Skip Header

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

Q08945

- SSRP1_HUMAN

UniProt

Q08945 - SSRP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

FACT complex subunit SSRP1

Gene

SSRP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

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
Complete GO annotation...

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-KW
  2. cytoplasm Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
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.

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 – 1701Phosphothreonine2 Publications
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei413 – 4131N6-acetyllysine1 Publication
Modified residuei437 – 4371Phosphoserine1 Publication
Modified residuei444 – 4441Phosphoserine6 Publications
Modified residuei510 – 5101Phosphoserine; by CK21 Publication
Modified residuei542 – 5421N6-acetyllysineBy similarity
Modified residuei657 – 6571Phosphoserine2 Publications
Modified residuei659 – 6591Phosphoserine1 Publication
Modified residuei667 – 6671Phosphoserine2 Publications
Modified residuei668 – 6681Phosphoserine2 Publications
Modified residuei671 – 6711Phosphoserine2 Publications
Modified residuei672 – 6721Phosphoserine1 Publication
Modified residuei673 – 6731Phosphoserine1 Publication
Modified residuei688 – 6881Phosphoserine; by CK21 Publication

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

BgeeiQ08945.
CleanExiHS_SSRP1.
ExpressionAtlasiQ08945. baseline and differential.
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. 86 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 – 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

eggNOGiCOG5165.
GeneTreeiENSGT00560000076898.
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

« 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 AAH91486.1 differs from that shown. Reason: 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.
CCDSi CCDS7952.1.
PIRi A41976.
RefSeqi NP_003137.1. NM_003146.2.
UniGenei Hs.523680.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 86 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.
GeneTreei ENSGT00560000076898.
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

Bgeei Q08945.
CleanExi HS_SSRP1.
ExpressionAtlasi Q08945. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 154 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