FR1OP_HUMAN - dbPTM
FR1OP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FR1OP_HUMAN
UniProt AC O95684
Protein Name FGFR1 oncogene partner
Gene Name FGFR1OP
Organism Homo sapiens (Human).
Sequence Length 399
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, cilium basal body . Associated with gamma-tubulin (PubMed:16314388). Localiz
Protein Description Required for anchoring microtubules to the centrosomes. [PubMed: 16314388]
Protein Sequence MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKGPTTGEGALDLSDVHSPPKSPEGKTSAQTTPSKIPRYKGQGKKKTSGQKAGDKKANDEANQSDTSVSLSEPKSKSSLHLLSHETKIGSFLSNRTLDGKDKAGLCPDEDDMEGDSFFDDPIPKPEKTYGLRKEPRKQAGSLASLSDAPPLKSGLSSLAGAPSLKDSESKRGNTVLKDLKLISDKIGSLGLGTGEDDDYVDDFNSTSHRSEKSEISIGEEIEEDLSVEIDDINTSDKLDDLTQDLTVSQLSDVADYLEDVA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
173AcetylationSAQTTPSKIPRYKGQ
CCCCCCCCCCCCCCC
58.9125953088
225AcetylationHLLSHETKIGSFLSN
HHHCCHHHHHHHHCC
41.9325953088
315AcetylationKRGNTVLKDLKLISD
CCCCCHHHHHHHHHC
57.5925953088
318AcetylationNTVLKDLKLISDKIG
CCHHHHHHHHHCCCC
54.6425953088
323AcetylationDLKLISDKIGSLGLG
HHHHHHCCCCCCCCC
42.0225953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of FR1OP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FR1OP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FR1OP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FR1OP_HUMANFGFR1OPphysical
20360068
PACS1_HUMANPACS1physical
20360068
CE350_HUMANCEP350physical
20360068
WRIP1_HUMANWRNIP1physical
17888034
ABL1_HUMANABL1physical
17888034
CEP19_HUMANCEP19physical
25416956
CE350_HUMANCEP350physical
26186194
POTEI_HUMANPOTEIphysical
26186194
MS3L1_HUMANMSL3physical
26186194
P2R3C_HUMANPPP2R3Cphysical
26186194
CEP19_HUMANCEP19physical
26186194
PUR8_HUMANADSLphysical
26638075
AKAP1_HUMANAKAP1physical
26638075
AKA11_HUMANAKAP11physical
26638075
ANR17_HUMANANKRD17physical
26638075
BCL10_HUMANBCL10physical
26638075
TM256_HUMANTMEM256physical
26638075
C2D1A_HUMANCC2D1Aphysical
26638075
CE350_HUMANCEP350physical
26638075
CSN4_HUMANCOPS4physical
26638075
CRBG3_HUMANCRYBG3physical
26638075
CT2NL_HUMANCTTNBP2NLphysical
26638075
DYN2_HUMANDNM2physical
26638075
ENAH_HUMANENAHphysical
26638075
EXOC4_HUMANEXOC4physical
26638075
GPTC1_HUMANGPATCH1physical
26638075
CSN1_HUMANGPS1physical
26638075
HAUS8_HUMANHAUS8physical
26638075
KLC1_HUMANKLC1physical
26638075
KLC2_HUMANKLC2physical
26638075
KLC4_HUMANKLC4physical
26638075
CARL1_HUMANLRRC16Aphysical
26638075
LRC47_HUMANLRRC47physical
26638075
PHOCN_HUMANMOB4physical
26638075
MRE11_HUMANMRE11Aphysical
26638075
NAV1_HUMANNAV1physical
26638075
NCOR1_HUMANNCOR1physical
26638075
GCR_HUMANNR3C1physical
26638075
PLK1_HUMANPLK1physical
26638075
P2R3C_HUMANPPP2R3Cphysical
26638075
RFIP1_HUMANRAB11FIP1physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB3I_HUMANRAB3IPphysical
26638075
RAD50_HUMANRAD50physical
26638075
RIPK2_HUMANRIPK2physical
26638075
RPAP2_HUMANRPAP2physical
26638075
SAV1_HUMANSAV1physical
26638075
SLN11_HUMANSLFN11physical
26638075
SNX30_HUMANSNX30physical
26638075
SPAS2_HUMANSPATS2physical
26638075
SPS2L_HUMANSPATS2Lphysical
26638075
SRA1_HUMANSRA1physical
26638075
SRSF2_HUMANSRSF2physical
26638075
STK3_HUMANSTK3physical
26638075
STK4_HUMANSTK4physical
26638075
TAF12_HUMANTAF12physical
26638075
TXLNA_HUMANTXLNAphysical
26638075
UN45A_HUMANUNC45Aphysical
26638075
WDR83_HUMANWDR83physical
26638075
BIG3_HUMANKIAA1244physical
26638075
AES_HUMANAESphysical
26496610
BTF3_HUMANBTF3physical
26496610
CATC_HUMANCTSCphysical
26496610
ERF1_HUMANETF1physical
26496610
GNS_HUMANGNSphysical
26496610
SP110_HUMANSP110physical
26496610
I5P2_HUMANINPP5Bphysical
26496610
KIFC3_HUMANKIFC3physical
26496610
LAMB1_HUMANLAMB1physical
26496610
LYN_HUMANLYNphysical
26496610
PCM1_HUMANPCM1physical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
KAPCB_HUMANPRKACBphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
TTC3_HUMANTTC3physical
26496610
OFD1_HUMANOFD1physical
26496610
DLG5_HUMANDLG5physical
26496610
MOONR_HUMANKIAA0753physical
26496610
CE350_HUMANCEP350physical
26496610
CE170_HUMANCEP170physical
26496610
RAD50_HUMANRAD50physical
26496610
AKAP9_HUMANAKAP9physical
26496610
RBM5_HUMANRBM5physical
26496610
PIBF1_HUMANPIBF1physical
26496610
HPS5_HUMANHPS5physical
26496610
COBL1_HUMANCOBLL1physical
26496610
CP131_HUMANCEP131physical
26496610
TTLL5_HUMANTTLL5physical
26496610
N4BP3_HUMANN4BP3physical
26496610
SYNEM_HUMANSYNMphysical
26496610
GOLI4_HUMANGOLIM4physical
26496610
PI3R4_HUMANPIK3R4physical
26496610
ASCC1_HUMANASCC1physical
26496610
SPN90_HUMANNCKIPSDphysical
26496610
CCHCR_HUMANCCHCR1physical
26496610
P2R3C_HUMANPPP2R3Cphysical
26496610
ELP3_HUMANELP3physical
26496610
CEP72_HUMANCEP72physical
26496610
CK5P2_HUMANCDK5RAP2physical
26496610
MIB1_HUMANMIB1physical
26496610
K1328_HUMANKIAA1328physical
26496610
CCD14_HUMANCCDC14physical
26496610
REN3A_HUMANUPF3Aphysical
26496610
CSPP1_HUMANCSPP1physical
26496610
CE290_HUMANCEP290physical
26496610
CEP78_HUMANCEP78physical
26496610
CCD77_HUMANCCDC77physical
26496610
CE295_HUMANCEP295physical
26496610
TIM29_HUMANC19orf52physical
26496610
TBC31_HUMANTBC1D31physical
26496610
ESCO1_HUMANESCO1physical
26496610
ADIP_HUMANSSX2IPphysical
26496610
FOPNL_HUMANFOPNLphysical
26496610
TATD3_HUMANTATDN3physical
26496610
SCLT1_HUMANSCLT1physical
26496610
B3GLT_HUMANB3GALTLphysical
26496610
SPICE_HUMANSPICE1physical
26496610
CC138_HUMANCCDC138physical
26496610
WDR90_HUMANWDR90physical
26496610
RABL3_HUMANRABL3physical
26496610
CCD18_HUMANCCDC18physical
26496610
CCD61_HUMANCCDC61physical
26496610
P2R3C_HUMANPPP2R3Cphysical
28514442
CE350_HUMANCEP350physical
28514442
MS3L1_HUMANMSL3physical
28514442
POTEI_HUMANPOTEIphysical
28514442
CEP19_HUMANCEP19physical
28514442
AIPL1_HUMANAIPL1physical
27173435
PDE5A_HUMANPDE5Aphysical
27173435
BLM_HUMANBLMphysical
27173435
SPT5H_HUMANSUPT5Hphysical
27173435
WDR24_HUMANWDR24physical
27173435
PATZ1_HUMANPATZ1physical
27173435
FKB15_HUMANFKBP15physical
27173435

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FR1OP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-204, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-160; SER-202AND SER-254, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, ANDMASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-204, AND MASS SPECTROMETRY.

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