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Protein

Polymerase I and transcript release factor

Gene

PTRF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in caveolae formation and organization. Required for the sequestration of mobile caveolin into immobile caveolae. Termination of transcription by RNA polymerase I involves pausing of transcription by TTF1, and the dissociation of the transcription complex, releasing pre-rRNA and RNA polymerase I from the template. PTRF is required for dissociation of the ternary transcription complex.3 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • rRNA primary transcript binding Source: UniProtKB

GO - Biological processi

  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • termination of RNA polymerase I transcription Source: UniProtKB
  • transcription initiation from RNA polymerase I promoter Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-73863. RNA Polymerase I Transcription Termination.

Names & Taxonomyi

Protein namesi
Recommended name:
Polymerase I and transcript release factor
Alternative name(s):
Cavin-1
Gene namesi
Name:PTRFImported
ORF Names:FKSG13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9688. PTRF.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • membrane raft Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Congenital generalized lipodystrophy 4 (CGL4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by the association of congenital generalized lipodystrophy with muscular dystrophy and cardiac anomalies. Congenital generalized lipodystrophy is characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes.
See also OMIM:613327

Keywords - Diseasei

Congenital generalized lipodystrophy, Diabetes mellitus

Organism-specific databases

MalaCardsiPTRF.
MIMi613327. phenotype.
Orphaneti228429. Generalized congenital lipodystrophy with myopathy.
PharmGKBiPA34031.

Polymorphism and mutation databases

BioMutaiPTRF.
DMDMi56749614.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Polymerase I and transcript release factorPRO_0000097094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei46 – 461PhosphoserineBy similarity
Cross-linki116 – 116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei156 – 1561PhosphotyrosineBy similarity
Cross-linki161 – 161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei167 – 1671PhosphoserineCombined sources
Modified residuei169 – 1691PhosphoserineCombined sources
Modified residuei171 – 1711PhosphoserineBy similarity
Modified residuei175 – 1751PhosphoserineBy similarity
Modified residuei202 – 2021PhosphoserineCombined sources
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei300 – 3001PhosphoserineCombined sources
Modified residuei302 – 3021PhosphothreonineCombined sources
Modified residuei308 – 3081PhosphotyrosineBy similarity
Modified residuei365 – 3651PhosphoserineCombined sources1 Publication
Modified residuei366 – 3661PhosphoserineCombined sources1 Publication
Modified residuei379 – 3791PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity (By similarity).By similarity
Five truncated forms are found in the caveolae. These are thought to be the result of proteolysis and may be phosphorylation-dependent.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6NZI2.
MaxQBiQ6NZI2.
PaxDbiQ6NZI2.
PeptideAtlasiQ6NZI2.
PRIDEiQ6NZI2.

PTM databases

iPTMnetiQ6NZI2.
PhosphoSiteiQ6NZI2.
SwissPalmiQ6NZI2.

Expressioni

Gene expression databases

BgeeiQ6NZI2.
CleanExiHS_PTRF.
GenevisibleiQ6NZI2. HS.

Organism-specific databases

HPAiHPA049838.

Interactioni

Subunit structurei

Interacts with RNA polymerase I and TTF1. Binds the 3' end of pre-rRNA. Interacts with transcription factor ZNF148 (By similarity). Interacts with LIPE in the adipocyte cytoplasm.By similarity1 Publication

Protein-protein interaction databases

BioGridi129767. 79 interactions.
DIPiDIP-48550N.
IntActiQ6NZI2. 31 interactions.
MINTiMINT-5005227.
STRINGi9606.ENSP00000349541.

Structurei

3D structure databases

ProteinModelPortaliQ6NZI2.
SMRiQ6NZI2. Positions 44-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili199 – 28284Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the PTRF/SDPR family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IV8W. Eukaryota.
ENOG410XT47. LUCA.
GeneTreeiENSGT00530000063058.
HOVERGENiHBG056807.
InParanoidiQ6NZI2.
KOiK19387.
OMAiHTIYARS.
OrthoDBiEOG708W02.
PhylomeDBiQ6NZI2.
TreeFamiTF331031.

Family and domain databases

InterProiIPR026752. Cavin_fam.
IPR033297. PTRF.
[Graphical view]
PANTHERiPTHR15240. PTHR15240. 2 hits.
PTHR15240:SF3. PTHR15240:SF3. 2 hits.
PfamiPF15237. PTRF_SDPR. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1Curated (identifier: Q6NZI2-1) [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
MEDPTLYIVE RPLPGYPDAE APEPSSAGAQ AAEEPSGAGS EELIKSDQVN
60 70 80 90 100
GVLVLSLLDK IIGAVDQIQL TQAQLEERQA EMEGAVQSIQ GELSKLGKAH
110 120 130 140 150
ATTSNTVSKL LEKVRKVSVN VKTVRGSLER QAGQIKKLEV NEAELLRRRN
160 170 180 190 200
FKVMIYQDEV KLPAKLSISK SLKESEALPE KEGEELGEGE RPEEDAAALE
210 220 230 240 250
LSSDEAVEVE EVIEESRAER IKRSGLRRVD DFKKAFSKEK MEKTKVRTRE
260 270 280 290 300
NLEKTRLKTK ENLEKTRHTL EKRMNKLGTR LVPAERREKL KTSRDKLRKS
310 320 330 340 350
FTPDHVVYAR SKTAVYKVPP FTFHVKKIRE GQVEVLKATE MVEVGADDDE
360 370 380 390
GGAERGEAGD LRRGSSPDVH ALLEITEESD AVLVDKSDSD
Length:390
Mass (Da):43,476
Last modified:July 5, 2004 - v1
Checksum:iE37945A9C9E819D4
GO
Isoform 2Curated (identifier: Q6NZI2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-185: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:300
Mass (Da):33,362
Checksum:i5C2646922C2ACD9F
GO
Isoform 3Curated (identifier: Q6NZI2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-193: MEDPTLYIVE...EELGEGERPE → M

Note: No experimental confirmation available.Curated
Show »
Length:198
Mass (Da):22,597
Checksum:i4822DAA1E67049D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471D → V AA sequence (PubMed:15242332).Curated
Sequence conflicti213 – 2131I → L AA sequence (PubMed:15242332).Curated
Sequence conflicti219 – 2191E → K in AAG27093 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141P → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035982
Natural varianti193 – 1931E → Q.
Corresponds to variant rs35308568 [ dbSNP | Ensembl ].
VAR_034416

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 193193MEDPT…GERPE → M in isoform 3. 1 PublicationVSP_051624Add
BLAST
Alternative sequencei96 – 18590Missing in isoform 2. 1 PublicationVSP_051625Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312393 mRNA. Translation: AAG27093.1.
AK314389 mRNA. Translation: BAG37014.1.
CH471152 Genomic DNA. Translation: EAW60828.1.
BC004295 mRNA. Translation: AAH04295.1.
BC008849 mRNA. Translation: AAH08849.1.
BC066123 mRNA. Translation: AAH66123.1.
BC073759 mRNA. Translation: AAH73759.1.
AF000421 mRNA. Translation: AAC63404.1.
CCDSiCCDS11425.1. [Q6NZI2-1]
RefSeqiNP_036364.2. NM_012232.5. [Q6NZI2-1]
UniGeneiHs.437191.

Genome annotation databases

EnsembliENST00000357037; ENSP00000349541; ENSG00000177469. [Q6NZI2-1]
GeneIDi284119.
KEGGihsa:284119.
UCSCiuc002hzo.4. human. [Q6NZI2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312393 mRNA. Translation: AAG27093.1.
AK314389 mRNA. Translation: BAG37014.1.
CH471152 Genomic DNA. Translation: EAW60828.1.
BC004295 mRNA. Translation: AAH04295.1.
BC008849 mRNA. Translation: AAH08849.1.
BC066123 mRNA. Translation: AAH66123.1.
BC073759 mRNA. Translation: AAH73759.1.
AF000421 mRNA. Translation: AAC63404.1.
CCDSiCCDS11425.1. [Q6NZI2-1]
RefSeqiNP_036364.2. NM_012232.5. [Q6NZI2-1]
UniGeneiHs.437191.

3D structure databases

ProteinModelPortaliQ6NZI2.
SMRiQ6NZI2. Positions 44-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129767. 79 interactions.
DIPiDIP-48550N.
IntActiQ6NZI2. 31 interactions.
MINTiMINT-5005227.
STRINGi9606.ENSP00000349541.

PTM databases

iPTMnetiQ6NZI2.
PhosphoSiteiQ6NZI2.
SwissPalmiQ6NZI2.

Polymorphism and mutation databases

BioMutaiPTRF.
DMDMi56749614.

Proteomic databases

EPDiQ6NZI2.
MaxQBiQ6NZI2.
PaxDbiQ6NZI2.
PeptideAtlasiQ6NZI2.
PRIDEiQ6NZI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357037; ENSP00000349541; ENSG00000177469. [Q6NZI2-1]
GeneIDi284119.
KEGGihsa:284119.
UCSCiuc002hzo.4. human. [Q6NZI2-1]

Organism-specific databases

CTDi284119.
GeneCardsiPTRF.
HGNCiHGNC:9688. PTRF.
HPAiHPA049838.
MalaCardsiPTRF.
MIMi603198. gene.
613327. phenotype.
neXtProtiNX_Q6NZI2.
Orphaneti228429. Generalized congenital lipodystrophy with myopathy.
PharmGKBiPA34031.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IV8W. Eukaryota.
ENOG410XT47. LUCA.
GeneTreeiENSGT00530000063058.
HOVERGENiHBG056807.
InParanoidiQ6NZI2.
KOiK19387.
OMAiHTIYARS.
OrthoDBiEOG708W02.
PhylomeDBiQ6NZI2.
TreeFamiTF331031.

Enzyme and pathway databases

ReactomeiR-HSA-73863. RNA Polymerase I Transcription Termination.

Miscellaneous databases

ChiTaRSiPTRF. human.
GeneWikiiPTRF.
GenomeRNAii284119.
PROiQ6NZI2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NZI2.
CleanExiHS_PTRF.
GenevisibleiQ6NZI2. HS.

Family and domain databases

InterProiIPR026752. Cavin_fam.
IPR033297. PTRF.
[Graphical view]
PANTHERiPTHR15240. PTHR15240. 2 hits.
PTHR15240:SF3. PTHR15240:SF3. 2 hits.
PfamiPF15237. PTRF_SDPR. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of FKSG13, a novel gene encoding a leucine-zipper protein."
    Wang Y.-G.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: LungImported.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: MuscleImported, PancreasImported and TestisImported.
  5. "Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes."
    Jansa P., Mason S.W., Hoffmann-Rohrer U., Grummt I.
    EMBO J. 17:2855-2864(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 187-390.
    Tissue: LungImported.
  6. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-95; 137-147; 153-165; 174-217; 299-310; 318-327; 338-355 AND 363-370 (ISOFORM 1), SUBCELLULAR LOCATION, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-36; SER-40; SER-365 AND SER-366.
    Tissue: Adipocyte1 Publication.
  7. "Association and insulin regulated translocation of hormone-sensitive lipase with PTRF."
    Aboulaich N., Oertegren U., Vener A.V., Stralfors P.
    Biochem. Biophys. Res. Commun. 350:657-661(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIPE, SUBCELLULAR LOCATION.
  8. "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.
  9. "PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function."
    Hill M.M., Bastiani M., Luetterforst R., Kirkham M., Kirkham A., Nixon S.J., Walser P., Abankwa D., Oorschot V.M., Martin S., Hancock J.F., Parton R.G.
    Cell 132:113-124(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "A critical role of cavin (polymerase I and transcript release factor) in caveolae formation and organization."
    Liu L., Pilch P.F.
    J. Biol. Chem. 283:4314-4322(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-202; SER-203; SER-300; THR-302; SER-365 AND SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy."
    Hayashi Y.K., Matsuda C., Ogawa M., Goto K., Tominaga K., Mitsuhashi S., Park Y.E., Nonaka I., Hino-Fukuyo N., Haginoya K., Sugano H., Nishino I.
    J. Clin. Invest. 119:2623-2633(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CGL4, FUNCTION.
  15. "Congenital generalized lipodystrophy, type 4 (CGL4) associated with myopathy due to novel PTRF mutations."
    Shastry S., Delgado M.R., Dirik E., Turkmen M., Agarwal A.K., Garg A.
    Am. J. Med. Genet. A 152:2245-2253(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CGL4.
  16. "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 SER-167; SER-202; SER-203; THR-302; SER-365; SER-366; SER-387 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-202; SER-203; SER-365; SER-366; SER-387 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-169; SER-202; SER-203; SER-365; SER-366; SER-379; SER-387 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-14.

Entry informationi

Entry nameiPTRF_HUMAN
AccessioniPrimary (citable) accession number: Q6NZI2
Secondary accession number(s): B2RAW7
, O00535, Q6GMY1, Q96H74, Q9BT85, Q9HAP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 127 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.