Sequence Browser (P23497-1)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
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1
879
Isoform
Remark
Ref
VSP_005982 VSP_005983
No experimental confirmation available.
VSP_045868 VSP_005978 VSP_005979
No experimental confirmation available.
VSP_045869 VSP_045870 VSP_005978 VSP_005979
P23497-1  
Major isoform.
VSP_005978 VSP_005979
Ref.2 (AAC50743) sequence is in conflict in position: 686:M->T.
VSP_005980 VSP_005981
Ref.4 (AAK51202) sequence is in conflict in position: 826:M->T.
VSP_005984
Click on Isoform of interest to be redirected to the corresponding page
Type
Variation
Position
splice variant
MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQR → M
1 - 36
splice variant
Missing
428 - 430
splice variant
Missing
473 - 879
splice variant
Missing
481 - 879
splice variant
Missing
689 - 879
sequence variant
M → V
433
sequence variant
E → G
699
mutagenesis site
L → A
168
sequence conflict
S → P
247
sequence conflict
A → R
651
splice variant
Missing
11 - 35
splice variant
RFSSSDFSDLSNGEELQETCSSSL → LKKKKKKKQCHPQPQPQRGLLEQS
449 - 472
splice variant
SQP → KED
478 - 480
splice variant
RILE → VMIK
685 - 688
splice variant
EEHKKKNPDASVKFSEFLKKCSETWKTIFAKEKGKFEDMAKADKAHYEREMKTYIPPKGEKKKKFKDPNAPKRPPLAFFLFCSEYRPKIKGEHPGLSIDDVVKKLAGMWNNTAAADKQFYEKKAAKLKEKYKKDIAAYRAKGKPNSAKKRVVKAEKSKKKKEEEEDEEDEQEEENEEDDDK → PENSNICEVCNKWGRLFCCDTCPRSFHEHCHIPSVEANKNPWSCIFCRIKTIQERCPESQSGHQESEVLMRQMLPEEQLKCEFLLLKVYCDSKSCFFASEPYYNREGSQGPQKPMWLNKVKTSLNEQMYTRVEGFVQDMRLIFHNHKEFYREDKFTRLGIQVQDIFEKNFRNIFAIQETSKNIIMFI
699 - 879
sequence variant
S → P
471
mutagenesis site
R → A
165
sequence conflict
R → M
47
sequence conflict
Q → H
402

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Protein:
Other Names:
Nuclear dot-associated Sp100 protein, Speckled 100 kDa
Primary Accession:
Other Accessions:
B4DDX5, B8ZZD8, E7EUA7, E9PH61, F8WFE2, O75450, Q13343, Q8TE34, Q96F70, Q96T24, Q96T95, Q9NP33, Q9UE32
Gene :
SP100*
Organism :
Human
Entry Name :
Length :
879
Mass (Da) :
100,417
Last modified :
27-Jan-2001
Version :
v3
Isoforms :
7 
Variants :
19 
Interactions :
18 
Structures :
Experimental 120 | Phyre prediction 4

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.

With
Entry
IntAct
Exp
Q59GP6
EBI-751145, EBI-10243413
3
AMOTL2
Q9Y2J4-4
EBI-751145, EBI-10187270
3
CBX5
P45973
EBI-6589365, EBI-78219
6
DYRK2
Q92630
EBI-751145, EBI-749432
3
GIPC2
Q8TF65
EBI-751145, EBI-712067
3
L3MBTL3
Q96JM7
EBI-751145, EBI-2686809
3
RTP5
Q14D33
EBI-751145, EBI-10217913
3
SUMO3
P55854
EBI-751145, EBI-474067
2
UL123
P03169
EBI-751145, EBI-6691147
4
ACTN2
P35609
EBI-751145, EBI-77797
5
CASP8AP2
Q9UKL3
EBI-751145, EBI-2339650
5
DNMT3A
Q9Y6K1
EBI-751145, EBI-923653
3
ETS1
P14921
EBI-751145, EBI-913209
4
HEL25
V9HWG0
EBI-751145, EBI-10183977
3
RBM39
Q14498-3
EBI-751145, EBI-6654703
3
SUMO1
P63165
EBI-751145, EBI-80140
6
TRAF3IP3
Q9Y228
EBI-751145, EBI-765817
3
ZC2HC1A
Q96GY0
EBI-751145, EBI-5458880
3