dbPTM

PCH2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCH2_HUMAN
UniProt AC	Q15645
Protein Name	Pachytene checkpoint protein 2 homolog
Gene Name	TRIP13
Organism	Homo sapiens (Human).
Sequence Length	432
Subcellular Localization
Protein Description	Plays a key role in chromosome recombination and chromosome structure development during meiosis. Required at early steps in meiotic recombination that leads to non-crossovers pathways. Also needed for efficient completion of homologous synapsis by influencing crossover distribution along the chromosomes affecting both crossovers and non-crossovers pathways. Also required for development of higher-order chromosome structures and is needed for synaptonemal-complex formation. In males, required for efficient synapsis of the sex chromosomes and for sex body formation. Promotes early steps of the DNA double-strand breaks (DSBs) repair process upstream of the assembly of RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from synapsed chromosomes (By similarity). Plays a role in mitotic spindle assembly checkpoint (SAC) activation. [PubMed: 28553959]
Protein Sequence	MDEAVGDLKQALPCVAESPTVHVEVHQRGSSTAKKEDINLSVRKLLNRHNIVFGDYTWTEFDEPFLTRNVQSVSIIDTELKVKDSQPIDLSACTVALHIFQLNEDGPSSENLEEETENIIAANHWVLPAAEFHGLWDSLVYDVEVKSHLLDYVMTTLLFSDKNVNSNLITWNRVVLLHGPPGTGKTSLCKALAQKLTIRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQDLIDDKDALVFVLIDEVESLTAARNACRAGTEPSDAIRVVNAVLTQIDQIKRHSNVVILTTSNITEKIDVAFVDRADIKQYIGPPSAAAIFKIYLSCLEELMKCQIIYPRQQLLTLRELEMIGFIENNVSKLSLLLNDISRKSEGLSGRVLRKLPFLAHALYVQAPTVTIEGFLQALSLAVDKQFEERKKLAAYI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDEAVGDL -------CCCHHHHH	10.69	22223895
9	Sumoylation	DEAVGDLKQALPCVA CCHHHHHHHHCHHEE	37.96	-
18	Phosphorylation	ALPCVAESPTVHVEV HCHHEECCCEEEEEE	19.01	30266825
20	Phosphorylation	PCVAESPTVHVEVHQ HHEECCCEEEEEEEE	32.30	30266825
30	Phosphorylation	VEVHQRGSSTAKKED EEEEECCCCCCCHHH	27.06	29214152
31	Phosphorylation	EVHQRGSSTAKKEDI EEEECCCCCCCHHHC	34.90	29214152
32	Phosphorylation	VHQRGSSTAKKEDIN EEECCCCCCCHHHCC	44.16	26055452
34	Ubiquitination	QRGSSTAKKEDINLS ECCCCCCCHHHCCHH	57.70	-
35	Ubiquitination	RGSSTAKKEDINLSV CCCCCCCHHHCCHHH	59.14	29967540
41	Phosphorylation	KKEDINLSVRKLLNR CHHHCCHHHHHHHHH	18.52	21815630
56	Phosphorylation	HNIVFGDYTWTEFDE CCCEEECCEECCCCC	12.45	22817900
72	Phosphorylation	FLTRNVQSVSIIDTE CCCCCCEEEEEEEEE	17.35	29214152
74	Phosphorylation	TRNVQSVSIIDTELK CCCCEEEEEEEEEEE	21.05	21712546
81	Ubiquitination	SIIDTELKVKDSQPI EEEEEEEEECCCCCC	40.79	21963094
83	Ubiquitination	IDTELKVKDSQPIDL EEEEEEECCCCCCCH	50.50	22817900
147	Phosphorylation	VYDVEVKSHLLDYVM EEEHHHHHHHHHHHH	25.25	20068231
152	Phosphorylation	VKSHLLDYVMTTLLF HHHHHHHHHHHHHHC	7.65	23898821
155	Phosphorylation	HLLDYVMTTLLFSDK HHHHHHHHHHHCCCC	12.30	20068231
156	Phosphorylation	LLDYVMTTLLFSDKN HHHHHHHHHHCCCCC	11.90	23898821
160	Phosphorylation	VMTTLLFSDKNVNSN HHHHHHCCCCCCCCC	47.87	23898821
183	Phosphorylation	LLHGPPGTGKTSLCK EECCCCCCCHHHHHH	41.08	-
185	Ubiquitination	HGPPGTGKTSLCKAL CCCCCCCHHHHHHHH	34.48	27667366
185 (in isoform 1)	Ubiquitination	-	34.48	21890473
190	Ubiquitination	TGKTSLCKALAQKLT CCHHHHHHHHHHHHH	52.29	22817900
190	Acetylation	TGKTSLCKALAQKLT CCHHHHHHHHHHHHH	52.29	27452117
195	Ubiquitination	LCKALAQKLTIRLSS HHHHHHHHHHHEHHH	41.83	27667366
206	Phosphorylation	RLSSRYRYGQLIEIN EHHHCCCCCEEEEEC	10.57	-
216	Phosphorylation	LIEINSHSLFSKWFS EEEECCHHHHHHHHH	30.82	-
219	Phosphorylation	INSHSLFSKWFSESG ECCHHHHHHHHHHHC	33.98	24719451
227	Acetylation	KWFSESGKLVTKMFQ HHHHHHCHHHHHHHH	49.41	27452117
227 (in isoform 1)	Ubiquitination	-	49.41	21890473
227	Ubiquitination	KWFSESGKLVTKMFQ HHHHHHCHHHHHHHH	49.41	22817900
231	Ubiquitination	ESGKLVTKMFQKIQD HHCHHHHHHHHHHHH	30.18	22817900
235	Ubiquitination	LVTKMFQKIQDLIDD HHHHHHHHHHHHCCC	30.94	29967540
288 (in isoform 1)	Ubiquitination	-	38.12	21890473
288	Ubiquitination	LTQIDQIKRHSNVVI HHHHHHHHHHCCEEE	38.12	21963094
288	2-Hydroxyisobutyrylation	LTQIDQIKRHSNVVI HHHHHHHHHHCCEEE	38.12	-
291	Phosphorylation	IDQIKRHSNVVILTT HHHHHHHCCEEEEEC	35.04	30576142
297	Phosphorylation	HSNVVILTTSNITEK HCCEEEEECCCCCCE	19.63	20860994
298	Phosphorylation	SNVVILTTSNITEKI CCEEEEECCCCCCEE	19.14	20860994
316 (in isoform 1)	Ubiquitination	-	37.28	21890473
316	Ubiquitination	FVDRADIKQYIGPPS EECHHHHHHHHCCHH	37.28	21963094
318	Phosphorylation	DRADIKQYIGPPSAA CHHHHHHHHCCHHHH	11.66	24043423
323	Phosphorylation	KQYIGPPSAAAIFKI HHHHCCHHHHHHHHH	33.40	20446291
331	Phosphorylation	AAAIFKIYLSCLEEL HHHHHHHHHHHHHHH	7.98	24043423
333	Phosphorylation	AIFKIYLSCLEELMK HHHHHHHHHHHHHHC	10.32	24043423
340	Ubiquitination	SCLEELMKCQIIYPR HHHHHHHCCCCCCCH	35.30	21963094
345	Phosphorylation	LMKCQIIYPRQQLLT HHCCCCCCCHHHHHH	8.26	24043423
358	Sulfoxidation	LTLRELEMIGFIENN HHHHHHHHHCCCCCC	5.92	21406390
367	Phosphorylation	GFIENNVSKLSLLLN CCCCCCHHHHHHHHH	29.97	21712546
370	Phosphorylation	ENNVSKLSLLLNDIS CCCHHHHHHHHHHHH	22.25	21712546
377	Phosphorylation	SLLLNDISRKSEGLS HHHHHHHHHCCCCCC	36.20	21406692
380	Phosphorylation	LNDISRKSEGLSGRV HHHHHHCCCCCCHHH	35.47	20068231
384	Phosphorylation	SRKSEGLSGRVLRKL HHCCCCCCHHHHHHH	35.10	20068231

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of PCH2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PCH2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PCH2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CK054_HUMAN	C11orf54	physical	16189514
GRIN2_HUMAN	GPRIN2	physical	16189514
TEX37_HUMAN	TEX37	physical	16189514
ASB13_HUMAN	ASB13	physical	16189514
PCH2_HUMAN	TRIP13	physical	16189514
MD2BP_HUMAN	MAD2L1BP	physical	16189514
NB5R2_HUMAN	CYB5R2	physical	16189514
STALP_HUMAN	STAMBPL1	physical	16189514
HDHD3_HUMAN	HDHD3	physical	16189514
GPSM1_HUMAN	GPSM1	physical	16189514
CAR14_HUMAN	CARD14	physical	16189514
ZN655_HUMAN	ZNF655	physical	16189514
TLDC1_HUMAN	TLDC1	physical	16189514
LNX1_HUMAN	LNX1	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
DTX2_HUMAN	DTX2	physical	16189514
PLS4_HUMAN	PLSCR4	physical	16189514
GLCTK_HUMAN	GLYCTK	physical	16189514
DDAH2_HUMAN	DDAH2	physical	16189514
LOXL4_HUMAN	LOXL4	physical	16189514
SC24A_HUMAN	SEC24A	physical	16189514
SMUG1_HUMAN	SMUG1	physical	16189514
PLAC8_HUMAN	PLAC8	physical	16189514
PBLD_HUMAN	PBLD	physical	16189514
NIF3L_HUMAN	NIF3L1	physical	16189514
SEM4G_HUMAN	SEMA4G	physical	16189514
PLS3_HUMAN	PLSCR3	physical	16189514
INT11_HUMAN	CPSF3L	physical	16189514
NTAQ1_HUMAN	WDYHV1	physical	16189514
KRA32_HUMAN	KRTAP3-2	physical	16189514
ARL11_HUMAN	ARL11	physical	16189514
DPYL1_HUMAN	CRMP1	physical	16169070
PCH2_HUMAN	TRIP13	physical	16169070
UBA1_HUMAN	UBA1	physical	22939629
TTC37_HUMAN	TTC37	physical	22939629
ADPPT_HUMAN	AASDHPPT	physical	22863883
S10A4_HUMAN	S100A4	physical	22863883
NIPA_HUMAN	ZC3HC1	physical	22863883
PCH2_HUMAN	TRIP13	physical	25416956
DPYL4_HUMAN	DPYSL4	physical	25416956
DIP2A_HUMAN	DIP2A	physical	25416956
TNR6A_HUMAN	TNRC6A	physical	25416956
NAGA_HUMAN	AMDHD2	physical	25416956
NB5R2_HUMAN	CYB5R2	physical	25416956
PCMD2_HUMAN	PCMTD2	physical	25416956
PLS3_HUMAN	PLSCR3	physical	25416956
PELI1_HUMAN	PELI1	physical	25416956
SPRY7_HUMAN	SPRYD7	physical	25416956
SEM4G_HUMAN	SEMA4G	physical	25416956
PBLD_HUMAN	PBLD	physical	25416956
TINAL_HUMAN	TINAGL1	physical	25416956
FND3B_HUMAN	FNDC3B	physical	25416956
ZNF34_HUMAN	ZNF34	physical	25416956
LOXL4_HUMAN	LOXL4	physical	25416956
RHXF2_HUMAN	RHOXF2	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
LLR1_HUMAN	LRR1	physical	25416956
M1AP_HUMAN	M1AP	physical	25416956
GLCTK_HUMAN	GLYCTK	physical	25416956
CD033_HUMAN	C4orf33	physical	25416956
MGT5B_HUMAN	MGAT5B	physical	25416956
MET15_HUMAN	METTL15	physical	25416956
TEX37_HUMAN	TEX37	physical	25416956
MORN3_HUMAN	MORN3	physical	25416956
KR122_HUMAN	KRTAP12-2	physical	25416956
KR121_HUMAN	KRTAP12-1	physical	25416956
KR261_HUMAN	KRTAP26-1	physical	25416956
MSH2_HUMAN	MSH2	physical	26344197
TADBP_HUMAN	TARDBP	physical	26344197
TTC4_HUMAN	TTC4	physical	26344197
MD2BP_HUMAN	MAD2L1BP	physical	26324890
MD2L1_HUMAN	MAD2L1	physical	26324890
BUB1B_HUMAN	BUB1B	physical	26324890
CDC20_HUMAN	CDC20	physical	26324890
PCH2_HUMAN	TRIP13	physical	26324890
MTG1_HUMAN	MTG1	physical	28514442
PUSL1_HUMAN	PUSL1	physical	28514442
ADAT3_HUMAN	ADAT3	physical	28514442
QOR_HUMAN	CRYZ	physical	28514442
P4K2B_HUMAN	PI4K2B	physical	28514442
INT11_HUMAN	CPSF3L	physical	28514442

Drug and Disease Associations

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

Regulatory Network of PCH2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, AND MASSSPECTROMETRY.	15592455 [Abstract]