RCN1_HUMAN - dbPTM
RCN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCN1_HUMAN
UniProt AC Q15293
Protein Name Reticulocalbin-1
Gene Name RCN1
Organism Homo sapiens (Human).
Sequence Length 331
Subcellular Localization Endoplasmic reticulum lumen.
Protein Description May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment..
Protein Sequence MARGGRGRRLGLALGLLLALVLAPRVLRAKPTVRKERVVRPDSELGERPPEDNQSFQYDHEAFLGKEDSKTFDQLTPDESKERLGKIVDRIDNDGDGFVTTEELKTWIKRVQKRYIFDNVAKVWKDYDRDKDDKISWEEYKQATYGYYLGNPAEFHDSSDHHTFKKMLPRDERRFKAADLNGDLTATREEFTAFLHPEEFEHMKEIVVLETLEDIDKNGDGFVDQDEYIADMFSHEENGPEPDWVLSEREQFNEFRDLNKDGKLDKDEIRHWILPQDYDHAQAEARHLVYESDKNKDEKLTKEEILENWNMFVGSQATNYGEDLTKNHDEL
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
43PhosphorylationERVVRPDSELGERPP
HHEECCCCCCCCCCC		37.0929457462
53N-linked_GlycosylationGERPPEDNQSFQYDH
CCCCCCCCCCCCCCH		37.4219159218
54UbiquitinationERPPEDNQSFQYDHE
CCCCCCCCCCCCCHH		58.92-
55PhosphorylationRPPEDNQSFQYDHEA
CCCCCCCCCCCCHHH		22.1425850435
55O-linked_GlycosylationRPPEDNQSFQYDHEA
CCCCCCCCCCCCHHH		22.1430059200
58PhosphorylationEDNQSFQYDHEAFLG
CCCCCCCCCHHHHCC		19.7725850435
69PhosphorylationAFLGKEDSKTFDQLT
HHCCCCCCCCHHHCC		34.3923312004
70UbiquitinationFLGKEDSKTFDQLTP
HCCCCCCCCHHHCCC		66.5821890473
702-HydroxyisobutyrylationFLGKEDSKTFDQLTP
HCCCCCCCCHHHCCC		66.58-
70AcetylationFLGKEDSKTFDQLTP
HCCCCCCCCHHHCCC		66.5827452117
70UbiquitinationFLGKEDSKTFDQLTP
HCCCCCCCCHHHCCC		66.5821890473
71UbiquitinationLGKEDSKTFDQLTPD
CCCCCCCCHHHCCCC		36.07-
71PhosphorylationLGKEDSKTFDQLTPD
CCCCCCCCHHHCCCC		36.0725159151
76PhosphorylationSKTFDQLTPDESKER
CCCHHHCCCCHHHHH		24.0620068231
80PhosphorylationDQLTPDESKERLGKI
HHCCCCHHHHHHHHH		47.3929255136
81SumoylationQLTPDESKERLGKIV
HCCCCHHHHHHHHHH		44.82-
812-HydroxyisobutyrylationQLTPDESKERLGKIV
HCCCCHHHHHHHHHH		44.82-
81AcetylationQLTPDESKERLGKIV
HCCCCHHHHHHHHHH		44.8223236377
81MethylationQLTPDESKERLGKIV
HCCCCHHHHHHHHHH		44.82-
83MethylationTPDESKERLGKIVDR
CCCHHHHHHHHHHHH		53.1024411213
86UbiquitinationESKERLGKIVDRIDN
HHHHHHHHHHHHHCC		44.1221890473
86AcetylationESKERLGKIVDRIDN
HHHHHHHHHHHHHCC		44.1219608861
86UbiquitinationESKERLGKIVDRIDN
HHHHHHHHHHHHHCC		44.1221890473
90UbiquitinationRLGKIVDRIDNDGDG
HHHHHHHHHCCCCCC		27.54-
90MethylationRLGKIVDRIDNDGDG
HHHHHHHHHCCCCCC		27.54115490981
100PhosphorylationNDGDGFVTTEELKTW
CCCCCCEEHHHHHHH		26.65-
101PhosphorylationDGDGFVTTEELKTWI
CCCCCEEHHHHHHHH		23.35-
105UbiquitinationFVTTEELKTWIKRVQ
CEEHHHHHHHHHHHH		45.1321890473
105UbiquitinationFVTTEELKTWIKRVQ
CEEHHHHHHHHHHHH		45.1321890473
114UbiquitinationWIKRVQKRYIFDNVA
HHHHHHHHHHHHHHH		16.82-
114MethylationWIKRVQKRYIFDNVA
HHHHHHHHHHHHHHH		16.82115490993
115PhosphorylationIKRVQKRYIFDNVAK
HHHHHHHHHHHHHHH		16.9928152594
1222-HydroxyisobutyrylationYIFDNVAKVWKDYDR
HHHHHHHHHHHHCCC		44.33-
122UbiquitinationYIFDNVAKVWKDYDR
HHHHHHHHHHHHCCC		44.3321890473
122UbiquitinationYIFDNVAKVWKDYDR
HHHHHHHHHHHHCCC		44.3321890473
1252-HydroxyisobutyrylationDNVAKVWKDYDRDKD
HHHHHHHHHCCCCCC		49.77-
125UbiquitinationDNVAKVWKDYDRDKD
HHHHHHHHHCCCCCC		49.77-
1342-HydroxyisobutyrylationYDRDKDDKISWEEYK
CCCCCCCCCCHHHHH		49.09-
134AcetylationYDRDKDDKISWEEYK
CCCCCCCCCCHHHHH		49.0926051181
134UbiquitinationYDRDKDDKISWEEYK
CCCCCCCCCCHHHHH		49.09-
136PhosphorylationRDKDDKISWEEYKQA
CCCCCCCCHHHHHHH		33.8925159151
141UbiquitinationKISWEEYKQATYGYY
CCCHHHHHHHHCCCC		36.4121890473
141UbiquitinationKISWEEYKQATYGYY
CCCHHHHHHHHCCCC		36.4121890473
145PhosphorylationEEYKQATYGYYLGNP
HHHHHHHCCCCCCCH		13.2225884760
147PhosphorylationYKQATYGYYLGNPAE
HHHHHCCCCCCCHHH		5.77-
158PhosphorylationNPAEFHDSSDHHTFK
CHHHCCCCCCCHHHH		29.1525627689
159PhosphorylationPAEFHDSSDHHTFKK
HHHCCCCCCCHHHHH		47.2025627689
1652-HydroxyisobutyrylationSSDHHTFKKMLPRDE
CCCCHHHHHHCCCCH		38.13-
165UbiquitinationSSDHHTFKKMLPRDE
CCCCHHHHHHCCCCH		38.1321890473
165AcetylationSSDHHTFKKMLPRDE
CCCCHHHHHHCCCCH		38.1326051181
165UbiquitinationSSDHHTFKKMLPRDE
CCCCHHHHHHCCCCH		38.1321890473
166AcetylationSDHHTFKKMLPRDER
CCCHHHHHHCCCCHH		41.29156545
176UbiquitinationPRDERRFKAADLNGD
CCCHHHHHHHHCCCC		40.6321890473
176UbiquitinationPRDERRFKAADLNGD
CCCHHHHHHHHCCCC		40.6321890473
1762-HydroxyisobutyrylationPRDERRFKAADLNGD
CCCHHHHHHHHCCCC		40.63-
185PhosphorylationADLNGDLTATREEFT
HHCCCCCCEEHHHHH		30.6225159151
187PhosphorylationLNGDLTATREEFTAF
CCCCCCEEHHHHHHH		33.1221406692
192PhosphorylationTATREEFTAFLHPEE
CEEHHHHHHHCCHHH		21.5625022875
192O-linked_GlycosylationTATREEFTAFLHPEE
CEEHHHHHHHCCHHH		21.56OGP
203SulfoxidationHPEEFEHMKEIVVLE
CHHHHHHHHEEEEEE		3.0730846556
211PhosphorylationKEIVVLETLEDIDKN
HEEEEEEEHHHHHHC		31.1423663014
228PhosphorylationGFVDQDEYIADMFSH
CCCCHHHHHHHHHCC		15.0828102081
234PhosphorylationEYIADMFSHEENGPE
HHHHHHHCCCCCCCC		24.2920071362
249MethylationPDWVLSEREQFNEFR
CCCCCCHHHHHHHHH		39.37115490987
2632-HydroxyisobutyrylationRDLNKDGKLDKDEIR
HHCCCCCCCCHHHHH		64.74-
266AcetylationNKDGKLDKDEIRHWI
CCCCCCCHHHHHHHH		68.6326051181
2662-HydroxyisobutyrylationNKDGKLDKDEIRHWI
CCCCCCCHHHHHHHH		68.63-
270MethylationKLDKDEIRHWILPQD
CCCHHHHHHHHCCCC		19.62115490969
278PhosphorylationHWILPQDYDHAQAEA
HHHCCCCCCHHHHHH		12.3727642862
286MethylationDHAQAEARHLVYESD
CHHHHHHHHHHHHCC		18.38115490975
290PhosphorylationAEARHLVYESDKNKD
HHHHHHHHHCCCCCC		18.9728152594
292PhosphorylationARHLVYESDKNKDEK
HHHHHHHCCCCCCCC		35.8828152594
294UbiquitinationHLVYESDKNKDEKLT
HHHHHCCCCCCCCCC		75.16-
2942-HydroxyisobutyrylationHLVYESDKNKDEKLT
HHHHHCCCCCCCCCC		75.16-
2962-HydroxyisobutyrylationVYESDKNKDEKLTKE
HHHCCCCCCCCCCHH		73.36-
2992-HydroxyisobutyrylationSDKNKDEKLTKEEIL
CCCCCCCCCCHHHHH		72.14-
311SulfoxidationEILENWNMFVGSQAT
HHHHHHHHHCCHHHH		1.8630846556
315PhosphorylationNWNMFVGSQATNYGE
HHHHHCCHHHHCCCC		16.0223663014
315O-linked_GlycosylationNWNMFVGSQATNYGE
HHHHHCCHHHHCCCC		16.02OGP
318PhosphorylationMFVGSQATNYGEDLT
HHCCHHHHCCCCCCC		22.7223663014
320PhosphorylationVGSQATNYGEDLTKN
CCHHHHCCCCCCCCC		19.9623663014
325PhosphorylationTNYGEDLTKNHDEL-
HCCCCCCCCCCCCC-		41.9623663014
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
80SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCN1_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 RCN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UFM1_HUMANUFM1physical
22939629
SC23A_HUMANSEC23Aphysical
22939629
TM1L2_HUMANTOM1L2physical
22939629
SMAP_HUMANC11orf58physical
22939629
SRXN1_HUMANSRXN1physical
22939629
ST1A1_HUMANSULT1A1physical
22939629
ZYX_HUMANZYXphysical
22939629
TBA1B_HUMANTUBA1Bphysical
22939629
GLRX3_HUMANGLRX3physical
22863883
GUAA_HUMANGMPSphysical
22863883
FCL_HUMANTSTA3physical
22863883
CYTSA_HUMANSPECC1Lphysical
26186194
MY18A_HUMANMYO18Aphysical
26186194
WIPI3_HUMANWDR45Bphysical
26186194
VWA1_HUMANVWA1physical
26186194
GNB1L_HUMANGNB1Lphysical
26186194
HNRLL_HUMANHNRNPLLphysical
26186194
LRFN1_HUMANLRFN1physical
26186194
PTH_HUMANPTRH1physical
26186194
NDST2_HUMANNDST2physical
26186194
RNF41_HUMANRNF41physical
26186194
CALR_HUMANCALRphysical
26344197
CCAR1_HUMANCCAR1physical
26344197
CY1_HUMANCYC1physical
26344197
ENOA_HUMANENO1physical
26344197
HCD2_HUMANHSD17B10physical
26344197
ENPL_HUMANHSP90B1physical
26344197
HS74L_HUMANHSPA4Lphysical
26344197
CH10_HUMANHSPE1physical
26344197
IPO9_HUMANIPO9physical
26344197
MYL6_HUMANMYL6physical
26344197
NACA2_HUMANNACA2physical
26344197
TEBP_HUMANPTGES3physical
26344197
RPN2_HUMANRPN2physical
26344197
MPCP_HUMANSLC25A3physical
26344197
PTH_HUMANPTRH1physical
28514442
VWA1_HUMANVWA1physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
RNF41_HUMANRNF41physical
28514442
MY18A_HUMANMYO18Aphysical
28514442
HNRLL_HUMANHNRNPLLphysical
28514442
NEB1_HUMANPPP1R9Aphysical
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 RCN1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53, AND MASS SPECTROMETRY.

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