CP1B1_HUMAN - dbPTM
CP1B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CP1B1_HUMAN
UniProt AC Q16678
Protein Name Cytochrome P450 1B1
Gene Name CYP1B1
Organism Homo sapiens (Human).
Sequence Length 543
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein. Microsome membrane
Peripheral membrane protein. Mitochondrion.
Protein Description Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression..
Protein Sequence MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAELDQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVVFVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQLFLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKETCQ
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
3Phosphorylation-----MGTSLSPNDP
-----CCCCCCCCCC		25.7924043423
4Phosphorylation----MGTSLSPNDPW
----CCCCCCCCCCC		22.5624043423
6Phosphorylation--MGTSLSPNDPWPL
--CCCCCCCCCCCCC		22.7924043423
17PhosphorylationPWPLNPLSIQQTTLL
CCCCCCCCHHHHHHH		21.4324043423
21PhosphorylationNPLSIQQTTLLLLLS
CCCCHHHHHHHHHHH		11.7524043423
22PhosphorylationPLSIQQTTLLLLLSV
CCCHHHHHHHHHHHH		15.8624043423
28PhosphorylationTTLLLLLSVLATVHV
HHHHHHHHHHHHHHH		18.3024043423
32PhosphorylationLLLSVLATVHVGQRL
HHHHHHHHHHHHHHH		13.6424043423
142UbiquitinationGHYSEHWKVQRRAAH
CCCCHHHHHHHHHHH		30.3321890473
172PhosphorylationVLEGHVLSEARELVA
HHCHHHHHHHHHHHH		28.2828555341
269PhosphorylationEQLNRNFSNFILDKF
HHHHHHHHHHHHHHH		34.0927499020
275UbiquitinationFSNFILDKFLRHCES
HHHHHHHHHHHHHHH		42.7421890473
299PhosphorylationMMDAFILSAEKKAAG
HHHHHHHHHHHHHCC		29.5726091039
302UbiquitinationAFILSAEKKAAGDSH
HHHHHHHHHHCCCCC		47.64-
303UbiquitinationFILSAEKKAAGDSHG
HHHHHHHHHCCCCCC		34.67-
448UbiquitinationDPARFLDKDGLINKD
CHHHHCCCCCCCCCC		56.7121890473
454UbiquitinationDKDGLINKDLTSRVM
CCCCCCCCCCCCCEE		47.31-
457PhosphorylationGLINKDLTSRVMIFS
CCCCCCCCCCEEEEE		25.31-
467UbiquitinationVMIFSVGKRRCIGEE
EEEEECCCCCCCCHH		34.22-
517AcetylationTIKPKSFKVNVTLRE
EECCCEEEEEEEHHH		39.7411792073
539AcetylationAVQNLQAKETCQ---
HHHHHHHHHHCC---		40.3611792083
539UbiquitinationAVQNLQAKETCQ---
HHHHHHHHHHCC---		40.36-
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 CP1B1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CP1B1_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 CP1B1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CP1B1_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00612 Primary open angle glaucoma
H01075 Peters anomaly, including: Peters plus syndrome; Peters anomaly plus systemic features
H01159 Anterior segment dysgenesis (ASD), including: Anterior segment mesenchymal dysgenesis; Aniridia; Axe
H01203 Primary congenital glaucoma (PCG)
OMIM Disease
604229Peters anomaly (PETAN)
231300Glaucoma 3, primary congenital, A (GLC3A)
137760Glaucoma, primary open angle (POAG)
137750Glaucoma 1, open angle, A (GLC1A)
Kegg Drug
D00105 Estradiol (JAN/USP/INN); Climara (TN); Divigel (TN); Estrace (TN); Estraderm (TN); Estrasorb (TN); E
DrugBank
DB00613Amodiaquine
DB01169Arsenic trioxide
DB00121Biotin
DB00201Caffeine
DB00363Clozapine
DB01254Dasatinib
DB00694Daunorubicin
DB01234Dexamethasone
DB01248Docetaxel
DB00997Doxorubicin
DB00530Erlotinib
DB00783Estradiol
DB00655Estrone
DB00499Flutamide
DB01026Ketoconazole
DB00448Lansoprazole
DB01065Melatonin
DB01204Mitoxantrone
DB00338Omeprazole
DB00526Oxaliplatin
DB01229Paclitaxel
DB01174Phenobarbital
DB01087Primaquine
DB01168Procarbazine
DB00396Progesterone
DB00818Propofol
DB00675Tamoxifen
DB00624Testosterone
DB00277Theophylline
Regulatory Network of CP1B1_HUMAN

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Related Literatures of Post-Translational Modification

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