dbPTM

PIN4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PIN4_HUMAN
UniProt AC	Q9Y237
Protein Name	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
Gene Name	PIN4
Organism	Homo sapiens (Human).
Sequence Length	131
Subcellular Localization	Isoform 1: Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Colocalizes in the nucleolus during interphase and on the spindle apparatus during mitosis with NPM1. Isoform 2: Mitochondrion. Mitochondrion matrix. Imported in a time
Protein Description	Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.; Isoform 2 binds to double-stranded DNA..
Protein Sequence	MPPKGKSGSGKAGKGGAASGSDSADKKAQGPKGGGNAVKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKFGYHIIMVEGRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MPPKGKSGSGKAG --CCCCCCCCCCCCC	58.74	7306959
11	Acetylation	KGKSGSGKAGKGGAA CCCCCCCCCCCCCCC	56.51	7306969
18 (in isoform 3)	Phosphorylation	-	20.07	-
18 (in isoform 2)	Phosphorylation	-	20.07	-
19	Phosphorylation	AGKGGAASGSDSADK CCCCCCCCCCCCCCH	37.99	12860119
23	Phosphorylation	GAASGSDSADKKAQG CCCCCCCCCCHHHCC	39.81	28985074
24 (in isoform 3)	Phosphorylation	-	37.32	-
24 (in isoform 2)	Phosphorylation	-	37.32	-
32	Acetylation	DKKAQGPKGGGNAVK CHHHCCCCCCCCCHH	76.61	19608861
39	Ubiquitination	KGGGNAVKVRHILCE CCCCCCHHHEEEEHH	31.01	33845483
44	Phosphorylation	AVKVRHILCEKHGKI CHHHEEEEHHHHHHH	2.23	12860119
45	S-nitrosocysteine	VKVRHILCEKHGKIM HHHEEEEHHHHHHHH	6.91	-
45	S-nitrosylation	VKVRHILCEKHGKIM HHHEEEEHHHHHHHH	6.91	19483679
47	2-Hydroxyisobutyrylation	VRHILCEKHGKIMEA HEEEEHHHHHHHHHH	57.57	-
47	Acetylation	VRHILCEKHGKIMEA HEEEEHHHHHHHHHH	57.57	23749302
47	Ubiquitination	VRHILCEKHGKIMEA HEEEEHHHHHHHHHH	57.57	-
57	2-Hydroxyisobutyrylation	KIMEAMEKLKSGMRF HHHHHHHHHHHCCCH	48.40	-
57	Acetylation	KIMEAMEKLKSGMRF HHHHHHHHHHHCCCH	48.40	19608861
72	Ubiquitination	NEVAAQYSEDKARQG HHHHHHHCHHHHHCC	27.52	32015554
72	Acetylation	NEVAAQYSEDKARQG HHHHHHHCHHHHHCC	27.52	-
75	Ubiquitination	AAQYSEDKARQGGDL HHHHCHHHHHCCCCC	41.22	29967540
75	Acetylation	AAQYSEDKARQGGDL HHHHCHHHHHCCCCC	41.22	25953088
75	2-Hydroxyisobutyrylation	AAQYSEDKARQGGDL HHHHCHHHHHCCCCC	41.22	-
100	Ubiquitination	PFQEAAFALPVSGMD CCHHHHHCCCCCCCC	13.26	24816145
100	Acetylation	PFQEAAFALPVSGMD CCHHHHHCCCCCCCC	13.26	-
119	Acetylation	TDPPVKTKFGYHIIM CCCCCCCCCEEEEEE	30.95	25953088
122	Phosphorylation	PVKTKFGYHIIMVEG CCCCCCEEEEEEEEC	7.93	21082442
147	Phosphorylation	----------------------- -----------------------		19901323

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
19	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
19	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
19	S	Phosphorylation	Kinase	CK2	-	Uniprot
19	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
19	S	Phosphorylation		19369196
Isoform 1 phosphorylation at Ser-19 does not affect its PPIase activity but is required for nuclear localization, and the dephosphorylation is a prerequisite for the binding to DNA.

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 PIN4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RRBP1_HUMAN	RRBP1	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
TIM44_HUMAN	TIMM44	physical	22939629
SRPRB_HUMAN	SRPRB	physical	22939629
RAD21_HUMAN	RAD21	physical	22939629
SCO2_HUMAN	SCO2	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
UBE2S_HUMAN	UBE2S	physical	22939629
PNMA1_HUMAN	PNMA1	physical	25416956
CEP72_HUMAN	CEP72	physical	25416956
FATE1_HUMAN	FATE1	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
ZBTB9_HUMAN	ZBTB9	physical	25416956
TCPE_HUMAN	CCT5	physical	26344197
DYHC1_HUMAN	DYNC1H1	physical	26344197
SYMC_HUMAN	MARS	physical	26344197
CHSTF_HUMAN	CHST15	physical	28514442

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 PIN4_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-32, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of the N-terminal domain regulates subcellularlocalization and DNA binding properties of the peptidyl-prolylcis/trans isomerase hPar14."; Reimer T., Weiwad M., Schierhorn A., Ruecknagel P.-K., Rahfeld J.-U.,Bayer P., Fischer G.; J. Mol. Biol. 330:955-966(2003). Cited for: PROTEIN SEQUENCE OF 15-25, IDENTIFICATION BY MASS SPECTROMETRY,PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19, AND SUBCELLULARLOCATION.	12860119 [Abstract]

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