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Protein

Nuclear autoantigen Sp-100

Gene

SP100

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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.9 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

  • chromo shadow domain binding Source: BHF-UCL
  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: BHF-UCL
  • kinase binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL
  • transcription corepressor activity Source: BHF-UCL
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
  • inflammatory response Source: InterPro
  • interferon-gamma-mediated signaling pathway Source: BHF-UCL
  • negative regulation of cellular component movement Source: BHF-UCL
  • negative regulation of DNA binding Source: BHF-UCL
  • negative regulation of endothelial cell migration Source: UniProtKB
  • negative regulation of protein export from nucleus Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of viral transcription Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • protein sumoylation Source: Reactome
  • regulation of angiogenesis Source: UniProtKB
  • regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
  • regulation of Fas signaling pathway Source: UniProtKB
  • response to cytokine Source: BHF-UCL
  • response to interferon-gamma Source: BHF-UCL
  • response to retinoic acid Source: BHF-UCL
  • response to type I interferon Source: BHF-UCL
  • retinoic acid receptor signaling pathway Source: BHF-UCL
  • telomere maintenance Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • type I interferon signaling pathway Source: BHF-UCL
  • 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

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-877300. 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
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: BHF-UCL
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear periphery Source: BHF-UCL
  • nucleolus Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • PML body 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.

Polymorphism and mutation databases

BioMutaiSP100.
DMDMi13878931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 879878Nuclear autoantigen Sp-100PRO_0000074096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei171 – 1711PhosphoserineCombined sources
Modified residuei180 – 1801PhosphoserineCombined sources
Modified residuei228 – 2281PhosphoserineCombined sources
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Cross-linki306 – 306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei331 – 3311PhosphoserineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources
Cross-linki387 – 387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei410 – 4101PhosphoserineCombined sources
Modified residuei451 – 4511PhosphoserineCombined sources

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

EPDiP23497.
MaxQBiP23497.
PaxDbiP23497.
PeptideAtlasiP23497.
PRIDEiP23497.

PTM databases

iPTMnetiP23497.
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

BgeeiENSG00000067066.
CleanExiHS_SP100.
ExpressionAtlasiP23497. baseline and differential.
GenevisibleiP23497. HS.

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
Q59GP63EBI-751145,EBI-10243413
ACTN2P356095EBI-751145,EBI-77797
AMOTL2Q9Y2J4-43EBI-751145,EBI-10187270
CASP8AP2Q9UKL35EBI-751145,EBI-2339650
DNMT3AQ9Y6K13EBI-751145,EBI-923653
DYRK2Q926303EBI-751145,EBI-749432
ETS1P149214EBI-751145,EBI-913209
GIPC2Q8TF653EBI-751145,EBI-712067
HEL25V9HWG03EBI-751145,EBI-10183977
L3MBTL3Q96JM73EBI-751145,EBI-2686809
RBM39Q14498-33EBI-751145,EBI-6654703
RTP5Q14D333EBI-751145,EBI-10217913
SUMO1P631656EBI-751145,EBI-80140
SUMO3P558542EBI-751145,EBI-474067
TRAF3IP3Q9Y2283EBI-751145,EBI-765817
UL123P031694EBI-751145,EBI-6691147From a different organism.
ZC2HC1AQ96GY03EBI-751145,EBI-5458880

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • kinase binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112555. 55 interactions.
DIPiDIP-5983N.
IntActiP23497. 35 interactions.
MINTiMINT-1188807.
STRINGi9606.ENSP00000343023.

Structurei

Secondary structure

1
879
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi600 – 6023Combined sources
Beta strandi603 – 6097Combined sources
Beta strandi612 – 6176Combined sources
Helixi618 – 6214Combined sources
Helixi624 – 6263Combined sources
Beta strandi630 – 6323Combined sources
Turni633 – 6353Combined sources
Beta strandi636 – 6383Combined sources
Helixi640 – 6478Combined sources
Helixi655 – 6584Combined sources
Helixi666 – 6727Combined sources
Beta strandi673 – 6753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H5PNMR-A595-688[»]
5FB0X-ray2.70A/C696-878[»]
5FB1X-ray2.10A696-875[»]
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

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00510000046835.
HOGENOMiHOG000089984.
HOVERGENiHBG057632.
InParanoidiP23497.
KOiK15413.
OMAiAGRETPC.
OrthoDBiEOG091G01MN.
PhylomeDBiP23497.
TreeFamiTF335091.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
3.10.390.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
IPR031076. HMGB1.
IPR004865. HSR_dom.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
[Graphical view]
PANTHERiPTHR13711:SF157. PTHR13711:SF157. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY
60 70 80 90 100
DIVFKHFKRN KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV
110 120 130 140 150
PVQRVVYNVL SELEKTFNLP VLEALFSDVN MQEYPDLIHI YKGFENVIHD
160 170 180 190 200
KLPLQESEEE EREERSGLQL SLEQGTGENS FRSLTWPPSG SPSHAGTTPP
210 220 230 240 250
ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ KAEPTESCEQ
260 270 280 290 300
IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK
310 320 330 340 350
PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS
360 370 380 390 400
EPVINNDNPL ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI
410 420 430 440 450
GQDHDFSESS EEEAPAEASS GALRSKHGEK APMTSRSTST WRIPSRKRRF
460 470 480 490 500
SSSDFSDLSN GEELQETCSS SLRRGSGSQP QEPENKKCSC VMCFPKGVPR
510 520 530 540 550
SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR SKVNGLQRGR
560 570 580 590 600
KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF
610 620 630 640 650
KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG
660 670 680 690 700
ASKNWKLSIR CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE
710 720 730 740 750
HKKKNPDASV KFSEFLKKCS ETWKTIFAKE KGKFEDMAKA DKAHYEREMK
760 770 780 790 800
TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC SEYRPKIKGE HPGLSIDDVV
810 820 830 840 850
KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG KPNSAKKRVV
860 870
KAEKSKKKKE EEEDEEDEQE EENEEDDDK
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.
Corresponds to variant rs12724 [ dbSNP | Ensembl ].
VAR_005621
Natural varianti471 – 4711S → P.
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:
EMBLi
GenBanki
DDBJi
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.3. human. [P23497-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H5PNMR-A595-688[»]
5FB0X-ray2.70A/C696-878[»]
5FB1X-ray2.10A696-875[»]
ProteinModelPortaliP23497.
SMRiP23497. Positions 595-684, 699-840.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112555. 55 interactions.
DIPiDIP-5983N.
IntActiP23497. 35 interactions.
MINTiMINT-1188807.
STRINGi9606.ENSP00000343023.

PTM databases

iPTMnetiP23497.
PhosphoSiteiP23497.

Polymorphism and mutation databases

BioMutaiSP100.
DMDMi13878931.

Proteomic databases

EPDiP23497.
MaxQBiP23497.
PaxDbiP23497.
PeptideAtlasiP23497.
PRIDEiP23497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.3. human. [P23497-1]

Organism-specific databases

CTDi6672.
GeneCardsiSP100.
HGNCiHGNC:11206. SP100.
HPAiHPA016707.
HPA017384.
MIMi604585. gene.
neXtProtiNX_P23497.
PharmGKBiPA36043.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00510000046835.
HOGENOMiHOG000089984.
HOVERGENiHBG057632.
InParanoidiP23497.
KOiK15413.
OMAiAGRETPC.
OrthoDBiEOG091G01MN.
PhylomeDBiP23497.
TreeFamiTF335091.

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiSP100. human.
EvolutionaryTraceiP23497.
GenomeRNAii6672.
PROiP23497.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000067066.
CleanExiHS_SP100.
ExpressionAtlasiP23497. baseline and differential.
GenevisibleiP23497. HS.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
3.10.390.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
IPR031076. HMGB1.
IPR004865. HSR_dom.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
[Graphical view]
PANTHERiPTHR13711:SF157. PTHR13711:SF157. 1 hit.
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]
ProtoNetiSearch...

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 7, 2016
This is version 192 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.