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Q08945

- SSRP1_HUMAN

UniProt

Q08945 - SSRP1_HUMAN

Protein

FACT complex subunit SSRP1

Gene

SSRP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. DNA replication Source: UniProtKB-KW
    3. gene expression Source: Reactome
    4. positive regulation of viral transcription Source: Reactome
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. transcription elongation from RNA polymerase II promoter Source: Reactome
    7. transcription from RNA polymerase II promoter Source: Reactome
    8. viral process Source: Reactome

    Keywords - Biological processi

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

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. 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
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11327. SSRP1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 709708FACT complex subunit SSRP1PRO_0000048606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei170 – 1701Phosphothreonine3 Publications
    Modified residuei233 – 2331N6-acetyllysine1 Publication
    Modified residuei413 – 4131N6-acetyllysine1 Publication
    Modified residuei437 – 4371Phosphoserine2 Publications
    Modified residuei444 – 4441Phosphoserine7 Publications
    Modified residuei510 – 5101Phosphoserine; by CK22 Publications
    Modified residuei542 – 5421N6-acetyllysineBy similarity
    Modified residuei657 – 6571Phosphoserine3 Publications
    Modified residuei659 – 6591Phosphoserine2 Publications
    Modified residuei667 – 6671Phosphoserine3 Publications
    Modified residuei668 – 6681Phosphoserine3 Publications
    Modified residuei671 – 6711Phosphoserine3 Publications
    Modified residuei672 – 6721Phosphoserine2 Publications
    Modified residuei673 – 6731Phosphoserine2 Publications
    Modified residuei688 – 6881Phosphoserine; by CK22 Publications

    Post-translational modificationi

    Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity.8 Publications
    Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein.1 Publication
    Sumoylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ08945.
    PaxDbiQ08945.
    PeptideAtlasiQ08945.
    PRIDEiQ08945.

    PTM databases

    PhosphoSiteiQ08945.

    Miscellaneous databases

    PMAP-CutDBQ08945.

    Expressioni

    Gene expression databases

    ArrayExpressiQ08945.
    BgeeiQ08945.
    CleanExiHS_SSRP1.
    GenevestigatoriQ08945.

    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
    MCM4P339915EBI-353771,EBI-374938
    MCM6Q145662EBI-353771,EBI-374900
    SUPT16HQ9Y5B93EBI-353771,EBI-1046849

    Protein-protein interaction databases

    BioGridi112627. 76 interactions.
    DIPiDIP-169N.
    IntActiQ08945. 29 interactions.
    MINTiMINT-5004485.
    STRINGi9606.ENSP00000278412.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    eggNOGiCOG5165.
    HOGENOMiHOG000180790.
    HOVERGENiHBG002932.
    InParanoidiQ08945.
    KOiK09272.
    OMAiIIQLDGF.
    OrthoDBiEOG7B31MG.
    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_like_dom.
    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.
    [Graphical view]
    SUPFAMiSSF47095. SSF47095. 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

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    MAETLEFNDV YQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE    50
    GIWRRVALGH GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK 100
    DLCVKGWNWG TVKFGGQLLS FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF 150
    HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA FAQNVLSKAD VIQATGDAIC 200
    IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL RLFLLPHKDQ 250
    RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG 300
    RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG 350
    LLYPLERGFI YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ 400
    YTFSSIEREE YGKLFDFVNA KKLNIKNRGL KEGMNPSYDE YADSDEDQHD 450
    AYLERMKEEG KIREENANDS SDDSGEETDE SFNPGEEEED VAEEFDSNAS 500
    ASSSSNEGDS DRDEKKRKQL KKAKMAKDRK SRKKPVEVKK GKDPNAPKRP 550
    MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA 600
    EDARRDYEKA MKEYEGGRGE SSKRDKSKKK KKVKVKMEKK STPSRGSSSK 650
    SSSRQLSESF KSKEFVSSDE SSSGENKSKK KRRRSEDSEE EELASTPPSS 700
    EDSASGSDE 709
    Length:709
    Mass (Da):81,075
    Last modified:February 1, 1995 - v1
    Checksum:i4E7EE3735EB41082
    GO

    Sequence cautioni

    The sequence AAH91486.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86737 mRNA. Translation: AAA58660.1 .
    BC005116 mRNA. Translation: AAH05116.1 .
    BC091486 mRNA. Translation: AAH91486.1 . Sequence problems.
    CCDSi CCDS7952.1.
    PIRi A41976.
    RefSeqi NP_003137.1. NM_003146.2.
    UniGenei Hs.523680.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IFS X-ray 1.93 A 196-430 [» ]
    ProteinModelPortali Q08945.
    SMRi Q08945. Positions 1-170, 197-427, 486-616.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112627. 76 interactions.
    DIPi DIP-169N.
    IntActi Q08945. 29 interactions.
    MINTi MINT-5004485.
    STRINGi 9606.ENSP00000278412.

    PTM databases

    PhosphoSitei Q08945.

    Proteomic databases

    MaxQBi Q08945.
    PaxDbi Q08945.
    PeptideAtlasi Q08945.
    PRIDEi Q08945.

    Protocols and materials databases

    DNASUi 6749.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278412 ; ENSP00000278412 ; ENSG00000149136 .
    GeneIDi 6749.
    KEGGi hsa:6749.
    UCSCi uc001njt.3. human.

    Organism-specific databases

    CTDi 6749.
    GeneCardsi GC11M057093.
    HGNCi HGNC:11327. SSRP1.
    HPAi HPA002697.
    MIMi 604328. gene.
    neXtProti NX_Q08945.
    PharmGKBi PA36151.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5165.
    HOGENOMi HOG000180790.
    HOVERGENi HBG002932.
    InParanoidi Q08945.
    KOi K09272.
    OMAi IIQLDGF.
    OrthoDBi EOG7B31MG.
    PhylomeDBi Q08945.
    TreeFami TF315228.

    Enzyme and pathway databases

    Reactomei REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6244. Pausing and recovery of HIV elongation.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    ChiTaRSi SSRP1. human.
    GeneWikii Structure_specific_recognition_protein_1.
    GenomeRNAii 6749.
    NextBioi 26328.
    PMAP-CutDB Q08945.
    PROi Q08945.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08945.
    Bgeei Q08945.
    CleanExi HS_SSRP1.
    Genevestigatori Q08945.

    Family and domain databases

    Gene3Di 1.10.30.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR013719. DUF1747.
    IPR009071. HMG_box_dom.
    IPR011993. PH_like_dom.
    IPR000969. SSrcognition.
    IPR024954. SSRP1_dom.
    [Graphical view ]
    Pfami PF00505. HMG_box. 1 hit.
    PF08512. Rtt106. 1 hit.
    PF03531. SSrecog. 1 hit.
    [Graphical view ]
    PRINTSi PR00887. SSRCOGNITION.
    SMARTi SM00398. HMG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47095. SSF47095. 1 hit.
    PROSITEi PS50118. HMG_BOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin."
      Bruhn S.L., Pil P.M., Essigmann J.M., Housman D.E., Lippard S.J.
      Proc. Natl. Acad. Sci. U.S.A. 89:2307-2311(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: B-cell.
    2. "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].
      Tissue: Lung and Uterus.
    3. Bienvenut W.V., Vousden K.H., Lukashchuk N.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 234-241; 252-264; 305-316; 388-396 AND 414-421, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Lung carcinoma.
    4. "FACT, a factor that facilitates transcript elongation through nucleosomes."
      Orphanides G., LeRoy G., Chang C.-H., Luse D.S., Reinberg D.
      Cell 92:105-116(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "The HMG domain protein SSRP1/PREIIBF is involved in activation of the human embryonic beta-like globin gene."
      Dyer M.A., Hayes P.J., Baron M.H.
      Mol. Cell. Biol. 18:2617-2628(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Requirement of RSF and FACT for transcription of chromatin templates in vitro."
      LeRoy G., Orphanides G., Lane W.S., Reinberg D.
      Science 282:1900-1904(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins."
      Orphanides G., Wu W.-H., Lane W.S., Hampsey M., Reinberg D.
      Nature 400:284-288(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH SUPT16H.
    8. "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH."
      Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.
      Mol. Cell 5:1067-1072(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Interaction of FACT, SSRP1, and the high mobility group (HMG) domain of SSRP1 with DNA damaged by the anticancer drug cisplatin."
      Yarnell A.T., Oh S., Reinberg D., Lippard S.J.
      J. Biol. Chem. 276:25736-25741(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    10. "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."
      Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.
      Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SUPT16H; CSNK2A1; CSNK2A2 AND CSNK2B.
    11. "SSRP1 functions as a co-activator of the transcriptional activator p63."
      Zeng S.X., Dai M.-S., Keller D.M., Lu H.
      EMBO J. 21:5487-5497(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP63.
    12. Erratum
      Zeng S.X., Dai M.-S., Keller D.M., Lu H.
      EMBO J. 23:1679-1679(2004)
    13. "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex."
      Keller D.M., Lu H.
      J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUPT16H; CSNK2A1; CSNK2A2 AND CSNK2B, PHOSPHORYLATION.
    14. "High prevalence of autoantibodies against the nuclear high mobility group (HMG) protein SSRP1 in sera from patients with systemic lupus erythematosus, but not other rheumatic diseases."
      Santoro P., De Andrea M., Migliaretti G., Trapani C., Landolfo S., Gariglio M.
      J. Rheumatol. 29:90-93(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOANTIBODIES.
    15. Cited for: FUNCTION.
    16. "Nek9, a novel FACT-associated protein, modulates interphase progression."
      Tan B.C.-M., Lee S.-C.
      J. Biol. Chem. 279:9321-9330(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK9.
    17. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
      Gocke C.B., Yu H., Kang J.
      J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    18. "CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity."
      Li Y., Keller D.M., Scott J.D., Lu H.
      J. Biol. Chem. 280:11869-11875(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-510; SER-657 AND SER-688, MUTAGENESIS OF SER-510; SER-657 AND SER-688.
    19. "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II."
      Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.
      Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Coupling caspase cleavage and ubiquitin-proteasome-dependent degradation of SSRP1 during apoptosis."
      Landais I., Lee H., Lu H.
      Cell Death Differ. 13:1866-1878(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITE, UBIQUITINATION, MUTAGENESIS OF ASP-450.
    22. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-437; SER-444; SER-667; SER-668; SER-671; SER-672 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA."
      Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T., Jones R., Ponting C.P., Dickman M.J., Wilson S.A.
      Curr. Biol. 19:1918-1924(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYTTD1.
    27. "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-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    28. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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 THR-170 AND SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-657; SER-659; SER-667; SER-668 AND SER-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    34. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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: October 1, 2014
    This is version 152 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

    External Data

    Dasty 3