P23497 (SP100_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear autoantigen Sp-100

Alternative name(s):
Lysp100b
Nuclear dot-associated Sp100 protein
Speckled 100 kDa

Gene names

Name:

SP100

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	879 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the control of gene expression.
Subunit structure	Homodimer. Splice variants heterodimerize. Interacts with members of the HP1 family of nonhistone chromosomal protein, such as CBX5 and CBX3 via the PxVxL motif. Interacts with Epstein-Barr virus EBNA-LP. Interacts with human cytomegalovirus/HHV-5 protein UL123. Ref.13 Ref.14 Ref.19
Subcellular location	Nucleus › PML body. Note: Found in the nuclear body, also known as nuclear domain 10 (ND10), PML oncogenic domain (POD), nuclear dots (ND) and KR body. The nuclear body is a nucleoplasmic structure of punctate shape, which varies in size and number. Induction by interferon and may be cell cycle stages modulate the subnuclear localization of the isoforms.
Tissue specificity	Widely expressed. Sp100-B is expressed only in spleen, tonsil, thymus, mature B-cell line and some T-cell line, but not in brain, liver, muscle or non-lymphoid cell lines.
Induction	By interferon.
Domain	The HSR domain is important for the nuclear body targeting as well as for the dimerization. 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.
Post-translational modification	Sumoylated. Sumoylation depends on a functional nuclear localization signal but is not necessary for nuclear import or nuclear body targeting. Ref.12
Miscellaneous	The major isoform Sp100-A, has a calculated MW of 54 kDa, but exhibits aberrant electrophoretic mobilities, with an apparent MW OF 100 kDa.
Sequence similarities	Contains 2 HMG box DNA-binding domains. Contains 1 HSR domain. Contains 1 SAND domain.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	DNA-binding
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from direct assay PubMed 14647468. Source: BHF-UCL interferon-gamma-mediated signaling pathway Inferred by curator Ref.8. Source: BHF-UCL negative regulation of DNA binding Inferred from direct assay PubMed 15247905. Source: BHF-UCL negative regulation of cellular component movement Inferred from mutant phenotype PubMed 15247905. Source: BHF-UCL negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 15247905. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 15247905. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 9636147. Source: BHF-UCL negative regulation of viral transcription Inferred from direct assay PubMed 16873258PubMed 16873258PubMed 16873258. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 11909962Ref.14. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 11909962. Source: BHF-UCL response to cytokine stimulus Inferred from direct assay PubMed 9412458. Source: BHF-UCL response to retinoic acid Inferred from direct assay Ref.4. Source: BHF-UCL response to type I interferon Inferred from direct assay PubMed 16873258PubMed 16873258PubMed 16873258PubMed 16873258. Source: BHF-UCL retinoic acid receptor signaling pathway Inferred by curator Ref.4. Source: BHF-UCL type I interferon-mediated signaling pathway Inferred by curator Ref.8. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from direct assay PubMed 14647468PubMed 15247905PubMed 9230084Ref.4Ref.2Ref.9PubMed 16873258PubMed 9412458. Source: BHF-UCL cytoplasm Inferred from direct assay PubMed 9412458. Source: BHF-UCL nuclear periphery Inferred from direct assay Ref.4. Source: BHF-UCL nucleolus Inferred from direct assay Ref.9. Source: BHF-UCL
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Inferred from direct assay PubMed 14647468Ref.14. Source: BHF-UCL transcription corepressor activity Inferred from direct assay PubMed 15247905PubMed 16873258PubMed 16873258PubMed 16873258. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SUMO3	P55854	2	EBI-751145,EBI-474067

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform Sp100-HMG (identifier: P23497-1)

Also known as: 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.

Note: Contains an almost complete and highly conserved copy of the DNA-binding HMG1 box.

Isoform Sp100-A (identifier: P23497-2)

Also known as: SP100;

The sequence of this isoform differs from the canonical sequence as follows:
     478-480: SQP → KED
     481-879: Missing.

Note: Major isoform.

Isoform Sp100-B (identifier: P23497-3)

Also known as: SpAlt-212;

The sequence of this isoform differs from the canonical sequence as follows:
     685-688: RILE → VTIK
     689-879: Missing.

Isoform Sp100-C (identifier: P23497-4)

The sequence of this isoform differs from the canonical sequence as follows:
     699-879: EEHKKKNPDA...EEENEEDDDK → PENSNICEVC...ETSKNIIMFI

Isoform SpAlt-C (identifier: P23497-5)

The sequence of this isoform differs from the canonical sequence as follows:
     449-472: RFSSSDFSDLSNGEELQETCSSSL → LKKKKKKKQCHPQPQPQRGLLEQS
     473-879: Missing.

Isoform 6 (identifier: P23497-6)

The sequence of this isoform differs from the canonical sequence as follows:
     11-35: Missing.
     428-430: Missing.
     478-480: SQP → KED
     481-879: Missing.

Note: No experimental confirmation available.

Isoform 7 (identifier: P23497-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQR → M
     478-480: SQP → KED
     481-879: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 879

879

Nuclear autoantigen Sp-100

PRO_0000074096

Regions

Domain

33 – 149

117

HSR

Domain

595 – 676

82

SAND

DNA binding

677 – 753

77

HMG box 1

DNA binding

769 – 837

69

HMG box 2

Motif

284 – 297

14

PxVxL motif

Motif

536 – 553

18

Nuclear localization signal Potential

Motif

568 – 592

25

Nuclear localization signal Potential

Motif

717 – 734

18

Nuclear localization signal Potential

Compositional bias

3 – 6

4

Poly-Gly

Compositional bias

156 – 164

9

Poly-Glu

Compositional bias

759 – 764

6

Poly-Lys

Compositional bias

854 – 859

6

Poly-Lys

Compositional bias

860 – 868

9

Poly-Glu

Amino acid modifications

Modified residue

18

1

Phosphoserine Ref.15

Modified residue

157

1

Phosphoserine Ref.18

Modified residue

171

1

Phosphoserine Ref.17

Modified residue

331

1

Phosphoserine Ref.15

Modified residue

362

1

Phosphoserine Ref.18

Modified residue

407

1

Phosphoserine Ref.16 Ref.17 Ref.18

Modified residue

409

1

Phosphoserine Ref.16 Ref.17 Ref.18

Modified residue

410

1

Phosphoserine Ref.16 Ref.17 Ref.18

Cross-link

297

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Natural variations

Alternative sequence

1 – 36

36

MAGGG…HDLQR → M in isoform 7.

VSP_045868

Alternative sequence

11 – 35

25

Missing in isoform 6.

VSP_045869

Alternative sequence

428 – 430

3

Missing in isoform 6.

VSP_045870

Alternative sequence

449 – 472

24

RFSSS…CSSSL → LKKKKKKKQCHPQPQPQRGL LEQS in isoform SpAlt-C.

VSP_005982

Alternative sequence

473 – 879

407

Missing in isoform SpAlt-C.

VSP_005983

Alternative sequence

478 – 480

3

SQP → KED in isoform Sp100-A, isoform 6 and isoform 7.

VSP_005978

Alternative sequence

481 – 879

399

Missing in isoform Sp100-A, isoform 6 and isoform 7.

VSP_005979

Alternative sequence

685 – 688

4

RILE → VTIK in isoform Sp100-B.

VSP_005980

Alternative sequence

689 – 879

191

Missing in isoform Sp100-B.

VSP_005981

Alternative sequence

699 – 879

181

EEHKK…EDDDK → PENSNICEVCNKWGRLFCCD TCPRSFHEHCHIPSVEANKN PWSCIFCRIKTIQERCPESQ SGHQESEVLMRQMLPEEQLK CEFLLLKVYCDSKSCFFASE PYYNREGSQGPQKPMWLNKV KTSLNEQMYTRVEGFVQDMR LIFHNHKEFYREDKFTRLGI QVQDIFEKNFRNIFAIQETS KNIIMFI in isoform Sp100-C.

VSP_005984

Natural variant

433

1

M → V in HeLa cells.
Corresponds to variant rs12724 [ dbSNP | Ensembl ].

VAR_005621

Natural variant

471

1

S → P in HeLa cells.

VAR_005622

Natural variant

699

1

E → G.
Corresponds to variant rs34700604 [ dbSNP | Ensembl ].

VAR_034510

Experimental info

Sequence conflict

47

1

R → M in BAG56886. Ref.5

Sequence conflict

247

1

S → P in BAG56886. Ref.5

Sequence conflict

402

1

Q → H in BAG56886. Ref.5

Sequence conflict

651

1

A → R in AAL77438. Ref.9

Sequence conflict

651

1

A → R in AAL77439. Ref.9

Isoform Sp100-B:

Sequence conflict

686

1

T → M in AAL77439. Ref.9

Isoform Sp100-C:

Sequence conflict

826

1

M → T in AAK51202. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

879

Helix Strand Turn

Details...

Helix

600 – 602

3

Beta strand

603 – 609

7

Beta strand

612 – 617

6

Helix

618 – 621

4

Helix

624 – 626

3

Beta strand

630 – 632

3

Turn

633 – 635

3

Beta strand

636 – 638

3

Helix

640 – 647

8

Helix

655 – 658

4

Helix

666 – 672

7

Beta strand

673 – 675

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Sp100-HMG (SpAlt-HMG) [UniParc]. Last modified April 27, 2001. Version 3. Checksum: CA55547DE21B2A10	FASTA	879	100,417
	10 20 30 40 50 60 MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 70 80 90 100 110 120 KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 130 140 150 160 170 180 VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 190 200 210 220 230 240 FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 250 260 270 280 290 300 KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 310 320 330 340 350 360 PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 370 380 390 400 410 420 ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 430 440 450 460 470 480 GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP 490 500 510 520 530 540 QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR 550 560 570 580 590 600 SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF 610 620 630 640 650 660 KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR 670 680 690 700 710 720 CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCEE HKKKNPDASV KFSEFLKKCS 730 740 750 760 770 780 ETWKTIFAKE KGKFEDMAKA DKAHYEREMK TYIPPKGEKK KKFKDPNAPK RPPLAFFLFC 790 800 810 820 830 840 SEYRPKIKGE HPGLSIDDVV KKLAGMWNNT AAADKQFYEK KAAKLKEKYK KDIAAYRAKG 850 860 870 KPNSAKKRVV KAEKSKKKKE EEEDEEDEQE EENEEDDDK
	Isoform Sp100-A (SP100) [UniParc]. Checksum: 10351A33BF3A4C12	FASTA	480	53,768
	10 20 30 40 50 60 MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 70 80 90 100 110 120 KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 130 140 150 160 170 180 VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 190 200 210 220 230 240 FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 250 260 270 280 290 300 KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 310 320 330 340 350 360 PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 370 380 390 400 410 420 ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 430 440 450 460 470 480 GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGKED
	Isoform Sp100-B (SpAlt-212) [UniParc]. Checksum: C0B467072DA75C96	FASTA	688	78,144
	10 20 30 40 50 60 MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 70 80 90 100 110 120 KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 130 140 150 160 170 180 VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 190 200 210 220 230 240 FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 250 260 270 280 290 300 KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 310 320 330 340 350 360 PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 370 380 390 400 410 420 ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 430 440 450 460 470 480 GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP 490 500 510 520 530 540 QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR 550 560 570 580 590 600 SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF 610 620 630 640 650 660 KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR 670 680 CGGYTLKVLM ENKFLPEPPS TRKKVTIK
	Isoform Sp100-C [UniParc]. Checksum: 3D33A477B171D7DE	FASTA	885	101,575
	10 20 30 40 50 60 MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 70 80 90 100 110 120 KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 130 140 150 160 170 180 VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 190 200 210 220 230 240 FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 250 260 270 280 290 300 KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 310 320 330 340 350 360 PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 370 380 390 400 410 420 ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 430 440 450 460 470 480 GALRSKHGEK APMTSRSTST WRIPSRKRRF SSSDFSDLSN GEELQETCSS SLRRGSGSQP 490 500 510 520 530 540 QEPENKKCSC VMCFPKGVPR SQEARTESSQ ASDMMDTMDV ENNSTLEKHS GKRRKKRRHR 550 560 570 580 590 600 SKVNGLQRGR KKDRPRKHLT LNNKVQKKRW QQRGRKANTR PLKRRRKRGP RIPKDENINF 610 620 630 640 650 660 KQSELPVTCG EVKGTLYKER FKQGTSKKCI QSEDKKWFTP REFEIEGDRG ASKNWKLSIR 670 680 690 700 710 720 CGGYTLKVLM ENKFLPEPPS TRKKRILESH NNTLVDPCPE NSNICEVCNK WGRLFCCDTC 730 740 750 760 770 780 PRSFHEHCHI PSVEANKNPW SCIFCRIKTI QERCPESQSG HQESEVLMRQ MLPEEQLKCE 790 800 810 820 830 840 FLLLKVYCDS KSCFFASEPY YNREGSQGPQ KPMWLNKVKT SLNEQMYTRV EGFVQDMRLI 850 860 870 880 FHNHKEFYRE DKFTRLGIQV QDIFEKNFRN IFAIQETSKN IIMFI
	Isoform SpAlt-C [UniParc]. Checksum: 3FD218C65A00100D	FASTA	472	53,113
	10 20 30 40 50 60 MAGGGGDLST RRLNECISPV ANEMNHLPAH SHDLQRMFTE DQGVDDRLLY DIVFKHFKRN 70 80 90 100 110 120 KVEISNAIKK TFPFLEGLRD RDLITNKMFE DSQDSCRNLV PVQRVVYNVL SELEKTFNLP 130 140 150 160 170 180 VLEALFSDVN MQEYPDLIHI YKGFENVIHD KLPLQESEEE EREERSGLQL SLEQGTGENS 190 200 210 220 230 240 FRSLTWPPSG SPSHAGTTPP ENGLSEHPCE TEQINAKRKD TTSDKDDSLG SQQTNEQCAQ 250 260 270 280 290 300 KAEPTESCEQ IAVQVNNGDA GREMPCPLPC DEESPEAELH NHGIQINSCS VRLVDIKKEK 310 320 330 340 350 360 PFSNSKVECQ AQARTHHNQA SDIIVISSED SEGSTDVDEP LEVFISAPRS EPVINNDNPL 370 380 390 400 410 420 ESNDEKEGQE ATCSRPQIVP EPMDFRKLST FRESFKKRVI GQDHDFSESS EEEAPAEASS 430 440 450 460 470 GALRSKHGEK APMTSRSTST WRIPSRKRLK KKKKKKQCHP QPQPQRGLLE QS
	Isoform 6 [UniParc]. Checksum: C957A23305439EE8	FASTA	452	50,590
	10 20 30 40 50 60 MAGGGGDLST RMFTEDQGVD DRLLYDIVFK HFKRNKVEIS NAIKKTFPFL EGLRDRDLIT 70 80 90 100 110 120 NKMFEDSQDS CRNLVPVQRV VYNVLSELEK TFNLPVLEAL FSDVNMQEYP DLIHIYKGFE 130 140 150 160 170 180 NVIHDKLPLQ ESEEEEREER SGLQLSLEQG TGENSFRSLT WPPSGSPSHA GTTPPENGLS 190 200 210 220 230 240 EHPCETEQIN AKRKDTTSDK DDSLGSQQTN EQCAQKAEPT ESCEQIAVQV NNGDAGREMP 250 260 270 280 290 300 CPLPCDEESP EAELHNHGIQ INSCSVRLVD IKKEKPFSNS KVECQAQART HHNQASDIIV 310 320 330 340 350 360 ISSEDSEGST DVDEPLEVFI SAPRSEPVIN NDNPLESNDE KEGQEATCSR PQIVPEPMDF 370 380 390 400 410 420 RKLSTFRESF KKRVIGQDHD FSESSEEEAP AEASSGALRS KHAPMTSRST STWRIPSRKR 430 440 450 RFSSSDFSDL SNGEELQETC SSSLRRGSGK ED
	Isoform 7 [UniParc]. Checksum: 05DF245B919FAA1B	FASTA	445	50,032
	10 20 30 40 50 60 MMFTEDQGVD DRLLYDIVFK HFKRNKVEIS NAIKKTFPFL EGLRDRDLIT NKMFEDSQDS 70 80 90 100 110 120 CRNLVPVQRV VYNVLSELEK TFNLPVLEAL FSDVNMQEYP DLIHIYKGFE NVIHDKLPLQ 130 140 150 160 170 180 ESEEEEREER SGLQLSLEQG TGENSFRSLT WPPSGSPSHA GTTPPENGLS EHPCETEQIN 190 200 210 220 230 240 AKRKDTTSDK DDSLGSQQTN EQCAQKAEPT ESCEQIAVQV NNGDAGREMP CPLPCDEESP 250 260 270 280 290 300 EAELHNHGIQ INSCSVRLVD IKKEKPFSNS KVECQAQART HHNQASDIIV ISSEDSEGST 310 320 330 340 350 360 DVDEPLEVFI SAPRSEPVIN NDNPLESNDE KEGQEATCSR PQIVPEPMDF RKLSTFRESF 370 380 390 400 410 420 KKRVIGQDHD FSESSEEEAP AEASSGALRS KHGEKAPMTS RSTSTWRIPS RKRRFSSSDF 430 440 SDLSNGEELQ ETCSSSLRRG SGKED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies." Dent A.L., Yewdell J., Puvion-Dutilleul F., Koken M.H.M., de The H., Staudt L.M. Blood 88:1423-1426(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-B).
[2]	"Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment." Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A. Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-HMG). Tissue: Mammary cancer.
[3]	"Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis." Szostecki C., Guldner H.H., Netter H.J., Will H. J. Immunol. 145:4338-4347(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-A). Tissue: Liver and Placenta.
[4]	"Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: role of SUMO modification." Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., Dejean A. Mol. Cell. Biol. 21:3314-3324(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP100-C).
[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]	"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: CHARACTERIZATION, SUMOYLATION.
[13]	"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.
[14]	"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: INTERACTION WITH EBV EBNA-LP.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-409 AND SER-410, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: INTERACTION WITH HHV-5 PROTEIN UL123.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U36501 mRNA. Translation: AAC50743.1.
AF056322 mRNA. Translation: AAC39790.1.
M60618 mRNA. Translation: AAA35537.1.
AF255565 mRNA. Translation: AAK51202.1.
AK293373 mRNA. Translation: BAG56886.1.
AC009949 Genomic DNA. No translation available.
AC010149 Genomic DNA. No translation available.
BC011562 mRNA. Translation: AAH11562.1.
X95472 Genomic DNA. Translation: CAA64744.1.
L79986 mRNA. Translation: AAL77441.1.
L79987 mRNA. Translation: AAL77439.1.
L79988 mRNA. Translation: AAL77438.1.
AF076675 Genomic DNA. Translation: AAF39781.1.
AF378670 Genomic DNA. Translation: AAK57703.1.

IPI

IPI00011675.
IPI00218324.
IPI00218325.
IPI00218326.
IPI00218327.
IPI00917048.
IPI00917345.

PIR

A37244.

RefSeq

NP_001073860.1. NM_001080391.1.
NP_001193630.1. NM_001206701.1.
NP_001193631.1. NM_001206702.1.
NP_001193632.1. NM_001206703.1.
NP_001193633.1. NM_001206704.1.
NP_003104.2. NM_003113.3.

UniGene

Hs.369056.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H5P	NMR	-	A	595-684	[»]

ProteinModelPortal

P23497.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5983N.

IntAct

P23497. 6 interactions.

MINT

MINT-1188807.

PTM databases

PhosphoSite

P23497.

Polymorphism databases

DMDM

13878931.

Proteomic databases

PaxDb

P23497.

PRIDE

P23497.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264052; ENSP00000264052; ENSG00000067066.
ENST00000340126; ENSP00000343023; ENSG00000067066.
ENST00000409341; ENSP00000386404; ENSG00000067066.
ENST00000409897; ENSP00000386998; ENSG00000067066.
ENST00000427101; ENSP00000399389; ENSG00000067066.

GeneID

6672.

KEGG

hsa:6672.

UCSC

uc002vqq.2. human.
uc002vqt.3. human.
uc002vqu.1. human.
uc010zmb.2. human.

Organism-specific databases

CTD

6672.

GeneCards

GC02P231280.

HGNC

HGNC:11206. SP100.

HPA

HPA016707.
HPA017384.

MIM

604585. gene.

neXtProt

NX_P23497.

PharmGKB

PA36043.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG249894.

HOVERGEN

HBG057632.

KO

K15413.

OMA

TESCEQV.

OrthoDB

EOG44QT09.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P23497.

Bgee

P23497.

CleanEx

HS_SP100.

Genevestigator

P23497.

GermOnline

ENSG00000067066. Homo sapiens.

Family and domain databases

Gene3D

1.10.30.10. 2 hits.
3.10.390.10. 1 hit.

InterPro

IPR009071. HMG_box_dom.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR004865. Sp100.
[Graphical view]

Pfam

PF09011. DUF1898. 1 hit.
PF00505. HMG_box. 1 hit.
PF01342. SAND. 1 hit.
PF03172. Sp100. 1 hit.
[Graphical view]

SMART

SM00398. HMG. 2 hits.
SM00258. SAND. 1 hit.
[Graphical view]

SUPFAM

SSF47095. HMG-box. 2 hits.
SSF63763. SAND_like. 1 hit.

PROSITE

PS50118. HMG_BOX_2. 2 hits.
PS51414. HSR. 1 hit.
PS50864. SAND. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SP100. human.

EvolutionaryTrace

P23497.

GenomeRNAi

6672.

NextBio

26015.

SOURCE

Search...

Entry information

Entry name

SP100_HUMAN

Accession

Primary (citable) accession number: P23497
Secondary accession number(s): B4DDX5 , B8ZZD8, E9PH61, F8WFE2, O75450, Q13343, Q8TE34, Q96F70, Q96T24, Q96T95, Q9NP33, Q9UE32

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	April 27, 2001
Last modified:	May 1, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.