Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Adenylyl cyclase-associated protein 2  

UniProtKB / Swiss-Prot ID :  CAP2_HUMAN

Gene Name (Synonyms) : 
CAP2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Peripheral membrane protein (By similarity). 

Protein Function :  May have a regulatory bifunctional role. 

Protein Sequence MANMQGLVERLERAVSRLESLSAESHRPPGNCGEVNGVIAGVAPSVEAFDKLMDSMVAEFLKNSRILAGD...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
311T -> A (in dbSNP:rs34620829). VAR_033717
316Y -> C (in dbSNP:rs34206659). VAR_033718
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
287PhosphotyrosineDQKTYKNPS
HHHHCCCCH
18.79Phosphositeplus
Link-
299PhosphothreonineQGGQTQSPT
CCCCCCCCC
34.00HPRD
Link-
299PhosphothreonineQGGQTQSPT
CCCCCCCCC
34.00Phosphositeplus
Link-
301PhosphoserineGQTQSPTKS
CCCCCCCCC
37.61HPRD
Link-
301PhosphoserineGQTQSPTKS
CCCCCCCCC
37.61PhosphoELM
Link-
301PhosphoserineGQTQSPTKS
CCCCCCCCC
37.61Phosphositeplus
Link-
301PhosphoserineGQTQSPTKS
CCCCCCCCC
37.61SysPTM
Link-
301Phosphoserine.GQTQSPTKS
CCCCCCCCC
37.61UniProtKB
Link-
305PhosphoserineSPTKSHTPS
CCCCCCCCC
34.76Phosphositeplus
Link-
307PhosphothreonineTKSHTPSPT
CCCCCCCCC
32.33Phosphositeplus
Link-
309PhosphoserineSHTPSPTSP
CCCCCCCCC
41.80HPRD
Link-
309PhosphoserineSHTPSPTSP
CCCCCCCCC
41.80Phosphositeplus
Link-
311PhosphothreonineTPSPTSPKS
CCCCCCCCC
63.10Phosphositeplus
Link-
312PhosphoserinePSPTSPKSY
CCCCCCCCC
33.44HPRD
Link-
312PhosphoserinePSPTSPKSY
CCCCCCCCC
33.44Phosphositeplus
Link-
355PhosphotyrosineKQVAYIFKC
CEEEEEEEE
14.18Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PR40A_HUMANphysical interactionMINT-61869MINT15231748
ACTG_HUMANin vivoHPRD:10808HPRD8761950
CAP1_HUMANin vivo
yeast 2-hybrid
HPRD:10808HPRD8761950
PR40A_HUMANyeast 2-hybridHPRD:10808HPRD15231748
CAP1_HUMANENSP00000229922STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures