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Protein

Peptidyl-prolyl cis-trans isomerase G

Gene

PPIG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Enzyme regulationi

Cyclosporin A (CsA)-sensitive.

GO - Molecular functioni

  • cyclosporin A binding Source: ProtInc
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • protein folding Source: InterPro
  • protein peptidyl-prolyl isomerization Source: GO_Central
  • RNA splicing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase G (EC:5.2.1.8)
Short name:
PPIase G
Short name:
Peptidyl-prolyl isomerase G
Alternative name(s):
CASP10
Clk-associating RS-cyclophilin
Short name:
CARS-Cyp
Short name:
CARS-cyclophilin
Short name:
SR-cyclophilin
Short name:
SR-cyp
Short name:
SRcyp
Cyclophilin G
Rotamase G
Gene namesi
Name:PPIG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14650. PPIG.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nuclear matrix Source: UniProtKB-SubCell
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33585.

Chemistry

DrugBankiDB00172. L-Proline.

Polymorphism and mutation databases

BioMutaiPPIG.
DMDMi229462749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 754754Peptidyl-prolyl cis-trans isomerase GPRO_0000064150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei254 – 2541Phosphoserine1 Publication
Modified residuei256 – 2561Phosphoserine1 Publication
Modified residuei257 – 2571Phosphoserine1 Publication
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine1 Publication
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei356 – 3561Phosphoserine2 Publications
Modified residuei358 – 3581Phosphothreonine2 Publications
Modified residuei397 – 3971Phosphoserine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei415 – 4151Phosphoserine1 Publication
Modified residuei687 – 6871Phosphoserine4 Publications
Modified residuei690 – 6901Phosphoserine2 Publications
Modified residuei696 – 6961Phosphoserine2 Publications
Modified residuei744 – 7441Phosphoserine1 Publication
Modified residuei745 – 7451Phosphoserine1 Publication
Modified residuei748 – 7481Phosphothreonine3 Publications
Modified residuei753 – 7531Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13427.
PaxDbiQ13427.
PRIDEiQ13427.

PTM databases

PhosphoSiteiQ13427.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ13427.
CleanExiHS_PPIG.
ExpressionAtlasiQ13427. baseline and differential.
GenevisibleiQ13427. HS.

Organism-specific databases

HPAiHPA021788.
HPA057469.

Interactioni

Subunit structurei

Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BEND7Q8N7W2-23EBI-396072,EBI-10181188
CEP70Q8NHQ13EBI-396072,EBI-739624
DAB1O755533EBI-396072,EBI-7875264
DACH1Q9UI36-23EBI-396072,EBI-10186082
FHL3Q96C983EBI-396072,EBI-10229248
KCTD6Q8NC693EBI-396072,EBI-2511344
LGALS3P179313EBI-396072,EBI-1170392
LGALS3Q6NVH93EBI-396072,EBI-10187804
PCBP1Q153652EBI-396072,EBI-946095
PNMA2Q9UL423EBI-396072,EBI-302355
PPCDCQ96CD23EBI-396072,EBI-724333
RBM39Q144983EBI-396072,EBI-395290
SMN2Q166374EBI-396072,EBI-395421
TFCP2Q128003EBI-396072,EBI-717422
THAP1Q9NVV93EBI-396072,EBI-741515

Protein-protein interaction databases

BioGridi114761. 33 interactions.
IntActiQ13427. 29 interactions.
MINTiMINT-1684213.
STRINGi9606.ENSP00000260970.

Structurei

Secondary structure

1
754
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 168Combined sources
Beta strandi19 – 2810Combined sources
Turni30 – 323Combined sources
Helixi34 – 4512Combined sources
Turni46 – 483Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 583Combined sources
Beta strandi64 – 696Combined sources
Turni70 – 723Combined sources
Beta strandi73 – 764Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 854Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 1343Combined sources
Turni135 – 1373Combined sources
Beta strandi140 – 1467Combined sources
Helixi148 – 1558Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi169 – 1768Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GW2X-ray1.80A1-179[»]
2WFIX-ray0.75A1-177[»]
2WFJX-ray0.75A1-177[»]
ProteinModelPortaliQ13427.
SMRiQ13427. Positions 6-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13427.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 176166PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi180 – 19213Arg/Lys-rich (basic)Add
BLAST
Compositional biasi193 – 22533Asp/Glu/Ser-richAdd
BLAST
Compositional biasi193 – 20816Poly-SerAdd
BLAST
Compositional biasi226 – 25328Arg/Lys-rich (basic)Add
BLAST
Compositional biasi540 – 639100Arg/Ser-rich (RS domain)Add
BLAST
Compositional biasi621 – 6266Poly-Arg

Domaini

The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II.

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00550000074595.
HOVERGENiHBG048162.
InParanoidiQ13427.
KOiK09566.
OMAiHNKSKDK.
OrthoDBiEOG79GT7W.
PhylomeDBiQ13427.
TreeFamiTF318563.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13427-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT
60 70 80 90 100
GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF
110 120 130 140 150
AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV
160 170 180 190 200
VREIENQKTD AASKPFAEVR ILSCGELIPK SKVKKEEKKR HKSSSSSSSS
210 220 230 240 250
SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK HKKEKKKRKK
260 270 280 290 300
SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK
310 320 330 340 350
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR
360 370 380 390 400
DRFRRSETPP HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR
410 420 430 440 450
VKERKITDHR NVSESPNRKN EKEKKVKDHK SNSKERDIRR NSEKDDKYKN
460 470 480 490 500
KVKKRAKSKS RSKSKEKSKS KERDSKHNRN EEKRMRSRSK GRDHENVKEK
510 520 530 540 550
EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR RAQSRSRECD
560 570 580 590 600
ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR
610 620 630 640 650
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK
660 670 680 690 700
SSHRKENSES EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE
710 720 730 740 750
LKSSMLKNKE DEKIRSSVEK ENQKSKGQEN DHVHEKNKKF DHESSPGTDE

DKSG
Length:754
Mass (Da):88,617
Last modified:May 5, 2009 - v2
Checksum:iD4884808D8060CD6
GO
Isoform 2 (identifier: Q13427-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-357: RYRTPSRSRSRDRFRRSE → VGDSFPRDLHNIAFVFLK
     358-754: Missing.

Show »
Length:357
Mass (Da):40,299
Checksum:i506BC6E24E1ADD4B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti445 – 4451D → E.
Corresponds to variant rs1050354 [ dbSNP | Ensembl ].
VAR_055084
Natural varianti699 – 6991N → D.4 Publications
Corresponds to variant rs8207 [ dbSNP | Ensembl ].
VAR_055085

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei340 – 35718RYRTP…FRRSE → VGDSFPRDLHNIAFVFLK in isoform 2. 1 PublicationVSP_009662Add
BLAST
Alternative sequencei358 – 754397Missing in isoform 2. 1 PublicationVSP_009663Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40763 mRNA. Translation: AAB40347.1.
X99717 mRNA. Translation: CAA68053.1.
AC093899 Genomic DNA. Translation: AAY24119.1.
AC016772 Genomic DNA. Translation: AAY24233.1.
CH471058 Genomic DNA. Translation: EAX11267.1.
CH471058 Genomic DNA. Translation: EAX11268.1.
CH471058 Genomic DNA. Translation: EAX11269.1.
CH471058 Genomic DNA. Translation: EAX11270.1.
BC001555 mRNA. Translation: AAH01555.1.
CCDSiCCDS2235.1. [Q13427-1]
PIRiJC5314.
RefSeqiNP_004783.2. NM_004792.2. [Q13427-1]
XP_005247023.1. XM_005246966.1. [Q13427-1]
XP_005247024.1. XM_005246967.1. [Q13427-1]
UniGeneiHs.470544.
Hs.593163.

Genome annotation databases

EnsembliENST00000260970; ENSP00000260970; ENSG00000138398. [Q13427-1]
ENST00000448752; ENSP00000407083; ENSG00000138398. [Q13427-1]
ENST00000462903; ENSP00000435987; ENSG00000138398. [Q13427-2]
GeneIDi9360.
KEGGihsa:9360.
UCSCiuc002uez.3. human. [Q13427-1]
uc002ufa.3. human. [Q13427-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40763 mRNA. Translation: AAB40347.1.
X99717 mRNA. Translation: CAA68053.1.
AC093899 Genomic DNA. Translation: AAY24119.1.
AC016772 Genomic DNA. Translation: AAY24233.1.
CH471058 Genomic DNA. Translation: EAX11267.1.
CH471058 Genomic DNA. Translation: EAX11268.1.
CH471058 Genomic DNA. Translation: EAX11269.1.
CH471058 Genomic DNA. Translation: EAX11270.1.
BC001555 mRNA. Translation: AAH01555.1.
CCDSiCCDS2235.1. [Q13427-1]
PIRiJC5314.
RefSeqiNP_004783.2. NM_004792.2. [Q13427-1]
XP_005247023.1. XM_005246966.1. [Q13427-1]
XP_005247024.1. XM_005246967.1. [Q13427-1]
UniGeneiHs.470544.
Hs.593163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GW2X-ray1.80A1-179[»]
2WFIX-ray0.75A1-177[»]
2WFJX-ray0.75A1-177[»]
ProteinModelPortaliQ13427.
SMRiQ13427. Positions 6-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114761. 33 interactions.
IntActiQ13427. 29 interactions.
MINTiMINT-1684213.
STRINGi9606.ENSP00000260970.

Chemistry

DrugBankiDB00172. L-Proline.

PTM databases

PhosphoSiteiQ13427.

Polymorphism and mutation databases

BioMutaiPPIG.
DMDMi229462749.

Proteomic databases

MaxQBiQ13427.
PaxDbiQ13427.
PRIDEiQ13427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260970; ENSP00000260970; ENSG00000138398. [Q13427-1]
ENST00000448752; ENSP00000407083; ENSG00000138398. [Q13427-1]
ENST00000462903; ENSP00000435987; ENSG00000138398. [Q13427-2]
GeneIDi9360.
KEGGihsa:9360.
UCSCiuc002uez.3. human. [Q13427-1]
uc002ufa.3. human. [Q13427-2]

Organism-specific databases

CTDi9360.
GeneCardsiGC02P170404.
H-InvDBHIX0029914.
HGNCiHGNC:14650. PPIG.
HPAiHPA021788.
HPA057469.
MIMi606093. gene.
neXtProtiNX_Q13427.
PharmGKBiPA33585.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00550000074595.
HOVERGENiHBG048162.
InParanoidiQ13427.
KOiK09566.
OMAiHNKSKDK.
OrthoDBiEOG79GT7W.
PhylomeDBiQ13427.
TreeFamiTF318563.

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.

Miscellaneous databases

ChiTaRSiPPIG. human.
EvolutionaryTraceiQ13427.
GeneWikiiPPIG_(gene).
GenomeRNAii9360.
NextBioi35051.
PROiQ13427.
SOURCEiSearch...

Gene expression databases

BgeeiQ13427.
CleanExiHS_PPIG.
ExpressionAtlasiQ13427. baseline and differential.
GenevisibleiQ13427. HS.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RS cyclophilins: identification of an NK-TR1-related cyclophilin."
    Nestel F.P., Colwill K., Harper S., Pawson T., Anderson S.K.
    Gene 180:151-155(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-699.
    Tissue: T-cell.
  2. "A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II."
    Bourquin J.-P., Stagljar I., Meier P., Moosmann P., Silke J., Baechi T., Georgiev O., Schaffner W.
    Nucleic Acids Res. 25:2055-2061(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLK1 AND RNA POLYMERASE II, VARIANT ASP-699.
    Tissue: B-cell.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
  6. "Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles."
    Lin C.L., Leu S., Lu M.C., Ouyang P.
    Biochem. Biophys. Res. Commun. 321:638-647(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PNN, SUBCELLULAR LOCATION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-696, VARIANT [LARGE SCALE ANALYSIS] ASP-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-256; SER-257; SER-259; SER-397 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-415; SER-687; SER-690; SER-696; THR-748 AND SER-753, VARIANT [LARGE SCALE ANALYSIS] ASP-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358; SER-687; SER-690 AND THR-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-744; SER-745 AND THR-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPPIG_HUMAN
AccessioniPrimary (citable) accession number: Q13427
Secondary accession number(s): D3DPC5
, D3DPC6, O00706, Q53R40, Q53SN4, Q96DG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 5, 2009
Last modified: June 24, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.