| Tag | Content |
|---|
| CPLM ID | CPLM-012092 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptidyl-prolyl cis-trans isomerase G |
Protein Synonyms/Alias | PPIase G; Peptidyl-prolyl isomerase G; CASP10; Clk-associating RS-cyclophilin; CARS-Cyp; CARS-cyclophilin; SR-cyclophilin; SR-cyp; SRcyp; Cyclophilin G; Rotamase G |
Gene Name | PPIG |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 720 | KIRSSVEKENQKSKG | acetylation | [1] | | 724 | SVEKENQKSKGQEND | acetylation | [1] |
|
Reference | [1] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] |
Functional Description | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. |
Sequence Annotation | DOMAIN 11 176 PPIase cyclophilin-type.
MOD_RES 254 254 Phosphoserine.
MOD_RES 256 256 Phosphoserine.
MOD_RES 257 257 Phosphoserine.
MOD_RES 259 259 Phosphoserine.
MOD_RES 315 315 Phosphoserine.
MOD_RES 345 345 Phosphoserine (By similarity).
MOD_RES 347 347 Phosphoserine (By similarity).
MOD_RES 356 356 Phosphoserine.
MOD_RES 358 358 Phosphothreonine.
MOD_RES 397 397 Phosphoserine.
MOD_RES 413 413 Phosphoserine.
MOD_RES 415 415 Phosphoserine.
MOD_RES 687 687 Phosphoserine.
MOD_RES 690 690 Phosphoserine.
MOD_RES 696 696 Phosphoserine.
MOD_RES 744 744 Phosphoserine (By similarity).
MOD_RES 745 745 Phosphoserine (By similarity).
MOD_RES 748 748 Phosphothreonine.
MOD_RES 753 753 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Cyclosporin; Isomerase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Rotamase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 754 AA |
Protein Sequence | MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY 60
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN 120
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK 180
SKVKKEEKKR HKSSSSSSSS SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK 240
HKKEKKKRKK SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK 300
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR DRFRRSETPP 360
HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR VKERKITDHR NVSESPNRKN 420
EKEKKVKDHK SNSKERDIRR NSEKDDKYKN KVKKRAKSKS RSKSKEKSKS KERDSKHNRN 480
EEKRMRSRSK GRDHENVKEK EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR 540
RAQSRSRECD ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR 600
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK SSHRKENSES 660
EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE LKSSMLKNKE DEKIRSSVEK 720
ENQKSKGQEN DHVHEKNKKF DHESSPGTDE DKSG 754 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:HPA. GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. GO:0005654; C:nucleoplasm; TAS:ProtInc. GO:0016018; F:cyclosporin A binding; TAS:ProtInc. GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. GO:0006457; P:protein folding; IEA:UniProtKB-KW. GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC. GO:0008380; P:RNA splicing; TAS:ProtInc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |