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P23497

- SP100_HUMAN

UniProt

P23497 - SP100_HUMAN

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Protein
Nuclear autoantigen Sp-100
Gene
SP100
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to 1 Publication. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to 1 Publication. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation.10 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi677 – 75377HMG box 1
Add
BLAST
DNA bindingi769 – 83769HMG box 2
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. chromo shadow domain binding Source: BHF-UCL
  3. identical protein binding Source: BHF-UCL
  4. kinase binding Source: BHF-UCL
  5. protein binding Source: BHF-UCL
  6. protein domain specific binding Source: UniProtKB
  7. protein homodimerization activity Source: BHF-UCL
  8. transcription coactivator activity Source: BHF-UCL
  9. transcription corepressor activity Source: BHF-UCL
  10. transcription factor binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
  2. cytokine-mediated signaling pathway Source: Reactome
  3. interferon-gamma-mediated signaling pathway Source: BHF-UCL
  4. negative regulation of DNA binding Source: BHF-UCL
  5. negative regulation of cellular component movement Source: BHF-UCL
  6. negative regulation of endothelial cell migration Source: UniProtKB
  7. negative regulation of protein export from nucleus Source: UniProtKB
  8. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  9. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  10. negative regulation of transcription, DNA-templated Source: BHF-UCL
  11. negative regulation of viral transcription Source: BHF-UCL
  12. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  13. positive regulation of transcription, DNA-templated Source: BHF-UCL
  14. regulation of Fas signaling pathway Source: UniProtKB
  15. regulation of angiogenesis Source: UniProtKB
  16. regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
  17. response to cytokine Source: BHF-UCL
  18. response to interferon-gamma Source: BHF-UCL
  19. response to retinoic acid Source: BHF-UCL
  20. response to type I interferon Source: BHF-UCL
  21. retinoic acid receptor signaling pathway Source: BHF-UCL
  22. telomere maintenance Source: UniProtKB
  23. transcription, DNA-templated Source: UniProtKB-KW
  24. type I interferon signaling pathway Source: BHF-UCL
  25. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_25078. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear autoantigen Sp-100
Alternative name(s):
Nuclear dot-associated Sp100 protein
Speckled 100 kDa
Gene namesi
Name:SP100
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11206. SP100.

Subcellular locationi

Nucleus. NucleusPML body. Cytoplasm
Note: Differences in the subnuclear localization of the different isoforms seem to exist and may also be cell cycle- and interferon-dependent. Accumulates in the cytoplasm upon FAS activation.4 Publications
Isoform Sp100-C : Nucleus
Note: Forms a reticulate or track-like nuclear pattern with denser concentrations at the nuclear lamina and surrounding the nucleoli, a pattern reminiscent of heterochromatin-rich regions according to 1 Publication.4 Publications

GO - Cellular componenti

  1. PML body Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. nuclear periphery Source: BHF-UCL
  4. nucleolus Source: BHF-UCL
  5. nucleoplasm Source: Reactome
  6. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651R → A: Prevents CDC20-mediated degradation; when associated with Ala-168. 1 Publication
Mutagenesisi168 – 1681L → A: Prevents CDC20-mediated degradation; when associated with Ala-165. 1 Publication

Organism-specific databases

PharmGKBiPA36043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 879878Nuclear autoantigen Sp-100
PRO_0000074096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei157 – 1571Phosphoserine1 Publication
Modified residuei171 – 1711Phosphoserine1 Publication
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei407 – 4071Phosphoserine3 Publications
Modified residuei409 – 4091Phosphoserine3 Publications
Modified residuei410 – 4101Phosphoserine3 Publications

Post-translational modificationi

Sumoylated. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting.3 Publications
Sumoylated. Sumoylated with SUMO1. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting. Sumoylation may stabilize the interaction with CBX5.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP23497.
PaxDbiP23497.
PRIDEiP23497.

PTM databases

PhosphoSiteiP23497.

Expressioni

Tissue specificityi

Widely expressed. Sp100-B is expressed only in spleen, tonsil, thymus, mature B-cell line and some T-cell line, but not in brain, liver, muscle or non-lymphoid cell lines.

Inductioni

Up-regulated by interferon, retinoic acid, TNF-alpha/TNFA and lipopolysaccharide (at protein level). Up-regulated following heat-shock.3 Publications

Gene expression databases

ArrayExpressiP23497.
BgeeiP23497.
CleanExiHS_SP100.
GenevestigatoriP23497.

Organism-specific databases

HPAiHPA016707.
HPA017384.

Interactioni

Subunit structurei

Homodimer; isoforms are able to heterodimerize. Interacts with members of the HP1 family of nonhistone chromosomal protein, such as CBX5 and CBX3 via the PxVxL motif. Interacts with ETS1; the interaction is direct and modulates ETS1 transcriptional activity. Interacts with the MRN complex which is composed of two heterodimers RAD50/MRE11A associated with a single NBN; recruits the complex to PML-related bodies. Interacts with HIPK2; positively regulates TP53-dependent transcription. Interacts with CASP8AP2; may negatively regulate CASP8AP2 export from the nucleus to the cytoplasm. Interacts with Epstein-Barr virus EBNA-LP; this interaction is important for EBNA-LP coactivator activity. Interacts with human cytomegalovirus/HHV-5 protein UL123; may play a role in infection by the virus.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP8AP2Q9UKL35EBI-751145,EBI-2339650
ETS1P149214EBI-751145,EBI-913209
SUMO3P558542EBI-751145,EBI-474067
UL123P031694EBI-751145,EBI-6691147From a different organism.

Protein-protein interaction databases

BioGridi112555. 37 interactions.
DIPiDIP-5983N.
IntActiP23497. 13 interactions.
MINTiMINT-1188807.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi600 – 6023
Beta strandi603 – 6097
Beta strandi612 – 6176
Helixi618 – 6214
Helixi624 – 6263
Beta strandi630 – 6323
Turni633 – 6353
Beta strandi636 – 6383
Helixi640 – 6478
Helixi655 – 6584
Helixi666 – 6727
Beta strandi673 – 6753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H5PNMR-A595-688[»]
ProteinModelPortaliP23497.
SMRiP23497. Positions 595-684, 699-840.

Miscellaneous databases

EvolutionaryTraceiP23497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 149117HSR
Add
BLAST
Domaini595 – 67682SAND
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni333 – 478146Sufficient to mediate interaction with ETS1
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi165 – 1684D-box; recognition signal for CDC20-mediated degradation
Motifi284 – 29714PxVxL motif
Add
BLAST
Motifi536 – 55318Nuclear localization signal Reviewed prediction
Add
BLAST
Motifi568 – 59225Nuclear localization signal Reviewed prediction
Add
BLAST
Motifi717 – 73418Nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 64Poly-Gly
Compositional biasi156 – 1649Poly-Glu
Compositional biasi759 – 7646Poly-Lys
Compositional biasi854 – 8596Poly-Lys
Compositional biasi860 – 8689Poly-Glu

Domaini

The HSR domain is important for the nuclear body targeting as well as for the dimerization.1 Publication
Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.1 Publication

Sequence similaritiesi

Contains 1 HSR domain.
Contains 1 SAND domain.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG249894.
HOVERGENiHBG057632.
KOiK15413.
OMAiGPRIPRD.
OrthoDBiEOG71VSS7.
PhylomeDBiP23497.
TreeFamiTF335091.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
3.10.390.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR004865. Sp100.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
PF01342. SAND. 1 hit.
PF03172. Sp100. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 2 hits.
SM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 2 hits.
SSF63763. SSF63763. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 2 hits.
PS51414. HSR. 1 hit.
PS50864. SAND. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform Sp100-HMG (identifier: P23497-1) [UniParc]FASTAAdd to Basket

Also known as: SP100HMG, SpAlt-HMG

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

MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY    50
DIVFKHFKRN KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV 100
PVQRVVYNVL SELEKTFNLP VLEALFSDVN MQEYPDLIHI YKGFENVIHD 150
KLPLQESEEE EREERSGLQL SLEQGTGENS FRSLTWPPSG SPSHAGTTPP 200
ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ KAEPTESCEQ 250
IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 300
PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS 350
EPVINNDNPL ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI 400
GQDHDFSESS EEEAPAEASS GALRSKHGEK APMTSRSTST WRIPSRKRRF 450
SSSDFSDLSN GEELQETCSS SLRRGSGSQP QEPENKKCSC VMCFPKGVPR 500
SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR SKVNGLQRGR 550
KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF 600
KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG 650
ASKNWKLSIR CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE 700
HKKKNPDASV KFSEFLKKCS ETWKTIFAKE KGKFEDMAKA DKAHYEREMK 750
TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC SEYRPKIKGE HPGLSIDDVV 800
KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG KPNSAKKRVV 850
KAEKSKKKKE EEEDEEDEQE EENEEDDDK 879
Length:879
Mass (Da):100,417
Last modified:April 27, 2001 - v3
Checksum:iCA55547DE21B2A10
GO
Isoform Sp100-A (identifier: P23497-2) [UniParc]FASTAAdd to Basket

Also known as: SP100A, SP100

The sequence of this isoform differs from the canonical sequence as follows:
     478-480: SQP → KED
     481-879: Missing.

Note: Major isoform.

Show »
Length:480
Mass (Da):53,768
Checksum:i10351A33BF3A4C12
GO
Isoform Sp100-B (identifier: P23497-3) [UniParc]FASTAAdd to Basket

Also known as: SP100B, SpAlt-212

The sequence of this isoform differs from the canonical sequence as follows:
     685-688: RILE → VMIK
     689-879: Missing.

Show »
Length:688
Mass (Da):78,174
Checksum:iC0B470372DA75C96
GO
Isoform Sp100-C (identifier: P23497-4) [UniParc]FASTAAdd to Basket

Also known as: SP100C

The sequence of this isoform differs from the canonical sequence as follows:
     699-879: EEHKKKNPDA...EEENEEDDDK → PENSNICEVC...ETSKNIIMFI

Show »
Length:885
Mass (Da):101,575
Checksum:i3D33A477B171D7DE
GO
Isoform SpAlt-C (identifier: P23497-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     449-472: RFSSSDFSDLSNGEELQETCSSSL → LKKKKKKKQCHPQPQPQRGLLEQS
     473-879: Missing.

Show »
Length:472
Mass (Da):53,113
Checksum:i3FD218C65A00100D
GO
Isoform 6 (identifier: P23497-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-35: Missing.
     428-430: Missing.
     478-480: SQP → KED
     481-879: Missing.

Note: No experimental confirmation available.

Show »
Length:452
Mass (Da):50,590
Checksum:iC957A23305439EE8
GO
Isoform 7 (identifier: P23497-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQR → M
     478-480: SQP → KED
     481-879: Missing.

Note: No experimental confirmation available.

Show »
Length:445
Mass (Da):50,032
Checksum:i05DF245B919FAA1B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti433 – 4331M → V in HeLa cells.
Corresponds to variant rs12724 [ dbSNP | Ensembl ].
VAR_005621
Natural varianti471 – 4711S → P in HeLa cells.
VAR_005622
Natural varianti699 – 6991E → G.
Corresponds to variant rs34700604 [ dbSNP | Ensembl ].
VAR_034510

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MAGGG…HDLQR → M in isoform 7.
VSP_045868Add
BLAST
Alternative sequencei11 – 3525Missing in isoform 6.
VSP_045869Add
BLAST
Alternative sequencei428 – 4303Missing in isoform 6.
VSP_045870
Alternative sequencei449 – 47224RFSSS…CSSSL → LKKKKKKKQCHPQPQPQRGL LEQS in isoform SpAlt-C.
VSP_005982Add
BLAST
Alternative sequencei473 – 879407Missing in isoform SpAlt-C.
VSP_005983Add
BLAST
Alternative sequencei478 – 4803SQP → KED in isoform Sp100-A, isoform 6 and isoform 7.
VSP_005978
Alternative sequencei481 – 879399Missing in isoform Sp100-A, isoform 6 and isoform 7.
VSP_005979Add
BLAST
Alternative sequencei685 – 6884RILE → VMIK in isoform Sp100-B.
VSP_005980
Alternative sequencei689 – 879191Missing in isoform Sp100-B.
VSP_005981Add
BLAST
Alternative sequencei699 – 879181EEHKK…EDDDK → PENSNICEVCNKWGRLFCCD TCPRSFHEHCHIPSVEANKN PWSCIFCRIKTIQERCPESQ SGHQESEVLMRQMLPEEQLK CEFLLLKVYCDSKSCFFASE PYYNREGSQGPQKPMWLNKV KTSLNEQMYTRVEGFVQDMR LIFHNHKEFYREDKFTRLGI QVQDIFEKNFRNIFAIQETS KNIIMFI in isoform Sp100-C.
VSP_005984Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471R → M in BAG56886. 1 Publication
Sequence conflicti247 – 2471S → P in BAG56886. 1 Publication
Sequence conflicti402 – 4021Q → H in BAG56886. 1 Publication
Sequence conflicti651 – 6511A → R in AAL77438. 1 Publication
Sequence conflicti651 – 6511A → R in AAL77439. 1 Publication
Isoform Sp100-B (identifier: P23497-3)
Sequence conflicti686 – 6861M → T in AAC50743. 1 Publication
Isoform Sp100-C (identifier: P23497-4)
Sequence conflicti826 – 8261M → T in AAK51202. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60618 mRNA. Translation: AAA35537.1.
U36501 mRNA. Translation: AAC50743.1.
AF056322 mRNA. Translation: AAC39790.1.
AF255565 mRNA. Translation: AAK51202.1.
AK293373 mRNA. Translation: BAG56886.1.
AC009949 Genomic DNA. No translation available.
AC010149 Genomic DNA. No translation available.
BC011562 mRNA. Translation: AAH11562.1.
X95472 Genomic DNA. Translation: CAA64744.1.
L79986 mRNA. Translation: AAL77441.1.
L79987 mRNA. Translation: AAL77439.1.
L79988 mRNA. Translation: AAL77438.1.
AF076675 Genomic DNA. Translation: AAF39781.1.
AF378670 Genomic DNA. Translation: AAK57703.1.
CCDSiCCDS2477.1. [P23497-1]
CCDS42832.1. [P23497-4]
CCDS56170.1. [P23497-3]
CCDS56171.1. [P23497-2]
CCDS56172.1. [P23497-6]
CCDS56173.1. [P23497-7]
PIRiA37244.
RefSeqiNP_001073860.1. NM_001080391.1. [P23497-4]
NP_001193630.1. NM_001206701.1. [P23497-3]
NP_001193631.1. NM_001206702.1. [P23497-2]
NP_001193632.1. NM_001206703.1. [P23497-6]
NP_001193633.1. NM_001206704.1. [P23497-7]
NP_003104.2. NM_003113.3. [P23497-1]
UniGeneiHs.369056.

Genome annotation databases

EnsembliENST00000264052; ENSP00000264052; ENSG00000067066. [P23497-1]
ENST00000340126; ENSP00000343023; ENSG00000067066. [P23497-4]
ENST00000409112; ENSP00000386427; ENSG00000067066.
ENST00000409341; ENSP00000386404; ENSG00000067066. [P23497-2]
ENST00000409897; ENSP00000386998; ENSG00000067066. [P23497-7]
ENST00000427101; ENSP00000399389; ENSG00000067066. [P23497-6]
GeneIDi6672.
KEGGihsa:6672.
UCSCiuc002vqq.2. human. [P23497-2]
uc002vqt.3. human. [P23497-1]
uc002vqu.1. human. [P23497-4]
uc010zmb.2. human. [P23497-5]

Polymorphism databases

DMDMi13878931.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60618 mRNA. Translation: AAA35537.1 .
U36501 mRNA. Translation: AAC50743.1 .
AF056322 mRNA. Translation: AAC39790.1 .
AF255565 mRNA. Translation: AAK51202.1 .
AK293373 mRNA. Translation: BAG56886.1 .
AC009949 Genomic DNA. No translation available.
AC010149 Genomic DNA. No translation available.
BC011562 mRNA. Translation: AAH11562.1 .
X95472 Genomic DNA. Translation: CAA64744.1 .
L79986 mRNA. Translation: AAL77441.1 .
L79987 mRNA. Translation: AAL77439.1 .
L79988 mRNA. Translation: AAL77438.1 .
AF076675 Genomic DNA. Translation: AAF39781.1 .
AF378670 Genomic DNA. Translation: AAK57703.1 .
CCDSi CCDS2477.1. [P23497-1 ]
CCDS42832.1. [P23497-4 ]
CCDS56170.1. [P23497-3 ]
CCDS56171.1. [P23497-2 ]
CCDS56172.1. [P23497-6 ]
CCDS56173.1. [P23497-7 ]
PIRi A37244.
RefSeqi NP_001073860.1. NM_001080391.1. [P23497-4 ]
NP_001193630.1. NM_001206701.1. [P23497-3 ]
NP_001193631.1. NM_001206702.1. [P23497-2 ]
NP_001193632.1. NM_001206703.1. [P23497-6 ]
NP_001193633.1. NM_001206704.1. [P23497-7 ]
NP_003104.2. NM_003113.3. [P23497-1 ]
UniGenei Hs.369056.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H5P NMR - A 595-688 [» ]
ProteinModelPortali P23497.
SMRi P23497. Positions 595-684, 699-840.
ModBasei Search...

Protein-protein interaction databases

BioGridi 112555. 37 interactions.
DIPi DIP-5983N.
IntActi P23497. 13 interactions.
MINTi MINT-1188807.

PTM databases

PhosphoSitei P23497.

Polymorphism databases

DMDMi 13878931.

Proteomic databases

MaxQBi P23497.
PaxDbi P23497.
PRIDEi P23497.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264052 ; ENSP00000264052 ; ENSG00000067066 . [P23497-1 ]
ENST00000340126 ; ENSP00000343023 ; ENSG00000067066 . [P23497-4 ]
ENST00000409112 ; ENSP00000386427 ; ENSG00000067066 .
ENST00000409341 ; ENSP00000386404 ; ENSG00000067066 . [P23497-2 ]
ENST00000409897 ; ENSP00000386998 ; ENSG00000067066 . [P23497-7 ]
ENST00000427101 ; ENSP00000399389 ; ENSG00000067066 . [P23497-6 ]
GeneIDi 6672.
KEGGi hsa:6672.
UCSCi uc002vqq.2. human. [P23497-2 ]
uc002vqt.3. human. [P23497-1 ]
uc002vqu.1. human. [P23497-4 ]
uc010zmb.2. human. [P23497-5 ]

Organism-specific databases

CTDi 6672.
GeneCardsi GC02P231280.
HGNCi HGNC:11206. SP100.
HPAi HPA016707.
HPA017384.
MIMi 604585. gene.
neXtProti NX_P23497.
PharmGKBi PA36043.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249894.
HOVERGENi HBG057632.
KOi K15413.
OMAi GPRIPRD.
OrthoDBi EOG71VSS7.
PhylomeDBi P23497.
TreeFami TF335091.

Enzyme and pathway databases

Reactomei REACT_25078. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSi SP100. human.
EvolutionaryTracei P23497.
GenomeRNAii 6672.
NextBioi 26015.
PROi P23497.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23497.
Bgeei P23497.
CleanExi HS_SP100.
Genevestigatori P23497.

Family and domain databases

Gene3Di 1.10.30.10. 2 hits.
3.10.390.10. 1 hit.
InterProi IPR009071. HMG_box_dom.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR004865. Sp100.
[Graphical view ]
Pfami PF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
PF01342. SAND. 1 hit.
PF03172. Sp100. 1 hit.
[Graphical view ]
SMARTi SM00398. HMG. 2 hits.
SM00258. SAND. 1 hit.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 2 hits.
SSF63763. SSF63763. 1 hit.
PROSITEi PS50118. HMG_BOX_2. 2 hits.
PS51414. HSR. 1 hit.
PS50864. SAND. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis."
    Szostecki C., Guldner H.H., Netter H.J., Will H.
    J. Immunol. 145:4338-4347(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-A).
    Tissue: Liver and Placenta.
  2. "LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies."
    Dent A.L., Yewdell J., Puvion-Dutilleul F., Koken M.H.M., de The H., Staudt L.M.
    Blood 88:1423-1426(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-B).
  3. "Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment."
    Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A.
    Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-HMG).
    Tissue: Mammary cancer.
  4. "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: role of SUMO modification."
    Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., Dejean A.
    Mol. Cell. Biol. 21:3314-3324(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-C), SUBCELLULAR LOCATION (ISOFORMS SP100-A; SP100-C AND SP100-HMG), SUMOYLATION WITH SUMO1, INTERACTION WITH CBX5.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
    Tissue: Kidney and Urinary bladder.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 SP100-A).
    Tissue: Kidney.
  8. "The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibility."
    Groetzinger T., Jensen K., Will H.
    J. Biol. Chem. 271:25253-25260(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
    Tissue: Lymphoma.
  9. "Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif."
    Guldner H.H., Szostecki C., Schroeder P., Matschl U., Jensen K., Lueders C., Will H., Sternsdorf T.
    J. Cell Sci. 112:733-747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-879 (ISOFORMS SP100-B AND SP100-HMG), PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SPALT-C).
    Tissue: Cervix carcinoma.
  10. "Back to the roots of a new exon-the molecular archaeology of a SP100 splice variant."
    Rogalla P., Kazmierczak B., Flohr A.M., Hauke S., Bullerdiek J.
    Genomics 63:117-122(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-879 (ISOFORM SP100-HMG).
    Tissue: Cervix carcinoma.
  11. "Molecular archeology of an SP100 splice variant revisited: dating the retrotranscription and Alu insertion events."
    Devor E.J.
    Genome Biol. 2:RESEARCH0040.1-RESEARCH0040.6(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-879 (ISOFORM SP100-HMG).
  12. "Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1."
    Sternsdorf T., Jensen K., Will H.
    J. Cell Biol. 139:1621-1634(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION WITH SUMO1, SUBCELLULAR LOCATION.
  13. "The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers."
    Sternsdorf T., Jensen K., Reich B., Will H.
    J. Biol. Chem. 274:12555-12566(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-297, HOMODIMERIZATION.
  14. "Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 protein."
    Naka K., Ikeda K., Motoyama N.
    Biochem. Biophys. Res. Commun. 299:863-871(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBN.
  15. "Sp100 interacts with ETS-1 and stimulates its transcriptional activity."
    Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.
    Mol. Cell. Biol. 22:2687-2702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TRANSCRIPTIONAL COACTIVATOR, INTERACTION WITH ETS1, SUBCELLULAR LOCATION.
  16. "Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression."
    Moeller A., Sirma H., Hofmann T.G., Staege H., Gresko E., Luedi K.S., Klimczak E., Droege W., Will H., Schmitz M.L.
    Oncogene 22:8731-8737(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TP53-DEPENDENT TRANSCRIPTION, INTERACTION WITH HIPK2.
  17. "SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion."
    Yordy J.S., Li R., Sementchenko V.I., Pei H., Muise-Helmericks R.C., Watson D.K.
    Oncogene 23:6654-6665(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TRANSCRIPTIONAL COREPRESSOR, INTERACTION WITH ETS1, INDUCTION BY INTERFERON ALPHA.
  18. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
    Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
    Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX5.
  19. "Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100."
    Ling P.D., Peng R.S., Nakajima A., Yu J.H., Tan J., Moses S.M., Yang W.H., Zhao B., Kieff E., Bloch K.D., Bloch D.B.
    EMBO J. 24:3565-3575(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN VIRAL INFECTION, INTERACTION WITH EBV EBNA-LP.
  20. "Suppression of alternative lengthening of telomeres by Sp100-mediated sequestration of the MRE11/RAD50/NBS1 complex."
    Jiang W.Q., Zhong Z.H., Henson J.D., Neumann A.A., Chang A.C., Reddel R.R.
    Mol. Cell. Biol. 25:2708-2721(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TELOMERE SHORTENING, INTERACTION WITH MRN COMPLEX.
  21. "SP100 inhibits ETS1 activity in primary endothelial cells."
    Yordy J.S., Moussa O., Pei H., Chaussabel D., Li R., Watson D.K.
    Oncogene 24:916-931(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOTHELIAL CELL MIGRATION, INDUCTION.
  22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies."
    Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.
    EMBO J. 26:391-401(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FAS-MEDIATED APOPTOSIS, INTERACTION WITH CASP8AP2, SUBCELLULAR LOCATION.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-409 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-407; SER-409 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  26. "Sp100 as a potent tumor suppressor: accelerated senescence and rapid malignant transformation of human fibroblasts through modulation of an embryonic stem cell program."
    Negorev D.G., Vladimirova O.V., Kossenkov A.V., Nikonova E.V., Demarest R.M., Capobianco A.J., Showe M.K., Rauscher F.J. III, Showe L.C., Maul G.G.
    Cancer Res. 70:9991-10001(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION.
  27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-362; SER-407; SER-409 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: DOMAIN D-BOX MOTIF, MUTAGENESIS OF ARG-165 AND LEU-168.
  29. Cited for: FUNCTION IN CELL PROLIFERATION.
  30. "Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression."
    Kim Y.E., Lee J.H., Kim E.T., Shin H.J., Gu S.Y., Seol H.S., Ling P.D., Lee C.H., Ahn J.H.
    J. Virol. 85:11928-11937(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN VIRAL INFECTION, INTERACTION WITH HHV-5 PROTEIN UL123, INDUCTION BY INTERFERON.
  31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSP100_HUMAN
AccessioniPrimary (citable) accession number: P23497
Secondary accession number(s): B4DDX5
, B8ZZD8, E7EUA7, E9PH61, F8WFE2, O75450, Q13343, Q8TE34, Q96F70, Q96T24, Q96T95, Q9NP33, Q9UE32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 27, 2001
Last modified: September 3, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The major isoform Sp100-A, has a calculated molecular weight of 54 kDa, but exhibits aberrant electrophoretic mobilities, with an apparent molecular weight of 100 kDa.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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