Q08945 (SSRP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SSRP1
Synonyms:	FACT80

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	709 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	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. Ref.7 Ref.10 Ref.11 Ref.13 Ref.16 Ref.25
Subcellular location	Nucleus. Nucleus › nucleolus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.7 Ref.31
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 process	DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of viral transcription Traceable author statement. Source: Reactome regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproductive process Traceable author statement. Source: Reactome
Cellular_component	chromosome 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
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc chromatin binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 709	708	FACT complex subunit SSRP1		PRO_0000048606
Regions
	DNA binding	547 – 615	69	HMG box
	Compositional bias	439 – 496	58	Asp/Glu-rich (acidic)
	Compositional bias	497 – 511	15	Ser-rich
	Compositional bias	512 – 534	23	Arg/Lys-rich (basic)
	Compositional bias	623 – 640	18	Arg/Lys-rich (basic)
	Compositional bias	641 – 709	69	Ser-rich
Sites
	Site	450 – 451	2	Cleavage; by caspase-3 and/or caspase-7
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3
	Modified residue	170	1	Phosphothreonine Ref.23 Ref.28
	Modified residue	233	1	N6-acetyllysine Ref.27
	Modified residue	413	1	N6-acetyllysine Ref.27
	Modified residue	437	1	Phosphoserine Ref.23
	Modified residue	441	1	Phosphotyrosine By similarity
	Modified residue	444	1	Phosphoserine Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.30
	Modified residue	510	1	Phosphoserine; by CK2 Probable
	Modified residue	657	1	Phosphoserine Ref.18 Ref.30
	Modified residue	659	1	Phosphoserine Ref.30
	Modified residue	667	1	Phosphoserine Ref.23 Ref.30
	Modified residue	668	1	Phosphoserine Ref.23 Ref.30
	Modified residue	671	1	Phosphoserine Ref.23 Ref.30
	Modified residue	672	1	Phosphoserine Ref.23
	Modified residue	673	1	Phosphoserine Ref.23
	Modified residue	688	1	Phosphoserine; by CK2 Probable
Natural variations
	Natural variant	225	1	L → V. Corresponds to variant rs768436 [ dbSNP | Ensembl ].		VAR_052495
	Natural variant	458	1	E → Q. Corresponds to variant rs11540304 [ dbSNP | Ensembl ].		VAR_052496
Experimental info
	Mutagenesis	450	1	D → A: Abolishes cleavage by caspase. Ref.21
	Mutagenesis	510	1	S → A: Unable to bind DNA; when associated with A-657 and A-688. Ref.18
	Mutagenesis	657	1	S → 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
	Mutagenesis	688	1	S → 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

Sequences

	Sequence		Length	Mass (Da)
	Q08945 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 4E7EE3735EB41082	FASTA	709	81,075
	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

References

	« Hide 'large scale' referencesShow '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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[25]	"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.
[26]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"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, MASS SPECTROMETRY.
[28]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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].
[30]	"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, MASS SPECTROMETRY.
[31]	"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].
+	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.
IPI	IPI00005154.
PIR	A41976.
RefSeq	NP_003137.1. NM_003146.2.
UniGene	Hs.523680.
3D structure databases
ProteinModelPortal	Q08945.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-169N.
IntAct	Q08945. 12 interactions.
MINT	MINT-5004485.
STRING	9606.ENSP00000278412.
PTM databases
PhosphoSite	Q08945.
Polymorphism databases
DMDM	730840.
Proteomic databases
PaxDb	Q08945.
PeptideAtlas	Q08945.
PRIDE	Q08945.
Protocols and materials databases
DNASU	6749.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278412; ENSP00000278412; ENSG00000149136.
GeneID	6749.
KEGG	hsa:6749.
UCSC	uc001njt.3. human.
Organism-specific databases
CTD	6749.
GeneCards	GC11M057093.
HGNC	HGNC:11327. SSRP1.
HPA	HPA002697.
MIM	604328. gene.
neXtProt	NX_Q08945.
PharmGKB	PA36151.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5165.
HOGENOM	HOG000180790.
HOVERGEN	HBG002932.
InParanoid	Q08945.
KO	K09272.
OMA	PVEVKKG.
OrthoDB	EOG41VK2K.
PhylomeDB	Q08945.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_1788. Transcription. REACT_1892. Elongation arrest and recovery. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q08945.
Bgee	Q08945.
CleanEx	HS_SSRP1.
Genevestigator	Q08945.
GermOnline	ENSG00000149136. Homo sapiens.
Family and domain databases
Gene3D	1.10.30.10. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR013719. DUF1747. IPR009071. HMG_box_dom. IPR011993. PH_like_dom. IPR000969. SSrcognition. IPR024954. SSRP1_dom. [Graphical view]
Pfam	PF00505. HMG_box. 1 hit. PF08512. Rtt106. 1 hit. PF03531. SSrecog. 1 hit. [Graphical view]
PRINTS	PR00887. SSRCOGNITION.
SMART	SM00398. HMG. 1 hit. [Graphical view]
SUPFAM	SSF47095. HMG-box. 1 hit.
PROSITE	PS50118. HMG_BOX_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SSRP1. human.
GenomeRNAi	6749.
NextBio	26328.
PMAP-CutDB	Q08945.
SOURCE	Search...

Entry information

Entry name

SSRP1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.