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Overview Data source: UniProt

Official Gene Symbol Other Aliases
TP53BP1 N/A
Sequence Length (AA) Molecular Weight (Da)
1972 213574
Protein Name
Tumor suppressor p53-binding protein 1
Sources
UniProt
PhosphoSitePlus ®
GeneCards
Human Protein Atlas

Protein Sequence hover to view complete sequence

10 20 30 40 50
MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEDDSGSHF SMLSRHLPNL
60 70 80 90 100
QTHKENPVLD VVSNPEQTAG EERGDGNSGF NEHLKENKVA DPVDSSNLDT
110 120 130 140 150
CGSISQVIEQ LPQPNRTSSV LGMSVESAPA VEEEKGEELE QKEKEKEEDT
160 170 180 190 200
SGNTTHSLGA EDTASSQLGF GVLELSQSQD VEENTVPYEV DKEQLQSVTT
210 220 230 240 250
NSGYTRLSDV DANTAIKHEE QSNEDIPIAE QSSKDIPVTA QPSKDVHVVK
260 270 280 290 300
EQNPPPARSE DMPFSPKASV AAMEAKEQLS AQELMESGLQ IQKSPEPEVL
310 320 330 340 350
STQEDLFDQS NKTVSSDGCS TPSREEGGCS LASTPATTLH LLQLSGQRSL
360 370 380 390 400
VQDSLSTNSS DLVAPSPDAF RSTPFIVPSS PTEQEGRQDK PMDTSVLSEE
410 420 430 440 450
GGEPFQKKLQ SGEPVELENP PLLPESTVSP QASTPISQST PVFPPGSLPI
460 470 480 490 500
PSQPQFSHDI FIPSPSLEEQ SNDGKKDGDM HSSSLTVECS KTSEIEPKNS
510 520 530 540 550
PEDLGLSLTG DSCKLMLSTS EYSQSPKMES LSSHRIDEDG ENTQIEDTEP
560 570 580 590 600
MSPVLNSKFV PAENDSILMN PAQDGEVQLS QNDDKTKGDD TDTRDDISIL
610 620 630 640 650
ATGCKGREET VAEDVCIDLT CDSGSQAVPS PATRSEALSS VLDQEEAMEI
660 670 680 690 700
KEHHPEEGSS GSEVEEIPET PCESQGEELK EENMESVPLH LSLTETQSQG
710 720 730 740 750
LCLQKEMPKK ECSEAMEVET SVISIDSPQK LAILDQELEH KEQEAWEEAT
760 770 780 790 800
SEDSSVVIVD VKEPSPRVDV SCEPLEGVEK CSDSQSWEDI APEIEPCAEN
810 820 830 840 850
RLDTKEEKSV EYEGDLKSGT AETEPVEQDS SQPSLPLVRA DDPLRLDQEL
860 870 880 890 900
QQPQTQEKTS NSLTEDSKMA NAKQLSSDAE AQKLGKPSAH ASQSFCESSS
910 920 930 940 950
ETPFHFTLPK EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI
960 970 980 990 1000
ATSDVMSESM VETHDPILGS GKGDSGAAPD VDDKLCLRMK LVSPETEASE
1010 1020 1030 1040 1050
ESLQFNLEKP ATGERKNGST AVAESVASPQ KTMSVLSCIC EARQENEARS
1060 1070 1080 1090 1100
EDPPTTPIRG NLLHFPSSQG EEEKEKLEGD HTIRQSQQPM KPISPVKDPV
1110 1120 1130 1140 1150
SPASQKMVIQ GPSSPQGEAM VTDVLEDQKE GRSTNKENPS KALIERPSQN
1160 1170 1180 1190 1200
NIGIQTMECS LRVPETVSAA TQTIKNVCEQ GTSTVDQNFG KQDATVQTER
1210 1220 1230 1240 1250
GSGEKPVSAP GDDTESLHSQ GEEEFDMPQP PHGHVLHRHM RTIREVRTLV
1260 1270 1280 1290 1300
TRVITDVYYV DGTEVERKVT EETEEPIVEC QECETEVSPS QTGGSSGDLG
1310 1320 1330 1340 1350
DISSFSSKAS SLHRTSSGTS LSAMHSSGSS GKGAGPLRGK TSGTEPADFA
1360 1370 1380 1390 1400
LPSSRGGPGK LSPRKGVSQT GTPVCEEDGD AGLGIRQGGK APVTPRGRGR
1410 1420 1430 1440 1450
RGRPPSRTTG TRETAVPGPL GIEDISPNLS PDDKSFSRVV PRVPDSTRRT
1460 1470 1480 1490 1500
DVGAGALRRS DSPEIPFQAA AGPSDGLDAS SPGNSFVGLR VVAKWSSNGY
1510 1520 1530 1540 1550
FYSGKITRDV GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED
1560 1570 1580 1590 1600
EYFSAGVVKG HRKESGELYY SIEKEGQRKW YKRMAVILSL EQGNRLREQY
1610 1620 1630 1640 1650
GLGPYEAVTP LTKAADISLD NLVEGKRKRR SNVSSPATPT ASSSSSTTPT
1660 1670 1680 1690 1700
RKITESPRAS MGVLSGKRKL ITSEEERSPA KRGRKSATVK PGAVGAGEFV
1710 1720 1730 1740 1750
SPCESGDNTG EPSALEEQRG PLPLNKTLFL GYAFLLTMAT TSDKLASRSK
1760 1770 1780 1790 1800
LPDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY
1810 1820 1830 1840 1850
QCLLIADQHC RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA
1860 1870 1880 1890 1900
GYSLEEQRIL DWQPRENPFQ NLKVLLVSDQ QQNFLELWSE ILMTGGAASV
1910 1920 1930 1940 1950
KQHHSSAHNK DIALGVFDVV VTDPSCPASV LKCAEALQLP VVSQEWVIQC
1960 1970 1972
LIVGERIGFK QHPKYKHDYV SH

Data source: UniProt


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

Uniprot Database Entry PhosphoSitePlus ®

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to view detailed assay information below
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Phosphorylation Acetylation Ubiquitylation Other

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Assay Details for CPTAC-1334 Collapse assay details

Data source: Panorama

Official Gene Symbol
TP53BP1
Peptide Modified Sequence
QYTES[+80.0]QLR
Modification Type
Phospho (ST)
Protein - Site of Modification
1778
Peptide - Site of Modification
5
Peptide Start
1774
Peptide End
1781
CPTAC ID
CPTAC-1334
Peptide Molecular Mass
1,103.4649
Species
Homo sapiens (Human)
Assay Type
Enrichment MRM
Enrichment Method
N/A
Matrix
Digested Cell Lysate
Submitting Laboratory
Broad Institute
Submitting Lab PI
Steven A. Carr

Publication

View Details (opens in a new window)

Abelin, et al. Mol Cell Proteomics. 2016 May;15(5):1622-41. doi: 10.1074/mcp.M116.058354. Epub 2016 Feb 24. PMID:26912667


Assay Parameters Collapse assay parameters Test button response curves

Data source: Panorama

Instrument
Quantiva TSQ
Internal Standard
medium stable isotope peptide (delta 6 amu)
Peptide Standard Purity
Crude (~60%)
Peptide Standard Label Type
13C and 15N at C-terminus R
LC
Easy NanoLC1000
Column Packing
Reprosil C18, 3 um, 200A
Column Dimensions
0.075 x 100 mm
Flow Rate
300 nL/min

Assay Multiplexing Expand assay panel

Johns Hopkins University-I


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
y6-98 (1+) 9 7.5 4.8 9.5 8.2 11.6 13.1 11.1 12.6 15 15 15
y5-98 (1+) 9.7 7.3 5.2 8.5 8.5 10.9 12.9 11.2 12.1 15 15 15
y4-98 (1+) 7 3.9 6.3 7.4 5.2 15.2 10.2 6.5 16.5 15 15 15
sum 5.1 3.6 4.4 6.1 5.3 11.7 8 6.4 12.5 15 15 15

Additional Resources and Comments


Assay Details for CPTAC-1014 Collapse assay details

Data source: Panorama

Official Gene Symbol
TP53BP1
Peptide Modified Sequence
NS[+80.0]PEDLGLSLTGDSC[+57.0]K
Modification Type
Phospho (ST), Carbamidomethyl Cysteine
Protein - Site of Modification
500, 513
Peptide - Site of Modification
2, 15
Peptide Start
499
Peptide End
514
CPTAC ID
CPTAC-1014
Peptide Molecular Mass
1,771.7336
Species
Homo sapiens (Human)
Assay Type
Enrichment MRM
Enrichment Method
N/A
Matrix
cell lysate
Submitting Laboratory
Fred Hutchinson Cancer Research Center
Submitting Lab PI
Amanda Paulovich

Publication

View Details (opens in a new window)

Kennedy JJ, Yan P, Zhao L, Ivey RG, Voytovich U, Moore HD, Lin C, Pogosova-Agadjanyan EL, Stirewalt DL, Reding KW, Whiteaker JR, Paulovich AG. Immobilized metal affinity chromatography coupled to multiple reaction monitoring enables reproducible quantification of phospho-signaling. Molecular and Cellular Proteomics. mcp.O115.054940


Assay Parameters Collapse assay parameters Test button response curves

Data source: Panorama

Instrument
QTrap 5500 (Sciex)
Internal Standard
synthetic peptide
Peptide Standard Purity
Crude
Peptide Standard Label Type
13C and 15N at C-terminus K
LC
nanoLC-2D (Eksigent)
Column Packing
ChromXP C18-CL, 3 µm, 120 Å
Column Dimensions
75 µm x 15cm
Flow Rate
300 nL/min

Assay Multiplexing Expand assay panel

Johns Hopkins University-I


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 (2+) 52.9 21.7 10.2 59.2 21.7 11.4 79.4 30.7 15.3 15 24 15
y8 (1+) 60.1 17.9 10.6 73.2 18.9 14 94.7 26 17.6 15 24 15
y10 (1+) 40.8 17.2 8.1 43.9 16.6 9 59.9 23.9 12.1 15 24 15
sum 19.3 14.2 7.1 26.3 15.4 10.1 32.6 20.9 12.3 15 24 15

Additional Resources and Comments


Assay Details for CPTAC-1015 Collapse assay details

Data source: Panorama

Official Gene Symbol
TP53BP1
Peptide Modified Sequence
SGTAETEPVEQDS[+80.0]SQPSLPLVR
Modification Type
Phospho (ST)
Protein - Site of Modification
830
Peptide - Site of Modification
13
Peptide Start
818
Peptide End
839
CPTAC ID
CPTAC-1015
Peptide Molecular Mass
2,406.0952
Species
Homo sapiens (Human)
Assay Type
Enrichment MRM
Enrichment Method
N/A
Matrix
cell lysate
Submitting Laboratory
Fred Hutchinson Cancer Research Center
Submitting Lab PI
Amanda Paulovich

Publication

View Details (opens in a new window)

Kennedy JJ, Yan P, Zhao L, Ivey RG, Voytovich U, Moore HD, Lin C, Pogosova-Agadjanyan EL, Stirewalt DL, Reding KW, Whiteaker JR, Paulovich AG. Immobilized metal affinity chromatography coupled to multiple reaction monitoring enables reproducible quantification of phospho-signaling. Molecular and Cellular Proteomics. mcp.O115.054940


Assay Parameters Collapse assay parameters Test button response curves

Data source: Panorama

Instrument
QTrap 5500 (Sciex)
Internal Standard
synthetic peptide
Peptide Standard Purity
Crude
Peptide Standard Label Type
13C and 15N at C-terminus R
LC
nanoLC-2D (Eksigent)
Column Packing
ChromXP C18-CL, 3 µm, 120 Å
Column Dimensions
75 µm x 15cm
Flow Rate
300 nL/min

Assay Multiplexing Expand assay panel

Johns Hopkins University-I


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 (2+) 31.5 43 35.7 31.2 31.5 55.8 44.3 53.3 66.2 12 23 15
y15 (2+) 33 12.3 14.1 41.6 16.6 18.3 53.1 20.7 23.1 12 23 15
y7 (1+) 35 15.1 5.7 34.6 19.5 12.7 49.2 24.7 13.9 12 23 15
sum 23.6 13.3 4.8 26 16.2 12.6 35.1 21 13.5 12 23 15

Additional Resources and Comments


Assay Details for CPTAC-2608 Collapse assay details

Data source: Panorama

Official Gene Symbol
TP53BP1
Peptide Sequence
ITDVYYVDGTEVER
Modification Type
unmodified
Protein - Site of Modification
N/A
Peptide - Site of Modification
N/A
Peptide Start
1254
Peptide End
1267
CPTAC ID
CPTAC-2608
Peptide Molecular Mass
1,657.7835
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 Test button response curves

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-I


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
y10 (1+) 19.3 4.1 4.6 17.5 7.4 5.6 26.1 8.5 7.2 15 15 15
y9 (1+) 11.7 6.9 5.9 12.7 8.8 5.9 17.3 11.2 8.3 15 15 15
y8 (1+) 12.4 4.1 5.1 12 8.7 7.7 17.3 9.6 9.2 15 15 15
sum 9.8 4.5 4.5 7.8 7.5 5.1 12.5 8.7 6.8 15 15 15

Additional Resources and Comments


Assay Details for CPTAC-2609 Collapse assay details

Data source: Panorama

Official Gene Symbol
TP53BP1
Peptide Sequence
WSSNGYFYSGK
Modification Type
unmodified
Protein - Site of Modification
N/A
Peptide - Site of Modification
N/A
Peptide Start
1495
Peptide End
1505
CPTAC ID
CPTAC-2609
Peptide Molecular Mass
1,294.5619
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 Test button response curves

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 K
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-I


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
y10 (1+) 17.6 7.2 7.1 20.4 11.8 7.1 26.9 13.8 10 15 15 15
y9 (1+) 12 5.6 5.7 13.2 9.1 6 17.8 10.7 8.3 15 15 15
y7 (1+) 30.6 5.7 9.6 26.3 12.8 10.1 40.3 14 13.9 15 15 15
sum 11.5 5.4 5.5 11.4 9.3 5.6 16.2 10.8 7.8 15 15 15

Additional Resources and Comments