Full text data of PPIL4
PPIL4
[Confidence: low (only semi-automatic identification from reviews)]
Peptidyl-prolyl cis-trans isomerase-like 4; PPIase; 5.2.1.8 (Cyclophilin-like protein PPIL4; Rotamase PPIL4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Peptidyl-prolyl cis-trans isomerase-like 4; PPIase; 5.2.1.8 (Cyclophilin-like protein PPIL4; Rotamase PPIL4)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8WUA2
ID PPIL4_HUMAN Reviewed; 492 AA.
AC Q8WUA2; B2RD34; Q7Z3Q5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2002, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 4;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-like protein PPIL4;
DE AltName: Full=Rotamase PPIL4;
GN Name=PPIL4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11978968;
RA Zeng L., Zhou Z., Xu J., Zhao W., Wang W., Huang Y., Cheng C., Xu M.,
RA Xie Y., Mao Y.;
RT "Molecular cloning, structure and expression of a novel nuclear RNA-
RT binding cyclophilin-like gene (PPIL4) from human fetal brain.";
RL Cytogenet. Cell Genet. 95:43-47(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- TISSUE SPECIFICITY: Abundantly expressed in kidney but has a
CC ubiquitously low expression pattern in other adult tissues.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily.
CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; AF357880; AAM63961.1; -; mRNA.
DR EMBL; AK315388; BAG37781.1; -; mRNA.
DR EMBL; BX537536; CAD97776.1; -; mRNA.
DR EMBL; AL078581; CAI19508.1; -; Genomic_DNA.
DR EMBL; AL357619; CAI19508.1; JOINED; Genomic_DNA.
DR EMBL; AL357619; CAI16471.1; -; Genomic_DNA.
DR EMBL; AL078581; CAI16471.1; JOINED; Genomic_DNA.
DR EMBL; CH471051; EAW47799.1; -; Genomic_DNA.
DR EMBL; BC020986; AAH20986.1; -; mRNA.
DR RefSeq; NP_624311.1; NM_139126.3.
DR UniGene; Hs.744238; -.
DR ProteinModelPortal; Q8WUA2; -.
DR SMR; Q8WUA2; 3-180, 238-316.
DR IntAct; Q8WUA2; 3.
DR MINT; MINT-1182736; -.
DR STRING; 9606.ENSP00000253329; -.
DR PhosphoSite; Q8WUA2; -.
DR DMDM; 74760546; -.
DR PaxDb; Q8WUA2; -.
DR PeptideAtlas; Q8WUA2; -.
DR PRIDE; Q8WUA2; -.
DR DNASU; 85313; -.
DR Ensembl; ENST00000253329; ENSP00000253329; ENSG00000131013.
DR GeneID; 85313; -.
DR KEGG; hsa:85313; -.
DR UCSC; uc003qmo.2; human.
DR CTD; 85313; -.
DR GeneCards; GC06M149867; -.
DR HGNC; HGNC:15702; PPIL4.
DR HPA; HPA031600; -.
DR MIM; 607609; gene.
DR neXtProt; NX_Q8WUA2; -.
DR PharmGKB; PA33590; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000186284; -.
DR HOVERGEN; HBG057731; -.
DR InParanoid; Q8WUA2; -.
DR KO; K12735; -.
DR OMA; HLERGTV; -.
DR OrthoDB; EOG7J446X; -.
DR PhylomeDB; Q8WUA2; -.
DR GeneWiki; PPIL4; -.
DR GenomeRNAi; 85313; -.
DR NextBio; 75805; -.
DR PRO; PR:Q8WUA2; -.
DR ArrayExpress; Q8WUA2; -.
DR Bgee; Q8WUA2; -.
DR CleanEx; HS_PPIL4; -.
DR Genevestigator; Q8WUA2; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; FALSE_NEG.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Rotamase.
FT CHAIN 1 492 Peptidyl-prolyl cis-trans isomerase-like
FT 4.
FT /FTId=PRO_0000233052.
FT DOMAIN 1 161 PPIase cyclophilin-type.
FT DOMAIN 240 318 RRM.
FT COMPBIAS 321 388 Lys-rich.
FT MOD_RES 178 178 Phosphoserine.
FT CONFLICT 389 389 T -> A (in Ref. 3; CAD97776).
SQ SEQUENCE 492 AA; 57225 MW; 6888B62802E15989 CRC64;
MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG
RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD
GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE
PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN
VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK
MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD
TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY
EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP
KKSKDKEKSK YR
//
ID PPIL4_HUMAN Reviewed; 492 AA.
AC Q8WUA2; B2RD34; Q7Z3Q5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2002, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 4;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-like protein PPIL4;
DE AltName: Full=Rotamase PPIL4;
GN Name=PPIL4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11978968;
RA Zeng L., Zhou Z., Xu J., Zhao W., Wang W., Huang Y., Cheng C., Xu M.,
RA Xie Y., Mao Y.;
RT "Molecular cloning, structure and expression of a novel nuclear RNA-
RT binding cyclophilin-like gene (PPIL4) from human fetal brain.";
RL Cytogenet. Cell Genet. 95:43-47(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- TISSUE SPECIFICITY: Abundantly expressed in kidney but has a
CC ubiquitously low expression pattern in other adult tissues.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily.
CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; AF357880; AAM63961.1; -; mRNA.
DR EMBL; AK315388; BAG37781.1; -; mRNA.
DR EMBL; BX537536; CAD97776.1; -; mRNA.
DR EMBL; AL078581; CAI19508.1; -; Genomic_DNA.
DR EMBL; AL357619; CAI19508.1; JOINED; Genomic_DNA.
DR EMBL; AL357619; CAI16471.1; -; Genomic_DNA.
DR EMBL; AL078581; CAI16471.1; JOINED; Genomic_DNA.
DR EMBL; CH471051; EAW47799.1; -; Genomic_DNA.
DR EMBL; BC020986; AAH20986.1; -; mRNA.
DR RefSeq; NP_624311.1; NM_139126.3.
DR UniGene; Hs.744238; -.
DR ProteinModelPortal; Q8WUA2; -.
DR SMR; Q8WUA2; 3-180, 238-316.
DR IntAct; Q8WUA2; 3.
DR MINT; MINT-1182736; -.
DR STRING; 9606.ENSP00000253329; -.
DR PhosphoSite; Q8WUA2; -.
DR DMDM; 74760546; -.
DR PaxDb; Q8WUA2; -.
DR PeptideAtlas; Q8WUA2; -.
DR PRIDE; Q8WUA2; -.
DR DNASU; 85313; -.
DR Ensembl; ENST00000253329; ENSP00000253329; ENSG00000131013.
DR GeneID; 85313; -.
DR KEGG; hsa:85313; -.
DR UCSC; uc003qmo.2; human.
DR CTD; 85313; -.
DR GeneCards; GC06M149867; -.
DR HGNC; HGNC:15702; PPIL4.
DR HPA; HPA031600; -.
DR MIM; 607609; gene.
DR neXtProt; NX_Q8WUA2; -.
DR PharmGKB; PA33590; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000186284; -.
DR HOVERGEN; HBG057731; -.
DR InParanoid; Q8WUA2; -.
DR KO; K12735; -.
DR OMA; HLERGTV; -.
DR OrthoDB; EOG7J446X; -.
DR PhylomeDB; Q8WUA2; -.
DR GeneWiki; PPIL4; -.
DR GenomeRNAi; 85313; -.
DR NextBio; 75805; -.
DR PRO; PR:Q8WUA2; -.
DR ArrayExpress; Q8WUA2; -.
DR Bgee; Q8WUA2; -.
DR CleanEx; HS_PPIL4; -.
DR Genevestigator; Q8WUA2; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; FALSE_NEG.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Rotamase.
FT CHAIN 1 492 Peptidyl-prolyl cis-trans isomerase-like
FT 4.
FT /FTId=PRO_0000233052.
FT DOMAIN 1 161 PPIase cyclophilin-type.
FT DOMAIN 240 318 RRM.
FT COMPBIAS 321 388 Lys-rich.
FT MOD_RES 178 178 Phosphoserine.
FT CONFLICT 389 389 T -> A (in Ref. 3; CAD97776).
SQ SEQUENCE 492 AA; 57225 MW; 6888B62802E15989 CRC64;
MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG
RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD
GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE
PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN
VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK
MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD
TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY
EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP
KKSKDKEKSK YR
//
MIM
607609
*RECORD*
*FIELD* NO
607609
*FIELD* TI
*607609 PEPTIDYL-PROLYL ISOMERASE-LIKE 4; PPIL4
*FIELD* TX
CLONING
During large-scale sequencing of a fetal brain cDNA library, Zeng et al.
read more(2001) cloned PPIL4. The deduced 492-amino acid protein has a calculated
molecular mass of about 57 kD. PPIL4 contains a conserved
peptidyl-prolyl cis-trans isomerase (PPIase) motif, an RNA recognition
motif, a pair of bipartite nuclear targeting sequences, and a
lysine-rich domain. The PPIase motif is, however, only weakly homologous
to classical cyclophilin motifs, and it lacks nearly half the residues
considered functionally essential. RT-PCR detected expression in all
tissues tested, with highest levels in adult kidney and lowest levels in
brain and skeletal muscle.
GENE STRUCTURE
By genomic sequence analysis, Zeng et al. (2001) determined that the
PPIL4 gene contains 13 exons and spans 56 kb.
MAPPING
By genomic sequence analysis and electronic PCR, Zeng et al. (2001)
mapped the PPIL4 gene to chromosome 6q24-q25.
*FIELD* RF
1. Zeng, L.; Zhou, Z.; Xu, J.; Zhao, W.; Wang, W.; Huang, Y.; Cheng,
C.; Xu, M.; Xie, Y.; Mao, Y.: Molecular cloning, structure and expression
of a novel nuclear RNA-binding cyclophilin-like gene (PPIL4) from
human fetal brain. Cytogenet. Cell Genet. 95: 43-47, 2001.
*FIELD* CD
Patricia A. Hartz: 3/7/2003
*FIELD* ED
mgross: 03/07/2003
*RECORD*
*FIELD* NO
607609
*FIELD* TI
*607609 PEPTIDYL-PROLYL ISOMERASE-LIKE 4; PPIL4
*FIELD* TX
CLONING
During large-scale sequencing of a fetal brain cDNA library, Zeng et al.
read more(2001) cloned PPIL4. The deduced 492-amino acid protein has a calculated
molecular mass of about 57 kD. PPIL4 contains a conserved
peptidyl-prolyl cis-trans isomerase (PPIase) motif, an RNA recognition
motif, a pair of bipartite nuclear targeting sequences, and a
lysine-rich domain. The PPIase motif is, however, only weakly homologous
to classical cyclophilin motifs, and it lacks nearly half the residues
considered functionally essential. RT-PCR detected expression in all
tissues tested, with highest levels in adult kidney and lowest levels in
brain and skeletal muscle.
GENE STRUCTURE
By genomic sequence analysis, Zeng et al. (2001) determined that the
PPIL4 gene contains 13 exons and spans 56 kb.
MAPPING
By genomic sequence analysis and electronic PCR, Zeng et al. (2001)
mapped the PPIL4 gene to chromosome 6q24-q25.
*FIELD* RF
1. Zeng, L.; Zhou, Z.; Xu, J.; Zhao, W.; Wang, W.; Huang, Y.; Cheng,
C.; Xu, M.; Xie, Y.; Mao, Y.: Molecular cloning, structure and expression
of a novel nuclear RNA-binding cyclophilin-like gene (PPIL4) from
human fetal brain. Cytogenet. Cell Genet. 95: 43-47, 2001.
*FIELD* CD
Patricia A. Hartz: 3/7/2003
*FIELD* ED
mgross: 03/07/2003