TPH2_HUMAN - dbPTM
TPH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPH2_HUMAN
UniProt AC Q8IWU9
Protein Name Tryptophan 5-hydroxylase 2
Gene Name TPH2
Organism Homo sapiens (Human).
Sequence Length 490
Subcellular Localization
Protein Description
Protein Sequence MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGSSTLNKPNSGKNDDKGNKGSSKREAATESGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI
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
9PhosphorylationQPAMMMFSSKYWARR
CCCCHHCCHHHHHHC
14.1829978859
10PhosphorylationPAMMMFSSKYWARRG
CCCHHCCHHHHHHCC
20.6429978859
12PhosphorylationMMMFSSKYWARRGFS
CHHCCHHHHHHCCCC
13.2729978859
19PhosphorylationYWARRGFSLDSAVPE
HHHHCCCCCCCCCCH
33.8118339632
79AcetylationNEVGGLVKALRLFQE
CCHHHHHHHHHHHHH
46.9020167786
104PhosphorylationRKSRRRSSEVEIFVD
HHHCCCCCCEEEEEE
43.8017973628
202UbiquitinationVDVAMGYKYGQPIPR
HHHHHCCCCCCCCCC
36.8625015289
212PhosphorylationQPIPRVEYTEEETKT
CCCCCEEECHHHHHH
19.3229759185
213PhosphorylationPIPRVEYTEEETKTW
CCCCEEECHHHHHHH
24.3429759185
217PhosphorylationVEYTEEETKTWGVVF
EEECHHHHHHHHHHH
36.7329759185
249PhosphorylationNFPLLTKYCGYREDN
CCCHHHHHCCCCCCC
5.9528111955
252PhosphorylationLLTKYCGYREDNVPQ
HHHHHCCCCCCCCCC
13.7828111955
264PhosphorylationVPQLEDVSMFLKERS
CCCHHHHHHHHHHCC
19.0129255136
271PhosphorylationSMFLKERSGFTVRPV
HHHHHHCCCCEEEEC
39.0729255136
274PhosphorylationLKERSGFTVRPVAGY
HHHCCCCEEEECCCC
21.0929255136
382PhosphorylationAYGAGLLSSIGELKH
HHCHHHHHHHHHHHH
25.5917287340
392PhosphorylationGELKHALSDKACVKA
HHHHHHHCCCHHHHH
37.5417287340
422PhosphorylationFQEAYFVSESFEEAK
HHHHHHCCCCHHHHH
20.0222210691
424PhosphorylationEAYFVSESFEEAKEK
HHHHCCCCHHHHHHH
30.3722210691
440PhosphorylationRDFAKSITRPFSVYF
HHHHHHCCCCCEEEE
39.1028509920

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
19SPhosphorylationKinasePRKACAP00517
GPS
19SPhosphorylationKinasePKACAP17612
PSP
19SPhosphorylationKinaseCAMK2AP11275
PSP
19SPhosphorylationKinaseCAMK2-FAMILY-GPS
19SPhosphorylationKinasePKA-FAMILY-GPS
104SPhosphorylationKinasePRKACAP00517
GPS
104SPhosphorylationKinasePKA-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPH2_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 TPH2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DJC12_HUMANDNAJC12physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608516Major depressive disorder (MDD)
613003Attention deficit-hyperactivity disorder 7 (ADHD7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00150L-Tryptophan
Regulatory Network of TPH2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-382 AND SER-392, ANDMASS SPECTROMETRY.

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