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Q8WUA2

- PPIL4_HUMAN

UniProt

Q8WUA2 - PPIL4_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase-like 4

Gene

PPIL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.By similarity

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase-like 4 (EC:5.2.1.8)
    Short name:
    PPIase
    Alternative name(s):
    Cyclophilin-like protein PPIL4
    Rotamase PPIL4
    Gene namesi
    Name:PPIL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:15702. PPIL4.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492Peptidyl-prolyl cis-trans isomerase-like 4PRO_0000233052Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei178 – 1781Phosphoserine6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8WUA2.
    PaxDbiQ8WUA2.
    PeptideAtlasiQ8WUA2.
    PRIDEiQ8WUA2.

    PTM databases

    PhosphoSiteiQ8WUA2.

    Expressioni

    Tissue specificityi

    Abundantly expressed in kidney but has a ubiquitously low expression pattern in other adult tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ8WUA2.
    BgeeiQ8WUA2.
    CleanExiHS_PPIL4.
    GenevestigatoriQ8WUA2.

    Organism-specific databases

    HPAiHPA031600.

    Interactioni

    Protein-protein interaction databases

    BioGridi124467. 6 interactions.
    IntActiQ8WUA2. 3 interactions.
    MINTiMINT-1182736.
    STRINGi9606.ENSP00000253329.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WUA2.
    SMRiQ8WUA2. Positions 3-180, 238-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 161161PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini240 – 31879RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi321 – 38868Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000186284.
    HOVERGENiHBG057731.
    InParanoidiQ8WUA2.
    KOiK12735.
    OMAiKDVRIRH.
    OrthoDBiEOG7J446X.
    PhylomeDBiQ8WUA2.
    TreeFamiTF351865.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PRINTSiPR00153. CSAPPISMRASE.
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS50072. CSA_PPIASE_2. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8WUA2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI    50
    IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG 100
    SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP 150
    YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF 200
    KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV 250
    TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK 300
    MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV 350
    LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED 400
    YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD 450
    GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR 492
    Length:492
    Mass (Da):57,225
    Last modified:March 1, 2002 - v1
    Checksum:i6888B62802E15989
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti389 – 3891T → A in CAD97776. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF357880 mRNA. Translation: AAM63961.1.
    AK315388 mRNA. Translation: BAG37781.1.
    BX537536 mRNA. Translation: CAD97776.1.
    AL078581, AL357619 Genomic DNA. Translation: CAI19508.1.
    AL357619, AL078581 Genomic DNA. Translation: CAI16471.1.
    CH471051 Genomic DNA. Translation: EAW47799.1.
    BC020986 mRNA. Translation: AAH20986.1.
    CCDSiCCDS34550.1.
    RefSeqiNP_624311.1. NM_139126.3.
    UniGeneiHs.744238.

    Genome annotation databases

    EnsembliENST00000253329; ENSP00000253329; ENSG00000131013.
    GeneIDi85313.
    KEGGihsa:85313.
    UCSCiuc003qmo.2. human.

    Polymorphism databases

    DMDMi74760546.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF357880 mRNA. Translation: AAM63961.1 .
    AK315388 mRNA. Translation: BAG37781.1 .
    BX537536 mRNA. Translation: CAD97776.1 .
    AL078581 , AL357619 Genomic DNA. Translation: CAI19508.1 .
    AL357619 , AL078581 Genomic DNA. Translation: CAI16471.1 .
    CH471051 Genomic DNA. Translation: EAW47799.1 .
    BC020986 mRNA. Translation: AAH20986.1 .
    CCDSi CCDS34550.1.
    RefSeqi NP_624311.1. NM_139126.3.
    UniGenei Hs.744238.

    3D structure databases

    ProteinModelPortali Q8WUA2.
    SMRi Q8WUA2. Positions 3-180, 238-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124467. 6 interactions.
    IntActi Q8WUA2. 3 interactions.
    MINTi MINT-1182736.
    STRINGi 9606.ENSP00000253329.

    PTM databases

    PhosphoSitei Q8WUA2.

    Polymorphism databases

    DMDMi 74760546.

    Proteomic databases

    MaxQBi Q8WUA2.
    PaxDbi Q8WUA2.
    PeptideAtlasi Q8WUA2.
    PRIDEi Q8WUA2.

    Protocols and materials databases

    DNASUi 85313.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253329 ; ENSP00000253329 ; ENSG00000131013 .
    GeneIDi 85313.
    KEGGi hsa:85313.
    UCSCi uc003qmo.2. human.

    Organism-specific databases

    CTDi 85313.
    GeneCardsi GC06M149867.
    HGNCi HGNC:15702. PPIL4.
    HPAi HPA031600.
    MIMi 607609. gene.
    neXtProti NX_Q8WUA2.
    PharmGKBi PA33590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000186284.
    HOVERGENi HBG057731.
    InParanoidi Q8WUA2.
    KOi K12735.
    OMAi KDVRIRH.
    OrthoDBi EOG7J446X.
    PhylomeDBi Q8WUA2.
    TreeFami TF351865.

    Miscellaneous databases

    GeneWikii PPIL4.
    GenomeRNAii 85313.
    NextBioi 75805.
    PROi Q8WUA2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WUA2.
    Bgeei Q8WUA2.
    CleanExi HS_PPIL4.
    Genevestigatori Q8WUA2.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00153. CSAPPISMRASE.
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS50072. CSA_PPIASE_2. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, structure and expression of a novel nuclear RNA-binding cyclophilin-like gene (PPIL4) from human fetal brain."
      Zeng L., Zhou Z., Xu J., Zhao W., Wang W., Huang Y., Cheng C., Xu M., Xie Y., Mao Y.
      Cytogenet. Cell Genet. 95:43-47(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    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].
      Tissue: Hippocampus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Colon.
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPPIL4_HUMAN
    AccessioniPrimary (citable) accession number: Q8WUA2
    Secondary accession number(s): B2RD34, Q7Z3Q5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 115 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3