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Q13356

- PPIL2_HUMAN

UniProt

Q13356 - PPIL2_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase-like 2

Gene

PPIL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.

    Catalytic activityi

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

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. ubiquitin-protein transferase activity Source: MGI
    4. ubiquitin-ubiquitin ligase activity Source: MGI

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. leukocyte migration Source: Reactome
    3. protein folding Source: UniProtKB-KW
    4. protein polyubiquitination Source: MGI

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    ReactomeiREACT_12560. Basigin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase-like 2 (EC:5.2.1.8)
    Short name:
    PPIase
    Alternative name(s):
    Cyclophilin-60
    Cyclophilin-like protein Cyp-60
    Rotamase PPIL2
    Gene namesi
    Name:PPIL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9261. PPIL2.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi lumen Source: Reactome
    2. nucleus Source: UniProtKB
    3. ubiquitin ligase complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33588.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 520520Peptidyl-prolyl cis-trans isomerase-like 2PRO_0000064171Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei482 – 4821N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13356.
    PaxDbiQ13356.
    PeptideAtlasiQ13356.
    PRIDEiQ13356.

    PTM databases

    PhosphoSiteiQ13356.

    Expressioni

    Tissue specificityi

    Highest expression in thymus, pancreas and testis. Also detected in heart, placenta, lung, liver, skeletal muscle, kidney, spleen, prostate, ovary, small intestine and colon. Poorly detected in brain and leukocytes. Strong protein expression in lymph node (cortical, paracortical and medullar regions), thyroid (follicular epithelial cells), testis (developing spermatozoa), stomach (cells lining the gastric pit), pancreas, kidney (proximal and distal-tubule cells and collecting duct cells but not in glomeruli), endometrium and colon (goblet cells). Moderate protein expression in spleen, prostate (epithelium and squamous cell carcinomas), placenta and adrenal gland. Weak protein expression in liver, heart, breast, ovary, and lung. No protein expression in brain and bladder. High protein expression in most lymphomas and melanomas.

    Gene expression databases

    ArrayExpressiQ13356.
    BgeeiQ13356.
    CleanExiHS_PPIL2.
    GenevestigatoriQ13356.

    Organism-specific databases

    HPAiHPA035344.
    HPA055637.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZNF830Q96NB32EBI-7705988,EBI-3920997

    Protein-protein interaction databases

    BioGridi117260. 10 interactions.
    IntActiQ13356. 2 interactions.
    MINTiMINT-4654541.
    STRINGi9606.ENSP00000390427.

    Structurei

    Secondary structure

    1
    520
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi280 – 2867
    Beta strandi289 – 2957
    Turni297 – 2993
    Helixi301 – 31212
    Turni313 – 3186
    Beta strandi323 – 3253
    Turni326 – 3283
    Beta strandi329 – 3324
    Beta strandi337 – 3404
    Beta strandi365 – 3684
    Beta strandi380 – 3856
    Helixi388 – 3903
    Turni391 – 3933
    Beta strandi396 – 4027
    Helixi404 – 4129
    Turni417 – 4193
    Beta strandi422 – 4243
    Beta strandi427 – 4359
    Helixi439 – 45517

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZKCX-ray1.65A/B280-457[»]
    ProteinModelPortaliQ13356.
    SMRiQ13356. Positions 277-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13356.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 10874U-boxAdd
    BLAST
    Domaini278 – 433156PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili197 – 21721Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
    Contains 1 U-box domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000177172.
    HOVERGENiHBG053655.
    InParanoidiQ13356.
    KOiK10598.
    OMAiCCALSFQ.
    OrthoDBiEOG769ZKZ.
    PhylomeDBiQ13356.
    TreeFamiTF300854.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR027799. Rtf2_RING-finger.
    IPR003613. Ubox_domain.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    PF04641. Rtf2. 1 hit.
    [Graphical view]
    PRINTSiPR00153. CSAPPISMRASE.
    SMARTiSM00504. Ubox. 1 hit.
    [Graphical view]
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS51698. U_BOX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13356-1) [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

    MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV    50
    YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK 100
    YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF 150
    SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT 200
    NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF 250
    TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 300
    PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF 350
    KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV 400
    VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK 450
    TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATK RAAEEEPSTS 500
    ATVPMSKKKP SRGFGDFSSW 520
    Length:520
    Mass (Da):58,823
    Last modified:November 1, 1996 - v1
    Checksum:i3FFA51C3D82F0957
    GO
    Isoform 2 (identifier: Q13356-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         490-520: KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW → EQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH

    Note: No experimental confirmation available.

    Show »
    Length:527
    Mass (Da):59,458
    Checksum:i9B494AE6D29EBAC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti455 – 4551V → I in AAH28385. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei490 – 52031KRAAE…DFSSW → EQQRKSPQPVPLSPCPRRSP VGVLGTSAPGSSRLPDDH in isoform 2. 1 PublicationVSP_005182Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37219 mRNA. Translation: AAC50376.1.
    U37220 mRNA. Translation: AAC50377.1.
    U37221 mRNA. Translation: AAC50378.1.
    CR456548 mRNA. Translation: CAG30434.1.
    BC028385 mRNA. Translation: AAH28385.1.
    BC000022 mRNA. Translation: AAH00022.1.
    CCDSiCCDS13793.1. [Q13356-1]
    CCDS46670.1. [Q13356-2]
    PIRiS64705.
    RefSeqiNP_055152.1. NM_014337.3. [Q13356-1]
    NP_680480.1. NM_148175.2. [Q13356-1]
    NP_680481.1. NM_148176.2. [Q13356-2]
    XP_005261504.1. XM_005261447.2. [Q13356-1]
    XP_005261505.1. XM_005261448.2. [Q13356-1]
    XP_006724260.1. XM_006724197.1. [Q13356-1]
    UniGeneiHs.438587.

    Genome annotation databases

    EnsembliENST00000335025; ENSP00000334553; ENSG00000100023. [Q13356-1]
    ENST00000398831; ENSP00000381812; ENSG00000100023. [Q13356-1]
    ENST00000406385; ENSP00000384299; ENSG00000100023. [Q13356-1]
    GeneIDi23759.
    KEGGihsa:23759.
    UCSCiuc002zvg.4. human. [Q13356-1]
    uc002zvh.4. human. [Q13356-2]

    Polymorphism databases

    DMDMi23813917.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37219 mRNA. Translation: AAC50376.1 .
    U37220 mRNA. Translation: AAC50377.1 .
    U37221 mRNA. Translation: AAC50378.1 .
    CR456548 mRNA. Translation: CAG30434.1 .
    BC028385 mRNA. Translation: AAH28385.1 .
    BC000022 mRNA. Translation: AAH00022.1 .
    CCDSi CCDS13793.1. [Q13356-1 ]
    CCDS46670.1. [Q13356-2 ]
    PIRi S64705.
    RefSeqi NP_055152.1. NM_014337.3. [Q13356-1 ]
    NP_680480.1. NM_148175.2. [Q13356-1 ]
    NP_680481.1. NM_148176.2. [Q13356-2 ]
    XP_005261504.1. XM_005261447.2. [Q13356-1 ]
    XP_005261505.1. XM_005261448.2. [Q13356-1 ]
    XP_006724260.1. XM_006724197.1. [Q13356-1 ]
    UniGenei Hs.438587.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZKC X-ray 1.65 A/B 280-457 [» ]
    ProteinModelPortali Q13356.
    SMRi Q13356. Positions 277-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117260. 10 interactions.
    IntActi Q13356. 2 interactions.
    MINTi MINT-4654541.
    STRINGi 9606.ENSP00000390427.

    PTM databases

    PhosphoSitei Q13356.

    Polymorphism databases

    DMDMi 23813917.

    Proteomic databases

    MaxQBi Q13356.
    PaxDbi Q13356.
    PeptideAtlasi Q13356.
    PRIDEi Q13356.

    Protocols and materials databases

    DNASUi 23759.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335025 ; ENSP00000334553 ; ENSG00000100023 . [Q13356-1 ]
    ENST00000398831 ; ENSP00000381812 ; ENSG00000100023 . [Q13356-1 ]
    ENST00000406385 ; ENSP00000384299 ; ENSG00000100023 . [Q13356-1 ]
    GeneIDi 23759.
    KEGGi hsa:23759.
    UCSCi uc002zvg.4. human. [Q13356-1 ]
    uc002zvh.4. human. [Q13356-2 ]

    Organism-specific databases

    CTDi 23759.
    GeneCardsi GC22P022006.
    HGNCi HGNC:9261. PPIL2.
    HPAi HPA035344.
    HPA055637.
    MIMi 607588. gene.
    neXtProti NX_Q13356.
    PharmGKBi PA33588.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000177172.
    HOVERGENi HBG053655.
    InParanoidi Q13356.
    KOi K10598.
    OMAi CCALSFQ.
    OrthoDBi EOG769ZKZ.
    PhylomeDBi Q13356.
    TreeFami TF300854.

    Enzyme and pathway databases

    Reactomei REACT_12560. Basigin interactions.

    Miscellaneous databases

    ChiTaRSi PPIL2. human.
    EvolutionaryTracei Q13356.
    GeneWikii PPIL2.
    GenomeRNAii 23759.
    NextBioi 46699.
    PROi Q13356.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13356.
    Bgeei Q13356.
    CleanExi HS_PPIL2.
    Genevestigatori Q13356.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR027799. Rtf2_RING-finger.
    IPR003613. Ubox_domain.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    PF04641. Rtf2. 1 hit.
    [Graphical view ]
    PRINTSi PR00153. CSAPPISMRASE.
    SMARTi SM00504. Ubox. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS51698. U_BOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c."
      Wang B.B., Hayenga K.J., Payan D.G., Fisher J.M.
      Biochem. J. 314:313-319(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Lymphocyte.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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 AND 2).
      Tissue: Hippocampus and Kidney.
    4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Crystal structure of the human peptidylprolyl isomerase-like 2 isoform B."
      Structural genomics consortium (SGC)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457.

    Entry informationi

    Entry nameiPPIL2_HUMAN
    AccessioniPrimary (citable) accession number: Q13356
    Secondary accession number(s): Q13357, Q8TAH2, Q9BWR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 134 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3