CP4F8_HUMAN - dbPTM
CP4F8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CP4F8_HUMAN
UniProt AC P98187
Protein Name Cytochrome P450 4F8
Gene Name CYP4F8
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein. Microsome membrane.
Protein Description Hydroxylates arachidonic acid (20:4n-6) to (18R)-hydroxyarachidonate. Shows little activity against prostaglandin (PG) D2, PGE1, PGE2, PGF2alpha, and leukotriene B4. Catalyzes omega-2 and omega-3-hydroxylation of PGH1 and PGH2. Catalyzes epoxidation of 4,7,10,13,16,19-(Z)-docosahexaenoic acid (22:6n-3) and 7,10,13,16,19-(Z)-docosapentaenoic acid (22:5n-3) and omega-3-hydroxylation of 4,7,10,13,16-(Z)-docosapentaenoic acid (22:5n-6). Catalyzes hydroxylation of PGI2 and carbaprostacyclin..
Protein Sequence MSLLSLSWLGLRPVAASPWLLLLVVGASWLLARILAWTYAFYHNGRRLRCFPQPRKQNWFLGHLGLVTPTEEGLRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVVKRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRVIPKGNVCNINIFAIHHNPSVWPDPEVYDPFRFDPENAQKRSPMAFIPFSAGPRNCIGQKFAMAEMKVVLALTLLRFRILPDHREPRRTPEIVLRAEDGLWLRVEPLG
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
2Phosphorylation------MSLLSLSWL
------CCCHHCHHC
37.7125002506
152PhosphorylationRHHRRLLTPAFHFNI
HHHHHCCCHHHHHHC
19.70-
168PhosphorylationKPYIKIFSKSANIMH
HHHHHHHHCCCCHHH
29.2224719451
170PhosphorylationYIKIFSKSANIMHAK
HHHHHHCCCCHHHHH
25.9124719451
187PhosphorylationRLAMEGSTCLDVFEH
HHHHCCCCHHHHHHH
28.1327762562
290UbiquitinationVDDFLQAKAKSKTLD
HHHHHHHHHHCCCCC
43.3027667366
292UbiquitinationDFLQAKAKSKTLDFI
HHHHHHHHCCCCCHH
52.3423503661
294UbiquitinationLQAKAKSKTLDFIDV
HHHHHHCCCCCHHHH
53.0221906983
314PhosphorylationDKNGKELSDEDIRAE
CCCCCCCCHHHHHHH
39.79-
332PhosphorylationFMFGGHDTTASGLSW
EEECCCCCHHHHHHH
20.70-
388PhosphorylationLTMCLKESLRLHPPI
HHHHHHHHHCCCCCC
19.73-
397PhosphorylationRLHPPIPTFARGCTQ
CCCCCCCCCCCCCCC
30.55-
501PhosphorylationDHREPRRTPEIVLRA
CCCCCCCCCCEEEEC
26.9324114839

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 CP4F8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CP4F8_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 CP4F8_HUMAN !!

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

Oops, there are no PPI records of CP4F8_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CP4F8_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP