CP51A_HUMAN - dbPTM
CP51A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CP51A_HUMAN
UniProt AC Q16850
Protein Name Lanosterol 14-alpha demethylase
Gene Name CYP51A1
Organism Homo sapiens (Human).
Sequence Length 503
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Microsome membrane
Single-pass membrane protein .
Protein Description Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol..
Protein Sequence MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK
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
12PhosphorylationGLLQAGGSVLGQAME
HHHHCCCCHHHHHHH		17.1622817900
22 (in isoform 2)Ubiquitination-50.9021890473
42 (in isoform 2)Ubiquitination-11.1621890473
57 (in isoform 2)Ubiquitination-25.9921890473
60PhosphorylationQLPAGVKSPPYIFSP
CCCCCCCCCCEECCC		28.8025159151
61 (in isoform 2)Ubiquitination-21.7221890473
65SumoylationVKSPPYIFSPIPFLG
CCCCCEECCCCCCCC		6.15-
66PhosphorylationKSPPYIFSPIPFLGH
CCCCEECCCCCCCCH		16.62-
72PhosphorylationFSPIPFLGHAIAFGK
CCCCCCCCHHHHHCC		14.46-
78 (in isoform 2)Ubiquitination-22.1021890473
81 (in isoform 2)Ubiquitination-33.3521890473
85SumoylationGKSPIEFLENAYEKY
CCCHHHHHHHHHHHH		3.00-
85UbiquitinationGKSPIEFLENAYEKY
CCCHHHHHHHHHHHH		3.00-
91UbiquitinationFLENAYEKYGPVFSF
HHHHHHHHHCCEEEE		42.71-
97UbiquitinationEKYGPVFSFTMVGKT
HHHCCEEEEEECCCC		21.75-
97 (in isoform 1)Ubiquitination-21.7521890473
114 (in isoform 2)Ubiquitination-12.0221890473
121UbiquitinationAALLFNSKNEDLNAE
HHHHHCCCCCCCCHH		66.51-
127UbiquitinationSKNEDLNAEDVYSRL
CCCCCCCHHHHHHHH		22.97-
127 (in isoform 1)Ubiquitination-22.9721890473
131PhosphorylationDLNAEDVYSRLTTPV
CCCHHHHHHHHCCCC		10.6127642862
132PhosphorylationLNAEDVYSRLTTPVF
CCHHHHHHHHCCCCC		22.21-
135PhosphorylationEDVYSRLTTPVFGKG
HHHHHHHCCCCCCCC		28.1324719451
136PhosphorylationDVYSRLTTPVFGKGV
HHHHHHCCCCCCCCC		23.2621815630
138PhosphorylationYSRLTTPVFGKGVAY
HHHHCCCCCCCCCCC		10.43-
141PhosphorylationLTTPVFGKGVAYDVP
HCCCCCCCCCCCCCC		38.4524719451
141UbiquitinationLTTPVFGKGVAYDVP
HCCCCCCCCCCCCCC		38.4521890473
142PhosphorylationTTPVFGKGVAYDVPN
CCCCCCCCCCCCCCC		15.07-
145PhosphorylationVFGKGVAYDVPNPVF
CCCCCCCCCCCCHHH		18.3127642862
147UbiquitinationGKGVAYDVPNPVFLE
CCCCCCCCCCHHHHH		3.00-
147 (in isoform 1)Ubiquitination-3.0021890473
156UbiquitinationNPVFLEQKKMLKSGL
CHHHHHHHHHHHCCC		30.6721890473
1562-HydroxyisobutyrylationNPVFLEQKKMLKSGL
CHHHHHHHHHHHCCC		30.67-
156MalonylationNPVFLEQKKMLKSGL
CHHHHHHHHHHHCCC		30.6726320211
156AcetylationNPVFLEQKKMLKSGL
CHHHHHHHHHHHCCC		30.6726051181
157UbiquitinationPVFLEQKKMLKSGLN
HHHHHHHHHHHCCCC		49.51-
160UbiquitinationLEQKKMLKSGLNIAH
HHHHHHHHCCCCHHH		38.6921890473
161PhosphorylationEQKKMLKSGLNIAHF
HHHHHHHCCCCHHHH		44.5530576142
162UbiquitinationQKKMLKSGLNIAHFK
HHHHHHCCCCHHHHH		22.58-
162 (in isoform 2)Ubiquitination-22.5821890473
162 (in isoform 1)Ubiquitination-22.5821890473
166UbiquitinationLKSGLNIAHFKQHVS
HHCCCCHHHHHHHHH		10.86-
166 (in isoform 1)Ubiquitination-10.8621890473
167 (in isoform 2)Ubiquitination-27.0021890473
175UbiquitinationFKQHVSIIEKETKEY
HHHHHHHHHHHHHHH		4.88-
177UbiquitinationQHVSIIEKETKEYFE
HHHHHHHHHHHHHHH		61.34-
178 (in isoform 2)Ubiquitination-52.93-
180UbiquitinationSIIEKETKEYFESWG
HHHHHHHHHHHHHHC		52.05-
183UbiquitinationEKETKEYFESWGESG
HHHHHHHHHHHCHHC		6.68-
183 (in isoform 1)Ubiquitination-6.6821890473
186UbiquitinationTKEYFESWGESGEKN
HHHHHHHHCHHCCCC		13.84-
186 (in isoform 1)Ubiquitination-13.8421890473
213UbiquitinationASHCLHGKEIRSQLN
HHHHHCHHHHHHHHH		38.94-
219UbiquitinationGKEIRSQLNEKVAQL
HHHHHHHHHHHHHHH		10.62-
219 (in isoform 1)Ubiquitination-10.6221890473
243 (in isoform 2)Ubiquitination-38.2221890473
259 (in isoform 2)Ubiquitination-44.5221890473
261UbiquitinationDRAHREIKDIFYKAI
HHHHHHHHHHHHHHH		39.7621890473
266UbiquitinationEIKDIFYKAIQKRRQ
HHHHHHHHHHHHHHH		28.4121890473
266AcetylationEIKDIFYKAIQKRRQ
HHHHHHHHHHHHHHH		28.4127452117
267UbiquitinationIKDIFYKAIQKRRQS
HHHHHHHHHHHHHHH		9.69-
267 (in isoform 1)Ubiquitination-9.6921890473
272UbiquitinationYKAIQKRRQSQEKID
HHHHHHHHHHHHHHH		47.76-
272 (in isoform 1)Ubiquitination-47.7621890473
274PhosphorylationAIQKRRQSQEKIDDI
HHHHHHHHHHHHHHH		38.2026434776
277UbiquitinationKRRQSQEKIDDILQT
HHHHHHHHHHHHHHH		43.74-
283UbiquitinationEKIDDILQTLLDATY
HHHHHHHHHHHHHHC		30.36-
297UbiquitinationYKDGRPLTDDEVAGM
CCCCCCCCHHHHHHH		44.05-
313 (in isoform 2)Ubiquitination-30.9521890473
337 (in isoform 2)Ubiquitination-6.3721890473
342UbiquitinationKKCYLEQKTVCGENL
HHHHCCCCCCCCCCC		33.28-
348UbiquitinationQKTVCGENLPPLTYD
CCCCCCCCCCCCCHH		43.03-
348 (in isoform 1)Ubiquitination-43.0321890473
358UbiquitinationPLTYDQLKDLNLLDR
CCCHHHHHHCCHHHH		55.31-
364UbiquitinationLKDLNLLDRCIKETL
HHHCCHHHHHHHHHH		46.72-
364 (in isoform 1)Ubiquitination-46.7221890473
365MethylationKDLNLLDRCIKETLR
HHCCHHHHHHHHHHH		24.83-
368UbiquitinationNLLDRCIKETLRLRP
CHHHHHHHHHHHCCC		48.55-
370PhosphorylationLDRCIKETLRLRPPI
HHHHHHHHHHCCCCE		16.5124719451
371MethylationDRCIKETLRLRPPIM
HHHHHHHHHCCCCEE		5.21-
374UbiquitinationIKETLRLRPPIMIMM
HHHHHHCCCCEEEEE		28.63-
376PhosphorylationETLRLRPPIMIMMRM
HHHHCCCCEEEEEEC		23.50-
386PhosphorylationIMMRMARTPQTVAGY
EEEECCCCCCEECCC		15.3720068231
389PhosphorylationRMARTPQTVAGYTIP
ECCCCCCEECCCCCC		17.3320068231
393PhosphorylationTPQTVAGYTIPPGHQ
CCCEECCCCCCCCCE		7.55-
394PhosphorylationPQTVAGYTIPPGHQV
CCEECCCCCCCCCEE		26.5320068231
404PhosphorylationPGHQVCVSPTVNQRL
CCCEEEECCCCCHHH		15.1020068231
410PhosphorylationVSPTVNQRLKDSWVE
ECCCCCHHHHHCHHH		38.20-
412UbiquitinationPTVNQRLKDSWVERL
CCCCHHHHHCHHHCC		52.48-
418UbiquitinationLKDSWVERLDFNPDR
HHHCHHHCCCCCCCH		29.91-
418 (in isoform 1)Ubiquitination-29.9121890473
433PhosphorylationYLQDNPASGEKFAYV
HCCCCCCCCCCCEEC		49.0625159151
436UbiquitinationDNPASGEKFAYVPFG
CCCCCCCCCEECCCC		38.5321890473
439PhosphorylationASGEKFAYVPFGAGR
CCCCCCEECCCCCCC		16.28-
442UbiquitinationEKFAYVPFGAGRHRC
CCCEECCCCCCCCCC		8.16-
442 (in isoform 1)Ubiquitination-8.1621890473
456PhosphorylationCIGENFAYVQIKTIW
CCCCCCEEEEHHHHH		6.69-
470PhosphorylationWSTMLRLYEFDLIDG
HHHHHHHHHHCCCCC		14.2325072903
478PhosphorylationEFDLIDGYFPTVNYT
HHCCCCCCCCCCCEE		11.5725072903
481PhosphorylationLIDGYFPTVNYTTMI
CCCCCCCCCCEEEEE		16.1025072903
484PhosphorylationGYFPTVNYTTMIHTP
CCCCCCCEEEEEECC		10.1525072903
485PhosphorylationYFPTVNYTTMIHTPE
CCCCCCEEEEEECCC		12.5125072903
486PhosphorylationFPTVNYTTMIHTPEN
CCCCCEEEEEECCCC		12.0825072903
490PhosphorylationNYTTMIHTPENPVIR
CEEEEEECCCCCCCC		22.7525072903
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 CP51A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CP51A_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
12Phosphorylation19 (7)V ⇒ Ars2229188
  • Lifespan
25918517
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN420_HUMANZNF420physical
21988832
POTEI_HUMANPOTEIphysical
26186194
YES_HUMANYES1physical
26186194
RASH_HUMANHRASphysical
26186194
CCNY_HUMANCCNYphysical
26186194
POTEI_HUMANPOTEIphysical
28514442
ACTBL_HUMANACTBL2physical
28514442
RASH_HUMANHRASphysical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CP51A_HUMAN

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Related Literatures of Post-Translational Modification

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