F126B_HUMAN - dbPTM
F126B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F126B_HUMAN
UniProt AC Q8IXS8
Protein Name Protein FAM126B
Gene Name FAM126B
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Cytoplasm, cytosol . Cell membrane .
Protein Description Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane..
Protein Sequence MLGTDRCVVEEWLSEFKALPDTQITSYAATLHRKKTLVPALYKVIQDSNNELLEPVCHQLFELYRSSEVRLKRFTLQFLPELMWVYLRLTVSRDRQSNGCIEALLLGIYNLEIADKDGNNKVLSFTIPSLSKPSIYHEPSTIGSMALTEGALCQHDLIRVVYSDLHPQRETFTAQNRFEVLSFLMLCYNSAIVYMPASSYQSLCRMGSRVCVSGFPRQHEKHWKELCGRIVLDPEFMVQLLTGVYYAMYNGQWDLGQEVLDDIIYRAQLELFSQPLLVANAMKNSLPFDAPDSTQEGQKVLKVEVTPTVPRISRTAITTASIRRHRWRREGAEGVNGGEESVNLNDADEGFSSGASLSSQPIGTKPSSSSQRGSLRKVATGRSAKDKETASAIKSSESPRDSVVRKQYVQQPTDLSVDSVELTPMKKHLSLPAGQVVPKINSLSLIRTASASSSKSFDYVNGSQASTSIGVGTEGGTNLAANNANRYSTVSLQEDRLGQAGEGKELLSPGAPLTKQSRSPSFNMQLISQV
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
4Phosphorylation----MLGTDRCVVEE
----CCCCCCHHHHH
19.1326074081
14PhosphorylationCVVEEWLSEFKALPD
HHHHHHHHHHHCCCC
41.9026074081
22PhosphorylationEFKALPDTQITSYAA
HHHCCCCCCCCHHHH
21.6728387310
25PhosphorylationALPDTQITSYAATLH
CCCCCCCCHHHHHHH
13.0827080861
26PhosphorylationLPDTQITSYAATLHR
CCCCCCCHHHHHHHC
17.8827080861
27PhosphorylationPDTQITSYAATLHRK
CCCCCCHHHHHHHCC
7.5127080861
30PhosphorylationQITSYAATLHRKKTL
CCCHHHHHHHCCCCH
18.2228387310
42PhosphorylationKTLVPALYKVIQDSN
CCHHHHHHHHHHCCC
12.81-
97PhosphorylationTVSRDRQSNGCIEAL
HCCCCHHCCCHHHHH
35.76-
129PhosphorylationVLSFTIPSLSKPSIY
EEEEEECCCCCCCCC
41.2322210691
134PhosphorylationIPSLSKPSIYHEPST
ECCCCCCCCCCCCCC
39.2420562096
136PhosphorylationSLSKPSIYHEPSTIG
CCCCCCCCCCCCCHH
12.4120562096
162PhosphorylationHDLIRVVYSDLHPQR
HHHHHHHHCCCCCCC
8.1327642862
299UbiquitinationDSTQEGQKVLKVEVT
CCCCCCCEEEEEEEE
61.46-
306PhosphorylationKVLKVEVTPTVPRIS
EEEEEEEECCCCCCC
10.3529255136
308PhosphorylationLKVEVTPTVPRISRT
EEEEEECCCCCCCCC
33.5030266825
313PhosphorylationTPTVPRISRTAITTA
ECCCCCCCCCEEEHH
25.5128348404
315PhosphorylationTVPRISRTAITTASI
CCCCCCCCEEEHHHH
18.6723186163
318PhosphorylationRISRTAITTASIRRH
CCCCCEEEHHHHHHH
17.5329978859
319PhosphorylationISRTAITTASIRRHR
CCCCEEEHHHHHHHH
16.5821712546
321PhosphorylationRTAITTASIRRHRWR
CCEEEHHHHHHHHHH
17.9723401153
341PhosphorylationGVNGGEESVNLNDAD
CCCCCCCCCCCCCCC
16.41-
367PhosphorylationQPIGTKPSSSSQRGS
CCCCCCCCCCCCCCC
44.39-
368PhosphorylationPIGTKPSSSSQRGSL
CCCCCCCCCCCCCCC
42.40-
369PhosphorylationIGTKPSSSSQRGSLR
CCCCCCCCCCCCCCC
34.52-
374PhosphorylationSSSSQRGSLRKVATG
CCCCCCCCCCHHHCC
27.47-
389PhosphorylationRSAKDKETASAIKSS
CCCCCHHHHHHHHCC
31.4928464451
391PhosphorylationAKDKETASAIKSSES
CCCHHHHHHHHCCCC
37.6428464451
395PhosphorylationETASAIKSSESPRDS
HHHHHHHCCCCCCHH
32.9728102081
396PhosphorylationTASAIKSSESPRDSV
HHHHHHCCCCCCHHH
36.7723312004
398PhosphorylationSAIKSSESPRDSVVR
HHHHCCCCCCHHHHH
27.4725849741
402PhosphorylationSSESPRDSVVRKQYV
CCCCCCHHHHHHHHC
24.6423312004
408PhosphorylationDSVVRKQYVQQPTDL
HHHHHHHHCCCCCCC
11.8523090842
413PhosphorylationKQYVQQPTDLSVDSV
HHHCCCCCCCCCCEE
45.2828450419
416PhosphorylationVQQPTDLSVDSVELT
CCCCCCCCCCEEECC
27.0428450419
419PhosphorylationPTDLSVDSVELTPMK
CCCCCCCEEECCCCC
18.4828450419
423PhosphorylationSVDSVELTPMKKHLS
CCCEEECCCCCCCCC
14.0828450419
430PhosphorylationTPMKKHLSLPAGQVV
CCCCCCCCCCCCCEE
31.8430266825
442PhosphorylationQVVPKINSLSLIRTA
CEECCCCHHHHEEEE
23.8622617229
444PhosphorylationVPKINSLSLIRTASA
ECCCCHHHHEEEECC
22.9026074081
448PhosphorylationNSLSLIRTASASSSK
CHHHHEEEECCCCCC
20.2626074081
450PhosphorylationLSLIRTASASSSKSF
HHHEEEECCCCCCCC
28.2426074081
452PhosphorylationLIRTASASSSKSFDY
HEEEECCCCCCCCCC
32.4226074081
453PhosphorylationIRTASASSSKSFDYV
EEEECCCCCCCCCCC
41.3126074081
454PhosphorylationRTASASSSKSFDYVN
EEECCCCCCCCCCCC
29.8026074081
456PhosphorylationASASSSKSFDYVNGS
ECCCCCCCCCCCCCC
25.8728348404
487PhosphorylationAANNANRYSTVSLQE
CCCCCCCCCEEECCC
14.4326657352
488PhosphorylationANNANRYSTVSLQED
CCCCCCCCEEECCCC
21.0628796482
489PhosphorylationNNANRYSTVSLQEDR
CCCCCCCEEECCCCC
12.7427794612
491PhosphorylationANRYSTVSLQEDRLG
CCCCCEEECCCCCCC
25.1525159151
496MethylationTVSLQEDRLGQAGEG
EEECCCCCCCCCCCC
39.71-
508PhosphorylationGEGKELLSPGAPLTK
CCCCCCCCCCCCCCC
33.6330266825
514PhosphorylationLSPGAPLTKQSRSPS
CCCCCCCCCCCCCCC
26.4430266825
517PhosphorylationGAPLTKQSRSPSFNM
CCCCCCCCCCCCHHC
35.9622210691
519PhosphorylationPLTKQSRSPSFNMQL
CCCCCCCCCCHHCHH
30.0926074081
521PhosphorylationTKQSRSPSFNMQLIS
CCCCCCCCHHCHHHC
30.4226074081
528PhosphorylationSFNMQLISQV-----
CHHCHHHCCC-----
33.2226074081

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 F126B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F126B_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 F126B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F126B_HUMAN

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Related Literatures of Post-Translational Modification
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-442 AND SER-491, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306, AND MASSSPECTROMETRY.

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