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Protein

Peptidyl-prolyl cis-trans isomerase-like 2

Gene

Ppil2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in transport to the cell membrane of BSG for instance. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation.By similarity

Catalytic activityi

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

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ligase, Rotamase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-210991. Basigin interactions.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase-like 2Curated (EC:5.2.1.8By similarity, EC:6.3.2.-By similarity)
Short name:
PPIase
Alternative name(s):
CYC41 Publication
Cyclophilin-60Curated
Cyclophilin-like protein Cyp-60Curated
Rotamase PPIL2Curated
Gene namesi
Name:Ppil2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:2447857. Ppil2.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Peptidyl-prolyl cis-trans isomerase-like 2PRO_0000064172Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei483 – 4831N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D787.
MaxQBiQ9D787.
PaxDbiQ9D787.
PeptideAtlasiQ9D787.
PRIDEiQ9D787.

PTM databases

iPTMnetiQ9D787.
PhosphoSiteiQ9D787.

Expressioni

Gene expression databases

BgeeiQ9D787.
CleanExiMM_PPIL2.
ExpressionAtlasiQ9D787. baseline and differential.
GenevisibleiQ9D787. MM.

Interactioni

Subunit structurei

Interacts with BSG. Interacts (via the PPIase cyclophilin-type domain) with CRNKL1; they may form a trimeric complex with HSP90.By similarity1 Publication

Protein-protein interaction databases

BioGridi211180. 1 interaction.
STRINGi10090.ENSMUSP00000023455.

Structurei

3D structure databases

ProteinModelPortaliQ9D787.
SMRiQ9D787. Positions 41-93, 277-458.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0883. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000177172.
HOVERGENiHBG053655.
InParanoidiQ9D787.
KOiK10598.
OMAiFEYPVCT.
OrthoDBiEOG769ZKZ.
PhylomeDBiQ9D787.
TreeFamiTF300854.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 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]

Sequencei

Sequence statusi: Complete.

Q9D787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKRQHQKDK MYITCAEYTH FYGGRKPDIS QTSFRRLPFD HCSLSLQPFV
60 70 80 90 100
YPVCTPEGVV FDLLNIVPWL KKYGTNPSTG EKLDGKSLIK LNFAKNSEGQ
110 120 130 140 150
YHCPVLYSVF TDNTHIVAIR TTGNVYTYEA VEQLNIKAKN LRDLLTDEPF
160 170 180 190 200
SRQDIITLQD PTNLDKFNVS NFFHVKNNMR IIDPDEEKAK QDPSYYLKNT
210 220 230 240 250
NSETRETLQE LYKEFKGDEI LAATMRPPEK KKVDQLNAAH YSTGKVSASF
260 270 280 290 300
TSTAMVPETT HEAAVIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT
310 320 330 340 350
PKTCENFIKL CKKQYYDGTI FHRSIRNFVI QGGDPTGTGT GGESFWGKPF
360 370 380 390 400
KDEFRPNLSH TGRGVLSMAN SGPNTNKSQF FITFRSCAYL DKKHTIFGRV
410 420 430 440 450
VGGFDTLTAM ENVESDPKTD RPKEEVLICT TTVFVDPYEE ADAQIAQERK
460 470 480 490 500
KTQHQVDPEA KVKMSQPQPG NQGPQTYRQG VGKYIHPAAT KRSAEEEPST
510 520
STATPTAKKR PSRGFGDFSS W
Length:521
Mass (Da):59,065
Last modified:October 10, 2002 - v2
Checksum:i9FFC202E7B4B9E7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721K → T in BAB26301 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009460 mRNA. Translation: BAB26301.1.
AK090052 mRNA. Translation: BAC41068.1.
AK161596 mRNA. Translation: BAE36483.1.
BC028899 mRNA. Translation: AAH28899.1.
CCDSiCCDS27993.1.
RefSeqiNP_001239373.1. NM_001252444.1.
NP_001239374.1. NM_001252445.1.
NP_659203.1. NM_144954.3.
UniGeneiMm.253614.
Mm.489721.

Genome annotation databases

EnsembliENSMUST00000023455; ENSMUSP00000023455; ENSMUSG00000022771.
ENSMUST00000115721; ENSMUSP00000111386; ENSMUSG00000022771.
ENSMUST00000164458; ENSMUSP00000131422; ENSMUSG00000022771.
GeneIDi66053.
KEGGimmu:66053.
UCSCiuc007yjx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009460 mRNA. Translation: BAB26301.1.
AK090052 mRNA. Translation: BAC41068.1.
AK161596 mRNA. Translation: BAE36483.1.
BC028899 mRNA. Translation: AAH28899.1.
CCDSiCCDS27993.1.
RefSeqiNP_001239373.1. NM_001252444.1.
NP_001239374.1. NM_001252445.1.
NP_659203.1. NM_144954.3.
UniGeneiMm.253614.
Mm.489721.

3D structure databases

ProteinModelPortaliQ9D787.
SMRiQ9D787. Positions 41-93, 277-458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211180. 1 interaction.
STRINGi10090.ENSMUSP00000023455.

PTM databases

iPTMnetiQ9D787.
PhosphoSiteiQ9D787.

Proteomic databases

EPDiQ9D787.
MaxQBiQ9D787.
PaxDbiQ9D787.
PeptideAtlasiQ9D787.
PRIDEiQ9D787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023455; ENSMUSP00000023455; ENSMUSG00000022771.
ENSMUST00000115721; ENSMUSP00000111386; ENSMUSG00000022771.
ENSMUST00000164458; ENSMUSP00000131422; ENSMUSG00000022771.
GeneIDi66053.
KEGGimmu:66053.
UCSCiuc007yjx.2. mouse.

Organism-specific databases

CTDi23759.
MGIiMGI:2447857. Ppil2.

Phylogenomic databases

eggNOGiKOG0883. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000177172.
HOVERGENiHBG053655.
InParanoidiQ9D787.
KOiK10598.
OMAiFEYPVCT.
OrthoDBiEOG769ZKZ.
PhylomeDBiQ9D787.
TreeFamiTF300854.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-210991. Basigin interactions.

Miscellaneous databases

PROiQ9D787.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D787.
CleanExiMM_PPIL2.
ExpressionAtlasiQ9D787. baseline and differential.
GenevisibleiQ9D787. MM.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Tongue.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  3. "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones."
    Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.
    Genes Cells 9:533-548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRNKL1 AND HSP90.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiPPIL2_MOUSE
AccessioniPrimary (citable) accession number: Q9D787
Secondary accession number(s): Q542A2, Q9CZL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: July 6, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.