MRPL38
Large ribosomal subunit protein mL38
Also known as: HSPC262, MGC4810, MRP-L3, RM38_HUMAN, RPML3
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q96DV4
- Gene
- MRPL38
- Ensembl
- ENSG00000204316
- Chromosome
- 17
- Canonical length
- 380 aa
- Protein class
- Predicted intracellular proteins, Ribosomal proteins
- Subcellular location
- Mitochondria
OverviewNCBI Gene
Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 39S subunit protein. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
380 residues, UniProt reviewed canonical sequence.
>Q96DV4|MRPL38
1 MAAPWWRAAL CECRRWRGFS TSAVLGRRTP PLGPMPNSDI DLSNLERLEK YRSFDRYRRR
61 AEQEAQAPHW WRTYREYFGE KTDPKEKIDI GLPPPKVSRT QQLLERKQAI QELRANVEEE
121 RAARLRTASV PLDAVRAEWE RTCGPYHKQR LAEYYGLYRD LFHGATFVPR VPLHVAYAVG
181 EDDLMPVYCG NEVTPTEAAQ APEVTYEAEE GSLWTLLLTS LDGHLLEPDA EYLHWLLTNI
241 PGNRVAEGQV TCPYLPPFPA RGSGIHRLAF LLFKQDQPID FSEDARPSPC YQLAQRTFRT
301 FDFYKKHQET MTPAGLSFFQ CRWDDSVTYI FHQLLDMREP VFEFVRPPPY HPKQKRFPHR
361 QPLRYLDRYR DSHEPTYGIYLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MRPL38 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)
- 0.4
- Highest tissue expression
- 137 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 137 nTPM
- heart muscle: 80 nTPM
- tongue: 79 nTPM
- liver: 76 nTPM
- adrenal gland: 54 nTPM
- kidney: 51 nTPM
Single-cell type
- bergmann glia: 25 nCPM
- oligodendrocytes: 25 nCPM
- astrocytes: 23 nCPM
- ependymal cells: 22 nCPM
- other brain neurons: 22 nCPM
- brain excitatory neurons: 18 nCPM
Immune cell
- naive B-cell: 114 nTPM
- myeloid DC: 107 nTPM
- memory B-cell: 102 nTPM
- NK-cell: 96 nTPM
- T-reg: 94 nTPM
- memory CD4 T-cell: 86 nTPM
Brain region
- thalamus: 41 nTPM
- cerebellum: 39 nTPM
- pons: 39 nTPM
- medulla oblongata: 38 nTPM
- cerebral cortex: 37 nTPM
- spinal cord: 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)
- 1.1
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.19
- DepMap mean gene effect
- -0.6
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of MRPL38 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 MRPL38 as an antibody target. Whether an autoantibody or antibody against MRPL38 could matter depends on whether native MRPL38 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MRPL38 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 MRPL38 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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