CETN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CETN2_MOUSE
• UniProt AC: Q9R1K9
• Protein Name: Centrin-2
• Gene Name: Cetn2
• Organism: Mus musculus (Mouse).
• Sequence Length: 172
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Nucleus. Centrosome of S-phase, interphase and mitotic cells.
• Protein Description: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110 (By similarity).; Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with Rad23b appears to stabilize Xpc. In vitro, stimulates DNA binding of the Xpc:Rad23b dimer (By similarity).; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (By similarity).; Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery..
• Protein Sequence: MASNFKKTTMASSAQRKRMSPKPELTEDQKQEIREAFDLFDADGTGTIDIKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFSDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVNEQEFLRIMKKTSLY

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
2	Acetylation	------MASNFKKTT ------CCCCCCHHH	17.12	-
20	Phosphorylation	SAQRKRMSPKPELTE HHHHHCCCCCCCCCH	33.53	25521595
26	Phosphorylation	MSPKPELTEDQKQEI CCCCCCCCHHHHHHH	35.53	22942356
87	Phosphorylation	GTGKMNFSDFLTVMT CCCCCCHHHHHHHHH	23.58	22817900
98	Phosphorylation	TVMTQKMSEKDTKEE HHHHHHCCCCCCHHH	48.83	28059163
103	Ubiquitination	KMSEKDTKEEILKAF HCCCCCCHHHHHHHH	64.58	27667366
118	Phosphorylation	KLFDDDETGKISFKN HHCCCCCCCCCCHHH	51.25	27180971
120	Ubiquitination	FDDDETGKISFKNLK CCCCCCCCCCHHHHH	42.47	22790023
122	Phosphorylation	DDETGKISFKNLKRV CCCCCCCCHHHHHHH	33.38	24719451
124	Ubiquitination	ETGKISFKNLKRVAK CCCCCCHHHHHHHHH	55.36	22790023
127	Ubiquitination	KISFKNLKRVAKELG CCCHHHHHHHHHHHH	54.97	-
131	Ubiquitination	KNLKRVAKELGENLT HHHHHHHHHHHHCCC	51.09	22790023
138	Phosphorylation	KELGENLTDEELQEM HHHHHCCCHHHHHHH	53.60	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CETN2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CETN2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CETN2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RD23B_HUMAN	RAD23B	physical	20360068
CETN3_HUMAN	CETN3	physical	20360068
CETN2_HUMAN	CETN2	physical	20360068
XPC_HUMAN	XPC	physical	20360068
POC5_HUMAN	POC5	physical	20360068
UBP44_MOUSE	Usp44	physical	23187126
CETN3_HUMAN	CETN3	physical	26496610
CTNA1_HUMAN	CTNNA1	physical	26496610
DIAP2_HUMAN	DIAPH2	physical	26496610
IMB1_HUMAN	KPNB1	physical	26496610
PCM1_HUMAN	PCM1	physical	26496610
RAD9A_HUMAN	RAD9A	physical	26496610
SSBP_HUMAN	SSBP1	physical	26496610
TBP_HUMAN	TBP	physical	26496610
TMOD1_HUMAN	TMOD1	physical	26496610
XPC_HUMAN	XPC	physical	26496610
DYSF_HUMAN	DYSF	physical	26496610
GANP_HUMAN	MCM3AP	physical	26496610
GCC2_HUMAN	GCC2	physical	26496610
US6NL_HUMAN	USP6NL	physical	26496610
SFI1_HUMAN	SFI1	physical	26496610
PDCD6_HUMAN	PDCD6	physical	26496610
STIP1_HUMAN	STIP1	physical	26496610
CP131_HUMAN	CEP131	physical	26496610
CAMP2_HUMAN	CAMSAP2	physical	26496610
PRDX5_HUMAN	PRDX5	physical	26496610
GPKOW_HUMAN	GPKOW	physical	26496610
GPAM1_HUMAN	GPALPP1	physical	26496610
GRDN_HUMAN	CCDC88A	physical	26496610
NEUL_HUMAN	NLN	physical	26496610
POC5_HUMAN	POC5	physical	26496610
KLC3_HUMAN	KLC3	physical	26496610

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.
PubMed: 19144319

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, AND MASSSPECTROMETRY.
PubMed: 19367708