Q9UMS4 (PRP19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pre-mRNA-processing factor 19

Alternative name(s):
Nuclear matrix protein 200
PRP19/PSO4 homolog
Short name=hPso4
Senescence evasion factor

Gene names

Name:	PRPF19
Synonyms:	NMP200, PRP19, SNEV

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	504 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	Plays a role in DNA double-strand break (DSB) repair. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.12
Subunit structure	Homooligomer. Identified in the spliceosome C complex. Component of the PSO4 complex, composed of PRPF19, CDC5L, PLRG1. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts in the complex directly with CDC5L, PLRG1 and BCAS2. Interacts with APEX1, DNTT and PSMB4. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16
Subcellular location	Nucleus. Nucleus › nucleoplasm. Cytoplasm › cytoskeleton › spindle. Note: Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Ref.1 Ref.7 Ref.14 Ref.16
Tissue specificity	Ubiquitous. Weakly expressed in senescent cells of different tissue origins. Highly expressed in tumor cell lines. Ref.1 Ref.2 Ref.6 Ref.12
Induction	By gamma irradiation and chemical mutagens but not by UV irradiation. Ref.2
Sequence similarities	Belongs to the WD repeat PRP19 family. Contains 1 U-box domain. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	DNA damage DNA repair mRNA processing mRNA splicing
Cellular component	Cytoplasm Cytoskeleton Nucleus Spliceosome
Domain	Repeat WD repeat
Ligand	DNA-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW inner cell mass cell proliferation Inferred from electronic annotation. Source: Compara lipid biosynthetic process Inferred from electronic annotation. Source: Compara negative regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of astrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of mRNA splicing, via spliceosome Inferred from electronic annotation. Source: Compara protein polyubiquitination Inferred from direct assay PubMed 11435423. Source: MGI spliceosomal complex assembly Inferred from mutant phenotype Ref.9. Source: BHF-UCL
Cellular_component	Prp19 complex Inferred from direct assay Ref.16. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.8. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 11435423. Source: MGI lipid particle Inferred from electronic annotation. Source: Compara nuclear speck Inferred from direct assay Ref.9. Source: BHF-UCL spindle Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-ubiquitin ligase activity Inferred from direct assay PubMed 11435423. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	Chain	2 – 504	503	Pre-mRNA-processing factor 19		PRO_0000051145
Regions
	Domain	2 – 68	67	U-box
	Repeat	219 – 259	41	WD 1
	Repeat	262 – 301	40	WD 2
	Repeat	304 – 345	42	WD 3
	Repeat	348 – 387	40	WD 4
	Repeat	390 – 429	40	WD 5
	Repeat	433 – 472	40	WD 6
	Repeat	473 – 503	31	WD 7
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.4 Ref.5
	Modified residue	122	1	N6-acetyllysine Ref.15
	Modified residue	261	1	N6-acetyllysine Ref.15

Sequences

	Sequence		Length	Mass (Da)
	Q9UMS4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B34C37496E8AA032	FASTA	504	55,181
	10 20 30 40 50 60 MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE QLIDIKVAHP 70 80 90 100 110 120 IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR QELSHALYQH DAACRVIARL 130 140 150 160 170 180 TKEVTAAREA LATLKPQAGL IVPQAVPSSQ PSVVGAGEPM DLGELVGMTP EIIQKLQDKA 190 200 210 220 230 240 TVLTTERKKR GKTVPEELVK PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG 250 260 270 280 290 300 GADKNVVVFD KSSEQILATL KGHTKKVTSV VFHPSQDLVF SASPDATIRI WSVPNASCVQ 310 320 330 340 350 360 VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG CSLTCAQFHP 370 380 390 400 410 420 DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF SENGYYLATA ADDSSVKLWD 430 440 450 460 470 480 LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL ALGGTDVQIY ICKQWTEILH FTEHSGLTTG 490 500 VAFGHHAKFI ASTGMDRSLK FYSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions." Gotzmann J., Gerner C., Meissner M., Holzmann K., Grimm R., Mikulits W., Sauermann G. Exp. Cell Res. 261:166-179(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-40; 100-115; 179-187; 192-199 AND 334-342, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHROMOSOMAL LOCATION. Tissue: Cervix.
[2]	"Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase." Mahajan K.N., Mitchell B.S. Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH DNTT.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[4]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-27; 33-56; 77-93; 101-115; 193-206; 209-236; 252-261 AND 266-303, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	Bienvenut W.V. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-27; 33-56; 63-93; 101-115; 193-206; 209-261; 266-303; 344-375 AND 429-439, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[6]	"Reassembling proteins and chaperones in human nuclear matrix protein fractions." Gerner C., Holzmann K., Meissner M., Gotzmann J., Grimm R., Sauermann G. J. Cell. Biochem. 74:145-151(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-40, TISSUE SPECIFICITY. Tissue: Peripheral blood.
[7]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[9]	"SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly." Grillari J., Ajuh P., Stadler G., Loescher M., Voglauer R., Ernst W., Chusainow J., Eisenhaber F., Pokar M., Fortschegger K., Grey M., Lamond A.I., Katinger H. Nucleic Acids Res. 33:6868-6883(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[10]	"Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome." Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R., Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H., Grillari J. Biochem. J. 388:593-603(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMB4, FUNCTION.
[11]	"The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links." Zhang N., Kaur R., Lu X., Shen X., Li L., Legerski R.J. J. Biol. Chem. 280:40559-40567(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[12]	"SNEV overexpression extends the life span of human endothelial cells." Voglauer R., Chang M.W.-F., Dampier B., Wieser M., Baumann K., Sterovsky T., Schreiber M., Katinger H., Grillari J. Exp. Cell Res. 312:746-759(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process." Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G. Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APEX1, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[15]	"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-122 AND LYS-261, MASS SPECTROMETRY.
[16]	"Molecular architecture of the human Prp19/CDC5L complex." Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., Fischle W., Urlaub H., Luhrmann R. Mol. Cell. Biol. 30:2105-2119(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH CDC5L; PLRG1 AND BCAS2.
[17]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ131186 mRNA. Translation: CAB51857.1. BC008719 mRNA. Translation: AAH08719.1. BC018665 mRNA. Translation: AAH18665.1. BC018698 mRNA. Translation: AAH18698.1.
IPI	IPI00004968.
RefSeq	NP_055317.1. NM_014502.4.
UniGene	Hs.502705.
3D structure databases
ProteinModelPortal	Q9UMS4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UMS4. 12 interactions.
MINT	MINT-1454442.
STRING	9606.ENSP00000227524.
PTM databases
PhosphoSite	Q9UMS4.
Polymorphism databases
DMDM	55976619.
2D gel databases
REPRODUCTION-2DPAGE	IPI00004968.
SWISS-2DPAGE	Q9UMS4.
Proteomic databases
PaxDb	Q9UMS4.
PeptideAtlas	Q9UMS4.
PRIDE	Q9UMS4.
Protocols and materials databases
DNASU	27339.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000227524; ENSP00000227524; ENSG00000110107.
GeneID	27339.
KEGG	hsa:27339.
UCSC	uc001nqf.3. human.
Organism-specific databases
CTD	27339.
GeneCards	GC11M060658.
HGNC	HGNC:17896. PRPF19.
HPA	CAB012448.
MIM	608330. gene.
neXtProt	NX_Q9UMS4.
PharmGKB	PA134941355.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000177308.
HOVERGEN	HBG053697.
InParanoid	Q9UMS4.
KO	K10599.
OMA	QWQELKV.
OrthoDB	EOG4V6ZGG.
PhylomeDB	Q9UMS4.
Gene expression databases
ArrayExpress	Q9UMS4.
Bgee	Q9UMS4.
CleanEx	HS_PRPF19.
Genevestigator	Q9UMS4.
GermOnline	ENSG00000110107. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 1 hit. 3.30.40.10. 1 hit.
InterPro	IPR020472. G-protein_beta_WD-40_rep. IPR013915. Pre-mRNA_splic_Prp19. IPR000772. Ricin_B_lectin. IPR003613. Ubox_domain. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF08606. Prp19. 1 hit. PF04564. U-box. 1 hit. PF00400. WD40. 5 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00504. Ubox. 1 hit. SM00320. WD40. 7 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 4 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	27339.
NextBio	50404.
SOURCE	Search...

Entry information

Entry name

PRP19_HUMAN

Accession

Primary (citable) accession number: Q9UMS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 113 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.