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Protein

FACT complex subunit SSRP1

Gene

SSRP1

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

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi547 – 615HMG boxPROSITE-ProRule annotationAdd BLAST69

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

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
SIGNORiQ08945

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

EuPathDBiHostDB:ENSG00000149136.8
HGNCiHGNC:11327 SSRP1
MIMi604328 gene
neXtProtiNX_Q08945

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi450D → A: Abolishes cleavage by caspase. 1 Publication1
Mutagenesisi510S → A: Unable to bind DNA; when associated with A-657 and A-688. 1 Publication1
Mutagenesisi657S → A: Unable to bind DNA; when associated with A-510 and A-688. Still able to bind DNA; when associated with A-688. 1 Publication1
Mutagenesisi688S → A: Unable to bind DNA; when associated with A-510 and A-657. Still able to bind DNA; when associated with A-657. 1 Publication1

Organism-specific databases

DisGeNETi6749
OpenTargetsiENSG00000149136
PharmGKBiPA36151

Polymorphism and mutation databases

BioMutaiSSRP1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000486062 – 709FACT complex subunit SSRP1Add BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Cross-linki90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei170PhosphothreonineCombined sources1
Modified residuei233N6-acetyllysineCombined sources1
Cross-linki296Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki364Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei413N6-acetyllysineCombined sources1
Modified residuei437PhosphoserineCombined sources1
Modified residuei441PhosphotyrosineBy similarity1
Modified residuei444PhosphoserineCombined sources1
Modified residuei452PhosphotyrosineBy similarity1
Modified residuei471PhosphoserineCombined sources1
Modified residuei510Phosphoserine; by CK21 Publication1
Modified residuei542N6-acetyllysineBy similarity1
Modified residuei657PhosphoserineCombined sources1 Publication1
Modified residuei659PhosphoserineCombined sources1
Modified residuei667PhosphoserineCombined sources1
Modified residuei668PhosphoserineCombined sources1
Modified residuei671PhosphoserineCombined sources1
Modified residuei672PhosphoserineCombined sources1
Modified residuei673PhosphoserineCombined sources1
Modified residuei688Phosphoserine; by CK21 Publication1

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)DescriptionActionsGraphical viewLength
Sitei450 – 451Cleavage; by caspase-3 and/or caspase-72

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ08945
MaxQBiQ08945
PaxDbiQ08945
PeptideAtlasiQ08945
PRIDEiQ08945
ProteomicsDBi58651

PTM databases

iPTMnetiQ08945
PhosphoSitePlusiQ08945
SwissPalmiQ08945

Miscellaneous databases

PMAP-CutDBiQ08945

Expressioni

Gene expression databases

BgeeiENSG00000149136 Expressed in 227 organ(s), highest expression level in tendon of biceps brachii
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 (PubMed:10421373). Also component of a CK2-SPT16-SSRP1 complex which forms following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B (PubMed:11239457, PubMed:12393879). Binds to histone H3-H4 tetramers, but not to intact nucleosomes. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292). Interacts with isoform gamma of TP63 (PubMed:12374749). Interacts with FYTTD1/UIF (PubMed:19836239). Interacts with SRF (By similarity). Interacts with NEK9 (PubMed:14660563).By similarity7 Publications
(Microbial infection) Interacts with Herpes simplex virus 1 (HHV-1) protein ICP22; this interaction relocalizes the FACT complex to viral genomes in infected cells.1 Publication

Binary interactionsi

Protein-protein interaction databases

BioGridi112627, 140 interactors
ComplexPortaliCPX-419 FACT complex
CORUMiQ08945
DIPiDIP-169N
IntActiQ08945, 48 interactors
MINTiQ08945
STRINGi9606.ENSP00000278412

Structurei

Secondary structure

1709
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ08945
SMRiQ08945
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi439 – 496Asp/Glu-rich (acidic)Add BLAST58
Compositional biasi497 – 511Ser-richAdd BLAST15
Compositional biasi512 – 534Arg/Lys-rich (basic)Add BLAST23
Compositional biasi623 – 640Arg/Lys-rich (basic)Add BLAST18
Compositional biasi641 – 709Ser-richAdd BLAST69

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

Phylogenomic databases

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

Family and domain databases

Gene3Di1.10.30.10, 1 hit
2.30.29.220, 1 hit
2.30.29.30, 2 hits
InterProiView protein in InterPro
IPR013719 DUF1747
IPR009071 HMG_box_dom
IPR036910 HMG_box_dom_sf
IPR011993 PH-like_dom_sf
IPR035417 POB3_N
IPR000969 SSrcognition
IPR024954 SSRP1_dom
IPR038167 SSRP1_sf
PfamiView protein in Pfam
PF00505 HMG_box, 1 hit
PF17292 POB3_N, 1 hit
PF08512 Rtt106, 1 hit
PF03531 SSrecog, 1 hit
PRINTSiPR00887 SSRCOGNITION
SMARTiView protein in SMART
SM00398 HMG, 1 hit
SM01287 Rtt106, 1 hit
SUPFAMiSSF47095 SSF47095, 1 hit
PROSITEiView protein in PROSITE
PS50118 HMG_BOX_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PMD4E9PMD4_HUMAN
FACT complex subunit SSRP1
SSRP1
173Annotation score:
A0A0U1RRK2A0A0U1RRK2_HUMAN
FACT complex subunit SSRP1
SSRP1
225Annotation score:
E9PPZ7E9PPZ7_HUMAN
FACT complex subunit SSRP1
SSRP1
89Annotation score:

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052495225L → V. Corresponds to variant dbSNP:rs768436Ensembl.1
Natural variantiVAR_052496458E → Q. Corresponds to variant dbSNP:rs11540304Ensembl.1

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

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IFSX-ray1.93A196-430[»]
5UMRX-ray1.50A1-100[»]
5UMSX-ray1.57A174-437[»]
5VWENMR-A551-617[»]
ProteinModelPortaliQ08945
SMRiQ08945
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112627, 140 interactors
ComplexPortaliCPX-419 FACT complex
CORUMiQ08945
DIPiDIP-169N
IntActiQ08945, 48 interactors
MINTiQ08945
STRINGi9606.ENSP00000278412

PTM databases

iPTMnetiQ08945
PhosphoSitePlusiQ08945
SwissPalmiQ08945

Polymorphism and mutation databases

BioMutaiSSRP1

Proteomic databases

EPDiQ08945
MaxQBiQ08945
PaxDbiQ08945
PeptideAtlasiQ08945
PRIDEiQ08945
ProteomicsDBi58651

Protocols and materials databases

DNASUi6749
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6749
DisGeNETi6749
EuPathDBiHostDB:ENSG00000149136.8
GeneCardsiSSRP1
HGNCiHGNC:11327 SSRP1
HPAiHPA002697
MIMi604328 gene
neXtProtiNX_Q08945
OpenTargetsiENSG00000149136
PharmGKBiPA36151
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0526 Eukaryota
COG5165 LUCA
GeneTreeiENSGT00560000076898
HOGENOMiHOG000180790
HOVERGENiHBG002932
InParanoidiQ08945
KOiK09272
OMAiPRGRYDV
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
SIGNORiQ08945

Miscellaneous databases

ChiTaRSiSSRP1 human
GeneWikiiStructure_specific_recognition_protein_1
GenomeRNAii6749
PMAP-CutDBiQ08945
PROiPR:Q08945
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149136 Expressed in 227 organ(s), highest expression level in tendon of biceps brachii
CleanExiHS_SSRP1
ExpressionAtlasiQ08945 baseline and differential
GenevisibleiQ08945 HS

Family and domain databases

Gene3Di1.10.30.10, 1 hit
2.30.29.220, 1 hit
2.30.29.30, 2 hits
InterProiView protein in InterPro
IPR013719 DUF1747
IPR009071 HMG_box_dom
IPR036910 HMG_box_dom_sf
IPR011993 PH-like_dom_sf
IPR035417 POB3_N
IPR000969 SSrcognition
IPR024954 SSRP1_dom
IPR038167 SSRP1_sf
PfamiView protein in Pfam
PF00505 HMG_box, 1 hit
PF17292 POB3_N, 1 hit
PF08512 Rtt106, 1 hit
PF03531 SSrecog, 1 hit
PRINTSiPR00887 SSRCOGNITION
SMARTiView protein in SMART
SM00398 HMG, 1 hit
SM01287 Rtt106, 1 hit
SUPFAMiSSF47095 SSF47095, 1 hit
PROSITEiView protein in PROSITE
PS50118 HMG_BOX_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSSRP1_HUMAN
AccessioniPrimary (citable) accession number: Q08945
Secondary accession number(s): Q5BJG8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 7, 2018
This is version 196 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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