type
- epididymal principal cells: 150 nCPM
- early spermatids: 106 nCPM
- late spermatids: 44 nCPM
- migrating cytotrophoblasts: 40 nCPM
- cytotrophoblasts: 37 nCPM
- basal keratinocytes: 34 nCPM
Immune cell
- MAIT T-cell: 34 nTPM
- naive CD8 T-cell: 31 nTPM
- NK-cell: 30 nTPM
- gdT-cell: 30 nTPM
- memory CD8 T-cell: 28 nTPM
- naive CD4 T-cell: 27 nTPM
Brain region
- basal ganglia: 53 nTPM
- hypothalamus: 50 nTPM
- cerebral cortex: 47 nTPM
- white matter: 38 nTPM
- hippocampal formation: 37 nTPM
- amygdala: 36 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.37
- gnomAD pLI
- 0.93
- gnomAD missense Z
- 1.02
- DepMap mean gene effect
- 0.04
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PJA1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PJA1 as an antibody target. Whether an autoantibody or antibody against PJA1 could matter depends on whether native PJA1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PJA1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PJA1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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