FBX34_HUMAN - dbPTM
FBX34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX34_HUMAN
UniProt AC Q9NWN3
Protein Name F-box only protein 34
Gene Name FBXO34
Organism Homo sapiens (Human).
Sequence Length 711
Subcellular Localization
Protein Description Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex..
Protein Sequence MHLKPYWKLQKKEHPPEVSRETQRTPMNHQKAVNDETCKASHITSSVFPSASLGKASSRKPFGILSPNVLCSMSGKSPVESSLNVKTKKNAPSATIHQGEEEGPLDIWAVVKPGNTKEKIAFFASHQCSNRIGSMKIKSSWDIDGRATKRRKKSGDLKKAKVQVERMREVNSRCYQPEPFACGIEHCSVHYVSDSGDGVYAGRPLSVIQMVAFLEQRASALLASCSKNCTNSPAIVRFSGQSRGVPAVSESYSAPGACEEPTERGNLEVGEPQSEPVRVLDMVAKLESECLKRQGQREPGSLSRNNSFRRNVGRVLLANSTQADEGKTKKGVLEAPDTQVNPVGSVSVDCGPSRADRCSPKEDQAWDGASQDCPPLPAGVSFHIDSAELEPGSQTAVKNSNRYDVEMTDELVGLPFSSHTYSQASELPTDAVDCMSRELVSLTSRNPDQRKESLCISITVSKVDKDQPSILNSCEDPVPGMLFFLPPGQHLSDYSQLNESTTKESSEASQLEDAAGGDSASEEKSGSAEPFVLPASSVESTLPVLEASSWKKQVSHDFLETRFKIQQLLEPQQYMAFLPHHIMVKIFRLLPTKSLVALKCTCCYFKFIIEYYNIRPADSRWVRDPRYREDPCKQCKKKYVKGDVSLCRWHPKPYCQALPYGPGYWMCCHRSQKGFPGCKLGLHDNHWVPACHSFNRAIHKKAKGTEAEEEY
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
41PhosphorylationNDETCKASHITSSVF
CHHHHHHHHHCHHHC
10.83-
44PhosphorylationTCKASHITSSVFPSA
HHHHHHHCHHHCCCC
14.9923532336
45PhosphorylationCKASHITSSVFPSAS
HHHHHHCHHHCCCCC
24.7323532336
46PhosphorylationKASHITSSVFPSASL
HHHHHCHHHCCCCCC
21.0823532336
77PhosphorylationLCSMSGKSPVESSLN
EEECCCCCCCCCCCC
37.3923532336
81PhosphorylationSGKSPVESSLNVKTK
CCCCCCCCCCCCCCC
40.12-
82PhosphorylationGKSPVESSLNVKTKK
CCCCCCCCCCCCCCC
15.51-
86UbiquitinationVESSLNVKTKKNAPS
CCCCCCCCCCCCCCC
54.26-
87PhosphorylationESSLNVKTKKNAPSA
CCCCCCCCCCCCCCC
42.86-
125PhosphorylationEKIAFFASHQCSNRI
HHEEEEECCCCCCCC
14.66-
129PhosphorylationFFASHQCSNRIGSMK
EEECCCCCCCCCCCE
23.67-
154PhosphorylationATKRRKKSGDLKKAK
CCCCCCCCCCHHHHH
40.34-
227UbiquitinationALLASCSKNCTNSPA
HHHHHHCCCCCCCCE
61.44-
227UbiquitinationALLASCSKNCTNSPA
HHHHHHCCCCCCCCE
61.44-
288PhosphorylationDMVAKLESECLKRQG
HHHHHHHHHHHHHCC
44.0119413330
301PhosphorylationQGQREPGSLSRNNSF
CCCCCCCCCCCCCHH
33.6123532336
307PhosphorylationGSLSRNNSFRRNVGR
CCCCCCCHHHHHHHH
24.5526437602
457PhosphorylationRKESLCISITVSKVD
HCEEEEEEEEEEECC
15.94-
461PhosphorylationLCISITVSKVDKDQP
EEEEEEEEECCCCCC
20.50-
519PhosphorylationEDAAGGDSASEEKSG
HHHCCCCCCCCCCCC
36.6528985074
552UbiquitinationLEASSWKKQVSHDFL
HHCCHHCHHCCHHHH
50.07-

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 FBX34_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX34_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 FBX34_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP1_HUMANSKP1physical
16169070
TGFR1_HUMANTGFBR1physical
15761153
TGFR2_HUMANTGFBR2physical
15761153
CUL1_HUMANCUL1physical
22268729
K1C40_HUMANKRT40physical
25416956
SKP1_HUMANSKP1physical
26087183
MYO6_HUMANMYO6physical
28514442
FBX30_HUMANFBXO30physical
28514442
GELS_HUMANGSNphysical
28514442
TMOD3_HUMANTMOD3physical
28514442
CUL1_HUMANCUL1physical
28514442

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 FBX34_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY.

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