Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q08943 (SSRP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ssrp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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 gammaof p63/TP63. Interacts with FYTTD1/UIF, SRF and NEK9 By similarity. Interacts with MYOG (via C-terminal region). Ref.8

Subcellular location

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

Post-translational modification

Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity By similarity.

Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein By similarity.

Sumoylated By similarity.

Disruption phenotype

Embryos die soon after implantation while preimplantation blastocysts are defective for cell outgrowth. Ref.4

Sequence similarities

Belongs to the SSRP1 family.

Contains 1 HMG box DNA-binding domain.

Sequence caution

The sequence AAH42502.1 differs from that shown. Reason: Frameshift at position 697.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08943-1)

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.
Isoform 2 (identifier: Q08943-2)

The sequence of this isoform differs from the canonical sequence as follows:
     621-621: S → SSKRDK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 708707FACT complex subunit SSRP1
PRO_0000048607

Regions

DNA binding547 – 61569HMG box
Compositional bias439 – 49658Asp/Glu-rich (acidic)
Compositional bias497 – 51115Ser-rich
Compositional bias512 – 53423Arg/Lys-rich (basic)
Compositional bias623 – 64018Arg/Lys-rich (basic)
Compositional bias641 – 70868Ser-rich

Sites

Site450 – 4512Cleavage; by caspase-3 and/or caspase-7 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1701Phosphothreonine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue4131N6-acetyllysine By similarity
Modified residue4441Phosphoserine Ref.5 Ref.6 Ref.7
Modified residue5101Phosphoserine; by CK2 By similarity
Modified residue5421N6-acetyllysine Ref.9
Modified residue6571Phosphoserine; by CK2 By similarity
Modified residue6591Phosphoserine By similarity
Modified residue6671Phosphoserine By similarity
Modified residue6681Phosphoserine By similarity
Modified residue6711Phosphoserine By similarity
Modified residue6721Phosphoserine By similarity
Modified residue6731Phosphoserine By similarity
Modified residue6881Phosphoserine; by CK2 By similarity

Natural variations

Alternative sequence6211S → SSKRDK in isoform 2.
VSP_019626

Experimental info

Sequence conflict27 – 282RQ → PS in AAB19500. Ref.1
Sequence conflict541R → P in AAB19500. Ref.1
Sequence conflict138 – 1447QCTTGKN → SVPQARI in AAB19500. Ref.1
Sequence conflict1561A → P in AAB19500. Ref.1
Sequence conflict589 – 5902SK → HE in AAH96682. Ref.3
Sequence conflict6041R → S in AAH96682. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: 8259C1A6E9899843

FASTA70880,860
        10         20         30         40         50         60 
MAETLEFNDI FQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE GIWRRVALGH 

        70         80         90        100        110        120 
GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK DLCVKGWNWG TVKFGGQLLS 

       130        140        150        160        170        180 
FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA 

       190        200        210        220        230        240 
FAQNVLSKAD VIQATGDAIC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL 

       250        260        270        280        290        300 
RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG 

       310        320        330        340        350        360 
RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG LLYPLERGFI 

       370        380        390        400        410        420 
YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ YTFSSIEREE YGKLFDFVNA 

       430        440        450        460        470        480 
KKLNIKNRGL KEGINPGYDD YADSDEDQHD AYLERMKEEG KIREENANDS SDDSGEETDE 

       490        500        510        520        530        540 
SFNPGEEEED VAEEFDSNAS ASSSSNEGDS DREEKKREQL KRAKMAKDRK SRRKSSEAKK 

       550        560        570        580        590        600 
GKDPNAPKRP MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA 

       610        620        630        640        650        660 
EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKMEKK STPSRGSSSK SSSRQLSDSF 

       670        680        690        700 
KSKEFVSSDE SSSGENKSKK KRRRSEDSEE ELASTPPSSE DSASGSDE 

« Hide

Isoform 2 [UniParc].

Checksum: 4216D673573637ED
Show »

FASTA71381,475

References

« Hide 'large scale' references
[1]"HMG1-related DNA-binding protein isolated with V-(D)-J recombination signal probes."
Shirakata M., Hueppi K., Usada S., Okazaki K., Yoshida K., Sakano H.
Mol. Cell. Biol. 11:4528-4536(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: B-cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow, Heart, Liver, Stomach and Visual cortex.
[3]"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-708 (ISOFORM 1).
Strain: C57BL/6J and FVB/N-3.
Tissue: Mammary gland and Mammary tumor.
[4]"The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos."
Cao S., Bendall H., Hicks G.G., Nashabi A., Sakano H., Shinkai Y., Gariglio M., Oltz E.M., Ruley H.E.
Mol. Cell. Biol. 23:5301-5307(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[8]"Myogenin recruits the histone chaperone facilitates chromatin transcription (FACT) to promote nucleosome disassembly at muscle-specific genes."
Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.
J. Biol. Chem. 288:7676-7687(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYOG.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS38165.1. [Q08943-1]
PIRA41265.
RefSeqNP_001129553.1. NM_001136081.2. [Q08943-1]
NP_892035.2. NM_182990.4. [Q08943-1]
XP_006499133.1. XM_006499070.1. [Q08943-1]
UniGeneMm.219793.
Mm.491456.

3D structure databases

ProteinModelPortalQ08943.
SMRQ08943. Positions 1-170, 197-427, 486-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203512. 3 interactions.
IntActQ08943. 3 interactions.
MINTMINT-4135570.

PTM databases

PhosphoSiteQ08943.

Proteomic databases

MaxQBQ08943.
PaxDbQ08943.
PRIDEQ08943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077798; ENSMUSP00000076971; ENSMUSG00000027067. [Q08943-1]
ENSMUST00000168266; ENSMUSP00000127058; ENSMUSG00000027067. [Q08943-1]
GeneID20833.
KEGGmmu:20833.
UCSCuc008kju.1. mouse. [Q08943-1]

Organism-specific databases

CTD6749.
MGIMGI:107912. Ssrp1.

Phylogenomic databases

eggNOGCOG5165.
GeneTreeENSGT00560000076898.
HOGENOMHOG000180790.
HOVERGENHBG002932.
KOK09272.
OMAIIQLDGF.
OrthoDBEOG7B31MG.
PhylomeDBQ08943.
TreeFamTF315228.

Gene expression databases

ArrayExpressQ08943.
BgeeQ08943.
CleanExMM_SSRP1.
GenevestigatorQ08943.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_like_dom.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSPR00887. SSRCOGNITION.
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299579.
PROQ08943.
SOURCESearch...

Entry information

Entry nameSSRP1_MOUSE
AccessionPrimary (citable) accession number: Q08943
Secondary accession number(s): Q3U9Z2 expand/collapse secondary AC list , Q3UJ75, Q4V9U4, Q8CGA6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 11, 2006
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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