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Q08945 (SSRP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SSRP1
Synonyms:FACT80
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length709 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 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. Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.15 Ref.19

Subunit structure

Interacts with MYOG (via C-terminus 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 gammaof TP63. Interacts with FYTTD1/UIF, SRF and NEK9. Ref.7 Ref.10 Ref.11 Ref.13 Ref.16 Ref.26

Subcellular location

Nucleus. Nucleusnucleolus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.7 Ref.33

Domain

The HMG box DNA-binding domain mediates DNA-binding. It has both affinity and specificity for DNA damaged globally with cisplatin. Ref.9

Post-translational modification

Phosphorylated by CK2 following UV but not gamma irradiation. Phosphorylation inhibits its DNA-binding activity. Ref.13 Ref.18

Ubiquitinated. Polyubiquitinated following caspase cleavage resulting in degradation of the N-terminal ubiquitinated part of the cleaved protein. Ref.21

Sumoylated. Ref.17

Miscellaneous

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

Sequence similarities

Belongs to the SSRP1 family.

Contains 1 HMG box DNA-binding domain.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

chromatin binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 709708FACT complex subunit SSRP1
PRO_0000048606

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 – 70969Ser-rich

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.25 Ref.32 Ref.34
Modified residue1701Phosphothreonine Ref.23 Ref.29
Modified residue2331N6-acetyllysine Ref.28
Modified residue4131N6-acetyllysine Ref.28
Modified residue4371Phosphoserine Ref.23
Modified residue4441Phosphoserine Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.31
Modified residue5101Phosphoserine; by CK2 Probable
Modified residue5421N6-acetyllysine By similarity
Modified residue6571Phosphoserine Ref.18 Ref.31
Modified residue6591Phosphoserine Ref.31
Modified residue6671Phosphoserine Ref.23 Ref.31
Modified residue6681Phosphoserine Ref.23 Ref.31
Modified residue6711Phosphoserine Ref.23 Ref.31
Modified residue6721Phosphoserine Ref.23
Modified residue6731Phosphoserine Ref.23
Modified residue6881Phosphoserine; by CK2 Probable

Natural variations

Natural variant2251L → V.
Corresponds to variant rs768436 [ dbSNP | Ensembl ].
VAR_052495
Natural variant4581E → Q.
Corresponds to variant rs11540304 [ dbSNP | Ensembl ].
VAR_052496

Experimental info

Mutagenesis4501D → A: Abolishes cleavage by caspase. Ref.21
Mutagenesis5101S → A: Unable to bind DNA; when associated with A-657 and A-688. Ref.18
Mutagenesis6571S → A: Unable to bind DNA; when associated with A-510 and A-688. Still able to bind DNA; when associated with A-688. Ref.18
Mutagenesis6881S → A: Unable to bind DNA; when associated with A-510 and A-657. Still able to bind DNA; when associated with A-657. Ref.18

Secondary structure

.......................................... 709
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08945 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 4E7EE3735EB41082

FASTA70981,075
        10         20         30         40         50         60 
MAETLEFNDV YQEVKGSMND 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 KEGMNPSYDE YADSDEDQHD AYLERMKEEG KIREENANDS SDDSGEETDE 

       490        500        510        520        530        540 
SFNPGEEEED VAEEFDSNAS ASSSSNEGDS DRDEKKRKQL KKAKMAKDRK SRKKPVEVKK 

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

       610        620        630        640        650        660 
EDARRDYEKA MKEYEGGRGE SSKRDKSKKK KKVKVKMEKK STPSRGSSSK SSSRQLSESF 

       670        680        690        700 
KSKEFVSSDE SSSGENKSKK KRRRSEDSEE EELASTPPSS EDSASGSDE 

« Hide

References

« Hide 'large scale' references
[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]"FACT facilitates transcription-dependent nucleosome alteration."
Belotserkovskaya R., Oh S., Bondarenko V.A., Orphanides G., Studitsky V.M., Reinberg D.
Science 301:1090-1093(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86737 mRNA. Translation: AAA58660.1.
BC005116 mRNA. Translation: AAH05116.1.
BC091486 mRNA. Translation: AAH91486.1. Sequence problems.
PIRA41976.
RefSeqNP_003137.1. NM_003146.2.
UniGeneHs.523680.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFSX-ray1.93A196-430[»]
ProteinModelPortalQ08945.
SMRQ08945. Positions 1-170, 196-427, 486-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112627. 74 interactions.
DIPDIP-169N.
IntActQ08945. 29 interactions.
MINTMINT-5004485.
STRING9606.ENSP00000278412.

PTM databases

PhosphoSiteQ08945.

Proteomic databases

PaxDbQ08945.
PeptideAtlasQ08945.
PRIDEQ08945.

Protocols and materials databases

DNASU6749.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278412; ENSP00000278412; ENSG00000149136.
GeneID6749.
KEGGhsa:6749.
UCSCuc001njt.3. human.

Organism-specific databases

CTD6749.
GeneCardsGC11M057093.
HGNCHGNC:11327. SSRP1.
HPAHPA002697.
MIM604328. gene.
neXtProtNX_Q08945.
PharmGKBPA36151.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5165.
HOGENOMHOG000180790.
HOVERGENHBG002932.
InParanoidQ08945.
KOK09272.
OMAIIQLDGF.
OrthoDBEOG7B31MG.
PhylomeDBQ08945.
TreeFamTF315228.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ08945.
BgeeQ08945.
CleanExHS_SSRP1.
GenevestigatorQ08945.

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

ChiTaRSSSRP1. human.
GeneWikiStructure_specific_recognition_protein_1.
GenomeRNAi6749.
NextBio26328.
PMAP-CutDBQ08945.
PROQ08945.
SOURCESearch...

Entry information

Entry nameSSRP1_HUMAN
AccessionPrimary (citable) accession number: Q08945
Secondary accession number(s): Q5BJG8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM