dbSNO 2.0

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Protein Name: T-complex protein 1 subunit alpha

UniprotKB/SwissProt ID: P11983 (P11983)

Gene Name: Tcp1

Organism: Mus musculus (Mouse)

Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Graphical Visualization of S-nitrosylation Sites:

InterPro ID	Domain Name
IPR012715	Chap_CCT_alpha
IPR017998	Chaperone_TCP-1
IPR002194	Chaperonin_TCP-1_CS
IPR002423	Cpn60/GroEL/TCP-1
IPR027409	GroEL-like_apical_dom_sf
IPR027413	GROEL-like_equatorial_sf
IPR027410	TCP-1-like_intermed_sf
IPR053374	TCP-1_chaperonin
IPR054827	thermosome_alpha

The S-nitrosylation sites of P11983

No.	Position	S-nitrosylated Peptide	Secondary Structure of S-nitrosylated Peptide	Solvent Accessibility of nitrosylated Site	PubMed ID
1	147	IINTDELGRD C LINAAKTSMS	CCCCCEECCC C CCCHHHHHHC	3.86%
2	236	PKRIVNAKIA C LDFSLQKTKM	CCCCCEECCC C CCCHHHHHHC	4.22%	21278135
3	357	QAEEVVQERI C DDELILIKNT	CCCCCEECCC C CCCHHHHHHC	7.26%	20925432 21278135
4	385	IILRGANDFM C DEMERSLHDA	CCCCCEECCC C CCCHHHHHHC	3.96%	24926564 21278135
5	397	EMERSLHDAL C VVKRVLELKS	CCCCCEECCC C CCCHHHHHHC	3.38%	24926564 20925432 21278135
6	76	EVEHPAAKVL C ELADLQDKEV	CCCCCEECCC C CCCHHHHHHC	4.51%

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