CA2D2_HUMAN - dbPTM
CA2D2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CA2D2_HUMAN
UniProt AC Q9NY47
Protein Name Voltage-dependent calcium channel subunit alpha-2/delta-2
Gene Name CACNA2D2
Organism Homo sapiens (Human).
Sequence Length 1150
Subcellular Localization Membrane
Single-pass type I membrane protein . Colocalizes with CACNA1A in lipid raft fractions..
Protein Description The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosis..
Protein Sequence MAVPARTCGASRPGPARTARPWPGCGPHPGPGTRRPTSGPPRPLWLLLPLLPLLAAPGASAYSFPQQHTMQHWARRLEQEVDGVMRIFGGVQQLREIYKDNRNLFEVQENEPQKLVEKVAGDIESLLDRKVQALKRLADAAENFQKAHRWQDNIKEEDIVYYDAKADAELDDPESEDVERGSKASTLRLDFIEDPNFKNKVNYSYAAVQIPTDIYKGSTVILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHLVQANVRNKKVFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRTVRVFTFSVGQHNYDVTPLQWMACANKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLGLVVTGTLPVFNLTQDGPGEKKNQLILGVMGIDVALNDIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNFREPVTLDFLDAELEDENKEEIRRSMIDGNKGHKQIRTLVKSLDERYIDEVTRNYTWVPIRSTNYSLGLVLPPYSTFYLQANLSDQILQVKLPISKLKDFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVERVWRDQDLNTYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAVELSLGRRTLRPAVVGVKLDLEAWAEKFKVLASNRTHQDQPQKCGPNSHCEMDCEVNNEDLLCVLIDDGGFLVLSNQNHQWDQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYGLIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAEKPLCSQCEAGRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCGRGASFPPSLGVLVSLQLLLLLGLPPRPQPQVLVHASRRL
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
37PhosphorylationGPGTRRPTSGPPRPL
CCCCCCCCCCCCCCH		44.5024719451
125PhosphorylationKVAGDIESLLDRKVQ
HHHHCHHHHHHHHHH		34.27-
162PhosphorylationKEEDIVYYDAKADAE
CHHHEEEEECCCCCC		9.8719664994
215PhosphorylationVQIPTDIYKGSTVIL
EECCCCCCCCCEEEE		16.4728258704
274PhosphorylationAPKKIDLYDVRRRPW
CCCCCCCCCCCCCCC		14.51-
386N-linked_GlycosylationFDQLQNSNITRANCN
HHHHHCCCCCCCCCC		47.3919349973
386N-linked_GlycosylationFDQLQNSNITRANCN
HHHHHCCCCCCCCCC		47.3919349973
413 (in isoform 2)Ubiquitination-32.21-
418N-linked_GlycosylationFEKYNWPNRTVRVFT
HHHCCCCCCEEEEEE		43.82UniProtKB CARBOHYD
478 (in isoform 2)Ubiquitination-49.22-
507N-linked_GlycosylationTGTLPVFNLTQDGPG
EEEECEEECCCCCCC		42.27UniProtKB CARBOHYD
540N-linked_GlycosylationDIKRLTPNYTLGANG
HHHHHCCCCEECCCC		36.87UniProtKB CARBOHYD
595PhosphorylationNKEEIRRSMIDGNKG
CHHHHHHHHCCCCHH		15.39-
611 (in isoform 2)Ubiquitination-48.70-
624N-linked_GlycosylationYIDEVTRNYTWVPIR
HHHHHHCCCEEEEEC		29.26UniProtKB CARBOHYD
686 (in isoform 2)Ubiquitination-5.12-
696N-linked_GlycosylationREYCKDLNASDNNTE
HHHHHCCCCCCCCHH		47.7519349973
699 (in isoform 2)Ubiquitination-50.41-
707 (in isoform 2)Ubiquitination-45.32-
766 (in isoform 2)Ubiquitination-2.45-
773UbiquitinationITRVFPNKAAEDWTE
EEEECCCCCCCCCCC		49.57-
778 (in isoform 4)Ubiquitination-9.3421906983
831PhosphorylationVSTAVELSLGRRTLR
EEEHHHHHCCCCCCC		18.4424670416
847 (in isoform 2)Ubiquitination-36.4221906983
847 (in isoform 3)Ubiquitination-36.4221906983
854 (in isoform 1)Ubiquitination-42.6221906983
854UbiquitinationDLEAWAEKFKVLASN
EHHHHHHHHHHHHCC		42.622190698
854 (in isoform 5)Ubiquitination-42.6221906983
861N-linked_GlycosylationKFKVLASNRTHQDQP
HHHHHHCCCCCCCCC		47.46UniProtKB CARBOHYD
928 (in isoform 2)Ubiquitination-38.22-
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 CA2D2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CA2D2_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 CA2D2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CA2D2_HUMAN !!
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 CA2D2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-386, AND MASSSPECTROMETRY.

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