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P23497 (SP100_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear autoantigen Sp-100
Alternative name(s):
Nuclear dot-associated Sp100 protein
Speckled 100 kDa
Gene names
Name:SP100
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 Ref.15. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to Ref.17. 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. Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.26 Ref.29 Ref.30

Subunit structure

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. Ref.4 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23 Ref.30

Subcellular location

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. Ref.4 Ref.12 Ref.15 Ref.23

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 Ref.4. Ref.4 Ref.12 Ref.15 Ref.23

Tissue specificity

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.

Induction

Up-regulated by interferon, retinoic acid, TNF-alpha/TNFA and lipopolysaccharide (at protein level). Up-regulated following heat-shock. Ref.17 Ref.21 Ref.30

Domain

The HSR domain is important for the nuclear body targeting as well as for the dimerization. Ref.28

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. Ref.28

Post-translational modification

Sumoylated. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting. Ref.4 Ref.12 Ref.13

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. Ref.4 Ref.12 Ref.13

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.

Sequence similarities

Contains 2 HMG box DNA-binding domains.

Contains 1 HSR domain.

Contains 1 SAND domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from direct assay Ref.16. Source: BHF-UCL

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Inferred by curator Ref.8. Source: BHF-UCL

negative regulation of DNA binding

Inferred from direct assay Ref.17. Source: BHF-UCL

negative regulation of cellular component movement

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

negative regulation of endothelial cell migration

Inferred from mutant phenotype Ref.21. Source: UniProtKB

negative regulation of protein export from nucleus

Inferred from mutant phenotype Ref.23. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.17. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.17. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9636147. Source: BHF-UCL

negative regulation of viral transcription

Inferred from direct assay PubMed 16873258PubMed 16873258PubMed 16873258. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.15Ref.19. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.15. Source: BHF-UCL

regulation of Fas signaling pathway

Inferred from mutant phenotype Ref.23. Source: UniProtKB

regulation of angiogenesis

Inferred from mutant phenotype Ref.21. Source: UniProtKB

regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype Ref.23. Source: UniProtKB

response to cytokine

Inferred from direct assay Ref.4Ref.12. Source: BHF-UCL

response to interferon-gamma

Inferred from direct assay PubMed 9230084. Source: BHF-UCL

response to retinoic acid

Inferred from direct assay Ref.4. Source: BHF-UCL

response to type I interferon

Inferred from direct assay Ref.17PubMed 9230084PubMed 16873258PubMed 16873258PubMed 16873258PubMed 16873258. Source: BHF-UCL

retinoic acid receptor signaling pathway

Inferred by curator Ref.4. Source: BHF-UCL

telomere maintenance

Inferred from mutant phenotype Ref.20. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

type I interferon signaling pathway

Inferred by curator Ref.8. Source: BHF-UCL

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from direct assay Ref.4Ref.2Ref.9PubMed 16873258Ref.12. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.12. Source: BHF-UCL

nuclear periphery

Inferred from direct assay Ref.4. Source: BHF-UCL

nucleolus

Inferred from direct assay Ref.9. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8PubMed 16873258Ref.3PubMed 16873258PubMed 16873258Ref.12. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromo shadow domain binding

Inferred from physical interaction Ref.18PubMed 9636147. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 9636147. Source: BHF-UCL

kinase binding

Inferred from physical interaction Ref.16. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction PubMed 9636147. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.2. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay Ref.16Ref.19. Source: BHF-UCL

transcription corepressor activity

Inferred from direct assay Ref.17PubMed 16873258PubMed 16873258PubMed 16873258. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction Ref.15. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform Sp100-HMG (identifier: P23497-1)

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.
Isoform Sp100-A (identifier: P23497-2)

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.
Isoform Sp100-B (identifier: P23497-3)

Also known as: SP100B; SpAlt-212;

The sequence of this isoform differs from the canonical sequence as follows:
     685-688: RILE → VTIK
     689-879: Missing.
Isoform Sp100-C (identifier: P23497-4)

Also known as: SP100C;

The sequence of this isoform differs from the canonical sequence as follows:
     699-879: EEHKKKNPDA...EEENEEDDDK → PENSNICEVC...ETSKNIIMFI
Isoform SpAlt-C (identifier: P23497-5)

The sequence of this isoform differs from the canonical sequence as follows:
     449-472: RFSSSDFSDLSNGEELQETCSSSL → LKKKKKKKQCHPQPQPQRGLLEQS
     473-879: Missing.
Isoform 6 (identifier: P23497-6)

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.
Isoform 7 (identifier: P23497-7)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.31
Chain2 – 879878Nuclear autoantigen Sp-100
PRO_0000074096

Regions

Domain33 – 149117HSR
Domain595 – 67682SAND
DNA binding677 – 75377HMG box 1
DNA binding769 – 83769HMG box 2
Region333 – 478146Sufficient to mediate interaction with ETS1
Motif165 – 1684D-box; recognition signal for CDC20-mediated degradation
Motif284 – 29714PxVxL motif
Motif536 – 55318Nuclear localization signal Potential
Motif568 – 59225Nuclear localization signal Potential
Motif717 – 73418Nuclear localization signal Potential
Compositional bias3 – 64Poly-Gly
Compositional bias156 – 1649Poly-Glu
Compositional bias759 – 7646Poly-Lys
Compositional bias854 – 8596Poly-Lys
Compositional bias860 – 8689Poly-Glu

Amino acid modifications

Modified residue21N-acetylalanine Ref.31
Modified residue181Phosphoserine Ref.22
Modified residue1571Phosphoserine Ref.27
Modified residue1711Phosphoserine Ref.25
Modified residue3311Phosphoserine Ref.22
Modified residue3621Phosphoserine Ref.27
Modified residue4071Phosphoserine Ref.24 Ref.25 Ref.27
Modified residue4091Phosphoserine Ref.24 Ref.25 Ref.27
Modified residue4101Phosphoserine Ref.24 Ref.25 Ref.27
Cross-link297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Natural variations

Alternative sequence1 – 3636MAGGG…HDLQR → M in isoform 7.
VSP_045868
Alternative sequence11 – 3525Missing in isoform 6.
VSP_045869
Alternative sequence428 – 4303Missing in isoform 6.
VSP_045870
Alternative sequence449 – 47224RFSSS…CSSSL → LKKKKKKKQCHPQPQPQRGL LEQS in isoform SpAlt-C.
VSP_005982
Alternative sequence473 – 879407Missing in isoform SpAlt-C.
VSP_005983
Alternative sequence478 – 4803SQP → KED in isoform Sp100-A, isoform 6 and isoform 7.
VSP_005978
Alternative sequence481 – 879399Missing in isoform Sp100-A, isoform 6 and isoform 7.
VSP_005979
Alternative sequence685 – 6884RILE → VTIK in isoform Sp100-B.
VSP_005980
Alternative sequence689 – 879191Missing in isoform Sp100-B.
VSP_005981
Alternative sequence699 – 879181EEHKK…EDDDK → PENSNICEVCNKWGRLFCCD TCPRSFHEHCHIPSVEANKN PWSCIFCRIKTIQERCPESQ SGHQESEVLMRQMLPEEQLK CEFLLLKVYCDSKSCFFASE PYYNREGSQGPQKPMWLNKV KTSLNEQMYTRVEGFVQDMR LIFHNHKEFYREDKFTRLGI QVQDIFEKNFRNIFAIQETS KNIIMFI in isoform Sp100-C.
VSP_005984
Natural variant4331M → V in HeLa cells.
Corresponds to variant rs12724 [ dbSNP | Ensembl ].
VAR_005621
Natural variant4711S → P in HeLa cells.
VAR_005622
Natural variant6991E → G.
Corresponds to variant rs34700604 [ dbSNP | Ensembl ].
VAR_034510

Experimental info

Mutagenesis1651R → A: Prevents CDC20-mediated degradation; when associated with Ala-168. Ref.28
Mutagenesis1681L → A: Prevents CDC20-mediated degradation; when associated with Ala-165. Ref.28
Sequence conflict471R → M in BAG56886. Ref.5
Sequence conflict2471S → P in BAG56886. Ref.5
Sequence conflict4021Q → H in BAG56886. Ref.5
Sequence conflict6511A → R in AAL77438. Ref.9
Sequence conflict6511A → R in AAL77439. Ref.9
Isoform Sp100-B:
Sequence conflict6861T → M in AAL77439. Ref.9
Isoform Sp100-C:
Sequence conflict8261M → T in AAK51202. Ref.4

Secondary structure

.................... 879
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Sp100-HMG (SP100HMG) (SpAlt-HMG) [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: CA55547DE21B2A10

FASTA879100,417
        10         20         30         40         50         60 
MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 

        70         80         90        100        110        120 
KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 

       130        140        150        160        170        180 
VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 

       190        200        210        220        230        240 
FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 

       250        260        270        280        290        300 
KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 

       310        320        330        340        350        360 
PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 

       370        380        390        400        410        420 
ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 

       430        440        450        460        470        480 
GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP 

       490        500        510        520        530        540 
QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR 

       550        560        570        580        590        600 
SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF 

       610        620        630        640        650        660 
KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR 

       670        680        690        700        710        720 
CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE HKKKNPDASV KFSEFLKKCS 

       730        740        750        760        770        780 
ETWKTIFAKE KGKFEDMAKA DKAHYEREMK TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC 

       790        800        810        820        830        840 
SEYRPKIKGE HPGLSIDDVV KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG 

       850        860        870 
KPNSAKKRVV KAEKSKKKKE EEEDEEDEQE EENEEDDDK 

« Hide

Isoform Sp100-A (SP100A) (SP100) [UniParc].

Checksum: 10351A33BF3A4C12
Show »

FASTA48053,768
Isoform Sp100-B (SP100B) (SpAlt-212) [UniParc].

Checksum: C0B467072DA75C96
Show »

FASTA68878,144
Isoform Sp100-C (SP100C) [UniParc].

Checksum: 3D33A477B171D7DE
Show »

FASTA885101,575
Isoform SpAlt-C [UniParc].

Checksum: 3FD218C65A00100D
Show »

FASTA47253,113
Isoform 6 [UniParc].

Checksum: C957A23305439EE8
Show »

FASTA45250,590
Isoform 7 [UniParc].

Checksum: 05DF245B919FAA1B
Show »

FASTA44550,032

References

« Hide 'large scale' references
[1]"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).
[2]"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.
[3]"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.
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Cdc20 mediates D-box-dependent degradation of Sp100."
Wang R., Li K.M., Zhou C.H., Xue J.L., Ji C.N., Chen J.Z.
Biochem. Biophys. Res. Commun. 415:702-706(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN D-BOX MOTIF, MUTAGENESIS OF ARG-165 AND LEU-168.
[29]"SP100 reduces malignancy of human glioma cells."
Held-Feindt J., Hattermann K., Knerlich-Lukoschus F., Mehdorn H.M., Mentlein R.
Int. J. Oncol. 38:1023-1030(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36501 mRNA. Translation: AAC50743.1.
AF056322 mRNA. Translation: AAC39790.1.
M60618 mRNA. Translation: AAA35537.1.
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.
PIRA37244.
RefSeqNP_001073860.1. NM_001080391.1.
NP_001193630.1. NM_001206701.1.
NP_001193631.1. NM_001206702.1.
NP_001193632.1. NM_001206703.1.
NP_001193633.1. NM_001206704.1.
NP_003104.2. NM_003113.3.
UniGeneHs.369056.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H5PNMR-A595-684[»]
ProteinModelPortalP23497.
SMRP23497. Positions 595-684, 699-840.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112555. 37 interactions.
DIPDIP-5983N.
IntActP23497. 13 interactions.
MINTMINT-1188807.

PTM databases

PhosphoSiteP23497.

Polymorphism databases

DMDM13878931.

Proteomic databases

PaxDbP23497.
PRIDEP23497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264052; ENSP00000264052; ENSG00000067066. [P23497-1]
ENST00000340126; ENSP00000343023; ENSG00000067066. [P23497-4]
ENST00000409341; ENSP00000386404; ENSG00000067066. [P23497-2]
ENST00000409897; ENSP00000386998; ENSG00000067066. [P23497-7]
ENST00000427101; ENSP00000399389; ENSG00000067066. [P23497-6]
GeneID6672.
KEGGhsa:6672.
UCSCuc002vqq.2. human. [P23497-2]
uc002vqt.3. human. [P23497-1]
uc002vqu.1. human. [P23497-4]
uc010zmb.2. human. [P23497-5]

Organism-specific databases

CTD6672.
GeneCardsGC02P231280.
HGNCHGNC:11206. SP100.
HPAHPA016707.
HPA017384.
MIM604585. gene.
neXtProtNX_P23497.
PharmGKBPA36043.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249894.
HOVERGENHBG057632.
KOK15413.
OMAGPRIPRD.
OrthoDBEOG71VSS7.
PhylomeDBP23497.
TreeFamTF335091.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP23497.
BgeeP23497.
CleanExHS_SP100.
GenevestigatorP23497.

Family and domain databases

Gene3D1.10.30.10. 2 hits.
3.10.390.10. 1 hit.
InterProIPR009071. HMG_box_dom.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR004865. Sp100.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
PF01342. SAND. 1 hit.
PF03172. Sp100. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 2 hits.
SM00258. SAND. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 2 hits.
SSF63763. SSF63763. 1 hit.
PROSITEPS50118. HMG_BOX_2. 2 hits.
PS51414. HSR. 1 hit.
PS50864. SAND. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSP100. human.
EvolutionaryTraceP23497.
GenomeRNAi6672.
NextBio26015.
PROP23497.
SOURCESearch...

Entry information

Entry nameSP100_HUMAN
AccessionPrimary (citable) accession number: P23497
Secondary accession number(s): B4DDX5 expand/collapse secondary AC list , B8ZZD8, E9PH61, F8WFE2, O75450, Q13343, Q8TE34, Q96F70, Q96T24, Q96T95, Q9NP33, Q9UE32
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM