Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RCN2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RCN2 Not known. Binds calcium. Belongs to the CREC family. Note: This description may include information from UniProtKB.
Protein type: Endoplasmic reticulum
Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; nucleolus
Molecular Function: protein binding; calcium ion binding
Reference #:  Q14257 (UniProtKB)
Alt. Names/Synonyms: Calcium-binding protein ERC-55; E6-binding protein; E6BP; ERC-55; ERC55; RCN2; reticulocalbin 2, EF-hand calcium binding domain; reticulocalbin 2, EF-hand calcium binding domain (endoplasmic reticulum calcium-binding protein, 55kD); Reticulocalbin-2; TCBP49
Gene Symbols: RCN2
Molecular weight: 36,876 Da
Basal Isoelectric point: 4.26  Predict pI for various phosphorylation states
Select Structure to View Below

RCN2

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 - gap
0 4 Y30-p GKAEELHyPLGERRS
0 1 K56-u EDVDEYVkLGHEEQQ
0 1 K64-u LGHEEQQkRLQAIIK
1 1 A68 EQQkRLQAIIKKIDL
0 2 K103-u HYAMQEAkQQFVEYD
0 1 T137-p VIDFDENtALDDAEE
0 2 K232-u PEWILVEkDRFVNDY
0 2 Y311-p GRQLHDDyFYHDEL_
  mouse

 
S6-p __MQRRPsVAAREAR
Y68 SKAEELHYPQGEHRA
K94 EDVDEYVKLGHEEQQ
R102 LGHEEQQRRLQsIIK
S106-p EQQRRLQsIIKKIDS
K141 HYAMQEAKQQFVEYD
T175 VIDFDENTALDDTEE
K270 PEWILVEKDRFVNDY
Y349 GRQLHDDYFYHDEL_
  rat

 
- gap
Y33 SKAEELHYPQGEHRA
K59 EDVDEYVKLGHEEQQ
R67 LGHEEQQRRLQsIIK
S71-p EQQRRLQsIIKKIDS
K106 HYAMQEAKQQFVEYD
T140 VIDFDENTALDDTEE
K235 PEWILVEKDRFVNDY
Y314 GRQLHDDYFYHDEL_
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.