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P23497

- SP100_HUMAN

UniProt

P23497 - SP100_HUMAN

Protein

Nuclear autoantigen Sp-100

Gene

SP100

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 3 (27 Apr 2001)
      Previous versions | rss
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    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 PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. 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 1PROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi769 – 83769HMG box 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromo shadow domain binding Source: BHF-UCL
    2. DNA binding Source: UniProtKB-KW
    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

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
    3. interferon-gamma-mediated signaling pathway Source: BHF-UCL
    4. negative regulation of cellular component movement Source: BHF-UCL
    5. negative regulation of DNA binding 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, DNA-templated Source: BHF-UCL
    10. negative regulation of transcription from RNA polymerase II promoter 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 angiogenesis Source: UniProtKB
    15. regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
    16. regulation of Fas signaling pathway 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

    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.
    Isoform Sp100-C : Nucleus 1 Publication
    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 PubMed:11313457.

    GO - Cellular componenti

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

    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-100PRO_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)Curated
    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.
    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.

    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.10 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. 14 interactions.
    MINTiMINT-1188807.

    Structurei

    Secondary structure

    1
    879
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23497.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 149117HSRPROSITE-ProRule annotationAdd
    BLAST
    Domaini595 – 67682SANDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni333 – 478146Sufficient to mediate interaction with ETS1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi165 – 1684D-box; recognition signal for CDC20-mediated degradation
    Motifi284 – 29714PxVxL motifAdd
    BLAST
    Motifi536 – 55318Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi568 – 59225Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi717 – 73418Nuclear localization signalSequence AnalysisAdd
    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 2 HMG box DNA-binding domains.PROSITE-ProRule annotation
    Contains 1 HSR domain.PROSITE-ProRule annotation
    Contains 1 SAND domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471R → M in BAG56886. (PubMed:14702039)Curated
    Sequence conflicti247 – 2471S → P in BAG56886. (PubMed:14702039)Curated
    Sequence conflicti402 – 4021Q → H in BAG56886. (PubMed:14702039)Curated
    Sequence conflicti651 – 6511A → R in AAL77438. (PubMed:9973607)Curated
    Sequence conflicti651 – 6511A → R in AAL77439. (PubMed:9973607)Curated
    Isoform Sp100-B (identifier: P23497-3)
    Sequence conflicti686 – 6861M → T in AAC50743. (PubMed:8695863)Curated
    Isoform Sp100-C (identifier: P23497-4)
    Sequence conflicti826 – 8261M → T in AAK51202. (PubMed:11313457)Curated

    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. 1 PublicationVSP_045868Add
    BLAST
    Alternative sequencei11 – 3525Missing in isoform 6. 1 PublicationVSP_045869Add
    BLAST
    Alternative sequencei428 – 4303Missing in isoform 6. 1 PublicationVSP_045870
    Alternative sequencei449 – 47224RFSSS…CSSSL → LKKKKKKKQCHPQPQPQRGL LEQS in isoform SpAlt-C. CuratedVSP_005982Add
    BLAST
    Alternative sequencei473 – 879407Missing in isoform SpAlt-C. CuratedVSP_005983Add
    BLAST
    Alternative sequencei478 – 4803SQP → KED in isoform Sp100-A, isoform 6 and isoform 7. 3 PublicationsVSP_005978
    Alternative sequencei481 – 879399Missing in isoform Sp100-A, isoform 6 and isoform 7. 3 PublicationsVSP_005979Add
    BLAST
    Alternative sequencei685 – 6884RILE → VMIK in isoform Sp100-B. 1 PublicationVSP_005980
    Alternative sequencei689 – 879191Missing in isoform Sp100-B. 1 PublicationVSP_005981Add
    BLAST
    Alternative sequencei699 – 879181EEHKK…EDDDK → PENSNICEVCNKWGRLFCCD TCPRSFHEHCHIPSVEANKN PWSCIFCRIKTIQERCPESQ SGHQESEVLMRQMLPEEQLK CEFLLLKVYCDSKSCFFASE PYYNREGSQGPQKPMWLNKV KTSLNEQMYTRVEGFVQDMR LIFHNHKEFYREDKFTRLGI QVQDIFEKNFRNIFAIQETS KNIIMFI in isoform Sp100-C. 1 PublicationVSP_005984Add
    BLAST

    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. [P23497-3]
    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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112555. 37 interactions.
    DIPi DIP-5983N.
    IntActi P23497. 14 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 . [P23497-3 ]
    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

    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: October 1, 2014
    This is version 170 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