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Protein

Peptidyl-prolyl cis-trans isomerase-like 4

Gene

PPIL4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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: GO_Central
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. protein folding Source: InterPro
  2. protein peptidyl-prolyl isomerization Source: GO_Central
  3. regulation of phosphorylation of RNA polymerase II C-terminal domain Source: GO_Central
Complete GO annotation...

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: GO_Central
Complete GO annotation...

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

BgeeiQ8WUA2.
CleanExiHS_PPIL4.
ExpressionAtlasiQ8WUA2. baseline and differential.
GenevestigatoriQ8WUA2.

Organism-specific databases

HPAiHPA031600.

Interactioni

Protein-protein interaction databases

BioGridi124467. 11 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.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000186284.
HOVERGENiHBG057731.
InParanoidiQ8WUA2.
KOiK12735.
OMAiRPPDNST.
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

        10         20         30         40         50
MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI
60 70 80 90 100
IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG
110 120 130 140 150
SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP
160 170 180 190 200
YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF
210 220 230 240 250
KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV
260 270 280 290 300
TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK
310 320 330 340 350
MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV
360 370 380 390 400
LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED
410 420 430 440 450
YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD
460 470 480 490
GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi124467. 11 interactions.
IntActiQ8WUA2. 3 interactions.
MINTiMINT-1182736.
STRINGi9606.ENSP00000253329.

PTM databases

PhosphoSiteiQ8WUA2.

Polymorphism databases

DMDMi74760546.

Proteomic databases

MaxQBiQ8WUA2.
PaxDbiQ8WUA2.
PeptideAtlasiQ8WUA2.
PRIDEiQ8WUA2.

Protocols and materials databases

DNASUi85313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi85313.
GeneCardsiGC06M149867.
HGNCiHGNC:15702. PPIL4.
HPAiHPA031600.
MIMi607609. gene.
neXtProtiNX_Q8WUA2.
PharmGKBiPA33590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000186284.
HOVERGENiHBG057731.
InParanoidiQ8WUA2.
KOiK12735.
OMAiRPPDNST.
OrthoDBiEOG7J446X.
PhylomeDBiQ8WUA2.
TreeFamiTF351865.

Miscellaneous databases

ChiTaRSiPPIL4. human.
GeneWikiiPPIL4.
GenomeRNAii85313.
NextBioi75805.
PROiQ8WUA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WUA2.
CleanExiHS_PPIL4.
ExpressionAtlasiQ8WUA2. baseline and differential.
GenevestigatoriQ8WUA2.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 119 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

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.