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Please include the following statement when referencing the CPTAC Assay Portal
We would like to acknowledge the National Cancer Institute’s Clinical Proteomic Tumor Analysis Consortium (CPTAC) Assay Portal (assays.cancer.gov) for developing assays and establishing criteria for the assays described in this publication.

Overview Data source: UniProt

Official Gene Symbol Other Aliases
GNPTG C16orf27, GNPTAG
Sequence Length (AA) Molecular Weight (Da)
305 33974
Protein Name
N-acetylglucosamine-1-phosphotransferase subunit gamma
Sources
UniProt
PhosphoSitePlus ®
GeneCards
Human Protein Atlas

Protein Sequence hover to view complete sequence

10 20 30 40 50
MAAGLARLLL LLGLSAGGPA PAGAAKMKVV EEPNAFGVNN PFLPQASRLQ
60 70 80 90 100
AKRDPSPVSG PVHLFRLSGK CFSLVESTYK YEFCPFHNVT QHEQTFRWNA
110 120 130 140 150
YSGILGIWHE WEIANNTFTG MWMRDGDACR SRSRQSKVEL ACGKSNRLAH
160 170 180 190 200
VSEPSTCVYA LTFETPLVCH PHALLVYPTL PEALQRQWDQ VEQDLADELI
210 220 230 240 250
TPQGHEKLLR TLFEDAGYLK TPEENEPTQL EGGPDSLGFE TLENCRKAHK
260 270 280 290 300
ELSKEIKRLK GLLTQHGIPY TRPTETSNLE HLGHETPRAK SPEQLRGDPG
305
LRGSL

Data source: UniProt


Position of Targeted Peptide Analytes Relative to SNPs, Isoforms, and PTMs

Uniprot Database Entry PhosphoSitePlus ®

Click a point on a node
to view detailed assay information below
All other points link out to UniProt



Phosphorylation Acetylation Ubiquitylation Other

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Assay Details for CPTAC-2710 Collapse assay details

Data source: Panorama

Official Gene Symbol
GNPTG
Peptide Modified Sequence
YEFC[+57.0]PFHN[+1.0]VTQHEQTFR
Modification Type
Carbamidomethyl (C), Deamidated (N)
Protein - Site of Modification
N/A
Peptide - Site of Modification
4, 8
Peptide Start
81
Peptide End
97
CPTAC ID
CPTAC-2710
Peptide Molecular Mass
2,239.9745
Species
Homo sapiens (Human)
Assay Type
Direct MRM
Matrix
Human ovarian tumor tissue digest
Submitting Laboratory
Johns Hopkins University
Submitting Lab PI
Daniel Chan, Hui Zhang, Zhen Zhang

Assay Parameters Collapse assay parameters

Data source: Panorama

Instrument
TSQ Vantage
Internal Standard
Stable isotope-labeled peptides
Peptide Standard Purity
Crude (~60%)
Peptide Standard Label Type
13C and 15N at C-terminus R
LC
Accela 1250 Quaternary Low Pump
Column Packing
C18, 3 µm, 300 Å
Column Dimensions
1.0 mm I.D. x 15 cm
Flow Rate
50 µL/min

Assay Multiplexing Expand assay panel

Johns Hopkins University-H


Chromatograms

Data source: Panorama


Response Curves

Data source: Panorama

Retrieving Data

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Repeatability

Data source: Panorama

  Average intra-assay CV
(within day CV)
Average inter-assay CV
(between day CV)
Total CV
equation
n=
Fragment ion / Transition Low Med High Low Med High Low Med High Low Med High
y13 (2+) 9.6 10.5 6.3 8.7 11.5 9.8 13 15.6 11.7 15 15 15
y11 (2+) 8.6 7.7 10.4 10.1 8.4 10.5 13.3 11.4 14.8 15 15 15
y6 (2+) 12.4 12.7 18.6 14.1 13.5 18.6 18.8 18.5 26.3 15 15 15
sum 4.1 6.5 5.1 5 6.7 4.9 6.5 9.3 7.1 15 15 15


Additional Resources and Comments


Assay Details for non-CPTAC-3984 Collapse assay details

Data source: Panorama

Official Gene Symbol
Gnptg
Peptide Sequence
VPGETHPTQLAGGSK
Modification Type
unmodified
Protein - Site of Modification
N/A
Peptide - Site of Modification
N/A
Peptide Start
221
Peptide End
235
CPTAC ID
non-CPTAC-3984
Peptide Molecular Mass
1,477.7525
Species
Mus musculus (Mouse)
Assay Type
Direct MRM
Matrix
Plasma
Submitting Laboratory
UVic-Genome BC Proteomics Centre
Submitting Lab PI
Christoph Borchers

Assay Parameters Collapse assay parameters

Data source: Panorama

Instrument
Agilent 6490/6495 QQQ
Internal Standard
synthetic peptide
Peptide Standard Purity
>80%
Peptide Standard Label Type
13C and 15N at C-terminus K
LC
1290 LC (Agilent)
Column Packing
Zorbax Eclipse Plus C18, 1.8 µm
Column Dimensions
2.1 x 150 mm
Flow Rate
400 µL/min

Assay Multiplexing Expand assay panel

Johns Hopkins University-H


Chromatograms

Data source: Panorama


Response Curves

Data source: Panorama

Retrieving Data

Loader

Repeatability

Data source: Panorama

  Average intra-assay CV
(within day CV)
Average inter-assay CV
(between day CV)
Total CV
equation
n=
Fragment ion / Transition Low Med High Low Med High Low Med High Low Med High
y14 (3+) 12.7 4.6 3 14.6 6.4 6.2 19.4 7.9 6.9 15 15 15
y9 (2+) 25.2 6.9 6.5 24.5 7.1 9 35.1 9.9 11.1 15 15 15
y13 (2+) 19.7 7.5 4 24.3 9.1 6.7 31.3 11.8 7.8 15 15 15
y14 (2+) 14 3.9 4 13.1 4.4 4.8 19.2 5.9 6.2 15 15 15
y9 (1+) 28.1 10 5.8 31 10.3 7.2 41.8 14.4 9.2 15 15 15
sum 11.5 3.1 2.5 11.7 5.5 5.2 16.4 6.3 5.8 15 15 15


Additional Resources and Comments