dbPTM

PIN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PIN1_HUMAN
UniProt AC	Q13526
Protein Name	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Gene Name	PIN1
Organism	Homo sapiens (Human).
Sequence Length	163
Subcellular Localization	Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122).
Protein Description	Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. [PubMed: 21497122]
Protein Sequence	MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Sumoylation	--MADEEKLPPGWEK --CCCHHCCCCCHHH	65.33	-
6	Sumoylation	--MADEEKLPPGWEK --CCCHHCCCCCHHH	65.33	-
6	Ubiquitination	--MADEEKLPPGWEK --CCCHHCCCCCHHH	65.33	30230243
13	Ubiquitination	KLPPGWEKRMSRSSG CCCCCHHHHCCCCCC	47.06	22817900
16	Phosphorylation	PGWEKRMSRSSGRVY CCHHHHCCCCCCCEE	32.80	11723108
18	Phosphorylation	WEKRMSRSSGRVYYF HHHHCCCCCCCEEEE	29.82	27251275
19	Phosphorylation	EKRMSRSSGRVYYFN HHHCCCCCCCEEEEE	29.52	27251275
23	Phosphorylation	SRSSGRVYYFNHITN CCCCCCEEEEECCCC	10.86	17360941
29	Phosphorylation	VYYFNHITNASQWER EEEEECCCCHHHCCC	19.72	28450419
32	Phosphorylation	FNHITNASQWERPSG EECCCCHHHCCCCCC	37.59	28450419
38	Phosphorylation	ASQWERPSGNSSSGG HHHCCCCCCCCCCCC	57.75	28450419
41	Phosphorylation	WERPSGNSSSGGKNG CCCCCCCCCCCCCCC	29.43	28450419
42	Phosphorylation	ERPSGNSSSGGKNGQ CCCCCCCCCCCCCCC	36.68	28450419
43	Phosphorylation	RPSGNSSSGGKNGQG CCCCCCCCCCCCCCC	51.92	22617229
46	Acetylation	GNSSSGGKNGQGEPA CCCCCCCCCCCCCCC	62.52	19608861
58	Phosphorylation	EPARVRCSHLLVKHS CCCEEHHHHHEECCC	13.45	27251275
63	Acetylation	RCSHLLVKHSQSRRP HHHHHEECCCCCCCC	37.19	23749302
63	Sumoylation	RCSHLLVKHSQSRRP HHHHHEECCCCCCCC	37.19	-
63	Ubiquitination	RCSHLLVKHSQSRRP HHHHHEECCCCCCCC	37.19	29967540
63	Sumoylation	RCSHLLVKHSQSRRP HHHHHEECCCCCCCC	37.19	-
65	Phosphorylation	SHLLVKHSQSRRPSS HHHEECCCCCCCCCC	24.92	22817900
67	Phosphorylation	LLVKHSQSRRPSSWR HEECCCCCCCCCCHH	33.02	27251275
71	Phosphorylation	HSQSRRPSSWRQEKI CCCCCCCCCHHHHHH	40.50	21497122
72	Phosphorylation	SQSRRPSSWRQEKIT CCCCCCCCHHHHHHH	29.03	23532336
77	Ubiquitination	PSSWRQEKITRTKEE CCCHHHHHHHCCHHH	40.83	22817900
82	Sumoylation	QEKITRTKEEALELI HHHHHCCHHHHHHHH	50.71	-
82	Ubiquitination	QEKITRTKEEALELI HHHHHCCHHHHHHHH	50.71	22817900
82	Sumoylation	QEKITRTKEEALELI HHHHHCCHHHHHHHH	50.71	-
82	Acetylation	QEKITRTKEEALELI HHHHHCCHHHHHHHH	50.71	30591337
87	Ubiquitination	RTKEEALELINGYIQ CCHHHHHHHHHHHHH	55.44	21890473
92	Phosphorylation	ALELINGYIQKIKSG HHHHHHHHHHHHHCC	8.83	28387310
95	Ubiquitination	LINGYIQKIKSGEED HHHHHHHHHHCCHHH	42.41	21139048
97	Ubiquitination	NGYIQKIKSGEEDFE HHHHHHHHCCHHHHH	60.49	33845483
98	Phosphorylation	GYIQKIKSGEEDFES HHHHHHHCCHHHHHH	55.71	30576142
100	Ubiquitination	IQKIKSGEEDFESLA HHHHHCCHHHHHHHH	62.58	21890473
105	Phosphorylation	SGEEDFESLASQFSD CCHHHHHHHHHHHCC	29.27	22210691
108	Phosphorylation	EDFESLASQFSDCSS HHHHHHHHHHCCCHH	36.73	17525332
111	Phosphorylation	ESLASQFSDCSSAKA HHHHHHHCCCHHCHH	30.03	28387310
114	Phosphorylation	ASQFSDCSSAKARGD HHHHCCCHHCHHHCC	38.02	21712546
115	Phosphorylation	SQFSDCSSAKARGDL HHHCCCHHCHHHCCC	39.87	25627689
117	Acetylation	FSDCSSAKARGDLGA HCCCHHCHHHCCCCC	40.33	25953088
117	Ubiquitination	FSDCSSAKARGDLGA HCCCHHCHHHCCCCC	40.33	32015554
122	Ubiquitination	SAKARGDLGAFSRGQ HCHHHCCCCCCCCCC	6.25	22505724
130	Sulfoxidation	GAFSRGQMQKPFEDA CCCCCCCCCCCCCCC	6.52	21406390
132	Ubiquitination	FSRGQMQKPFEDASF CCCCCCCCCCCCCCH	46.46	22817900
137	Ubiquitination	MQKPFEDASFALRTG CCCCCCCCCHHHHCC	10.19	21890473
138	Phosphorylation	QKPFEDASFALRTGE CCCCCCCCHHHHCCC	24.31	28857561
142	Methylation	EDASFALRTGEMSGP CCCCHHHHCCCCCCC	36.94	115487563
147	Phosphorylation	ALRTGEMSGPVFTDS HHHCCCCCCCEECCC	35.33	27080861
152	Phosphorylation	EMSGPVFTDSGIHII CCCCCEECCCEEEEE	29.50	28450419
154	Phosphorylation	SGPVFTDSGIHIILR CCCEECCCEEEEEEE	36.27	25849741

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
16	S	Phosphorylation	Kinase	AURKA	O14965	GPS
16	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
16	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
16	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
65	S	Phosphorylation	Kinase	PLK1	P53350	PSP
71	S	Phosphorylation	Kinase	DAPK1	P53355	Uniprot
71	S	Phosphorylation	Kinase	PKACA	P17612	PSP
138	S	Phosphorylation	Kinase	MAP3K11	Q16584	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
71	S	Phosphorylation		21497122
Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.

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 PIN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF2_HUMAN	TRAF2	physical	16189514
T22D4_HUMAN	TSC22D4	physical	16189514
RAI1_HUMAN	RAI1	physical	16189514
GGA2_HUMAN	GGA2	physical	16189514
ZMIZ2_HUMAN	ZMIZ2	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
CTIP_HUMAN	RBBP8	physical	16189514
DAB2_HUMAN	DAB2	physical	12881709
CSK21_HUMAN	CSNK2A1	physical	11940573
CSK22_HUMAN	CSNK2A2	physical	11940573
TOP2A_HUMAN	TOP2A	physical	11940573
WEE1_HUMAN	WEE1	physical	9499405
PLK1_HUMAN	PLK1	physical	9499405
CDC27_HUMAN	CDC27	physical	9499405
PMYT1_HUMAN	PKMYT1	physical	9499405
MPIP3_HUMAN	CDC25C	physical	9499405
SOX3A_XENLA	sox3	physical	9499405
WEE1B_XENLA	wee1B	physical	9499405
PMYT1_XENLA	pkmyt1	physical	9499405
JUN_HUMAN	JUN	physical	11432833
P53_HUMAN	TP53	physical	12388558
NFAC2_HUMAN	NFATC2	physical	11356192
TAU_HUMAN	MAPT	physical	10391244
P53_HUMAN	TP53	physical	12397362
KI20B_HUMAN	KIF20B	physical	11470801
MPIP3_HUMAN	CDC25C	physical	11604498
SPT5H_HUMAN	SUPT5H	physical	11575923
RPB1_HUMAN	POLR2A	physical	10393805
MPIP3_HUMAN	CDC25C	physical	10037602
PLK1_HUMAN	PLK1	physical	10037602
CDC27_HUMAN	CDC27	physical	10037602
SMAD2_HUMAN	SMAD2	physical	19122240
SMAD3_HUMAN	SMAD3	physical	19122240
FOXO4_HUMAN	FOXO4	physical	18794148
MCL1_HUMAN	MCL1	physical	17670986
PLK1_HUMAN	PLK1	physical	16118204
RARA_HUMAN	RARA	physical	15670742
RED1_HUMAN	ADARB1	physical	21847096
CDN1B_HUMAN	CDKN1B	physical	19584057
DEAF1_HUMAN	DEAF1	physical	21900206
TSC2_HUMAN	TSC2	physical	21900206
CASP6_HUMAN	CASP6	physical	21900206
COBA2_HUMAN	COL11A2	physical	21900206
KIF5A_HUMAN	KIF5A	physical	21900206
CENPB_HUMAN	CENPB	physical	21900206
P53_HUMAN	TP53	physical	21900206
CSAD_HUMAN	CSAD	physical	21900206
ATPB_HUMAN	ATP5B	physical	21900206
CPNE6_HUMAN	CPNE6	physical	21900206
KPYM_HUMAN	PKM	physical	21900206
CC90B_HUMAN	CCDC90B	physical	21900206
DC1I1_HUMAN	DYNC1I1	physical	21900206
EIF3G_HUMAN	EIF3G	physical	21900206
U119A_HUMAN	UNC119	physical	21900206
DDAH2_HUMAN	DDAH2	physical	21900206
APLP1_HUMAN	APLP1	physical	21900206
CHSP1_HUMAN	CARHSP1	physical	21900206
SYQ_HUMAN	QARS	physical	21900206
WIZ_HUMAN	WIZ	physical	21900206
KMT2B_HUMAN	KMT2B	physical	21900206
TRM2A_HUMAN	TRMT2A	physical	21900206
BAG6_HUMAN	BAG6	physical	21900206
LRIF1_HUMAN	LRIF1	physical	21900206
DMPK_HUMAN	DMPK	physical	21900206
CDK10_HUMAN	CDK10	physical	22158035
CCNE1_HUMAN	CCNE1	physical	16223725
CDK2_HUMAN	CDK2	physical	16223725
NCOA3_HUMAN	NCOA3	physical	16227615
EP300_HUMAN	EP300	physical	16227615
FBXW7_HUMAN	FBXW7	physical	22608923
RUNX3_HUMAN	RUNX3	physical	22580604
BCL6_HUMAN	BCL6	physical	17828269
DAXX_HUMAN	DAXX	physical	17938171
TF65_HUMAN	RELA	physical	14690596
AATF_HUMAN	AATF	physical	17468107
IRF3_HUMAN	IRF3	physical	16699525
PML_HUMAN	PML	physical	18039859
P73_HUMAN	TP73	physical	15175157
PML_HUMAN	PML	physical	20100838
PML_HUMAN	PML	physical	22033920
SYUA_HUMAN	SNCA	physical	16365047
TAU_HUMAN	MAPT	physical	16365047
SNCAP_HUMAN	SNCAIP	physical	16365047
UBE2A_HUMAN	UBE2A	physical	22939629
PP2AA_HUMAN	PPP2CA	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
SMAD3_HUMAN	SMAD3	physical	19920136
SMAD2_HUMAN	SMAD2	physical	19920136
MYB_MOUSE	Myb	physical	18359295
RAF1_HUMAN	RAF1	physical	15664191
IPKB_HUMAN	PKIB	physical	21988832
SHKB1_HUMAN	SHKBP1	physical	21988832
SMAD3_HUMAN	SMAD3	physical	21988832
SPT5H_HUMAN	SUPT5H	physical	21988832
TNIP1_HUMAN	TNIP1	physical	21988832
BCLF1_HUMAN	BCLAF1	physical	16055720
CCNK_HUMAN	CCNK	physical	16055720
CDK12_HUMAN	CDK12	physical	16055720
ETV6_HUMAN	ETV6	physical	16055720
MED1_HUMAN	MED1	physical	16055720
TR150_HUMAN	THRAP3	physical	16055720
TLE3_HUMAN	TLE3	physical	16055720
DDX17_HUMAN	DDX17	physical	16055720
DDX3X_HUMAN	DDX3X	physical	16055720
DDX5_HUMAN	DDX5	physical	16055720
DHX15_HUMAN	DHX15	physical	16055720
VIR_HUMAN	KIAA1429	physical	16055720
STPAP_HUMAN	TUT1	physical	16055720
G3BP2_HUMAN	G3BP2	physical	16055720
G3BP1_HUMAN	G3BP1	physical	16055720
HNRH1_HUMAN	HNRNPH1	physical	16055720
HNRPK_HUMAN	HNRNPK	physical	16055720
HNRPU_HUMAN	HNRNPU	physical	16055720
U5S1_HUMAN	EFTUD2	physical	16055720
NONO_HUMAN	NONO	physical	16055720
PABP1_HUMAN	PABPC1	physical	16055720
PRP8_HUMAN	PRPF8	physical	16055720
RNPS1_HUMAN	RNPS1	physical	16055720
SFPQ_HUMAN	SFPQ	physical	16055720
SRS11_HUMAN	SRSF11	physical	16055720
SRRM1_HUMAN	SRRM1	physical	16055720
SRRM2_HUMAN	SRRM2	physical	16055720
U2AF2_HUMAN	U2AF2	physical	16055720
U520_HUMAN	SNRNP200	physical	16055720
RL4_HUMAN	RPL4	physical	16055720
DDB1_HUMAN	DDB1	physical	16055720
WRIP1_HUMAN	WRNIP1	physical	16055720
CD11B_HUMAN	CDK11B	physical	16055720
CD11A_HUMAN	CDK11A	physical	16055720
XRCC6_HUMAN	XRCC6	physical	16055720
MAP1S_HUMAN	MAP1S	physical	16055720
AP2A1_HUMAN	AP2A1	physical	16055720
REPS1_HUMAN	REPS1	physical	16055720
CHAP1_HUMAN	CHAMP1	physical	16055720
PRRC1_HUMAN	PRRC1	physical	16055720
CAPR1_HUMAN	CAPRIN1	physical	16055720
TBCD4_HUMAN	TBC1D4	physical	16055720
TFG_HUMAN	TFG	physical	16055720
ECHA_HUMAN	HADHA	physical	16055720
KPYM_HUMAN	PKM	physical	16055720
CTIP_HUMAN	RBBP8	physical	25416956
ITF2_HUMAN	TCF4	physical	25416956
TRAF1_HUMAN	TRAF1	physical	25416956
TRAF2_HUMAN	TRAF2	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
ZBT14_HUMAN	ZBTB14	physical	25416956
KRT38_HUMAN	KRT38	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
ZBT22_HUMAN	ZBTB22	physical	25416956
JKIP2_HUMAN	JAKMIP2	physical	25416956
ABI2_HUMAN	ABI2	physical	25416956
CNKR1_HUMAN	CNKSR1	physical	25416956
TNIP1_HUMAN	TNIP1	physical	25416956
IKZF1_HUMAN	IKZF1	physical	25416956
RAI1_HUMAN	RAI1	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
ARHGF_HUMAN	ARHGEF15	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
NUP62_HUMAN	NUP62	physical	25416956
SSBP3_HUMAN	SSBP3	physical	25416956
ZBT7B_HUMAN	ZBTB7B	physical	25416956
ATL4_HUMAN	ADAMTSL4	physical	25416956
CEP55_HUMAN	CEP55	physical	25416956
ZN446_HUMAN	ZNF446	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
CEP76_HUMAN	CEP76	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
THAP7_HUMAN	THAP7	physical	25416956
T22D4_HUMAN	TSC22D4	physical	25416956
ZMIZ2_HUMAN	ZMIZ2	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
ANR40_HUMAN	ANKRD40	physical	25416956
FOXP2_HUMAN	FOXP2	physical	25416956
HEXI2_HUMAN	HEXIM2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
PRRC1_HUMAN	PRRC1	physical	25416956
AMOT_HUMAN	AMOT	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
ZBTB9_HUMAN	ZBTB9	physical	25416956
TAB3_HUMAN	TAB3	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR101_HUMAN	KRTAP10-1	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
CC184_HUMAN	CCDC184	physical	25416956
SP1_HUMAN	SP1	physical	25398907
PML_HUMAN	PML	physical	24586174
P53_HUMAN	TP53	physical	17906639
POL_HV1H2	gag-pol	physical	24001231
PPARG_HUMAN	PPARG	physical	19996102
FKB1A_HUMAN	FKBP1A	physical	26344197
FKB1B_HUMAN	FKBP1B	physical	26344197
HINT1_HUMAN	HINT1	physical	26344197
MSI2H_HUMAN	MSI2	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
SODC_HUMAN	SOD1	physical	26344197
TBCA_HUMAN	TBCA	physical	26344197
ZO1_HUMAN	TJP1	physical	26344197
T22D4_HUMAN	TSC22D4	physical	21516116
SGK1_HUMAN	SGK1	physical	25667458
CPEB1_HUMAN	CPEB1	physical	26456073
REST_HUMAN	REST	physical	25197063
KPYM_HUMAN	PKM	physical	23178880
ATCAY_HUMAN	ATCAY	physical	18628984
FADD_HUMAN	FADD	physical	23606538

Drug and Disease Associations

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

Regulatory Network of PIN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Death-associated protein kinase 1 phosphorylates Pin1 and inhibitsits prolyl isomerase activity and cellular function."; Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S.,Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.; Mol. Cell 42:147-159(2011). Cited for: FUNCTION, PHOSPHORYLATION AT SER-71, INTERACTION WITH DAPK1,SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, AND TISSUE SPECIFICITY.	21497122 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.	17525332 [Abstract]

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