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Q13427

- PPIG_HUMAN

UniProt

Q13427 - PPIG_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase G

Gene

PPIG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    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

    1. cyclosporin A binding Source: ProtInc
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW
    2. RNA splicing Source: ProtInc

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Cyclosporin

    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14650. PPIG.

    Subcellular locationi

    Nucleus matrix 1 Publication. Nucleus speckle 1 Publication
    Note: Colocalizes with RNA splicing factors at nuclear speckles.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear matrix Source: UniProtKB-SubCell
    3. nuclear speck Source: UniProtKB-SubCell
    4. nucleoplasm Source: ProtInc
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33585.

    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 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 residuei748 – 7481Phosphothreonine2 Publications
    Modified residuei753 – 7531Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13427.
    PaxDbiQ13427.
    PRIDEiQ13427.

    PTM databases

    PhosphoSiteiQ13427.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ13427.
    BgeeiQ13427.
    CleanExiHS_PPIG.
    GenevestigatoriQ13427.

    Organism-specific databases

    HPAiHPA021788.

    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
    PCBP1Q153652EBI-396072,EBI-946095

    Protein-protein interaction databases

    BioGridi114761. 15 interactions.
    IntActiQ13427. 16 interactions.
    MINTiMINT-1684213.
    STRINGi9606.ENSP00000260970.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG048162.
    InParanoidiQ13427.
    KOiK09566.
    OMAiHDKNKKF.
    OrthoDBiEOG79GT7W.
    PhylomeDBiQ13427.
    TreeFamiTF318563.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    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. Align

    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

    MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT    50
    GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF 100
    AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV 150
    VREIENQKTD AASKPFAEVR ILSCGELIPK SKVKKEEKKR HKSSSSSSSS 200
    SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK HKKEKKKRKK 250
    SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK 300
    NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR 350
    DRFRRSETPP HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR 400
    VKERKITDHR NVSESPNRKN EKEKKVKDHK SNSKERDIRR NSEKDDKYKN 450
    KVKKRAKSKS RSKSKEKSKS KERDSKHNRN EEKRMRSRSK GRDHENVKEK 500
    EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR RAQSRSRECD 550
    ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR 600
    RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK 650
    SSHRKENSES EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE 700
    LKSSMLKNKE DEKIRSSVEK ENQKSKGQEN DHVHEKNKKF DHESSPGTDE 750
    DKSG 754
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi229462749.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2235.1. [Q13427-1 ]
    PIRi JC5314.
    RefSeqi NP_004783.2. NM_004792.2. [Q13427-1 ]
    XP_005247023.1. XM_005246966.1. [Q13427-1 ]
    XP_005247024.1. XM_005246967.1. [Q13427-1 ]
    UniGenei Hs.470544.
    Hs.593163.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GW2 X-ray 1.80 A 1-179 [» ]
    2WFI X-ray 0.75 A 1-177 [» ]
    2WFJ X-ray 0.75 A 1-177 [» ]
    ProteinModelPortali Q13427.
    SMRi Q13427. Positions 6-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114761. 15 interactions.
    IntActi Q13427. 16 interactions.
    MINTi MINT-1684213.
    STRINGi 9606.ENSP00000260970.

    Chemistry

    DrugBanki DB00172. L-Proline.

    PTM databases

    PhosphoSitei Q13427.

    Polymorphism databases

    DMDMi 229462749.

    Proteomic databases

    MaxQBi Q13427.
    PaxDbi Q13427.
    PRIDEi Q13427.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260970 ; ENSP00000260970 ; ENSG00000138398 . [Q13427-1 ]
    ENST00000448752 ; ENSP00000407083 ; ENSG00000138398 . [Q13427-1 ]
    ENST00000462903 ; ENSP00000435987 ; ENSG00000138398 . [Q13427-2 ]
    GeneIDi 9360.
    KEGGi hsa:9360.
    UCSCi uc002uez.3. human. [Q13427-1 ]
    uc002ufa.3. human. [Q13427-2 ]

    Organism-specific databases

    CTDi 9360.
    GeneCardsi GC02P170404.
    H-InvDB HIX0029914.
    HGNCi HGNC:14650. PPIG.
    HPAi HPA021788.
    MIMi 606093. gene.
    neXtProti NX_Q13427.
    PharmGKBi PA33585.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOVERGENi HBG048162.
    InParanoidi Q13427.
    KOi K09566.
    OMAi HDKNKKF.
    OrthoDBi EOG79GT7W.
    PhylomeDBi Q13427.
    TreeFami TF318563.

    Miscellaneous databases

    ChiTaRSi PPIG. human.
    EvolutionaryTracei Q13427.
    GeneWikii PPIG_(gene).
    GenomeRNAii 9360.
    NextBioi 35051.
    PROi Q13427.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13427.
    Bgeei Q13427.
    CleanExi HS_PPIG.
    Genevestigatori Q13427.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 130 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