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Q13427

- PPIG_HUMAN

UniProt

Q13427 - PPIG_HUMAN

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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

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

GO - Biological processi

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

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. nucleoplasm Source: ProtInc
  3. nucleus Source: HPA
Complete GO annotation...

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

BgeeiQ13427.
CleanExiHS_PPIG.
ExpressionAtlasiQ13427. baseline and differential.
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. 18 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.
GeneTreeiENSGT00550000074595.
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

        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:
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. 18 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.
GeneTreei ENSGT00550000074595.
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

Bgeei Q13427.
CleanExi HS_PPIG.
ExpressionAtlasi Q13427. baseline and differential.
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

« 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].

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 29, 2014
This is version 131 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