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Peptidyl-prolyl cis-trans isomerase-like 2 (PPIase) (EC 2.3.2.27) (EC 5.2.1.8) (CYC4) (Cyclophilin-60) (Cyclophilin-like protein Cyp-60) (Cyp60) (hCyP-60) (RING-type E3 ubiquitin transferase isomerase-like 2) (Rotamase PPIL2)

 PPIL2_HUMAN             Reviewed;         520 AA.
Q13356; Q13357; Q8TAH2; Q9BWR8;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 164.
RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000305};
Short=PPIase {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752, ECO:0000303|PubMed:8660300};
AltName: Full=CYC4 {ECO:0000303|PubMed:11435423};
AltName: Full=Cyclophilin-60 {ECO:0000303|PubMed:8660300};
Short=Cyclophilin-like protein Cyp-60 {ECO:0000303|PubMed:8660300};
Short=Cyp60 {ECO:0000303|PubMed:8660300};
Short=hCyP-60 {ECO:0000303|PubMed:8660300};
AltName: Full=RING-type E3 ubiquitin transferase isomerase-like 2 {ECO:0000305};
AltName: Full=Rotamase PPIL2 {ECO:0000305};
Name=PPIL2 {ECO:0000312|HGNC:HGNC:9261};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Lymphocyte;
PubMed=8660300; DOI=10.1042/bj3140313;
Wang B.B., Hayenga K.J., Payan D.G., Fisher J.M.;
"Identification of a nuclear-specific cyclophilin which interacts with
the proteinase inhibitor eglin c.";
Biochem. J. 314:313-319(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hippocampus, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=11435423; DOI=10.1074/jbc.M102755200;
Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
"U box proteins as a new family of ubiquitin-protein ligases.";
J. Biol. Chem. 276:33111-33120(2001).
[5]
INTERACTION WITH CRNKL1 AND HSP90.
PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
"Interaction of U-box-type ubiquitin-protein ligases (E3s) with
molecular chaperones.";
Genes Cells 9:533-548(2004).
[6]
FUNCTION, INTERACTION WITH BSG, AND SUBCELLULAR LOCATION.
PubMed=15946952; DOI=10.1074/jbc.M503770200;
Pushkarsky T., Yurchenko V., Vanpouille C., Brichacek B., Vaisman I.,
Hatakeyama S., Nakayama K.I., Sherry B., Bukrinsky M.I.;
"Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin
60.";
J. Biol. Chem. 280:27866-27871(2005).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[11]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457.
Structural genomics consortium (SGC);
"Crystal structure of the human peptidylprolyl isomerase-like 2
isoform B.";
Submitted (JAN-2006) to the PDB data bank.
-!- FUNCTION: May catalyze the cis-trans isomerization of proline
imidic peptide bonds in oligopeptides thereby assisting the
folding of proteins (By similarity). May also function as a
chaperone, playing a role in transport to the cell membrane of BSG
for instance (PubMed:15946952). May also have a protein ubiquitin
ligase activity acting as an E3 ubiquitin protein ligase or as an
ubiquitin-ubiquitin ligase promoting elongation of ubiquitin
chains on substrates. By mediating 'Lys-48'-linked
polyubiquitination of proteins could target them for proteasomal
degradation (PubMed:11435423). {ECO:0000250|UniProtKB:Q08752,
ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:15946952,
ECO:0000303|PubMed:8660300}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000250|UniProtKB:Q08752,
ECO:0000303|PubMed:8660300}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:11435423}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:11435423}.
-!- SUBUNIT: Interacts with BSG. Interacts (via the PPIase
cyclophilin-type domain) with CRNKL1; they may form a trimeric
complex with HSP90. {ECO:0000269|PubMed:15189447,
ECO:0000269|PubMed:15946952}.
-!- INTERACTION:
P36406:TRIM23; NbExp=3; IntAct=EBI-7705988, EBI-740098;
Q96NB3:ZNF830; NbExp=2; IntAct=EBI-7705988, EBI-3920997;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11435423,
ECO:0000269|PubMed:8660300}. Note=May also localize to the
cytoplasm and the cell membrane. {ECO:0000269|PubMed:15946952}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13356-1; Sequence=Displayed;
Name=2;
IsoId=Q13356-2; Sequence=VSP_005182;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:8660300}.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
subfamily. {ECO:0000305}.
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EMBL; U37219; AAC50376.1; -; mRNA.
EMBL; U37220; AAC50377.1; -; mRNA.
EMBL; U37221; AAC50378.1; -; mRNA.
EMBL; CR456548; CAG30434.1; -; mRNA.
EMBL; BC028385; AAH28385.1; -; mRNA.
EMBL; BC000022; AAH00022.1; -; mRNA.
CCDS; CCDS13793.1; -. [Q13356-1]
CCDS; CCDS46670.1; -. [Q13356-2]
PIR; S64705; S64705.
RefSeq; NP_001304925.1; NM_001317996.1. [Q13356-1]
RefSeq; NP_055152.1; NM_014337.3. [Q13356-1]
RefSeq; NP_680480.1; NM_148175.2. [Q13356-1]
RefSeq; NP_680481.1; NM_148176.2. [Q13356-2]
RefSeq; XP_005261505.1; XM_005261448.3. [Q13356-1]
RefSeq; XP_011528348.1; XM_011530046.2. [Q13356-1]
RefSeq; XP_011528349.1; XM_011530047.2. [Q13356-1]
UniGene; Hs.438587; -.
PDB; 1ZKC; X-ray; 1.65 A; A/B=280-457.
PDBsum; 1ZKC; -.
ProteinModelPortal; Q13356; -.
SMR; Q13356; -.
BioGrid; 117260; 32.
CORUM; Q13356; -.
IntAct; Q13356; 15.
MINT; MINT-4654541; -.
STRING; 9606.ENSP00000390427; -.
iPTMnet; Q13356; -.
PhosphoSitePlus; Q13356; -.
BioMuta; PPIL2; -.
DMDM; 23813917; -.
EPD; Q13356; -.
MaxQB; Q13356; -.
PaxDb; Q13356; -.
PeptideAtlas; Q13356; -.
PRIDE; Q13356; -.
DNASU; 23759; -.
Ensembl; ENST00000335025; ENSP00000334553; ENSG00000100023. [Q13356-1]
Ensembl; ENST00000398831; ENSP00000381812; ENSG00000100023. [Q13356-1]
Ensembl; ENST00000406385; ENSP00000384299; ENSG00000100023. [Q13356-1]
Ensembl; ENST00000626352; ENSP00000486725; ENSG00000100023. [Q13356-2]
GeneID; 23759; -.
KEGG; hsa:23759; -.
UCSC; uc002zvg.5; human. [Q13356-1]
CTD; 23759; -.
DisGeNET; 23759; -.
EuPathDB; HostDB:ENSG00000100023.17; -.
GeneCards; PPIL2; -.
HGNC; HGNC:9261; PPIL2.
HPA; HPA035344; -.
HPA; HPA055637; -.
MIM; 607588; gene.
neXtProt; NX_Q13356; -.
OpenTargets; ENSG00000100023; -.
PharmGKB; PA33588; -.
eggNOG; KOG0883; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00760000119072; -.
HOGENOM; HOG000177172; -.
HOVERGEN; HBG053655; -.
InParanoid; Q13356; -.
KO; K10598; -.
OMA; YRSCKHL; -.
OrthoDB; EOG091G05AW; -.
PhylomeDB; Q13356; -.
TreeFam; TF300854; -.
Reactome; R-HSA-210991; Basigin interactions.
UniPathway; UPA00143; -.
ChiTaRS; PPIL2; human.
EvolutionaryTrace; Q13356; -.
GeneWiki; PPIL2; -.
GenomeRNAi; 23759; -.
PRO; PR:Q13356; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100023; -.
CleanEx; HS_PPIL2; -.
ExpressionAtlas; Q13356; baseline and differential.
Genevisible; Q13356; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
Gene3D; 2.40.100.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
PRINTS; PR00153; CSAPPISMRASE.
SMART; SM00504; Ubox; 1.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
PROSITE; PS51698; U_BOX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Isomerase; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Rotamase; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 520 Peptidyl-prolyl cis-trans isomerase-like
2.
/FTId=PRO_0000064171.
DOMAIN 35 108 U-box.
DOMAIN 278 433 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
COILED 197 217 {ECO:0000255}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 482 482 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 216 216 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 490 520 KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW -> EQQRKS
PQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_005182.
CONFLICT 455 455 V -> I (in Ref. 3; AAH28385).
{ECO:0000305}.
STRAND 280 286 {ECO:0000244|PDB:1ZKC}.
STRAND 289 295 {ECO:0000244|PDB:1ZKC}.
TURN 297 299 {ECO:0000244|PDB:1ZKC}.
HELIX 301 312 {ECO:0000244|PDB:1ZKC}.
TURN 313 318 {ECO:0000244|PDB:1ZKC}.
STRAND 323 325 {ECO:0000244|PDB:1ZKC}.
TURN 326 328 {ECO:0000244|PDB:1ZKC}.
STRAND 329 332 {ECO:0000244|PDB:1ZKC}.
STRAND 337 340 {ECO:0000244|PDB:1ZKC}.
STRAND 365 368 {ECO:0000244|PDB:1ZKC}.
STRAND 380 385 {ECO:0000244|PDB:1ZKC}.
HELIX 388 390 {ECO:0000244|PDB:1ZKC}.
TURN 391 393 {ECO:0000244|PDB:1ZKC}.
STRAND 396 402 {ECO:0000244|PDB:1ZKC}.
HELIX 404 412 {ECO:0000244|PDB:1ZKC}.
TURN 417 419 {ECO:0000244|PDB:1ZKC}.
STRAND 422 424 {ECO:0000244|PDB:1ZKC}.
STRAND 427 435 {ECO:0000244|PDB:1ZKC}.
HELIX 439 455 {ECO:0000244|PDB:1ZKC}.
SEQUENCE 520 AA; 58823 MW; 3FFA51C3D82F0957 CRC64;
MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV
FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR
TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK
IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH
YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT
PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH
TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD
RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV
GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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