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Protein

FACT complex subunit SSRP1

Gene

SSRP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi547 – 61569HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • DNA binding Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit SSRP1
Alternative name(s):
Chromatin-specific transcription elongation factor 80 kDa subunit
Facilitates chromatin transcription complex 80 kDa subunit
Short name:
FACT 80 kDa subunit
Short name:
FACTp80
Facilitates chromatin transcription complex subunit SSRP1
Recombination signal sequence recognition protein 1
Structure-specific recognition protein 1
Short name:
hSSRP1
T160
Gene namesi
Name:SSRP1
Synonyms:FACT80
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:11327. SSRP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi450 – 4501D → A: Abolishes cleavage by caspase. 1 Publication
Mutagenesisi510 – 5101S → A: Unable to bind DNA; when associated with A-657 and A-688. 1 Publication
Mutagenesisi657 – 6571S → A: Unable to bind DNA; when associated with A-510 and A-688. Still able to bind DNA; when associated with A-688. 1 Publication
Mutagenesisi688 – 6881S → A: Unable to bind DNA; when associated with A-510 and A-657. Still able to bind DNA; when associated with A-657. 1 Publication

Organism-specific databases

PharmGKBiPA36151.

Polymorphism and mutation databases

BioMutaiSSRP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 709708FACT complex subunit SSRP1PRO_0000048606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei170 – 1701PhosphothreonineCombined sources
Modified residuei233 – 2331N6-acetyllysineCombined sources
Modified residuei413 – 4131N6-acetyllysineCombined sources
Modified residuei437 – 4371PhosphoserineCombined sources
Modified residuei441 – 4411PhosphotyrosineBy similarity
Modified residuei444 – 4441PhosphoserineCombined sources
Modified residuei452 – 4521PhosphotyrosineBy similarity
Modified residuei471 – 4711PhosphoserineCombined sources
Modified residuei510 – 5101Phosphoserine; by CK21 Publication
Modified residuei542 – 5421N6-acetyllysineBy similarity
Modified residuei657 – 6571PhosphoserineCombined sources1 Publication
Modified residuei659 – 6591PhosphoserineCombined sources
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei668 – 6681PhosphoserineCombined sources
Modified residuei671 – 6711PhosphoserineCombined sources
Modified residuei672 – 6721PhosphoserineCombined sources
Modified residuei673 – 6731PhosphoserineCombined sources
Modified residuei688 – 6881Phosphoserine; by CK21 Publication

Post-translational modificationi

Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity.2 Publications
Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein.1 Publication
Sumoylated.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei450 – 4512Cleavage; by caspase-3 and/or caspase-7

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ08945.
MaxQBiQ08945.
PaxDbiQ08945.
PeptideAtlasiQ08945.
PRIDEiQ08945.

PTM databases

iPTMnetiQ08945.
PhosphoSiteiQ08945.
SwissPalmiQ08945.

Miscellaneous databases

PMAP-CutDBQ08945.

Expressioni

Gene expression databases

BgeeiENSG00000149136.
CleanExiHS_SSRP1.
ExpressionAtlasiQ08945. baseline and differential.
GenevisibleiQ08945. HS.

Organism-specific databases

HPAiHPA002697.

Interactioni

Subunit structurei

Interacts with MYOG (via C-terminal region) (By similarity). Component of the FACT complex, a stable heterodimer of SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B. Binds to histone H3-H4 tetramers, but not to intact nucleosomes. Interacts with isoform gamma of TP63. Interacts with FYTTD1/UIF, SRF and NEK9.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK2A1P684002EBI-353771,EBI-347804
MCM4P339915EBI-353771,EBI-374938
MCM6Q145662EBI-353771,EBI-374900
SUPT16HQ9Y5B93EBI-353771,EBI-1046849

Protein-protein interaction databases

BioGridi112627. 128 interactions.
DIPiDIP-169N.
IntActiQ08945. 38 interactions.
MINTiMINT-5004485.
STRINGi9606.ENSP00000278412.

Structurei

Secondary structure

1
709
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi199 – 20911Combined sources
Beta strandi212 – 2187Combined sources
Beta strandi220 – 2267Combined sources
Beta strandi231 – 2355Combined sources
Helixi236 – 2383Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi250 – 26516Combined sources
Beta strandi268 – 27811Combined sources
Beta strandi282 – 2865Combined sources
Helixi291 – 2988Combined sources
Beta strandi304 – 3096Combined sources
Helixi310 – 32213Combined sources
Helixi335 – 3373Combined sources
Beta strandi339 – 3457Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi356 – 36510Combined sources
Beta strandi367 – 3704Combined sources
Helixi371 – 3733Combined sources
Beta strandi374 – 3818Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi389 – 3957Combined sources
Beta strandi400 – 4067Combined sources
Helixi408 – 42013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFSX-ray1.93A196-430[»]
ProteinModelPortaliQ08945.
SMRiQ08945. Positions 1-170, 197-427, 486-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi439 – 49658Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi497 – 51115Ser-richAdd
BLAST
Compositional biasi512 – 53423Arg/Lys-rich (basic)Add
BLAST
Compositional biasi623 – 64018Arg/Lys-rich (basic)Add
BLAST
Compositional biasi641 – 70969Ser-richAdd
BLAST

Domaini

The HMG box DNA-binding domain mediates DNA-binding. It has both affinity and specificity for DNA damaged globally with cisplatin.1 Publication

Sequence similaritiesi

Belongs to the SSRP1 family.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0526. Eukaryota.
COG5165. LUCA.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
HOVERGENiHBG002932.
InParanoidiQ08945.
KOiK09272.
OMAiHEVFTTV.
OrthoDBiEOG091G04JP.
PhylomeDBiQ08945.
TreeFamiTF315228.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_dom-like.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM00398. HMG. 1 hit.
SM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETLEFNDV YQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE
60 70 80 90 100
GIWRRVALGH GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK
110 120 130 140 150
DLCVKGWNWG TVKFGGQLLS FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF
160 170 180 190 200
HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA FAQNVLSKAD VIQATGDAIC
210 220 230 240 250
IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL RLFLLPHKDQ
260 270 280 290 300
RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG
310 320 330 340 350
RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG
360 370 380 390 400
LLYPLERGFI YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ
410 420 430 440 450
YTFSSIEREE YGKLFDFVNA KKLNIKNRGL KEGMNPSYDE YADSDEDQHD
460 470 480 490 500
AYLERMKEEG KIREENANDS SDDSGEETDE SFNPGEEEED VAEEFDSNAS
510 520 530 540 550
ASSSSNEGDS DRDEKKRKQL KKAKMAKDRK SRKKPVEVKK GKDPNAPKRP
560 570 580 590 600
MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA
610 620 630 640 650
EDARRDYEKA MKEYEGGRGE SSKRDKSKKK KKVKVKMEKK STPSRGSSSK
660 670 680 690 700
SSSRQLSESF KSKEFVSSDE SSSGENKSKK KRRRSEDSEE EELASTPPSS

EDSASGSDE
Length:709
Mass (Da):81,075
Last modified:February 1, 1995 - v1
Checksum:i4E7EE3735EB41082
GO

Sequence cautioni

The sequence AAH91486 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti225 – 2251L → V.
Corresponds to variant rs768436 [ dbSNP | Ensembl ].
VAR_052495
Natural varianti458 – 4581E → Q.
Corresponds to variant rs11540304 [ dbSNP | Ensembl ].
VAR_052496

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86737 mRNA. Translation: AAA58660.1.
BC005116 mRNA. Translation: AAH05116.1.
BC091486 mRNA. Translation: AAH91486.1. Sequence problems.
CCDSiCCDS7952.1.
PIRiA41976.
RefSeqiNP_003137.1. NM_003146.2.
UniGeneiHs.523680.

Genome annotation databases

EnsembliENST00000278412; ENSP00000278412; ENSG00000149136.
GeneIDi6749.
KEGGihsa:6749.
UCSCiuc001njt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86737 mRNA. Translation: AAA58660.1.
BC005116 mRNA. Translation: AAH05116.1.
BC091486 mRNA. Translation: AAH91486.1. Sequence problems.
CCDSiCCDS7952.1.
PIRiA41976.
RefSeqiNP_003137.1. NM_003146.2.
UniGeneiHs.523680.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFSX-ray1.93A196-430[»]
ProteinModelPortaliQ08945.
SMRiQ08945. Positions 1-170, 197-427, 486-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112627. 128 interactions.
DIPiDIP-169N.
IntActiQ08945. 38 interactions.
MINTiMINT-5004485.
STRINGi9606.ENSP00000278412.

PTM databases

iPTMnetiQ08945.
PhosphoSiteiQ08945.
SwissPalmiQ08945.

Polymorphism and mutation databases

BioMutaiSSRP1.

Proteomic databases

EPDiQ08945.
MaxQBiQ08945.
PaxDbiQ08945.
PeptideAtlasiQ08945.
PRIDEiQ08945.

Protocols and materials databases

DNASUi6749.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278412; ENSP00000278412; ENSG00000149136.
GeneIDi6749.
KEGGihsa:6749.
UCSCiuc001njt.3. human.

Organism-specific databases

CTDi6749.
GeneCardsiSSRP1.
HGNCiHGNC:11327. SSRP1.
HPAiHPA002697.
MIMi604328. gene.
neXtProtiNX_Q08945.
PharmGKBiPA36151.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0526. Eukaryota.
COG5165. LUCA.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
HOVERGENiHBG002932.
InParanoidiQ08945.
KOiK09272.
OMAiHEVFTTV.
OrthoDBiEOG091G04JP.
PhylomeDBiQ08945.
TreeFamiTF315228.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiSSRP1. human.
GeneWikiiStructure_specific_recognition_protein_1.
GenomeRNAii6749.
PMAP-CutDBQ08945.
PROiQ08945.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149136.
CleanExiHS_SSRP1.
ExpressionAtlasiQ08945. baseline and differential.
GenevisibleiQ08945. HS.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_dom-like.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM00398. HMG. 1 hit.
SM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSSRP1_HUMAN
AccessioniPrimary (citable) accession number: Q08945
Secondary accession number(s): Q5BJG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 174 of the entry and version 1 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

Autoantibodies against SSRP1 are present in sera from patients with systemic lupus erythematosus, but not other rheumatic diseases.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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.