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Protein

Pre-mRNA-processing factor 19

Gene

Prpf19

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: Ubiquitin-protein ligase which is a core component of several complexes mainly involved in pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex. Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries. The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair. Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response. May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA. As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process. In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:17349974). May play a role in the biogenesis of lipid droplets (PubMed:17118936). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity).By similarity2 Publications
Isoform 2: Forced expression leads to suppression of neuronal differentiation, and on the contrary to stimulation of astroglial cell differentiation in retinoic acid-primed P19 cells (PubMed:16352598).1 Publication

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, mRNA processing, mRNA splicing, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_307866. mRNA Splicing - Major Pathway.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing factor 19Curated (EC:6.3.2.-By similarity)
Alternative name(s):
Nuclear matrix protein 2001 Publication
PRP19/PSO4 homolog
Senescence evasion factor1 Publication
Gene namesi
Name:Prpf19Imported
Synonyms:Prp19, Snev1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:106247. Prpf19.

Subcellular locationi

Isoform 1 :
  • Nucleus 1 Publication
  • Nucleusnucleoplasm By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Cytoplasm By similarity
  • Lipid droplet 1 Publication

  • 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. Recruited on damaged DNA at sites of double-strand break (By similarity).By similarity
Isoform 2 :

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: MGI
  • cytoplasm Source: MGI
  • DNA replication factor A complex Source: Ensembl
  • lipid particle Source: MGI
  • membrane Source: MGI
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • Prp19 complex Source: UniProtKB
  • site of double-strand break Source: UniProtKB
  • spindle Source: UniProtKB-SubCell
  • spliceosomal complex Source: MGI
  • U2-type catalytic step 1 spliceosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Lipid droplet, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 504503Pre-mRNA-processing factor 19PRO_0000051146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei122 – 1221N6-acetyllysineBy similarity
Modified residuei179 – 1791N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-acetyllysine1 Publication
Modified residuei261 – 2611N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99KP6.
PaxDbiQ99KP6.
PRIDEiQ99KP6.

2D gel databases

REPRODUCTION-2DPAGEQ99KP6.

PTM databases

PhosphoSiteiQ99KP6.

Expressioni

Tissue specificityi

Expressed in white and brown adipose tissues, brain and to a lower extent in liver, kidney, muscle, lung and spleen (at protein level).1 Publication

Inductioni

Up-regulated in differentiating adipocytes (PubMed:17118936). Isoform 2 maximal expression level during the neural differentiation of P19 cells treated with retinoic acid (RA) is estimated to be 2.5-fold of the expression level of the untreated cells and it is detected 1-2 days after RA treatment and it decreases steeply thereafter to the basal level. Isoform 2 expression level increases steeply after 1 day of RA treatment and is estimated to be 4.2-fold of the original level at 0 hours (PubMed:16352598).2 Publications

Gene expression databases

BgeeiQ99KP6.
ExpressionAtlasiQ99KP6. baseline and differential.
GenevisibleiQ99KP6. MM.

Interactioni

Subunit structurei

Homotetramer. Component of the Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes described as PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The Prp19 complex associates with the spliceosome during its assembly and remodeling recruiting additional proteins. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it interacts with the replication protein A complex (RPA). Interacts with SETMAR; required for SETMAR recruitment to site of DNA damage. Interacts with U2AF2; the interaction is direct and recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with KNSTRN (By similarity). Interacts with PSMC5 (PubMed:17349974). Isoform 2 (via N-terminus) interacts with PPIA. Isoform 2 does not interact with CDC5L (PubMed:16352598).By similarity2 Publications

Protein-protein interaction databases

BioGridi205709. 2 interactions.
IntActiQ99KP6. 4 interactions.
MINTiMINT-1867830.
STRINGi10090.ENSMUSP00000025642.

Structurei

3D structure databases

ProteinModelPortaliQ99KP6.
SMRiQ99KP6. Positions 3-55, 195-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7372U-boxAdd
BLAST
Repeati219 – 25941WD 1Add
BLAST
Repeati262 – 30140WD 2Add
BLAST
Repeati304 – 34542WD 3Add
BLAST
Repeati348 – 38740WD 4Add
BLAST
Repeati390 – 42940WD 5Add
BLAST
Repeati433 – 47240WD 6Add
BLAST
Repeati473 – 50331WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 223156May mediate interaction with PSMC51 PublicationAdd
BLAST

Domaini

The 7 WD repeats are necessary and sufficient to support interaction with the RPA complex.By similarity

Sequence similaritiesi

Belongs to the WD repeat PRP19 family.Curated
Contains 1 U-box domain.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00790000122971.
HOGENOMiHOG000177308.
HOVERGENiHBG053697.
InParanoidiQ99KP6.
KOiK10599.
OMAiVYICKQW.
PhylomeDBiQ99KP6.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR020472. 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]
PfamiPF08606. Prp19. 1 hit.
PF04564. U-box. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00504. Ubox. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS51698. U_BOX. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99KP6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE
60 70 80 90 100
QLIDIKVAHP IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR
110 120 130 140 150
QELSHALYQH DAACRVIARL TKEVTAAREA LATLKPQAGL IVPQAVPSSQ
160 170 180 190 200
PSVVGAGEPM DLGELVGMTP EIIQKLQDKA TVLTTERKKR GKTVPEELVK
210 220 230 240 250
PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG GADKNVVVFD
260 270 280 290 300
KSTEQILATL KGHTKKVTSV VFHPSQELVF SASPDATIRI WSVPNTSCVQ
310 320 330 340 350
VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG
360 370 380 390 400
CSLTCAQFHP DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF
410 420 430 440 450
SENGYYLATA ADDSSVKLWD LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL
460 470 480 490 500
ALGGTDVQIY ICKQWTEILH FTEHSGLTTG VAFGHHAKFI ASTGMDRSLK

FYSL
Length:504
Mass (Da):55,239
Last modified:June 1, 2001 - v1
Checksum:iB2918188A0651024
GO
Isoform 2 (identifier: Q99KP6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-82: W → WGWPNSPALPQSSQWPTLSQ

Show »
Length:523
Mass (Da):57,302
Checksum:i4867008E9F3D969E
GO
Isoform 3 (identifier: Q99KP6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Note: No experimental confirmation available.
Show »
Length:419
Mass (Da):45,789
Checksum:i56AD02B0FBFB1B48
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform 3. 1 PublicationVSP_012192Add
BLAST
Alternative sequencei82 – 821W → WGWPNSPALPQSSQWPTLSQ in isoform 2. 1 Publication1 PublicationVSP_011945

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB222602 mRNA. Translation: BAE16340.1.
AF251503 mRNA. Translation: AAK49039.1.
AF386760 Genomic DNA. Translation: AAM21468.1.
AK047693 mRNA. Translation: BAC33127.1.
AK076998 mRNA. Translation: BAC36557.1.
AK088769 mRNA. Translation: BAC40560.1.
AK164681 mRNA. Translation: BAE37873.1.
BC004070 mRNA. Translation: AAH04070.1.
CCDSiCCDS57135.1. [Q99KP6-2]
RefSeqiNP_001240772.1. NM_001253843.1. [Q99KP6-2]
NP_001240773.1. NM_001253844.1. [Q99KP6-3]
NP_598890.1. NM_134129.4. [Q99KP6-1]
UniGeneiMm.491104.

Genome annotation databases

EnsembliENSMUST00000025642; ENSMUSP00000025642; ENSMUSG00000024735. [Q99KP6-1]
ENSMUST00000179297; ENSMUSP00000136858; ENSMUSG00000024735. [Q99KP6-2]
GeneIDi28000.
KEGGimmu:28000.
UCSCiuc008grf.2. mouse. [Q99KP6-1]
uc008grg.2. mouse. [Q99KP6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB222602 mRNA. Translation: BAE16340.1.
AF251503 mRNA. Translation: AAK49039.1.
AF386760 Genomic DNA. Translation: AAM21468.1.
AK047693 mRNA. Translation: BAC33127.1.
AK076998 mRNA. Translation: BAC36557.1.
AK088769 mRNA. Translation: BAC40560.1.
AK164681 mRNA. Translation: BAE37873.1.
BC004070 mRNA. Translation: AAH04070.1.
CCDSiCCDS57135.1. [Q99KP6-2]
RefSeqiNP_001240772.1. NM_001253843.1. [Q99KP6-2]
NP_001240773.1. NM_001253844.1. [Q99KP6-3]
NP_598890.1. NM_134129.4. [Q99KP6-1]
UniGeneiMm.491104.

3D structure databases

ProteinModelPortaliQ99KP6.
SMRiQ99KP6. Positions 3-55, 195-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205709. 2 interactions.
IntActiQ99KP6. 4 interactions.
MINTiMINT-1867830.
STRINGi10090.ENSMUSP00000025642.

PTM databases

PhosphoSiteiQ99KP6.

2D gel databases

REPRODUCTION-2DPAGEQ99KP6.

Proteomic databases

MaxQBiQ99KP6.
PaxDbiQ99KP6.
PRIDEiQ99KP6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025642; ENSMUSP00000025642; ENSMUSG00000024735. [Q99KP6-1]
ENSMUST00000179297; ENSMUSP00000136858; ENSMUSG00000024735. [Q99KP6-2]
GeneIDi28000.
KEGGimmu:28000.
UCSCiuc008grf.2. mouse. [Q99KP6-1]
uc008grg.2. mouse. [Q99KP6-2]

Organism-specific databases

CTDi27339.
MGIiMGI:106247. Prpf19.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00790000122971.
HOGENOMiHOG000177308.
HOVERGENiHBG053697.
InParanoidiQ99KP6.
KOiK10599.
OMAiVYICKQW.
PhylomeDBiQ99KP6.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_307866. mRNA Splicing - Major Pathway.

Miscellaneous databases

NextBioi306504.
PROiQ99KP6.
SOURCEiSearch...

Gene expression databases

BgeeiQ99KP6.
ExpressionAtlasiQ99KP6. baseline and differential.
GenevisibleiQ99KP6. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR020472. 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]
PfamiPF08606. Prp19. 1 hit.
PF04564. U-box. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00504. Ubox. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS51698. U_BOX. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Involvement of the mouse Prp19 gene in neuronal/astroglial cell fate decisions."
    Urano Y., Iiduka M., Sugiyama A., Akiyama H., Uzawa K., Matsumoto G., Kawasaki Y., Tashiro F.
    J. Biol. Chem. 281:7498-7514(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PPIA, SUBCELLULAR LOCATION, INDUCTION.
    Strain: ICRImported.
    Tissue: BrainImported.
  2. "Cloning of mSNEV, the mouse homologue of the human nuclear matrix protein NMP200."
    Grillari J., Gross S., Katinger H.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Swiss albino.
  3. Fortschegger K., Grillari J., Katinger H.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Strain: 129/SvJ.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J and NOD.
    Tissue: Corpus striatum, Stomach, Testis and Thymus.
  5. "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] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary gland.
  6. "Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome."
    Sihn C.R., Cho S.Y., Lee J.H., Lee T.R., Kim S.H.
    Biochem. Biophys. Res. Commun. 356:175-180(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSMC5.
  7. "Identification of mouse Prp19p as a lipid droplet-associated protein and its possible involvement in the biogenesis of lipid droplets."
    Cho S.Y., Shin E.S., Park P.J., Shin D.W., Chang H.K., Kim D., Lee H.H., Lee J.H., Kim S.H., Song M.J., Chang I.S., Lee O.S., Lee T.R.
    J. Biol. Chem. 282:2456-2465(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPRP19_MOUSE
AccessioniPrimary (citable) accession number: Q99KP6
Secondary accession number(s): Q3TP64
, Q4ADG5, Q8BKZ5, Q8BVQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.