CPLM-012093

Genbank Nucleotide ID

Protein Synonyms/Alias

Treacher Collins syndrome protein

Homo sapiens (Human)

Position	Peptide	Type	References
155	VANLLSGKSPRKSAE	acetylation	[1]
296	SQVKASEKILQVRAA	acetylation	[1]
600	GPVAVQVKAEKPMDN	acetylation	[1]
755	GPTVTQVKAEKQEDS	acetylation	[1]
755	GPTVTQVKAEKQEDS	sumoylation	[2]
1346	RKGWESRKRKLSGDQ	acetylation	[3]
1362	AARTPRSKKKKKLGA	acetylation	[3]
1403	SGDVKEKKGKGSLGS	acetylation	[4]
1405	DVKEKKGKGSLGSQG	acetylation	[4]
1414	SLGSQGAKDEPEEEL	acetylation	[1, 3]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
[3] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[4] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]

Functional Description

May be involved in nucleolar-cytoplasmic transport. May play a fundamental role in early embryonic development, particularly in development of the craniofacial complex (By similarity). May participate in certain stages of ribosome biogenesis.

DOMAIN 6 38 LisH.
MOD_RES 83 83 Phosphoserine.
MOD_RES 84 84 Phosphothreonine.
MOD_RES 85 85 Phosphoserine.
MOD_RES 87 87 Phosphoserine.
MOD_RES 88 88 Phosphoserine.
MOD_RES 153 153 Phosphoserine.
MOD_RES 155 155 N6-acetyllysine.
MOD_RES 156 156 Phosphoserine.
MOD_RES 171 171 Phosphoserine (By similarity).
MOD_RES 173 173 Phosphothreonine (By similarity).
MOD_RES 233 233 Phosphoserine.
MOD_RES 249 249 Phosphothreonine.
MOD_RES 296 296 N6-acetyllysine.
MOD_RES 310 310 Phosphothreonine.
MOD_RES 316 316 Phosphothreonine.
MOD_RES 339 339 Phosphoserine (By similarity).
MOD_RES 342 342 Phosphoserine (By similarity).
MOD_RES 343 343 Phosphoserine (By similarity).
MOD_RES 347 347 Phosphoserine (By similarity).
MOD_RES 349 349 Phosphoserine (By similarity).
MOD_RES 381 381 Phosphoserine.
MOD_RES 413 413 Phosphoserine (By similarity).
MOD_RES 414 414 Phosphoserine (By similarity).
MOD_RES 417 417 Phosphoserine (By similarity).
MOD_RES 419 419 Phosphoserine (By similarity).
MOD_RES 430 430 Phosphoserine (By similarity).
MOD_RES 446 446 Phosphoserine.
MOD_RES 503 503 Phosphoserine.
MOD_RES 545 545 Phosphoserine (By similarity).
MOD_RES 547 547 Phosphoserine (By similarity).
MOD_RES 548 548 Phosphoserine (By similarity).
MOD_RES 549 549 Phosphoserine (By similarity).
MOD_RES 581 581 Phosphothreonine.
MOD_RES 583 583 Phosphoserine.
MOD_RES 600 600 N6-acetyllysine.
MOD_RES 608 608 Phosphoserine (By similarity).
MOD_RES 610 610 Phosphoserine (By similarity).
MOD_RES 611 611 Phosphoserine (By similarity).
MOD_RES 614 614 Phosphoserine (By similarity).
MOD_RES 615 615 Phosphoserine (By similarity).
MOD_RES 620 620 Phosphoserine.
MOD_RES 679 679 Phosphoserine (By similarity).
MOD_RES 686 686 Phosphothreonine (By similarity).
MOD_RES 693 693 Phosphoserine (By similarity).
MOD_RES 694 694 Phosphoserine (By similarity).
MOD_RES 695 695 Phosphoserine (By similarity).
MOD_RES 755 755 N6-acetyllysine.
MOD_RES 762 762 Phosphoserine.
MOD_RES 764 764 Phosphoserine.
MOD_RES 765 765 Phosphoserine.
MOD_RES 769 769 Phosphoserine.
MOD_RES 771 771 Phosphoserine.
MOD_RES 777 777 Phosphoserine.
MOD_RES 868 868 Phosphoserine.
MOD_RES 870 870 Phosphoserine.
MOD_RES 871 871 Phosphoserine.
MOD_RES 875 875 Phosphoserine.
MOD_RES 877 877 Phosphoserine.
MOD_RES 906 906 Phosphoserine.
MOD_RES 914 914 Phosphothreonine.
MOD_RES 967 967 Phosphoserine.
MOD_RES 983 983 Phosphothreonine.
MOD_RES 998 998 Phosphoserine.
MOD_RES 1111 1111 Phosphoserine.
MOD_RES 1149 1149 Phosphoserine (By similarity).
MOD_RES 1150 1150 Phosphoserine (By similarity).
MOD_RES 1153 1153 Phosphoserine (By similarity).
MOD_RES 1154 1154 Phosphoserine (By similarity).
MOD_RES 1190 1190 Phosphoserine.
MOD_RES 1228 1228 Phosphoserine.
MOD_RES 1234 1234 Phosphothreonine.
MOD_RES 1257 1257 Phosphoserine.
MOD_RES 1350 1350 Phosphoserine.
MOD_RES 1376 1376 Phosphoserine.
MOD_RES 1378 1378 Phosphoserine.
MOD_RES 1407 1407 Phosphoserine.
MOD_RES 1410 1410 Phosphoserine.
MOD_RES 1414 1414 N6-acetyllysine.

Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0005215; F:transporter activity; TAS:ProtInc.
GO:0001501; P:skeletal system development; TAS:ProtInc.
GO:0042790; P:transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IEA:Compara.

IPR006594; LisH_dimerisation.
IPR003993; TCS_treacle.
IPR017859; Treacle-like_TCS.