LOCUS       NP_004783                754 aa            linear   PRI 09-FEB-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase G [Homo sapiens].
ACCESSION   NP_004783
VERSION     NP_004783.2
DBSOURCE    REFSEQ: accession NM_004792.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Szlavicz,E., Szabo,K., Groma,G., Bata-Csorgo,Z., Pagani,F.,
            Kemeny,L. and Szell,M.
  TITLE     Splicing factors differentially expressed in psoriasis alter mRNA
            maturation of disease-associated EDA+ fibronectin
  JOURNAL   Mol Cell Biochem 436 (1-2), 189-199 (2017)
   PUBMED   28589370
  REMARK    GeneRIF: results indicate that LUC7L3, PPIG, and SFRS18 are not
            only implicated in EDA+ fibronectin formation, but also that they
            could possess multiple roles in psoriasis-associated molecular
            abnormalities.
            Erratum:[Mol Cell Biochem. 2017 Dec;436(1-2):201. doi:
            10.1007/s11010-017-3105-y.. PMID: 28770468]
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Nakamura,K., Aizawa,K., Aung,K.H., Yamauchi,J. and Tanoue,A.
  TITLE     Zebularine upregulates expression of CYP genes through inhibition
            of DNMT1 and PKR in HepG2 cells
  JOURNAL   Sci Rep 7, 41093 (2017)
   PUBMED   28112215
  REMARK    GeneRIF: The finding that zebularine upregulates CYP gene
            expression through DNMT1 and PKR modulation sheds light on the
            mechanisms controlling hepatocyte function and thus may aid in the
            development of new in-vitro systems using high-functioning
            hepatocytes
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Dubourg,B., Kamphausen,T., Weiwad,M., Jahreis,G., Feunteun,J.,
            Fischer,G. and Modjtahedi,N.
  TITLE     The human nuclear SRcyp is a cell cycle-regulated cyclophilin
  JOURNAL   J Biol Chem 279 (21), 22322-22330 (2004)
   PUBMED   15016823
  REMARK    GeneRIF: human nuclear SRcyp is a cell cycle-regulated cyclophilin
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Bourquin,J.P., Stagljar,I., Meier,P., Moosmann,P., Silke,J.,
            Baechi,T., Georgiev,O. and Schaffner,W.
  TITLE     A serine/arginine-rich nuclear matrix cyclophilin interacts with
            the C-terminal domain of RNA polymerase II
  JOURNAL   Nucleic Acids Res 25 (11), 2055-2061 (1997)
   PUBMED   9153302
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Nestel,F.P., Colwill,K., Harper,S., Pawson,T. and Anderson,S.K.
  TITLE     RS cyclophilins: identification of an NK-TR1-related cyclophilin
  JOURNAL   Gene 180 (1-2), 151-155 (1996)
   PUBMED   8973360
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG615922.1, X99717.1, CA418130.1 and AC016772.9.
            
            On Feb 17, 2004 this sequence version replaced NP_004783.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.83671.1,
                                           SRR1803617.72391.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260970.8/ ENSP00000260970.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..754
                     /product="peptidyl-prolyl cis-trans isomerase G"
                     /EC_number="5.2.1.8"
                     /note="Clk-associating RS-cyclophilin; peptidyl-prolyl
                     isomerase G (cyclophilin G); SR-related CTD-associated
                     factor 10; CASP10; SR-cyp; PPIase G; rotamase G;
                     SR-cyclophilin; CARS-cyclophilin"
                     /calculated_mol_wt=88486
     Region          8..175
                     /region_name="cyclophilin"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases. This family contains eukaryotic, bacterial and
                     archeal proteins which exhibit a peptidylprolyl cis- trans
                     isomerases activity (PPIase, Rotamase) and in addition
                     bind the immunosuppressive drug...; cl00197"
                     /db_xref="CDD:469651"
     Site            order(67,69,72..73,75,113..114,123,125,133..134,138)
                     /site_type="active"
                     /db_xref="CDD:238907"
     Region          182..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Region          <392..752
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     CDS             1..754
                     /gene="PPIG"
                     /gene_synonym="CARS-Cyp; CYP; SCAF10; SRCyp"
                     /coded_by="NM_004792.3:210..2474"
                     /db_xref="CCDS:CCDS2235.1"
                     /db_xref="GeneID:9360"
                     /db_xref="HGNC:HGNC:14650"
                     /db_xref="MIM:606093"
ORIGIN      
        1 mgikvqrprc ffdiainnqp agrvvfelfs dvcpktcenf rclctgekgt gkstqkplhy
       61 ksclfhrvvk dfmvqggdfs egngrggesi yggffedesf avkhnkefll smanrgkdtn
      121 gsqffittkp tphldghhvv fgqvisgqev vreienqktd aaskpfaevr ilscgelipk
      181 skvkkeekkr hkssssssss ssdsdsssds qsssdssdse sateekskkr kkkhrknsrk
      241 hkkekkkrkk skksassese aenleaqpqs tvrpeeippi penrflmrks ppkadekerk
      301 nrerererec nppnsqpasy qrrllvtrsg rkikgrgprr yrtpsrsrsr drfrrsetpp
      361 hwrqemqraq rmrvssgerw ikgdkselne ikenqrspvr vkerkitdhr nvsespnrkn
      421 ekekkvkdhk snskerdirr nsekddkykn kvkkraksks rskskeksks kerdskhnrn
      481 eekrmrsrsk grdhenvkek ekqsdskgkd qersrskeks kqlesksneh dhskskekdr
      541 raqsrsrecd itkgkhsyns rtrersrsrd rsrrvrsrth drdrsrskey hryreqeyrr
      601 rgrsrsrerr tppgrsrskd rrrrrrdsrs sereesqsrn kdkyrnqesk sshrkenses
      661 ekrmysksrd hnssnnsrek kadrdqspfs kikqssqdne lkssmlknke dekirssvek
      721 enqkskgqen dhvheknkkf dhesspgtde dksg
//
