Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

FACT complex subunit SSRP1

Gene

Ssrp1

Organism
Mus musculus (Mouse)
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. Also acts as a transcriptional coactivator for p63/TP63.1 Publication

Regions

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

GO - Molecular functioni

  • chromatin binding Source: MGI
  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: MGI

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-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-112387. Elongation arrest and recovery.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit SSRP1
Alternative name(s):
Facilitates chromatin transcription complex subunit SSRP1
Recombination signal sequence recognition protein 1
Structure-specific recognition protein 1
T160
Gene namesi
Name:Ssrp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:107912. Ssrp1.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome By similarity
  • Nucleusnucleolus By similarity

  • Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryos die soon after implantation while preimplantation blastocysts are defective for cell outgrowth.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000486072 – 708FACT complex subunit SSRP1Add BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei170PhosphothreonineBy similarity1
Modified residuei233N6-acetyllysineBy similarity1
Modified residuei413N6-acetyllysineBy similarity1
Modified residuei441PhosphotyrosineCombined sources1
Modified residuei444PhosphoserineCombined sources1
Modified residuei452PhosphotyrosineCombined sources1
Modified residuei471PhosphoserineBy similarity1
Modified residuei510Phosphoserine; by CK2By similarity1
Modified residuei542N6-acetyllysineCombined sources1
Modified residuei657Phosphoserine; by CK2By similarity1
Modified residuei659PhosphoserineBy similarity1
Modified residuei667PhosphoserineBy similarity1
Modified residuei668PhosphoserineBy similarity1
Modified residuei671PhosphoserineBy similarity1
Modified residuei672PhosphoserineBy similarity1
Modified residuei673PhosphoserineBy similarity1
Modified residuei688Phosphoserine; by CK2By similarity1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei450 – 451Cleavage; by caspase-3 and/or caspase-7By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ08943.
MaxQBiQ08943.
PaxDbiQ08943.
PeptideAtlasiQ08943.
PRIDEiQ08943.

PTM databases

iPTMnetiQ08943.
PhosphoSitePlusiQ08943.
SwissPalmiQ08943.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027067.
CleanExiMM_SSRP1.
ExpressionAtlasiQ08943. baseline and differential.
GenevisibleiQ08943. MM.

Interactioni

Subunit structurei

Interacts with MYOG (via C-terminal region) (PubMed:23364797). 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. Identified in a centromere complex containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Interacts with isoform gamma of TP63. Interacts with FYTTD1/UIF (By similarity). Interacts with SRF (By similarity). Interacts with NEK9 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi203512. 3 interactors.
IntActiQ08943. 4 interactors.
MINTiMINT-4135570.
STRINGi10090.ENSMUSP00000076971.

Structurei

3D structure databases

ProteinModelPortaliQ08943.
SMRiQ08943.
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 – 708Ser-richAdd BLAST68

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.
InParanoidiQ08943.
KOiK09272.
OMAiHEVFTTV.
OrthoDBiEOG091G04JP.
PhylomeDBiQ08943.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q08943-1) [UniParc]FASTAAdd to basket

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
MAETLEFNDI FQEVKGSMND 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 KEGINPGYDD YADSDEDQHD
460 470 480 490 500
AYLERMKEEG KIREENANDS SDDSGEETDE SFNPGEEEED VAEEFDSNAS
510 520 530 540 550
ASSSSNEGDS DREEKKREQL KRAKMAKDRK SRRKSSEAKK GKDPNAPKRP
560 570 580 590 600
MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA
610 620 630 640 650
EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKMEKK STPSRGSSSK
660 670 680 690 700
SSSRQLSDSF KSKEFVSSDE SSSGENKSKK KRRRSEDSEE ELASTPPSSE

DSASGSDE
Length:708
Mass (Da):80,860
Last modified:July 11, 2006 - v2
Checksum:i8259C1A6E9899843
GO
Isoform 2 (identifier: Q08943-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     621-621: S → SSKRDK

Note: No experimental confirmation available.
Show »
Length:713
Mass (Da):81,475
Checksum:i4216D673573637ED
GO

Sequence cautioni

The sequence AAH42502 differs from that shown. Reason: Frameshift at position 697.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27 – 28RQ → PS in AAB19500 (PubMed:1678855).Curated2
Sequence conflicti54R → P in AAB19500 (PubMed:1678855).Curated1
Sequence conflicti138 – 144QCTTGKN → SVPQARI in AAB19500 (PubMed:1678855).Curated7
Sequence conflicti156A → P in AAB19500 (PubMed:1678855).Curated1
Sequence conflicti589 – 590SK → HE in AAH96682 (PubMed:15489334).Curated2
Sequence conflicti604R → S in AAH96682 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_019626621S → SSKRDK in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50213 mRNA. Translation: AAB19500.2.
AK146446 mRNA. Translation: BAE27178.1.
AK146585 mRNA. Translation: BAE27280.1.
AK146607 mRNA. Translation: BAE27299.1.
AK151584 mRNA. Translation: BAE30524.1.
AK158552 mRNA. Translation: BAE34555.1.
BC042502 mRNA. Translation: AAH42502.1. Frameshift.
BC096682 mRNA. Translation: AAH96682.1.
CCDSiCCDS38165.1. [Q08943-1]
PIRiA41265.
RefSeqiNP_001129553.1. NM_001136081.2. [Q08943-1]
NP_892035.2. NM_182990.4. [Q08943-1]
XP_006499133.1. XM_006499070.1. [Q08943-1]
UniGeneiMm.219793.
Mm.491456.

Genome annotation databases

EnsembliENSMUST00000077798; ENSMUSP00000076971; ENSMUSG00000027067. [Q08943-1]
ENSMUST00000168266; ENSMUSP00000127058; ENSMUSG00000027067. [Q08943-1]
GeneIDi20833.
KEGGimmu:20833.
UCSCiuc008kju.2. mouse. [Q08943-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50213 mRNA. Translation: AAB19500.2.
AK146446 mRNA. Translation: BAE27178.1.
AK146585 mRNA. Translation: BAE27280.1.
AK146607 mRNA. Translation: BAE27299.1.
AK151584 mRNA. Translation: BAE30524.1.
AK158552 mRNA. Translation: BAE34555.1.
BC042502 mRNA. Translation: AAH42502.1. Frameshift.
BC096682 mRNA. Translation: AAH96682.1.
CCDSiCCDS38165.1. [Q08943-1]
PIRiA41265.
RefSeqiNP_001129553.1. NM_001136081.2. [Q08943-1]
NP_892035.2. NM_182990.4. [Q08943-1]
XP_006499133.1. XM_006499070.1. [Q08943-1]
UniGeneiMm.219793.
Mm.491456.

3D structure databases

ProteinModelPortaliQ08943.
SMRiQ08943.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203512. 3 interactors.
IntActiQ08943. 4 interactors.
MINTiMINT-4135570.
STRINGi10090.ENSMUSP00000076971.

PTM databases

iPTMnetiQ08943.
PhosphoSitePlusiQ08943.
SwissPalmiQ08943.

Proteomic databases

EPDiQ08943.
MaxQBiQ08943.
PaxDbiQ08943.
PeptideAtlasiQ08943.
PRIDEiQ08943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077798; ENSMUSP00000076971; ENSMUSG00000027067. [Q08943-1]
ENSMUST00000168266; ENSMUSP00000127058; ENSMUSG00000027067. [Q08943-1]
GeneIDi20833.
KEGGimmu:20833.
UCSCiuc008kju.2. mouse. [Q08943-1]

Organism-specific databases

CTDi6749.
MGIiMGI:107912. Ssrp1.

Phylogenomic databases

eggNOGiKOG0526. Eukaryota.
COG5165. LUCA.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
HOVERGENiHBG002932.
InParanoidiQ08943.
KOiK09272.
OMAiHEVFTTV.
OrthoDBiEOG091G04JP.
PhylomeDBiQ08943.
TreeFamiTF315228.

Enzyme and pathway databases

ReactomeiR-MMU-112382. Formation of RNA Pol II elongation complex.
R-MMU-112387. Elongation arrest and recovery.
R-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

ChiTaRSiSsrp1. mouse.
PROiQ08943.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027067.
CleanExiMM_SSRP1.
ExpressionAtlasiQ08943. baseline and differential.
GenevisibleiQ08943. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q08943
Secondary accession number(s): Q3U9Z2
, Q3UJ75, Q4V9U4, Q8CGA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 11, 2006
Last modified: November 30, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.