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Q8WUA2

- PPIL4_HUMAN

UniProt

Q8WUA2 - PPIL4_HUMAN

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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

Functioni

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

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 161161PPIase cyclophilin-typeAdd
BLAST
Domaini240 – 31879RRMAdd
BLAST

Compositional bias

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti389 – 3891T → A in CAD97776. 1 Publication

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

« 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: July 9, 2014
This is version 114 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