SP100

Protein identityUniProt · HPA

UniProt accession

P23497

Gene

SP100

Ensembl

ENSG00000067066

Chromosome

2

Canonical length

879 aa

Protein class

Predicted intracellular proteins, Transcription factors

Subcellular location

Nucleoplasm,Nuclear bodies

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes a subnuclear organelle and major component of the PML (promyelocytic leukemia)-SP100 nuclear bodies. PML and SP100 are covalently modified by the SUMO-1 modifier, which is considered crucial to nuclear body interactions. The encoded protein binds heterochromatin proteins and is thought to play a role in tumorigenesis, immunity, and gene regulation. Alternatively spliced variants have been identified for this gene; one of which encodes a high-mobility group protein. [provided by RefSeq, Aug 2011]

Canonical amino-acid sequenceUniProt

879 residues, UniProt reviewed canonical sequence.

>P23497|SP100
     1  MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN
    61  KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP
   121  VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS
   181  FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ
   241  KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK
   301  PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL
   361  ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS
   421  GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP
   481  QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR
   541  SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF
   601  KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR
   661  CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE HKKKNPDASV KFSEFLKKCS
   721  ETWKTIFAKE KGKFEDMAKA DKAHYEREMK TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC
   781  SEYRPKIKGE HPGLSIDDVV KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG
   841  KPNSAKKRVV KAEKSKKKKE EEEDEEDEQE EENEEDDDK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against SP100 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)

0.57

Highest tissue expression

178 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about SP100.

Disease | ImmuneIEDB

Conditions an epitope on SP100 was assayed in.

• primary biliary cholangitis B and T cell
• human immunodeficiency virus infectious disease T cell
• systemic lupus erythematosus B cell
• rheumatoid arthritis B cell
• systemic scleroderma B cell

Disease | AutoantibodyPubMed

Conditions in which antibodies against SP100 are reported. Each links to that disease's full target list.

• Liver Cirrhosis, Biliary 46
• Scleroderma, Systemic 5
• Hepatitis, Autoimmune 3
• Lupus Erythematosus, Systemic 3

ReferencesPubMed · IEDB

Publications for SP100 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

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)

0.68

gnomAD pLI

0

gnomAD missense Z

0.6

DepMap mean gene effect

0.08

DepMap dependency class

none

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

• DNA damage response, signal transduction by p53 class mediator
• negative regulation of DNA-templated transcription
• negative regulation of endothelial cell migration
• negative regulation of protein export from nucleus
• negative regulation of transcription by RNA polymerase II
• negative regulation of viral transcription
• positive regulation of transcription by RNA polymerase II
• regulation of angiogenesis
• regulation of extrinsic apoptotic signaling pathway via death domain receptors
• regulation of Fas signaling pathway
• regulation of transcription by RNA polymerase II
• regulation of viral process
• response to cytokine
• response to retinoic acid
• response to type I interferon
• response to type II interferon
• retinoic acid receptor signaling pathway
• telomere maintenance
• type I interferon-mediated signaling pathway
• type II interferon-mediated signaling pathway
• maintenance of protein location

Molecular functions

• chromo shadow domain binding
• DNA binding
• DNA-binding transcription activator activity, RNA polymerase II-specific
• DNA-binding transcription factor activity, RNA polymerase II-specific
• identical protein binding
• kinase binding
• protein dimerization activity
• protein domain specific binding
• protein homodimerization activity
• RNA polymerase II-specific DNA-binding transcription factor binding
• transcription corepressor activity

Cellular components

• chromosome, telomeric region
• cytoplasm
• nuclear body
• nuclear periphery
• nucleolus
• nucleoplasm
• nucleus
• PML body

Protein domainsUniProt · Pfam · InterPro

• SAND domain
• HSR domain
• High mobility group box domain
• SAND-like domain superfamily
• High mobility group box domain superfamily
• Nuclear body protein Sp110/Sp140/Sp140L-like
• HMG (high mobility group) box
• SAND domain
• HSR domain
• HMG-box domain

KeywordsUniProt

• Acetylation
• Coiled coil
• Cytoplasm
• DNA-binding
• Host-virus interaction
• Isopeptide bond
• Nucleus
• Phosphoprotein
• Repeat
• Transcription
• Transcription regulation
• Ubl conjugation

InteractionsUniProt · HPA

Protein binding partners of SP100 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CASP8AP2
• CBX3
• ETS1
• HIPK2
• NBN
• SUMO1P1
• HMGB1
• SUMO1