SAMD1
Sterile alpha motif domain-containing protein 1
Also known as: SAMD1_HUMAN
Protein identityUniProt · HPA
- UniProt accession
- Q6SPF0
- Gene
- SAMD1
- Canonical length
- 538 aa
- Protein class
- Predicted intracellular proteins
- Quaternary structure
- Homopolymer
OverviewNCBI Gene
No narrative summary is available for SAMD1 in this catalog release; identity and structured annotations are shown without generated factual claims.
Canonical amino-acid sequenceUniProt
538 residues, UniProt reviewed canonical sequence.
>Q6SPF0|SAMD1
1 MAGPPALPPP ETAAAATTAA AASSSAASPH YQEWILDTID SLRSRKARPD LERICRMVRR
61 RHGPEPERTR AELEKLIQQR AVLRVSYKGS ISYRNAARVQ PPRRGATPPA PPRAPRGAPA
121 AAAAAAPPPT PAPPPPPAPV AAAAPARAPR AAAAAATAPP SPGPAQPGPR AQRAAPLAAP
181 PPAPAAPPAV APPAGPRRAP PPAVAAREPP LPPPPQPPAP PQQQQPPPPQ PQPPPEGGAV
241 RAGGAARPVS LREVVRYLGG SGGAGGRLTR GRVQGLLEEE AAARGRLERT RLGALALPRG
301 DRPGRAPPAA SARPSRSKRG GEERVLEKEE EEDDDEDEDE EDDVSEGSEV PESDRPAGAQ
361 HHQLNGERGP QSAKERVKEW TPCGPHQGQD EGRGPAPGSG TRQVFSMAAM NKEGGTASVA
421 TGPDSPSPVP LPPGKPALPG ADGTPFGCPP GRKEKPSDPV EWTVMDVVEY FTEAGFPEQA
481 TAFQEQEIDG KSLLLMQRTD VLTGLSIRLG PALKIYEHHI KVLQQGHFED DDPDGFLGLocalizationUniProt · AlphaFold · HPA
Whether an antibody against SAMD1 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
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.61
- Highest tissue expression
- 49 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 49 nTPM
- amygdala: 48 nTPM
- spinal cord: 47 nTPM
- midbrain: 45 nTPM
- hippocampal formation: 44 nTPM
- thymus: 41 nTPM
Single-cell type
- astrocytes: 13 nCPM
- bergmann glia: 12 nCPM
- microglia: 12 nCPM
- ependymal cells: 12 nCPM
- oligodendrocyte progenitor cells: 11 nCPM
- papillary tip epithelial cells: 11 nCPM
Immune cell
- NK-cell: 3.8 nTPM
- eosinophil: 2.5 nTPM
- memory B-cell: 2.1 nTPM
- naive B-cell: 1.4 nTPM
- classical monocyte: 1.3 nTPM
- myeloid DC: 1.2 nTPM
Brain region
- medulla oblongata: 69 nTPM
- white matter: 61 nTPM
- amygdala: 61 nTPM
- thalamus: 60 nTPM
- spinal cord: 59 nTPM
- pons: 59 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)
- 0.67
- gnomAD pLI
- 0.24
- gnomAD missense Z
- 0.06
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- chromatin organization
- foam cell differentiation
- negative regulation of transcription by RNA polymerase II
- negative regulation of transcription initiation-coupled chromatin remodeling
- protein homooligomerization
- lipoprotein lipid oxidation
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Sterile alpha motif domain
- Sterile alpha motif/pointed domain superfamily
- SAM domain-containing protein 1-like, WH domain
- SAM domain (Sterile alpha motif)
- SAM domain-containing protein 1, WH domain
- SAMD1-like, small helical domain
- SAMD1 small helical domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of SAMD1 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 SAMD1 as an antibody target. Whether an autoantibody or antibody against SAMD1 could matter depends on whether native SAMD1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
SAMD1 is annotated as secreted, so native SAMD1 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label SAMD1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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