RCAN1_HUMAN - dbPTM
RCAN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCAN1_HUMAN
UniProt AC P53805
Protein Name Calcipressin-1
Gene Name RCAN1
Organism Homo sapiens (Human).
Sequence Length 252
Subcellular Localization
Protein Description Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. [PubMed: 12809556 Could play a role during central nervous system development (By similarity]
Protein Sequence MEDGVAGPQLGAAAEAAEAAEARARPGVTLRPFAPLSGAAEADEGGGDWSFIDCEMEEVDLQDLPSATIACHLDPRVFVDGLCRAKFESLFRTYDKDITFQYFKSFKRVRINFSNPFSAADARLQLHKTEFLGKEMKLYFAQTLHIGSSHLAPPNPDKQFLISPPASPPVGWKQVEDATPVINYDLLYAISKLGPGEKYELHAATDTTPSVVVHVCESDQEKEEEEEMERMRRPKPKIIQTRRPEYTPIHLS
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
28 (in isoform 4)Phosphorylation-5.16-
32 (in isoform 4)Phosphorylation-32.63-
86UbiquitinationVDGLCRAKFESLFRT
CCHHHHHHHHHHHHH
30.25-
93 (in isoform 2)Phosphorylation-28.83-
94PhosphorylationFESLFRTYDKDITFQ
HHHHHHHCCCCCCHH
19.4222817900
96NeddylationSLFRTYDKDITFQYF
HHHHHCCCCCCHHHH
40.39-
104NeddylationDITFQYFKSFKRVRI
CCCHHHHHCCCEEEE
50.47-
107NeddylationFQYFKSFKRVRINFS
HHHHHCCCEEEEECC
58.01-
108PhosphorylationQYFKSFKRVRINFSN
HHHHCCCEEEEECCC
22.4212063245
108 (in isoform 2)Phosphorylation-22.42-
112PhosphorylationSFKRVRINFSNPFSA
CCCEEEEECCCCCCH
24.5912063245
112 (in isoform 2)Phosphorylation-24.59-
128UbiquitinationDARLQLHKTEFLGKE
HHHHHHHHHHHCCHH
59.34-
129PhosphorylationARLQLHKTEFLGKEM
HHHHHHHHHHCCHHH
22.63-
134UbiquitinationHKTEFLGKEMKLYFA
HHHHHCCHHHHHHEE
57.70-
148PhosphorylationAQTLHIGSSHLAPPN
EEEEECCCCCCCCCC
17.62-
163PhosphorylationPDKQFLISPPASPPV
CCCCCEECCCCCCCC
27.2912809556
163DephosphorylationPDKQFLISPPASPPV
CCCCCEECCCCCCCC
27.2912063245
167PhosphorylationFLISPPASPPVGWKQ
CEECCCCCCCCCCCC
35.1912809556
179PhosphorylationWKQVEDATPVINYDL
CCCCCCCCCCCCHHH
30.3425332170
184PhosphorylationDATPVINYDLLYAIS
CCCCCCCHHHHHHHH
9.2428796482
188PhosphorylationVINYDLLYAISKLGP
CCCHHHHHHHHHHCC
14.8028796482
191PhosphorylationYDLLYAISKLGPGEK
HHHHHHHHHHCCCCC
17.4128796482
192UbiquitinationDLLYAISKLGPGEKY
HHHHHHHHHCCCCCE
51.88-
207PhosphorylationELHAATDTTPSVVVH
EEEEECCCCCCEEEE
35.9327251275
208PhosphorylationLHAATDTTPSVVVHV
EEEECCCCCCEEEEE
19.1727251275
210PhosphorylationAATDTTPSVVVHVCE
EECCCCCCEEEEEEC
26.0030576142
218PhosphorylationVVVHVCESDQEKEEE
EEEEEECCHHHHHHH
39.1930576142
241PhosphorylationPKPKIIQTRRPEYTP
CCCCEECCCCCCCCC
20.4523186163
247PhosphorylationQTRRPEYTPIHLS--
CCCCCCCCCCCCC--
17.6921965663
252PhosphorylationEYTPIHLS-------
CCCCCCCC-------
24.8228555341

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
93SPhosphorylationKinasePRKACAP17612
GPS
108SPhosphorylationKinaseGSK-3_GROUP-PhosphoELM
112SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
163SPhosphorylationKinaseGSK3BP49841
PSP
163SPhosphorylationKinaseMAP3K3Q99759
GPS
163SPhosphorylationKinaseGSK-FAMILY-GPS
167SPhosphorylationKinaseDYRK1AQ13627
PSP
167SPhosphorylationKinaseMAP3K3Q99759
GPS
167SPhosphorylationKinaseMAPK-FAMILY-GPS
247TPhosphorylationKinaseDYRK1AQ13627
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:18575781
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:22426484

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCAN1_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 RCAN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2BA_HUMANPPP3CAphysical
10861295
STAT2_HUMANSTAT2physical
22426484
TOLIP_HUMANTOLLIPphysical
19716405
IRAK1_HUMANIRAK1physical
19716405
TRAF6_HUMANTRAF6physical
19716405
HS90A_HUMANHSP90AA1physical
19716405
FBW1A_HUMANBTRCphysical
18575781
FBXW4_HUMANFBXW4physical
18575781
FBW1B_HUMANFBXW11physical
18575781
A4_HUMANAPPphysical
21832049
PP2BA_HUMANPPP3CAphysical
23118980
UBP22_HUMANUSP22physical
25546086
PP2BC_HUMANPPP3CCphysical
28514442
PP2BA_HUMANPPP3CAphysical
28514442
GSK3A_HUMANGSK3Aphysical
28514442
PP2BB_HUMANPPP3CBphysical
28514442
CANB1_HUMANPPP3R1physical
28514442
ARMT1_HUMANC6orf211physical
28514442
CYTT_HUMANCST2physical
28514442
CYTD_HUMANCST5physical
28514442
GSK3B_HUMANGSK3Bphysical
28514442
ZG16B_HUMANZG16Bphysical
28514442
CLC3A_HUMANCLEC3Aphysical
28514442

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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCAN1_HUMAN

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Related Literatures of Post-Translational Modification

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