PCDA2_HUMAN - dbPTM
PCDA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCDA2_HUMAN
UniProt AC Q9Y5H9
Protein Name Protocadherin alpha-2
Gene Name PCDHA2
Organism Homo sapiens (Human).
Sequence Length 948
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain..
Protein Sequence MASSIRRGRGAWTRLLSLLLLAAWEVGSGQLRYSVPEEAKHGTFVGRIAQDLGLELEELVPRLFRVASKRHGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHVEVIVDRPLQVFHVEVEVKDINDNPPIFPMTVKTIRFPESRLLDSRFPLEGASDADIGVNALLSYKLSSSEFFFLDIQANDELSESLSLVLGKSLDREETAEVNLLLVATDGGKPELTGTVQILIKVLDVNDNEPTFAQSVYKVKLLENTANGTLVVKLNASDADEGPNSEIVYSLGSDVSSTIQTKFTIDPISGEIRTKGKLDYEEAKSYEIQVTATDKGTPSMSGHCKISLKLVDINDNTPEVSITSLSLPISENASLGTVIALITVSDRDSGTNGHVTCSLTPHVPFKLVSTFKNYYSLVLDSALDRESVSAYELVVTARDGGSPSLWATTSVSIEVADVNDNAPAFAQPEYTVFVKENNPPGCHIFTVSAWDADAQENALVSYSLVERRVGERALSSYVSVHAESGKVYALQPLDHEEVELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLAPRAGTAAGAVSELVPWSVGAGHVVAKVRAVDADSGYNAWLSYELQLGTGSARIPFRVGLYTGEISTTRALDEADSPRHRLLVLVKDHGEPALTATATVLVSLVESGQAPKASSRAWVGAAGSEATLVDVNVYLIIAICAVSSLLVLTVLLYTALRCSVPPTEGARAPGKPTLVCSSAVGSWSYSQQRRQRVCSGEDPPKTDLMAFSPSLSQGPDSAEEKQLSESEYVGKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
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
17PhosphorylationGAWTRLLSLLLLAAW
HHHHHHHHHHHHHHH
22.89-
33PhosphorylationVGSGQLRYSVPEEAK
HCCCCCEECCCHHHC
23.70-
257N-linked_GlycosylationKLLENTANGTLVVKL
EEEEECCCCEEEEEE
41.78UniProtKB CARBOHYD
265N-linked_GlycosylationGTLVVKLNASDADEG
CEEEEEECCCCCCCC
31.51UniProtKB CARBOHYD
321PhosphorylationKSYEIQVTATDKGTP
CEEEEEEEEECCCCC
13.89-
323PhosphorylationYEIQVTATDKGTPSM
EEEEEEEECCCCCCC
28.95-
362N-linked_GlycosylationLSLPISENASLGTVI
EECCCCCCCCCCEEE
28.21UniProtKB CARBOHYD
506PhosphorylationVGERALSSYVSVHAE
HHHHHHHHEEEEEEC
30.33-
514PhosphorylationYVSVHAESGKVYALQ
EEEEEECCCCEEEEC
44.7029759185
548N-linked_GlycosylationGVPPLGSNVTLQVFV
CCCCCCCCEEEEEEE
29.06UniProtKB CARBOHYD
601PhosphorylationVRAVDADSGYNAWLS
EEEEECCCCCCEEEE
44.9218187866
603PhosphorylationAVDADSGYNAWLSYE
EEECCCCCCEEEEEE
12.98-
660PhosphorylationDHGEPALTATATVLV
CCCCCCCEEEEEEHH
24.86-
662PhosphorylationGEPALTATATVLVSL
CCCCCEEEEEEHHHH
20.02-
664PhosphorylationPALTATATVLVSLVE
CCCEEEEEEHHHHHH
15.26-
679PhosphorylationSGQAPKASSRAWVGA
CCCCCCCCCCEECCC
26.87-
680PhosphorylationGQAPKASSRAWVGAA
CCCCCCCCCEECCCC
30.77-
738PhosphorylationARAPGKPTLVCSSAV
CCCCCCCEEEEECCC
35.00-
743PhosphorylationKPTLVCSSAVGSWSY
CCEEEEECCCCCCCH
23.1122468782
747PhosphorylationVCSSAVGSWSYSQQR
EEECCCCCCCHHHHH
13.2722210691
749PhosphorylationSSAVGSWSYSQQRRQ
ECCCCCCCHHHHHHH
19.3222210691
750PhosphorylationSAVGSWSYSQQRRQR
CCCCCCCHHHHHHHH
12.3028857561
751PhosphorylationAVGSWSYSQQRRQRV
CCCCCCHHHHHHHHH
17.8328857561
760PhosphorylationQRRQRVCSGEDPPKT
HHHHHHCCCCCCCCC
42.2223532336
767PhosphorylationSGEDPPKTDLMAFSP
CCCCCCCCCCEEECC
39.8929759185
773PhosphorylationKTDLMAFSPSLSQGP
CCCCEEECCCHHCCC
12.2129759185
782PhosphorylationSLSQGPDSAEEKQLS
CHHCCCCCHHHHHCC
40.4929759185
789PhosphorylationSAEEKQLSESEYVGK
CHHHHHCCCCCCCCC
36.2628387310
806PhosphorylationQPNPDWRYSASLRAG
CCCCCCCCEEEHHCC
12.34-
807PhosphorylationPNPDWRYSASLRAGM
CCCCCCCEEEHHCCC
11.6524719451
809PhosphorylationPDWRYSASLRAGMHS
CCCCCEEEHHCCCCC
16.6724719451
816PhosphorylationSLRAGMHSSVHLEEA
EHHCCCCCCEEHHHC
25.7628857561
817PhosphorylationLRAGMHSSVHLEEAG
HHCCCCCCEEHHHCC
10.0124719451
819 (in isoform 2)Phosphorylation-29.4823663014
820 (in isoform 2)Phosphorylation-6.2823663014
821 (in isoform 2)Phosphorylation-30.8123663014
824 (in isoform 2)Phosphorylation-23.8123663014
875UbiquitinationKYGPGNPKQSGPGEL
ECCCCCCCCCCCCCC
62.1833845483
891PhosphorylationDKFIIPGSPAIISIR
CCEEECCCCEEEEEE
13.0527050516
896PhosphorylationPGSPAIISIRQEPTN
CCCCEEEEEECCCCC
12.9527732954
902PhosphorylationISIRQEPTNSQIDKS
EEEECCCCCCCCCHH
46.91-

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 PCDA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCDA2_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 PCDA2_HUMAN !!

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

Oops, there are no PPI records of PCDA2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCDA2_HUMAN

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Related Literatures of Post-Translational Modification

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