CA2D1_HUMAN - dbPTM
CA2D1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CA2D1_HUMAN
UniProt AC P54289
Protein Name Voltage-dependent calcium channel subunit alpha-2/delta-1
Gene Name CACNA2D1
Organism Homo sapiens (Human).
Sequence Length 1103
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling (By similarity)..
Protein Sequence MAAGCLLALTLTLFQSLLIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVNQLVDIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAKDDLDPEKNDSEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNIQNPKSQEPVTLDFLDAELENDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYSFYYIKAKLEETITQARYSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVEMEDDDFTASLSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCPCDTRLLIQAEQTSDGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWYIIGIQFLLLWLVSGSTHRLL
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
52PhosphorylationVTLAKTASGVNQLVD
HHHHHHHHHHHHHHH		48.80-
92N-linked_GlycosylationDIEKLLSNRSKALVR
HHHHHHCCHHHHHHH		52.82UniProtKB CARBOHYD
119PhosphorylationQWREDFASNEVVYYN
HHHHHHHCCEEEEEE		33.25-
136N-linked_GlycosylationDDLDPEKNDSEPGSQ
CCCCCCCCCCCCCCC		57.27UniProtKB CARBOHYD
184N-linked_GlycosylationTIVLNELNWTSALDE
EEEEECCCHHHHHHH		33.53UniProtKB CARBOHYD
217PhosphorylationSATGLARYYPASPWV
HCHHHHHHCCCCCCC		14.2720393185
218PhosphorylationATGLARYYPASPWVD
CHHHHHHCCCCCCCC		6.1820393185
227PhosphorylationASPWVDNSRTPNKID
CCCCCCCCCCCCCCC		32.8220393185
236PhosphorylationTPNKIDLYDVRRRPW
CCCCCCCCCCCCCCC		14.51-
324N-linked_GlycosylationVLKDAVNNITAKGIT
HHHHHHHHCCCCCCC		26.79UniProtKB CARBOHYD
348N-linked_GlycosylationFEQLLNYNVSRANCN
HHHHHCCCCCCCCCC		24.98UniProtKB CARBOHYD
468N-linked_GlycosylationTGTLPVFNITGQFEN
EECCEEEEECCCCCC		31.01UniProtKB CARBOHYD
475N-linked_GlycosylationNITGQFENKTNLKNQ
EECCCCCCCCCCCCC		58.71UniProtKB CARBOHYD
505PhosphorylationKRLTPRFTLCPNGYY
HHHCCCEEECCCCEE		28.8224719451
530 (in isoform 3)Acetylation-35.98-
604N-linked_GlycosylationERYIDKGNRTYTWTP
CEEEECCCCEEEEEE		38.57UniProtKB CARBOHYD
613N-linked_GlycosylationTYTWTPVNGTDYSLA
EEEEEECCCCCCEEE		49.18UniProtKB CARBOHYD
675N-linked_GlycosylationNDLKISDNNTEFLLN
CCEECCCCCCEEEEC		51.00UniProtKB CARBOHYD
781N-linked_GlycosylationVFTAPYFNKSGPGAY
EEEECCCCCCCCCHH		31.57UniProtKB CARBOHYD
824N-linked_GlycosylationDVNSWIENFTKTSIR
EHHHHHHHCCCCCCC		40.53UniProtKB CARBOHYD
888N-linked_GlycosylationSLMRHLVNISVYAFN
HHHHHHHHEEEEECC		27.46UniProtKB CARBOHYD
895N-linked_GlycosylationNISVYAFNKSYDYQS
HEEEEECCCCCCCCC		24.96UniProtKB CARBOHYD
918PhosphorylationKQGAGHRSAYVPSVA
CCCCCCCCCCCCCHH		20.4824043423
920PhosphorylationGAGHRSAYVPSVADI
CCCCCCCCCCCHHHH		17.7224043423
923PhosphorylationHRSAYVPSVADILQI
CCCCCCCCHHHHHHH		21.6424043423
935PhosphorylationLQIGWWATAAAWSIL
HHHHHHHHHHHHHHH		11.7824043423
940PhosphorylationWATAAAWSILQQFLL
HHHHHHHHHHHHHHH		14.5424043423
948PhosphorylationILQQFLLSLTFPRLL
HHHHHHHHCHHHHHH		27.7524043423
950PhosphorylationQQFLLSLTFPRLLEA
HHHHHHCHHHHHHHH		28.3724043423
985N-linked_GlycosylationQTQYFFDNDSKSFSG
CEEEEECCCCCCEEE		50.74UniProtKB CARBOHYD
989PhosphorylationFFDNDSKSFSGVLDC
EECCCCCCEEEEEEC		28.7027732954
991PhosphorylationDNDSKSFSGVLDCGN
CCCCCCEEEEEECCC		34.7727732954
998N-linked_GlycosylationSGVLDCGNCSRIFHG
EEEEECCCCCCEECC		27.24UniProtKB CARBOHYD
1000PhosphorylationVLDCGNCSRIFHGEK
EEECCCCCCEECCEE		32.2027732954
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 CA2D1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CA2D1_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 CA2D1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB11A_HUMANRAB11Aphysical
22939629
NDUS4_HUMANNDUFS4physical
22939629
STT3B_HUMANSTT3Bphysical
22939629
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
D00332 Gabapentin (JAN/USAN/INN); Neurontin (TN); Gralise (TN)
D02716 Pregabalin (JAN/USAN/INN); Lyrica (TN)
D09539 Gabapentin enacarbil (JAN/USAN/INN); Horizant (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CA2D1_HUMAN

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Related Literatures of Post-Translational Modification

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