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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)DescriptionActionsGraphical viewLength
DNA bindingi677 – 753HMG box 1PROSITE-ProRule annotationAdd BLAST77
DNA bindingi769 – 837HMG box 2PROSITE-ProRule annotationAdd BLAST69

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

BioCyciZFISH:ENSG00000067066-MONOMER.
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)DescriptionActionsGraphical viewLength
Mutagenesisi165R → A: Prevents CDC20-mediated degradation; when associated with Ala-168. 1 Publication1
Mutagenesisi168L → A: Prevents CDC20-mediated degradation; when associated with Ala-165. 1 Publication1

Organism-specific databases

DisGeNETi6672.
OpenTargetsiENSG00000067066.
PharmGKBiPA36043.

Polymorphism and mutation databases

BioMutaiSP100.
DMDMi13878931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000740962 – 879Nuclear autoantigen Sp-100Add BLAST878

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei18PhosphoserineCombined sources1
Modified residuei157PhosphoserineCombined sources1
Modified residuei171PhosphoserineCombined sources1
Modified residuei180PhosphoserineCombined sources1
Modified residuei228PhosphoserineCombined sources1
Cross-linki297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei331PhosphoserineCombined sources1
Modified residuei362PhosphoserineCombined sources1
Cross-linki387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei394PhosphoserineCombined sources1
Modified residuei407PhosphoserineCombined sources1
Modified residuei409PhosphoserineCombined sources1
Modified residuei410PhosphoserineCombined sources1
Modified residuei451PhosphoserineCombined sources1

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.
PhosphoSitePlusiP23497.

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
CBX5P459736EBI-6589365,EBI-78219
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 interactors.
DIPiDIP-5983N.
IntActiP23497. 38 interactors.
MINTiMINT-1188807.
STRINGi9606.ENSP00000343023.

Structurei

Secondary structure

1879
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi600 – 602Combined sources3
Beta strandi603 – 609Combined sources7
Beta strandi612 – 617Combined sources6
Helixi618 – 621Combined sources4
Helixi624 – 626Combined sources3
Beta strandi630 – 632Combined sources3
Turni633 – 635Combined sources3
Beta strandi636 – 638Combined sources3
Helixi640 – 647Combined sources8
Helixi655 – 658Combined sources4
Helixi666 – 672Combined sources7
Beta strandi673 – 675Combined sources3
Beta strandi703 – 705Combined sources3
Turni706 – 708Combined sources3
Beta strandi712 – 716Combined sources5
Beta strandi718 – 721Combined sources4
Beta strandi723 – 725Combined sources3
Turni726 – 728Combined sources3
Beta strandi729 – 731Combined sources3
Helixi743 – 753Combined sources11
Helixi763 – 768Combined sources6
Helixi773 – 787Combined sources15
Helixi790 – 795Combined sources6
Helixi812 – 820Combined sources9
Helixi827 – 839Combined sources13
Helixi848 – 868Combined sources21

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP23497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 149HSRPROSITE-ProRule annotationAdd BLAST117
Domaini595 – 676SANDPROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni333 – 478Sufficient to mediate interaction with ETS1Add BLAST146

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi165 – 168D-box; recognition signal for CDC20-mediated degradation4
Motifi284 – 297PxVxL motifAdd BLAST14
Motifi536 – 553Nuclear localization signalSequence analysisAdd BLAST18
Motifi568 – 592Nuclear localization signalSequence analysisAdd BLAST25
Motifi717 – 734Nuclear localization signalSequence analysisAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3 – 6Poly-Gly4
Compositional biasi156 – 164Poly-Glu9
Compositional biasi759 – 764Poly-Lys6
Compositional biasi854 – 859Poly-Lys6
Compositional biasi860 – 868Poly-Glu9

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.
PF03172. HSR. 1 hit.
PF01342. SAND. 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)DescriptionActionsGraphical viewLength
Sequence conflicti47R → M in BAG56886 (PubMed:14702039).Curated1
Sequence conflicti247S → P in BAG56886 (PubMed:14702039).Curated1
Sequence conflicti402Q → H in BAG56886 (PubMed:14702039).Curated1
Sequence conflicti651A → R in AAL77438 (PubMed:9973607).Curated1
Sequence conflicti651A → R in AAL77439 (PubMed:9973607).Curated1
Isoform Sp100-B (identifier: P23497-3)
Sequence conflicti686M → T in AAC50743 (PubMed:8695863).Curated1
Isoform Sp100-C (identifier: P23497-4)
Sequence conflicti826M → T in AAK51202 (PubMed:11313457).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005621433M → V.Corresponds to variant rs12724dbSNPEnsembl.1
Natural variantiVAR_005622471S → P.1
Natural variantiVAR_034510699E → G.Corresponds to variant rs34700604dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0458681 – 36MAGGG…HDLQR → M in isoform 7. 1 PublicationAdd BLAST36
Alternative sequenceiVSP_04586911 – 35Missing in isoform 6. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_045870428 – 430Missing in isoform 6. 1 Publication3
Alternative sequenceiVSP_005982449 – 472RFSSS…CSSSL → LKKKKKKKQCHPQPQPQRGL LEQS in isoform SpAlt-C. CuratedAdd BLAST24
Alternative sequenceiVSP_005983473 – 879Missing in isoform SpAlt-C. CuratedAdd BLAST407
Alternative sequenceiVSP_005978478 – 480SQP → KED in isoform Sp100-A, isoform 6 and isoform 7. 3 Publications3
Alternative sequenceiVSP_005979481 – 879Missing in isoform Sp100-A, isoform 6 and isoform 7. 3 PublicationsAdd BLAST399
Alternative sequenceiVSP_005980685 – 688RILE → VMIK in isoform Sp100-B. 1 Publication4
Alternative sequenceiVSP_005981689 – 879Missing in isoform Sp100-B. 1 PublicationAdd BLAST191
Alternative sequenceiVSP_005984699 – 879EEHKK…EDDDK → PENSNICEVCNKWGRLFCCD TCPRSFHEHCHIPSVEANKN PWSCIFCRIKTIQERCPESQ SGHQESEVLMRQMLPEEQLK CEFLLLKVYCDSKSCFFASE PYYNREGSQGPQKPMWLNKV KTSLNEQMYTRVEGFVQDMR LIFHNHKEFYREDKFTRLGI QVQDIFEKNFRNIFAIQETS KNIIMFI in isoform Sp100-C. 1 PublicationAdd BLAST181

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H5PNMR-A595-688[»]
5FB0X-ray2.70A/C696-878[»]
5FB1X-ray2.10A696-875[»]
ProteinModelPortaliP23497.
SMRiP23497.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112555. 55 interactors.
DIPiDIP-5983N.
IntActiP23497. 38 interactors.
MINTiMINT-1188807.
STRINGi9606.ENSP00000343023.

PTM databases

iPTMnetiP23497.
PhosphoSitePlusiP23497.

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.
DisGeNETi6672.
GeneCardsiSP100.
HGNCiHGNC:11206. SP100.
HPAiHPA016707.
HPA017384.
MIMi604585. gene.
neXtProtiNX_P23497.
OpenTargetsiENSG00000067066.
PharmGKBiPA36043.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000067066-MONOMER.
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.
PF03172. HSR. 1 hit.
PF01342. SAND. 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: November 30, 2016
This is version 195 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.