CPLM-022933

Genbank Nucleotide ID

Cysteine and histidine-rich domain-containing protein 1

Protein Synonyms/Alias

CHORD domain-containing protein 1; CHORD-containing protein 1; CHP-1; Protein morgana

Homo sapiens (Human)

Position	Peptide	Type	References
89	KKELCELKPKFQEHI	ubiquitination	[1]
91	ELCELKPKFQEHIIQ	ubiquitination	[1, 2, 3]
198	YWSCCRRKTSDFNTF	acetylation	[4]
198	YWSCCRRKTSDFNTF	ubiquitination	[1]
220	KGKHMWTKKDAGKKV	acetylation	[4]
289	LWGVIDVKRSYVTMT	ubiquitination	[2, 3, 5, 6]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[4] 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]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]

Functional Description

Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis.

DOMAIN 5 64 CHORD 1.
DOMAIN 157 216 CHORD 2.
DOMAIN 227 316 CS.
REGION 2 77 Interaction with PPP5C (By similarity).
REGION 65 316 Interaction with HSP90AA1 and HSP90AB1
METAL 5 5 Zinc 1.
METAL 10 10 Zinc 1.
METAL 24 24 Zinc 1.
METAL 27 27 Zinc 2.
METAL 42 42 Zinc 2.
METAL 43 43 Zinc 2.
METAL 59 59 Zinc 2.
METAL 64 64 Zinc 1.
METAL 157 157 Zinc 3 (By similarity).
METAL 162 162 Zinc 3 (By similarity).
METAL 176 176 Zinc 3 (By similarity).
METAL 179 179 Zinc 4 (By similarity).
METAL 194 194 Zinc 4 (By similarity).
METAL 195 195 Zinc 4 (By similarity).
METAL 211 211 Zinc 4 (By similarity).
METAL 216 216 Zinc 3 (By similarity).
MOD_RES 2 2 N-acetylalanine.
MOD_RES 47 47 Phosphothreonine.
MOD_RES 51 51 Phosphoserine.
MOD_RES 204 204 Phosphothreonine (By similarity).

3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Direct protein sequencing; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Stress response; Zinc.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0008270; F:zinc ion binding; IEA:Compara.
GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IEA:Compara.
GO:0010824; P:regulation of centrosome duplication; IEA:Compara.
GO:0080134; P:regulation of response to stress; ISS:UniProtKB.
GO:0006950; P:response to stress; IEA:UniProtKB-KW.

IPR007051; CHORD.
IPR007052; CS-like_domain.
IPR017447; CS_domain.
IPR008978; HSP20-like_chaperone.

PF04968; CHORD
PF04969; CS

PS51401; CHORD
PS51203; CS