PPIG | ENSG00000138398 | NCBI 9360

Details for: PPIG

Gene ID: 9360

Symbol: PPIG

Ensembl ID: ENSG00000138398

Description: peptidylprolyl isomerase G

Associated with

Disease
(R-HSA-1643685)
Infectious disease
(R-HSA-5663205)
Metabolism of rna
(R-HSA-8953854)
Mrna splicing
(R-HSA-72172)
Mrna splicing - major pathway
(R-HSA-72163)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Sars-cov-1 activates/modulates innate immune responses
(R-HSA-9692916)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov infections
(R-HSA-9679506)
Viral infection pathways
(R-HSA-9824446)
Cyclosporin a binding
(GO:0016018)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Mitochondrion
(GO:0005739)
Nuclear matrix
(GO:0016363)
Nuclear speck
(GO:0016607)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Peptidyl-prolyl cis-trans isomerase activity
(GO:0003755)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein peptidyl-prolyl isomerization
(GO:0000413)
Rna binding
(GO:0003723)
Rna splicing
(GO:0008380)

Other Information

Proteins

Peptidyl-prolyl cis-trans isomerase G

Genular Protein ID: 2773051889

Symbol: PPIG_HUMAN

Name: Peptidyl-prolyl cis-trans isomerase G

UniProtKB Accession Codes:

Q13427 D3DPC5 D3DPC6 O00706 Q53R40 Q53SN4 Q96DG9

Database IDs:

Citations:

PubMed ID: 8973360

Title: RS cyclophilins: identification of an NK-TR1-related cyclophilin.

PubMed ID: 8973360

DOI: 10.1016/s0378-1119(96)00436-2

PubMed ID: 9153302

Title: A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II.

PubMed ID: 9153302

DOI: 10.1093/nar/25.11.2055

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 15358154

Title: Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles.

PubMed ID: 15358154

DOI: 10.1016/j.bbrc.2004.07.013

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 20676357

Title: Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.

PubMed ID: 20676357

DOI: 10.1371/journal.pbio.1000439

Sequence Information:

Length: 754
Mass: 88617
Checksum: D4884808D8060CD6
Sequence:

MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY 
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN 
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK 
SKVKKEEKKR HKSSSSSSSS SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK 
HKKEKKKRKK SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK 
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR DRFRRSETPP 
HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR VKERKITDHR NVSESPNRKN 
EKEKKVKDHK SNSKERDIRR NSEKDDKYKN KVKKRAKSKS RSKSKEKSKS KERDSKHNRN 
EEKRMRSRSK GRDHENVKEK EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR 
RAQSRSRECD ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR 
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK SSHRKENSES 
EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE LKSSMLKNKE DEKIRSSVEK 
ENQKSKGQEN DHVHEKNKKF DHESSPGTDE DKSG

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: PPIG

Associated with

Other Information

RS cyclophilins: identification of an NK-TR1-related cyclophilin. PubMed ID: 8973360

A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II. PubMed ID: 9153302

Generation and annotation of the DNA sequences of human chromosomes 2 and 4. PubMed ID: 15815621

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles. PubMed ID: 15358154

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PubMed ID: 17525332

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PubMed ID: 20676357